|
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: 970.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 116 QPYEWLSYKQVAEMSECLGSALIQKGFTATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAEL 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 196 SLVFVDKpekaklllegvenkltpslkiivlmdaygselvergqkcGVEIISLKAMEDLGRANRRKPKPPAPEDLAVVCF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 276 TSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 356 KVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGKVRLMVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 434 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA--EGEGEVCVK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 512 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGE 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 592 SLQAFLIAIVVPDVETLRPWA-QKRGFDGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGIALHPELFSIDNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1622942221 671 TPTMKAKRPELRNYFRSQIDELYS 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
88-696 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 704.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 88 DVTTLYEGFQRGIQVSNNGPCLGSR-KPDQ---PYEWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVII 163
Cdd:PLN02736 42 EIGTLHDNFVYAVETFRDYKYLGTRiRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWLIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 164 EQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVdKPEKAKLLLEGVENklTPSLKIIVLMDAYGSELVERGQKCGV 243
Cdd:PLN02736 120 DHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGTGV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 244 EIISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENsvnpCPDDTLISFLPLA 323
Cdd:PLN02736 197 EIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF----YPSDVHISYLPLA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 324 HMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAEL 401
Cdd:PLN02736 273 HIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQAL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 402 RSGiiRNNS-LWDRLIFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSM--PGDWTAG 478
Cdd:PLN02736 353 ENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTE--TSCVISGmdEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 479 HVGAPMPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PLN02736 429 HVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 556 KKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESLQAFLIAIVVPDVETLRPWAQKRGFD-GSFEELCRNKDVKKAI 634
Cdd:PLN02736 509 KKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAV 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622942221 635 LEDMVRLGKDSGLKPFEQVKGIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYSTI 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: 536.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 86 YEDVTTLYEGFQRGIQVSNNGPCLgSRKPDQPYEWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQ 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVK--PGDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 166 GCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVDKPEKAKLLLEGVENklTPSLKIIVLMDaygselvERGQKCGVEI 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 246 ISLKAMEDLGRANR------RKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKAtensVNPCPDDTLISF 319
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 320 LPLAHMFERVVECVMLCHGAKIGFfQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLDFA---S 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 395 KRKEAELRSGiiRNNSLW--------DRLIFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 467 CCLSMPGDWTAGHVGAPMPCNLIKLvdveemnymaAEgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI----------AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 547 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESlQAFLIAIVVPDVETLRPWAQKRGFD-GSFEELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622942221 626 RNKDVKKAILEDMVRLGKdsGLKPFEQVKGIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYS 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 |
1.02e-170 |
|
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: 496.35 E-value: 1.02e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 116 QPYEWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAEL 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVE--PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 196 SLVFVDKPEkaklllegvenkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkppapeDLAVVCF 275
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 276 TSGTTGNPKGALITHRNIVSDCSAFVKAtensVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIGFFQgDIRLLMDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 355 LKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslGGKVRLMVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 435 AAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 515 VFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESlQ 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 595 AFLIAIVVPDVETLRPWAQKRG-FDGSFEELCRNKDVKKAILEDMVRLGKdsGLKPFEQVKGIALHPELFSIDNGLLTPT 673
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1622942221 674 MKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
87-698 |
1.53e-159 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 475.49 E-value: 1.53e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 87 EDVTTLYEGFQRGIQVSNNGPCLGSRKPDQ----PYEWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVI 162
Cdd:PLN02861 40 ADIDSPWQFFSDAVKKYPNNQMLGRRQVTDskvgPYVWLTYKEVYDAAIRIGSAIRSRG--VNPGDRCGIYGSNCPEWII 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 163 IEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVDKPEKAKLLleGVENKLTPSLKIIVLMDAYGSELVERGQKCG 242
Cdd:PLN02861 118 AMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 243 VEIISLKAMEDLGRANRRKPkPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSA---FVKATENSVNPcpDDTLISF 319
Cdd:PLN02861 196 VSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLStdhLLKVTDRVATE--EDSYFSY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 320 LPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLlnrmFDRIFG------QANTTLKRWLLDFA 393
Cdd:PLN02861 273 LPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 394 SKRKEAELRSGIIRNNS--LWDRLIFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSM 471
Cdd:PLN02861 349 YNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 472 PGDWT-AGHVGAPMPCNLIKLVDVEEMNYMAAEG--EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNG 548
Cdd:PLN02861 429 ANVFSmVGTVGVPMTTIEARLESVPEMGYDALSDvpRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNG 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 549 TLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESLQAFLIAIVVPDVETLRPWAQKRGFDGSFEELCRNK 628
Cdd:PLN02861 508 AMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNL 587
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 629 DVKKAILEDMVRLGKDSGLKPFEQVKGIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYSTIKV 698
Cdd:PLN02861 588 KARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
5.92e-158 |
|
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: 465.92 E-value: 5.92e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 117 PYEWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELS 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 197 LVFVDkpekaklllegvenkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkpPAPEDLAVVCFT 276
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 SGTTGNPKGALITHRNIVSDCSAFVKatenSVN--PCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD- 353
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGD----RVPelLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDk 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 354 -------DLKVLQPTVFPVVPRLLNRMFDRIFGQANT--TLKRWLLDFASKRKEAELRSGIirNNSLWDRLIFHKVQSSL 424
Cdd:cd17639 171 skrgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAAL 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 GGKVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYM--AA 502
Cdd:cd17639 249 GGRLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYStdKP 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 503 EGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEA 582
Cdd:cd17639 328 PPRGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPL 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 583 IAQVFVHGESLQAFLIAIVVPDVETLRPWAQKRGF-DGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGIALHPE 661
Cdd:cd17639 408 VNNICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDE 487
|
570
....*....|....*..
gi 1622942221 662 LFSIDNGLLTPTMKAKR 678
Cdd:cd17639 488 EWTPENGLVTAAQKLKR 504
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-696 |
1.31e-157 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 470.45 E-value: 1.31e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 88 DVTTLYEGFQRGIQVSNNGPCLGSRKPDQ----PYEWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVII 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASG--AEPGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 164 EQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV-DKpeKAKLLLEGvENKLTPSLKIIVLMDAYGSELVERGQKCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 243 VEIISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRN---IVSDCSAFVKATENSVNPcpDDTLISF 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFEDKMTH--DDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 320 LPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 398 EAELRSGIIRNNS--LWDRLIFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 476 TA-GHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKI 552
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 553 IDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESLQAFLIAIVVPDVETLRPWAQKRGFDGSFEELCRNKDVKK 632
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942221 633 AILEDMVRLGKDSGLKPFEQVKGIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYSTI 696
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-697 |
1.20e-156 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 468.35 E-value: 1.20e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 87 EDVTTLYEGFQRGIQVSNNGPCLGSR-----KPDQpYEWLSYKQVAEMSECLGSALIQKGFTAtpDQFIGIFAQNRPEWV 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 162 IIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVDKpEKAKLLLEGVENKlTPSLKIIVLMDAYGSELVERGQKC 241
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEE-KKISELFKTCPNS-TEYMKTVVSFGGVSREQKEEAETF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 242 GVEIISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPCPD-DTLISFL 320
Cdd:PLN02614 197 GLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAALTVkDVYLSYL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 321 PLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKE 398
Cdd:PLN02614 277 PLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKF 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 399 AELRSGI--IRNNSLWDRLIFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDW- 475
Cdd:PLN02614 357 GNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELd 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 476 TAGHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PLN02614 437 MLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKII 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 554 DRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESLQAFLIAIVVPDVETLRPWAQKRGFDGSFEELCRNKDVKKA 633
Cdd:PLN02614 516 DRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEF 595
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942221 634 ILEDMVRLGKDSGLKPFEQVKGIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYSTIK 697
Cdd:PLN02614 596 ILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-694 |
1.50e-136 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 417.21 E-value: 1.50e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 62 VEVAGSGG-ARRSALLDsdEPLVYFYEDVTTLYEGFQRGIQVSNNGPCLGSRK---------PDQ---------PYEWLS 122
Cdd:PLN02387 31 VDVGGEPGyAIRNARFP--ELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisrefetsSDGrkfeklhlgEYEWIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 123 YKQVAEMSECLGSALIQKGFTAtpDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVDK 202
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 203 PEKAKLLleGVENKLTpSLKIIVLMDAYGSELVERG-QKCGVEIISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTTG 281
Cdd:PLN02387 187 KQLKKLI--DISSQLE-TVKRVIYMDDEGVDSDSSLsGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 282 NPKGALITHRNIVSDCSAfVKATENSVNPcpDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD-------- 353
Cdd:PLN02387 264 LPKGVMMTHGNIVATVAG-VMTVVPKLGK--NDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 354 ---DLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKEAELR------SGIIRnnSLWDRLIFHKVQS 422
Cdd:PLN02387 339 tkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 423 SLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA 502
Cdd:PLN02387 417 VLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLIS 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 503 EG---EGEVCVKGPNVFQGYLKDPAKTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN 575
Cdd:PLN02387 497 DKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEA 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 576 IYIRSEAIAQVFVHGESLQAFLIAIVVPDVETLRPWAQKRGFD-GSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVK 654
Cdd:PLN02387 577 ALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPA 656
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1622942221 655 GIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYS 694
Cdd:PLN02387 657 KIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
112-563 |
7.75e-129 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 387.82 E-value: 7.75e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 112 RKPDQP------YEWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 185
Cdd:pfam00501 7 RTPDKTalevgeGRRLTYRELDERANRLAAGLRALG--VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 186 VTYIVNKAELSLVFVDKPEKAKLLLEGVENKLTPSLKIIVLMDAYGSELVergqkcgveiisLKAMEDLGRANRRKPKPP 265
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPCPDDTLISFLPLAHMFERVVEC-VMLCHGAKIGFF 344
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 QGDIRL----LMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfaSKRKEAELRSGiirnnslwdrlifhkv 420
Cdd:pfam00501 233 PGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------------------AGAPKRALLSS---------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 qsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDW---TAGHVGAPMPCNLIKLVDVEEM 497
Cdd:pfam00501 279 -------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETG 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622942221 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
121-693 |
5.08e-102 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 327.32 E-value: 5.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVfV 200
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELG--LTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI-V 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKPEKAKLLLEGVENKLTPSLKIIvlmdaYGSELVERGQKCGVEIISLKAMEDLGRANRRKPKPPAPE---DLAVVCFTS 277
Cdd:PTZ00216 199 CNGKNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 278 GTTGNPKGALITHRNIVSDCSAFvkatENSVNPC-----PDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLM 352
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILAL----EDRLNDLigppeEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 353 D-------DLKVLQPTVFPVVPRLlnrmFDRI----------FGqantTLKRWLLDFASKRKEAELRSGiiRNNSLWDRL 415
Cdd:PTZ00216 348 DtfarphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWNEK 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 416 IFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCqFYEGYGQTECTagCCLSM--PGDWTAGHVGAPMPCNLIKLVD 493
Cdd:PTZ00216 418 VFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCGGIqrTGDLEPNAVGQLLKGVEMKLLD 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 494 VEEMNYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEK 572
Cdd:PTZ00216 495 TEEYKHTdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEA 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 573 IENIYIRSEAIAQ----VFVHgeSLQAFLIAIVVPDVETLRPWAQKRGFDGSFEELCRNKDVKKAILEDMVRLGKDSGLK 648
Cdd:PTZ00216 575 LEALYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRK 652
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1622942221 649 PFEQVKGIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELY 693
Cdd:PTZ00216 653 SFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
5.70e-94 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 299.27 E-value: 5.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 116 QPYEWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAEL 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 196 SLVFVdkpekaklllegvENkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkppAPEDLAVVCF 275
Cdd:cd17640 79 VALVV-------------EN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 276 TSGTTGNPKGALITHRNIVSDCSAFVKAtensVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMDDL 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDI----VPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 356 KVLQPTVFPVVPRLlnrmfdrifgqanttlkrWlldfaskrkEAeLRSGI---IRNNSLWDRLIFHKVQSslGGKVRLMV 432
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 433 TGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKG 512
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 513 PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGES 592
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 593 lQAFLIAIVVPDVETLRPWAQKRG--FDGSFEELCRNKDVKKAI-LEDMVRLGKDSGLKPFEQVKGIALHPELFsIDNGL 669
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGE 456
|
570
....*....|
gi 1622942221 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 |
1.19e-79 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 262.79 E-value: 1.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 118 YEWLSYKQVAEMSECLGSALiqKGFTATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSL 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAAL--RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 198 VFVDK----PEKAKLLLEGVENKLTPSLKiiVLMDAYG-SELVERGQKCGVEIislkamedlgranrrkpkPPAPEDLAV 272
Cdd:cd05932 82 LFVGKlddwKAMAPGVPEGLISISLPPPS--AANCQYQwDDLIAQHPPLEERP------------------TRFPEQLAT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 273 VCFTSGTTGNPKGALITHRNIVSDCSAFVkateNSVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIgFFQGDIRLL 351
Cdd:cd05932 142 LIYTSGTTGQPKGVMLTFGSFAWAAQAGI----EHIGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 352 MDDLKVLQPTVFPVVPRLLNRMFDRIFgqanttlkrwlldfaSKRKEAELRsgIIRNNSLWDRLIFHKVQSSLG-GKVRL 430
Cdd:cd05932 217 VEDVQRARPTLFFSVPRLWTKFQQGVQ---------------DKIPQQKLN--LLLKIPVVNSLVKRKVLKGLGlDQCRL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 431 MVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCV 510
Cdd:cd05932 280 AGCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 511 KGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:cd05932 348 RSPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIG 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 591 ESLQAfLIAIVVPDVEtlrpwAQKRGFDGSFEELCRNkdvKKAILEDMvrlgkDSGLKPFEQVKGIALHPELFSIDNGLL 670
Cdd:cd05932 428 SGLPA-PLALVVLSEE-----ARLRADAFARAELEAS---LRAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGIL 493
|
....*...
gi 1622942221 671 TPTMKAKR 678
Cdd:cd05932 494 TPTLKIKR 501
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-693 |
1.40e-72 |
|
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: 246.50 E-value: 1.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 113 KPDQPYEWLSYKQVAEMSECLGSALIQKGFtatpDQF--IGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIV 190
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFLKLGL----ERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 191 NKAELSLVFVDKPEKAKLLLEgVENKLtPSLKIIVLmdaYGSELVERGQKcgveIISLKAMEDLGR-----ANRRKPKPP 265
Cdd:cd05933 77 ETSEANILVVENQKQLQKILQ-IQDKL-PHLKAIIQ---YKEPLKEKEPN----LYSWDEFMELGRsipdeQLDAIISSQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPCPDDTLISFLPLAHMFERVVEcVMLC--HGAKIGF 343
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPikVGGQVYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 344 FQGDIR--LLMDDLKVLQPTVFPVVPRLLNRMFDRI--FGQANTTLKRWLLDFAsKRKEAE-------LRSGIIRNNSLW 412
Cdd:cd05933 227 AQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSPLFYRLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 413 DRLIFHKVQSSLG-GKVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKL 491
Cdd:cd05933 306 KKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 492 VDVEemnymaAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 571
Cdd:cd05933 385 HNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 572 KIENIyIRSE--AIAQVFVHGESLQaFLIAIVV----PDVETLRP----------WAQKRGFDGS-FEELCRNKD--VKK 632
Cdd:cd05933 459 PIEDA-VKKElpIISNAMLIGDKRK-FLSMLLTlkceVNPETGEPldelteeaieFCRKLGSQATrVSEIAGGKDpkVYE 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622942221 633 AILEDMVRLGKDSGLKPfEQVKGIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELY 693
Cdd:cd05933 537 AIEEGIKRVNKKAISNA-QKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
112-615 |
1.70e-72 |
|
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: 242.02 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 112 RKPDQP-----YEWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAV 186
Cdd:COG0318 11 RHPDRPalvfgGRRLTYAELDARARRLAAALRALGVG--PGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 187 TYIVNKAELSLVFVdkpekaklllegvenkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkppa 266
Cdd:COG0318 89 AYILEDSGARALVT------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 pedlAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI---- 341
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT----PGDVVLVALPLFHVFGLTVGLLApLLAGATLvllp 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELRSgiirnnslwdrlifhkvq 421
Cdd:COG0318 175 RF---DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------ 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 sslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTA--GHVGAPMPCNLIKLVDvEEMNY 499
Cdd:COG0318 217 ------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIR 579
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAA 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622942221 580 SEAIAQVFV-------HGESLQAFLI--AIVVPDVETLRPWAQKR 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 |
2.11e-72 |
|
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: 245.41 E-value: 2.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 122 SYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIE---QGCFAYSMvivPLYDTLGNEAVTYIVNKAELSLV 198
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAElaaQAIGALSL---GIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 199 FVDKPEKAKLLLEgVENKLtPSLKIIVLMDAYGSELVERGQkcgveIISLKAMEDLGRA-NRRKPK-------PPAPEDL 270
Cdd:cd17641 88 IAEDEEQVDKLLE-IADRI-PSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 271 AVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQgDIR 349
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLG----PGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 350 LLMDDLKVLQPTVFPVVPRLLNRM--FDRIFGQANTTLKRWLLDF--------ASKRKEAELRSGIIRNNS-LWDRLIFH 418
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 419 KVQSSLG-GKVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVeem 497
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 nymaaegeGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIY 577
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 578 IRSEAIAQVFVHGESlQAFLIAIVVPDVETLRPWAQKRGFD-GSFEELCRNKDVKKAILEDMVRLGKDsgLKPFEQVKGI 656
Cdd:cd17641 464 KFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRIRRF 540
|
570 580
....*....|....*....|..
gi 1622942221 657 ALHPELFSIDNGLLTPTMKAKR 678
Cdd:cd17641 541 LLLYKELDADDGELTRTRKVRR 562
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
89-671 |
1.22e-66 |
|
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: 230.03 E-value: 1.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 89 VTTLYEGF-QRgiqvsnngPCLGSRK---PDQPYE-WLSYKQVAEMSECLGSALIQK----------GFTATPDQFIGIF 153
Cdd:cd17632 28 IATVMTGYaDR--------PALGQRAtelVTDPATgRTTLRLLPRFETITYAELWERvgavaaahdpEQPVRPGDFVAVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 154 AQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVDkPEKAKLLLEGVENKLTPSlKIIVL-----MD 228
Cdd:cd17632 100 GFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS-AEHLDLAVEAVLEGGTPP-RLVVFdhrpeVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 229 AYGSELV---ERGQKCGVEIISLKAMEDLGRANRRKPKPPAPED---LAVVCFTSGTTGNPKGALITHRNIVSdcsAFVK 302
Cdd:cd17632 178 AHRAALEsarERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTERLVAT---FWLK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 303 ATENSVNPCPDDTLISFLPLAHMFERVVECVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIfgQ 380
Cdd:cd17632 255 VSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRY--Q 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 381 AntTLKRWLLDFA-----SKRKEAELRsgiirnnslwdrlifhkvQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFY 455
Cdd:cd17632 332 A--ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 456 EGYGQTEctAGCCLsmpgdwTAGHVGAPmPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDK 532
Cdd:cd17632 392 DGYGSTE--AGAVI------LDGVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 533 DGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESLQAFLIAIVVPDVETLRpwa 612
Cdd:cd17632 463 DGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALA--- 539
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622942221 613 qkrgfDGSFEELcrnkdvKKAILEDMVRLGKDSGLKPFEQVKGIALHPELFSIDNGLLT 671
Cdd:cd17632 540 -----GEDTARL------RAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-678 |
3.88e-66 |
|
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: 225.40 E-value: 3.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAE----MSECLGSALIQKGftatpDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELS 196
Cdd:cd05914 8 LTYKDLADniakFALLLKINGVGTG-----DR-VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 197 LVFVDKPEkaklllegvenkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkppapeDLAVVCFT 276
Cdd:cd05914 82 AIFVSDED----------------------------------------------------------------DVALINYT 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 SGTTGNPKGALITHRNIVSD---CSAFVKATENsvnpcpdDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQGDIRLLM 352
Cdd:cd05914 98 SGTTGNSKGVMLTYRNIVSNvdgVKEVVLLGKG-------DKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKI 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 353 DDLKVLQPTVFPVVPRLLNRMFDRIFGQAN-TTLKRWLLDFASKRKEAELRSgiirnnslwdrLIFHKVQSSLGGKVRLM 431
Cdd:cd05914 171 IALAFAQVTPTLGVPVPLVIEKIFKMDIIPkLTLKKFKFKLAKKINNRKIRK-----------LAFKKVHEAFGGNIKEF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 432 VTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPmpcnlIKLVDVEEMNYMAAEGEGEVCVK 511
Cdd:cd05914 240 VIGGAKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVR 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 512 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRS--EAIAQVFVH 589
Cdd:cd05914 314 GPNVMKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMpfVLESLVVVQ 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 590 GESLQAflIAIVVPDvetlrpwaqkrgFDGSFEELCRNKdvKKAILEDmVRLGKDSGLKPFEQVKGIALHPELFSidngl 669
Cdd:cd05914 394 EKKLVA--LAYIDPD------------FLDVKALKQRNI--IDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFE----- 451
|
....*....
gi 1622942221 670 LTPTMKAKR 678
Cdd:cd05914 452 KTPKGKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-615 |
3.65e-64 |
|
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: 216.00 E-value: 3.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVsdcsAFVKATENSVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKI----GFF 344
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 QGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiirnnslwdrlifhkvqssl 424
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 ggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWT--AGHVGAPMPCNLIKLVDVEEmNYMAA 502
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 503 EGEGEVCVKGPNVFQGYLKDPAKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSEA 582
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622942221 583 IAQVFVHG---ESLQAFLIAIVVP------DVETLRPWAQKR 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 |
9.16e-62 |
|
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: 214.38 E-value: 9.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKPEKAKLLleGVENKLTPSLKIIVLMDaygselveRGQKCGVEIISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTT 280
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKIIVLDD--------KPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSDCSaFVKATENsVNPCPDDTLISFLPLAHMFervveCVMLCHGAKIgffQG---------DIRLL 351
Cdd:cd05911 159 GLPKGVCLSHRNLIANLS-QVQTFLY-GNDGSNDVILGFLPLYHIY-----GLFTTLASLL---NGatviimpkfDSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 352 MDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRlifHKVQSslggkVRLM 431
Cdd:cd05911 229 LDLIEKYKITFLYLVPPIAAALA---------------------------------KSPLLDK---YDLSS-----LRVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 432 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCV 510
Cdd:cd05911 268 LSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 511 KGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:cd05911 348 RGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
110-615 |
2.51e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 210.92 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 110 GSRKPDQPY-----EWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIieqGCFAYSM---VIVPLYDTL 181
Cdd:PRK07656 15 ARRFGDKEAyvfgdQRLTYAELNARVRRAAAALAALGIG--KGDRVAIWAPNSPHWVI---AALGALKagaVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 182 GNEAVTYIVNKAELSLVFVdkpekAKLLLeGVENKLT---PSLKIIVLMDaygselVERGQKCGVEIISLKAMedLGRAN 258
Cdd:PRK07656 90 TADEAAYILARGDAKALFV-----LGLFL-GVDYSATtrlPALEHVVICE------TEEDDPHTEKMKTFTDF--LAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 259 RRKPKPP-APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATenSVNPcpDDTLISFLPLAHMF---ERVVECVM 334
Cdd:PRK07656 156 PAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYL--GLTE--GDRYLAANPFFHVFgykAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 335 lcHGAKIgffqgDIRLLMDDLKVLQ------PTVFPVVPrllnrmfdrifgqantTLKRWLLDFAsKRKEAELRSgiirn 408
Cdd:PRK07656 232 --RGATI-----LPLPVFDPDEVFRlieterITVLPGPP----------------TMYNSLLQHP-DRSAEDLSS----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 409 nslwdrlifhkvqsslggkVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLSMPGD---WTAGHVGAPM 484
Cdd:PRK07656 283 -------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 485 PCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 563
Cdd:PRK07656 344 AGVENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622942221 564 QGEYIAPEKIENIYIRSEAIAQVFV-------HGESLQAFliaiVVP------DVETLRPWAQKR 615
Cdd:PRK07656 421 GGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
122-615 |
6.32e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 204.65 E-value: 6.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 122 SYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIieqgC-FAYSM---VIVPLYDTLGNEAVTYIVNKAELSL 197
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVK--KGDRVAVFDWNSHEYLE----AyFAVPKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 198 VFVDkPEKAKLLlEGVENKLtPSLKIIVLMDAYGSELvergqkCGVEIISLKAMedLGRANRRKPKPPAPE-DLAVVCFT 276
Cdd:PRK06187 107 VLVD-SEFVPLL-AAILPQL-PTVRTVIVEGDGPAAP------LAPEVGEYEEL--LAAASDTFDFPDIDEnDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 SGTTGNPKGALITHRNIVSD---CSAFVKATensvnpcPDDTLISFLPLAHMFERVVECVMLCHGAKI---GFFqgDIRL 350
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHslaVCAWLKLS-------RDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPEN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 351 LMDDLKVLQPTVFPVVPRLLNRMFdrifgQANTTLKRWLldfaskrkeaelrsgiirnnslwdrlifhkvqSSLggkvRL 430
Cdd:PRK06187 247 LLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF--------------------------------SSL----RL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 431 MVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCL----SMPGDWT-AGHVGAPMPCNLIKLVDvEEMNYMAAEG 504
Cdd:PRK06187 286 VIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLppedQLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 505 E--GEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSEA 582
Cdd:PRK06187 365 GevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPA 442
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622942221 583 IAQVFVHG---ESLQAFLIAIVVP------DVETLRPWAQKR 615
Cdd:PRK06187 443 VAEVAVIGvpdEKWGERPVAVVVLkpgatlDAKELRAFLRGR 484
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
112-603 |
9.82e-58 |
|
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: 202.79 E-value: 9.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 112 RKPDQPY-----EWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAV 186
Cdd:cd05936 11 RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 187 TYIVNKAELSLVFVDKPekaklllegvenkltpslkiivlmdaygselvergqkcgveiislkaMEDLGRANRRKPKPPA 266
Cdd:cd05936 89 EHILNDSGAKALIVAVS-----------------------------------------------FTDLLAAGAPLGERVA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 --PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAfVKATENSVNPcPDDTLISFLPLAHMFERVVECV-MLCHGAKIGF 343
Cdd:cd05936 122 ltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWLEDLLE-GDDVVLAALPLFHVFGLTVALLlPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 344 FQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiirnnslwdrlifhkvqs 422
Cdd:cd05936 200 IPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 423 slggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMA 501
Cdd:cd05936 244 -----LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSE 581
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHP 395
|
490 500
....*....|....*....|....*....
gi 1622942221 582 AIAQVFV-------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 |
4.79e-45 |
|
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: 167.08 E-value: 4.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMFERVV----------ECVMLchg 338
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGLVNallcplfagaSVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 339 akiGFF---QGDIRLLMDDLkvlqpTVFPVVPRllnrMFDRIFGQANTTLKrwllDFASKRKEAElrsgiirnnslwdrl 415
Cdd:cd05941 163 ---PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 416 ifhkvqsslgGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSMP--GDWTAGHVGAPMPCNLIKLVD 493
Cdd:cd05941 212 ----------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 494 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEK 572
Cdd:cd05941 280 EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALE 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1622942221 573 IENIYIRSEAIAQVFVHGESLQAF---LIAIVVP-------DVETLRPWAQKR 615
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-616 |
9.73e-42 |
|
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: 158.65 E-value: 9.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSeCLGSALIQKgFTAtPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd05909 8 LTYRKLLTGA-IALARKLAK-MTK-EGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKP--EKAKLL-------------LEGVENKLTPSLKIIVLMDAYgselvergqkcgveIISLKAMEDLGRANRRkpkpp 265
Cdd:cd05909 85 SKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFLAGK--------------FPPKWLLRIFGVAPVQ----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 aPEDLAVVCFTSGTTGNPKGALITHRNIVSDcsafVKATENSVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQ 345
Cdd:cd05909 146 -PDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFHSF---------------GLTG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 346 GDIRLLMDDLKVLQ---PTVFPVVPRLLNRMFDRIFGQANTTLKRWLldfasKRKEAELRSGIirnnslwdrlifhkvqs 422
Cdd:cd05909 206 CLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPTFLRGYA-----RAAHPEDFSSL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 423 slggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMA 501
Cdd:cd05909 264 ------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYirSE 581
Cdd:cd05909 338 IGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDIL--SE 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1622942221 582 AIAQVFVH----------GESLQAFLIAIvVPDVETLRPWAQKRG 616
Cdd:cd05909 414 ILPEDNEVavvsvpdgrkGEKIVLLTTTT-DTDPSSLNDILKNAG 457
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
111-604 |
1.03e-39 |
|
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: 151.61 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 111 SRKPDQP-YEW----LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 185
Cdd:cd17631 6 RRHPDRTaLVFggrsLTYAELDERVNRLAHALRALGVA--KGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 186 VTYIVNKAElslvfvdkpekAKLLLEgvenkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkpp 265
Cdd:cd17631 84 VAYILADSG-----------AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 apeDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI--- 341
Cdd:cd17631 99 ---DLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLG----PDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVvil 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 -GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTlkrwllDFASkrkeaelrsgiirnnslwdrlifhkv 420
Cdd:cd17631 172 rKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS-------------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 qsslggkVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLSMPGDW--TAGHVGAPMPCNLIKLVDvEEMN 498
Cdd:cd17631 215 -------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGR 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 499 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYI 578
Cdd:cd17631 286 EVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLY 363
|
490 500 510
....*....|....*....|....*....|...
gi 1622942221 579 RSEAIAQVFV-------HGESlqafLIAIVVPD 604
Cdd:cd17631 364 EHPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
205-588 |
1.09e-39 |
|
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: 153.16 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 205 KAKLLL---EGVEnKLTPSLKIIVLMDaygsELVERGQKCGVEIISLKAMEdlgranrrKPKPP-APEDLAVVCFTSGTT 280
Cdd:cd05904 104 GAKLAFttaELAE-KLASLALPVVLLD----SAEFDSLSFSDLLFEADEAE--------PPVVViKQDDVAALLYSSGTT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSDCSAFVKATENsvNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----GFfqgDIRLLMDDL 355
Cdd:cd05904 171 GRSKGVMLTHRNLIAMVAQFVAGEGS--NSDSEDVFLCVLPMFHIYGLSSFALgLLRLGATVvvmpRF---DLEELLAAI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 356 KVLQPTVFPVVPRLLNRMfdrifgqanttlkrwlldfaskrkeaeLRSGIIRNNSLwdrlifhkvqSSLggkvRLMVTGA 435
Cdd:cd05904 246 ERYKVTHLPVVPPIVLAL---------------------------VKSPIVDKYDL----------SSL----RQIMSGA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 436 APVSATVLTFLRAAL-GCQFYEGYGQTECTAG---CCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVK 511
Cdd:cd05904 285 APLGKELIEAFRAKFpNVDLGQGYGMTESTGVvamCFAPEKDRAKYGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIR 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942221 512 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFV 588
Cdd:cd05904 365 GPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEALLLSHPEILDAAV 440
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
233-694 |
4.89e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 154.11 E-value: 4.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 233 ELVERGQKCGVEIISLKAMEDlGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNI------VSDCSAFVKaten 306
Cdd:PTZ00342 270 DLKEKAKKLGISIILFDDMTK-NKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 307 sVNPcpdDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TT 384
Cdd:PTZ00342 345 -YNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPP 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 385 LKRWLLdfaskRKEAELRSGiiRNNSLWDRL---IFH---KVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGY 458
Cdd:PTZ00342 421 LKRFLV-----KKILSLRKS--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGY 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 459 GQTECTAGCCLSMPGDWTAGHVGAPM-PCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH 537
Cdd:PTZ00342 494 GLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFK 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 538 TGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESLQAFLIAIVVPDVETLRPWAQKrgf 617
Cdd:PTZ00342 574 TGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKD--- 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 618 DGSFEELCRN-KDVKKAILED--------------MVRLGKDSGLKPFEQVKGIALHPELFSIDNgLLTPTMKAKRPEL- 681
Cdd:PTZ00342 651 DNMLESTGINeKNYLEKLTDEtinnniyvdyvkgkMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVf 729
|
490
....*....|....*
gi 1622942221 682 --RNYFRSQIDELYS 694
Cdd:PTZ00342 730 kdYAFFIDQVKKIYK 744
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
115-615 |
1.09e-38 |
|
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: 150.16 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 115 DQPYEWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVI-----IEQGCfaysmVIVPLYDTLGNEAVTYI 189
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIK--KGDRVAIALPNGLEFVVaflaaARAGA-----VVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 190 VNKAELSLVFVDKPEKAKLLlegvenKLTPSLKIIVLmdaygsELVERGQKCGVEII--SLKAMEDLGRANRRkPKPPAP 267
Cdd:cd05926 82 LADLGSKLVLTPKGELGPAS------RAASKLGLAIL------ELALDVGVLIRAPSaeSLSNLLADKKNAKS-EGVPLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 268 EDLAVVCFTSGTTGNPKGALITHRNIVSDcsafVKATENSVNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----G 342
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLsTLAAGGSVvlppR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 343 FfqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqs 422
Cdd:cd05926 225 F---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEPNPESPP--------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 423 slgGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgcclSM------PGDWTAGHVGAPMPcNLIKLVDvEE 496
Cdd:cd05926 265 ---PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH----QMtsnplpPGPRKPGSVGKPVG-VEVRILD-ED 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:cd05926 336 GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGV 414
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622942221 577 YIRSEAIAQ--VF-----VHGESLQAFliaiVVP------DVETLRPWAQKR 615
Cdd:cd05926 415 LLSHPAVLEavAFgvpdeKYGEEVAAA----VVLregasvTEEELRAFCRKH 462
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
254-608 |
9.87e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 145.29 E-value: 9.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 254 LGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSD---CSAFVKATENsvNPCpdDTLISFLPLAHMFERVV 330
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLN--EGC--EILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 331 ECVMLchgakigffqgdirLLMDDLKVLQPTvfpvvPRLLNRMFdrifgqanTTLKRWLLdfaskrkeaelrSGIIRNNS 410
Cdd:PRK05677 269 HCMAM--------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 411 LWDRLI----FHKVQSSlggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPC 486
Cdd:PRK05677 310 LFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 487 NLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK05677 387 TLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGF 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622942221 567 YIAPEKIENIYIRSEAIAQVFV-------HGESLQAFliaIVVPDVETL 608
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-615 |
4.99e-36 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 141.05 E-value: 4.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 123 YKQVAEMSECLGSALIQKGFTatpdqfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVDk 202
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSGSR------VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 203 pekAKLLLEGVenkLTPSLKIIVLMDAygselvergqkCGVEIISLKAMEDLgranrrkpkppapedlAVVCFTSGTTGN 282
Cdd:TIGR01923 79 ---SLLEEKDF---QADSLDRIEAAGR-----------YETSLSASFNMDQI----------------ATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 283 PKGALITHRNIvsdcSAFVKATENSVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLmDDLKVLQPTV 362
Cdd:TIGR01923 126 PKAVPHTFRNH----YASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 363 FPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkvqsslggkvrlmvtGAAPVSATV 442
Cdd:TIGR01923 201 ISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGSAIPAPL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 443 LTFLRAaLGCQFYEGYGQTE-CTAGCCLSMPGDWTAGHVGAPMPCNLIKL-VDveemnymAAEGEGEVCVKGPNVFQGYL 520
Cdd:TIGR01923 236 IEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVD-------NKEGHGEIMVKGANLMKGYL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 521 kDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFV-------HGESL 593
Cdd:TIGR01923 308 -YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQVP 385
|
490 500
....*....|....*....|..
gi 1622942221 594 QAFLIAIVVPDVETLRPWAQKR 615
Cdd:TIGR01923 386 VAYIVSESDISQAKLIAYLTEK 407
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-615 |
9.97e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 138.18 E-value: 9.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDcSAFV----KATENSVNPCPddtlisfLPLAHMFERVVEcVMLC--HGAK 340
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIgerlGLTEQDRLCIP-------VPLFHCFGSVLG-VLACltHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 341 IGFfqgdIRLLMDDLKVLQP------TVFPVVPRllnrMFDRIFGQAnttlKRWLLDFASkrkeaeLRSGIIrnnslwdr 414
Cdd:cd05917 72 MVF----PSPSFDPLAVLEAiekekcTALHGVPT----MFIAELEHP----DFDKFDLSS------LRTGIM-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 415 lifhkvqsslggkvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLSMPGD---WTAGHVGAPMPCNLIK 490
Cdd:cd05917 126 -------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 491 LVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:cd05917 187 IVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIY 264
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622942221 570 PEKIENIYIRSEAIAQVFV-------HGESLQAFLI--AIVVPDVETLRPWAQKR 615
Cdd:cd05917 265 PREIEEFLHTHPKVSDVQVvgvpderYGEEVCAWIRlkEGAELTEEDIKAYCKGK 319
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
254-615 |
1.93e-35 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 141.68 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 254 LGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCS---AFVKATENSvnpcpDDTLISFLPLAHMF--ER 328
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGLGDG-----PERVLAALPMFHAYglTL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 329 VVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLlnrmFDRIfgqanttlkrwlldfaskRKEAELRsGIirn 408
Cdd:PRK05605 280 CLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 409 nslwdrlifhkvqsSLGGkVRLMVTGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLSMPGDWTAGHVGAPMP 485
Cdd:PRK05605 334 --------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFP 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 486 CNLIKLVDVEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 564
Cdd:PRK05605 397 DTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKELI-ITG 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942221 565 GEYIAPEKIENIYIRSEAIAQVFVHG-------ESLQAfliAIV-----VPDVETLRPWAQKR 615
Cdd:PRK05605 475 GFNVYPAEVEEVLREHPGVEDAAVVGlpredgsEEVVA---AVVlepgaALDPEGLRAYCREH 534
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-590 |
2.10e-35 |
|
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: 141.13 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 122 SYKQVAEMSECLGSALIQKGFTAtpDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVD 201
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 202 KPEKAKLLleGVENKLtPSLKIIVLMDaygSELVERGQKCgveIISLKAMEDLGRANRRKPKPPA---PEDLAVVCFTSG 278
Cdd:cd17642 124 KKGLQKVL--NVQKKL-KIIKTIIILD---SKEDYKGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 279 TTGNPKGALITHRNIVSDCSAFVKATENSvNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGF---FQGDIRL-LMDD 354
Cdd:cd17642 195 STGLPKGVQLTHKNIVARFSHARDPIFGN-QIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrSLQD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 355 LKV----LQPTVFPVVPRllnrmfdrifgqanttlkrwlldfaskrkeaelrSGIIRNNSLwdrlifhkvqSSLggkvRL 430
Cdd:cd17642 274 YKVqsalLVPTLFAFFAK----------------------------------STLVDKYDL----------SNL----HE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 431 MVTGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVC 509
Cdd:cd17642 306 IASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 510 VKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFVH 589
Cdd:cd17642 386 VKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILLQHPKIFDAGVA 464
|
.
gi 1622942221 590 G 590
Cdd:cd17642 465 G 465
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
267-599 |
5.69e-35 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 140.19 E-value: 5.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAfVKATENSVNPCPDDTLISFLPLAHMFERVVECVMLCH-GAKigffq 345
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQ-AKAAYGPLLHPGKELVVTALPLYHIFALTVNCLLFIElGGQ----- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 346 gdirllmdDLKVLQPTVFP-VVPRLLNRMFDRIFGqANTTLKRWLldfaskrkeaelrsgiirNNSLwdrliFHKVQSSl 424
Cdd:PRK08974 279 --------NLLITNPRDIPgFVKELKKYPFTAITG-VNTLFNALL------------------NNEE-----FQELDFS- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 ggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLSMPGdwTAGHVGAPMPCNLIKLVDvEEMNYMA 501
Cdd:PRK08974 326 --SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVP 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSE 581
Cdd:PRK08974 401 PGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHP 478
|
330 340
....*....|....*....|....*
gi 1622942221 582 AIAQVF-------VHGESLQAFLIA 599
Cdd:PRK08974 479 KVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-625 |
6.28e-35 |
|
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: 139.30 E-value: 6.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 111 SRKPDQPYEWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIV 190
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLG--VKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 191 NKAELSLVFVDkPEKAKLLlEGVENKLtPSLKIIVLMDAYGSELVERGqkcgveiISLKAMEDL-GRANRRKPKPPAPE- 268
Cdd:cd12119 94 NHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAG-------VGVLAYEELlAAESPEYDWPDFDEn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVSdcSAFVKATENSVNPCPDDTlisFLPLAHMFErvVE-------CVMLchGAKI 341
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVL--HAMAALLTDGLGLSESDV---VLPVVPMFH--VNawglpyaAAMV--GAKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 ----GFFQGDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRifgqanttLKRWLLDFASKRkeaelrsgiirnnslwdrli 416
Cdd:cd12119 235 vlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLDH--------LEANGRDLSSLR-------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 417 fhkvqsslggkvRLMVTGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLSMPGDWTAGHV----------GAPMP 485
Cdd:cd12119 284 ------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPVP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 486 CNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:cd12119 350 GVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942221 564 qGEYIAPEKIENIYIRSEAIAQVFVhgeslqafliaIVVPD---VEtlRPWA---QKRGFDGSFEELC 625
Cdd:cd12119 428 -GEWISSVELENAIMAHPAVAEAAV-----------IGVPHpkwGE--RPLAvvvLKEGATVTAEELL 481
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-590 |
2.07e-34 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 133.78 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVSDCSAF---VKATEnsvnpcpDDTLISFLPLAHMFERVVECVM-LCHGAKI--- 341
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWadcADLTE-------DDRYLIINPFFHTFGYKAGIVAcLLTGATVvpv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 GFFqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELrsgiirnnslwdrlifhkvq 421
Cdd:cd17638 74 AVF--DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL-------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 SSLggkvRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCcLSMPGD---WTAGHVGAPMPcnliklvDVEem 497
Cdd:cd17638 115 SSL----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVAT-MCRPGDdaeTVATTCGRACP-------GFE-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 nyMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:cd17638 181 --VRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGAL 257
|
330
....*....|...
gi 1622942221 578 IRSEAIAQVFVHG 590
Cdd:cd17638 258 AEHPGVAQVAVIG 270
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
246-599 |
1.21e-33 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 136.10 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 246 ISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSD------CSAFVKATENSVNPCPDDTLISF 319
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 320 LPLAHMFERVVECVMLchgakigFFQGDIRLLMDDlkvlqptvfpvvPRLLNRMFDRifgqanttLKRWLLdfaskrkea 399
Cdd:PRK12492 265 LPLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF--------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 400 elrSGIIRNNSLWDRLIFHKVQSSLGGKvRLMVT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCLSMPGDWT 476
Cdd:PRK12492 309 ---SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 477 A-GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PRK12492 384 RlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDR 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622942221 556 KKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFV-------HGESLQAFLIA 599
Cdd:PRK12492 463 KKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
266-588 |
1.84e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 135.49 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPCPDDTLISFLPLAHMFErvVECVMLCH---GAKIG 342
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 343 FFQG-DIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlLDFAskrkeaelRSGIIRNNSLwdrlifhkvq 421
Cdd:PLN02246 255 IMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL---------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 SSlggkVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLSM-------PGDWTAGHVGAPMPCNLIKLVD 493
Cdd:PLN02246 298 SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 494 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:PLN02246 372 PETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAEL 450
|
330
....*....|....*
gi 1622942221 574 ENIYIRSEAIAQVFV 588
Cdd:PLN02246 451 EALLISHPSIADAAV 465
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
254-683 |
3.52e-33 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 135.00 E-value: 3.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 254 LGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSD---CSAFVKATENSVNPCpdDTLISFLPLAHMFERVV 330
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKLEEGC--EVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 331 ECVMLchgAKIGFFQG------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsg 404
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 405 iirNNSLWDRLIFHKVQSSLGGkvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLS-MPGDWTAGHVGAP 483
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 484 MPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 562
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 563 AQGEYIAPEKIENIYIRSEAIAQVfvhgeslqaflIAIVVPDvetlrpwaQKRGfdgsfeELCRNKDVKK--AILEDMVR 640
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1622942221 641 LGKDSGLKPFEQVKGIALHPELFSIDNGlltptmKAKRPELRN 683
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-598 |
1.81e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 132.63 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 114 PDQPYEWlSYKQVAEMSECLGSAL----IQKGftatpDQfIGIFAQNRPEWVIIEqgcFAYS-----MV-IVPLYDTlgN 183
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLlalgIEKG-----DR-VGIWAPNVPEWVLTQ---FATAkigaiLVtINPAYRL--S 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 184 EaVTYIVNKAELS-LVFVDK--------------PEKAKLLLEGVENKLTPSLKIIVLMDAYGSelveRGQKCGVEIISL 248
Cdd:PRK08315 106 E-LEYALNQSGCKaLIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGDEKH----PGMLNFDELLAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 249 KAMEDLGRANRRKPKPpAPEDLAVVCFTSGTTGNPKGALITHRNIVSDcSAFVkaTENsVNPCPDDTLISFLPLAHMFEr 328
Cdd:PRK08315 181 GRAVDDAELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNILNN-GYFI--GEA-MKLTEEDRLCIPVPLYHCFG- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 329 vveCVM-----LCHGAKI-----GFfqgdirllmDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttl 385
Cdd:PRK08315 255 ---MVLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR--------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 386 krwlLDFASkrkeaeLRSGI-------IRnnslwdrlIFHKVQSSLGgkvrlM--VTGAapvsatvltflraalgcqfye 456
Cdd:PRK08315 312 ----FDLSS------LRTGImagspcpIE--------VMKRVIDKMH-----MseVTIA--------------------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 457 gYGQTECTAGCCLSMPGD------WTaghVGAPMPCNLIKLVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEA 529
Cdd:PRK08315 348 -YGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEA 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622942221 530 LDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAI--AQVF-V----HGESLQAFLI 598
Cdd:PRK08315 423 IDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGEEVCAWII 497
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
255-603 |
3.65e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 130.49 E-value: 3.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 255 GRANRRKPKPPaPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMfervvecvm 334
Cdd:PRK07787 116 ARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHV--------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 335 lcHGAKIGffqgdirllmddlkVLQPTvfpvvprllnrmfdRIFGQANTTLKrwlldFASKRKEAELRSGiirnNSL--- 411
Cdd:PRK07787 182 --HGLVLG--------------VLGPL--------------RIGNRFVHTGR-----PTPEAYAQALSEG----GTLyfg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 412 ----WDRLIFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCN 487
Cdd:PRK07787 223 vptvWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 488 LIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHI 559
Cdd:PRK07787 303 ETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGG 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622942221 560 FKLAQGEyiapekIENIYIRSEAIAQVFVHGE---SLQAFLIAIVVP 603
Cdd:PRK07787 382 YRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVG 422
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
266-615 |
1.01e-31 |
|
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: 128.80 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAH-MFerVVE-CVMLCHGAKI-- 341
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEiFGALLAGATLvv 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 --GFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhk 419
Cdd:cd05930 165 lpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL-------------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 420 vqsslggkvrLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGC----CLSMPGDWTAGHVGAPMPCNLIKLVDvE 495
Cdd:cd05930 213 ----------VLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDAtyyrVPPDDEEDGRVPIGRPIPNTRVYVLD-E 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 569
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIE 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622942221 570 PEKIENIYIRSEAIAQVFV---HGESLQAFLIAIVVP------DVETLRPWAQKR 615
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPdeggelDEEELRAHLAER 415
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
269-610 |
1.56e-31 |
|
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: 127.79 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVSdcSAFVKATENSVNPcpDDTLISFLPLAHMFERVVEC-VMLCHGAKI------ 341
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTF--AGYYSARRFGLGE--DDVYLTVLPLFHINAQAVSVlAALSVGATLvllprf 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 --GFFQGDIRllmddlkVLQPTVF---PVVPRLLNRMFDRIFGQANttlkrwlldfaskrkeaelrsgiirnnslwdrli 416
Cdd:cd05934 158 saSRFWSDVR-------RYGATVTnylGAMLSYLLAQPPSPDDRAH---------------------------------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 417 fhkvqsslggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEE 496
Cdd:cd05934 197 ------------RLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 497 MNYMAAEGEGEVCVK---GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 573
Cdd:cd05934 264 GQELPAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEV 341
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622942221 574 ENIYIRSEAIAQVFVHG----ESLQAFLIAIVVPDVETLRP 610
Cdd:cd05934 342 ERAILRHPAVREAAVVAvpdeVGEDEVKAVVVLRPGETLDP 382
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
222-588 |
2.03e-31 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 127.00 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 222 KIIVLMDAYGSELVERGQKCGVEIISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFV 301
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 302 KATENSvnpcPDDTLISFLPLAHMFervveCVM-----LCHGAK--------IGFFQGDIRLLMDDLKVlqpTVFPVVPr 368
Cdd:TIGR01733 154 RRYGLD----PDDRVLQFASLSFDA-----SVEeifgaLLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLTP- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 369 llnrmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGgkVRLMVTGA-APVSATVLTFLR 447
Cdd:TIGR01733 221 -----------------------------------------SLLALLAAALPPALAS--LRLVILGGeALTPALVDRWRA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 448 AALGCQFYEGYGQTECTAGCC-----LSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKD 522
Cdd:TIGR01733 258 RGPGARLINLYGPTETTVWSTatlvdPDDAPRESPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNR 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942221 523 PAKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFV 588
Cdd:TIGR01733 337 PELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
111-613 |
2.61e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 128.57 E-value: 2.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 111 SRKPDQP-YEW----LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPE-WVIIEQGCFAySMVIVPLYDTLGNE 184
Cdd:PRK06188 23 KRYPDRPaLVLgdtrLTYGQLADRISRYIQAFEALG--LGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 185 AVTYIVNKAELSLVFVDK---PEKAKLLLEGVenkltPSLKIIVLMDA--YGSELvergqkcgveiislkamedLGRANR 259
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDL-------------------LAAAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 260 RKPKPP----APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATEnsvnpCPDDtlISFL---PLAHMFERVVEC 332
Cdd:PRK06188 156 FGPAPLvaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE-----WPAD--PRFLmctPLSHAGGAFFLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 333 VMLCHGAKI---GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFASKRKeAELrsgiirnn 409
Cdd:PRK06188 229 TLLRGGTVIvlaKF---DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDL-------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 410 slwdrlifhkvqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHV------GAP 483
Cdd:PRK06188 281 ------------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 484 MPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 562
Cdd:PRK06188 345 TPGLRVALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-V 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942221 563 AQGEYIAPEKIENIYIRSEAIAQVFV-------HGESLQafliAIVVpdvetLRPWAQ 613
Cdd:PRK06188 421 TGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVV-----LRPGAA 469
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-683 |
5.01e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 128.33 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 113 KPDQPYEWlSYKQVAEMSECLGSALIQKGfTATPDqfigIFAQNRPEW---VIIEQGCFAYSMVIVPLYDTLGNEAVTYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKG-IEPGD----RVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 190 VNKAElSLVF-----VDKPEKAKLLLEgVENKLtPSLKIIVLMDAYG--------SELVERGQkcgveiiSLKAmedlgr 256
Cdd:PRK06087 117 LNKCQ-AKMFfaptlFKQTRPVDLILP-LQNQL-PQLQQIVGVDKLApatsslslSQIIADYE-------PLTT------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 257 anrrkPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATensvNPCPDDTLISFLPLAHmfervvecvmlc 336
Cdd:PRK06087 181 -----AITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARL----NLTWQDVFMMPAPLGH------------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 337 hgaKIGFFQGDIR-LLMDDLKVLQPTVFPVVP-RLLNRmfDRIFGQANTTlkRWLLDFASKRKEAELRSgiirnnslwdr 414
Cdd:PRK06087 240 ---ATGFLHGVTApFLIGARSVLLDIFTPDAClALLEQ--QRCTCMLGAT--PFIYDLLNLLEKQPADL----------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 415 lifhkvqSSLggkvRLMVTGAAPVSATVLtflRAAL--GCQFYEGYGQTECT--AGCCLSMPGDWTAGHVGAPMPCNLIK 490
Cdd:PRK06087 302 -------SAL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 491 LVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 570
Cdd:PRK06087 368 VVD-EARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 571 EKIENIYIRSEAIAQVFVHG---ESLQAFLIAIVVPDVETLRPwaqkrgfdgsfeelcrnkdvkkaILEDMVrlgkdsgl 647
Cdd:PRK06087 446 REVEDILLQHPKIHDACVVAmpdERLGERSCAYVVLKAPHHSL-----------------------TLEEVV-------- 494
|
570 580 590
....*....|....*....|....*....|....*....
gi 1622942221 648 kPFEQVKGIA--LHPE-LFSIDNGLLTPTMKAKRPELRN 683
Cdd:PRK06087 495 -AFFSRKRVAkyKYPEhIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
91-615 |
8.56e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 127.58 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 91 TLYEGFQRGIQVSNNGPCLGSRKPDQPYewlSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEqgcFAY 170
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGVQ--PGDRVGIWAPNCAEWLLTQ---FAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 171 SMV------IVPLYDTlgnEAVTYIVNKAELSLVFVDK---------------PEKAKLLLEGVENKLTPSLKIIVLMDA 229
Cdd:PRK12583 91 ARIgailvnINPAYRA---SELEYALGQSGVRWVICADafktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 230 YGS-------ELVERGqkcgvEIISLKAMEDLGRANRRkpkppapEDLAVVCFTSGTTGNPKGALITHRNIVSDcSAFVK 302
Cdd:PRK12583 168 APPpgflawhELQARG-----ETVSREALAERQASLDR-------DDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 303 ateNSVNPCPDDTLISFLPLAHMFERVVeCVMLC--HGAKIgFFQGDirlLMDDLKVLQ-------------PTVFpvVP 367
Cdd:PRK12583 235 ---ESLGLTEHDRLCVPVPLYHCFGMVL-ANLGCmtVGACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 368 RLLNRMFDRifgqanttlkrwlLDFASkrkeaeLRSGIIrnnslwdrlifhkvqsslggkvrlmvtGAAPVSATVLTFLR 447
Cdd:PRK12583 305 ELDHPQRGN-------------FDLSS------LRTGIM---------------------------AGAPCPIEVMRRVM 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 448 AALGC-QFYEGYGQTECTAGCCLSMPGD---WTAGHVGAPMPCNLIKLVDVEemNYMAAEGE-GEVCVKGPNVFQGYLKD 522
Cdd:PRK12583 339 DEMHMaEVQIAYGMTETSPVSLQTTAADdleRRVETVGRTQPHLEVKVVDPD--GATVPRGEiGELCTRGYSVMKGYWNN 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 523 PAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFV-------HGESLQA 595
Cdd:PRK12583 417 PEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVfgvpdekYGEEIVA 495
|
570 580
....*....|....*....|....
gi 1622942221 596 FLiaIVVP----DVETLRPWAQKR 615
Cdd:PRK12583 496 WV--RLHPghaaSEEELREFCKAR 517
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
246-576 |
7.53e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 124.75 E-value: 7.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 246 ISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDC--------SAFVKatensvnPCPDDTLI 317
Cdd:PRK07059 182 VRFNDALAEGARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 318 SF--LPLAHMFERVVECVMlchGAKIGffqG---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlk 386
Cdd:PRK07059 255 FVcaLPLYHIFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL------------ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 387 rwlldfaskrkeaelrsgiirNNSLWDRLIFHKVQSSLGGkvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTEcTAG 466
Cdd:PRK07059 317 ---------------------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGLSE-TSP 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 467 CCLSMPGDWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKW 544
Cdd:PRK07059 367 VATCNPVDATEfsGTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVM 445
|
330 340 350
....*....|....*....|....*....|..
gi 1622942221 545 LPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 576
Cdd:PRK07059 446 DERGYTKIVDRKKDMI-LVSGFNVYPNEIEEV 476
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
264-615 |
3.26e-29 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 120.88 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 264 PPAPEDLAVVCFTSGTTGNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 341
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIFstLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 gFFQGDIRLLMDDLKVLqpTVFPVVPRLLnrmfdrifgqanTTLKRwlLDFASkrkeaelrsgiirnnslwdrlifhkvq 421
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSIL------------STLSP--QDFPN--------------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 sslggkVRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTagCCLSM----PGDWTagHVGAPMPCNLIKLVDVEEM 497
Cdd:cd17653 211 ------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECT--ISSTMtellPGQPV--TIGKPIPNSTCYILDADLQ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 NYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 571
Cdd:cd17653 279 PVPEGV-VGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLE 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622942221 572 KIENIYIRSEAIAQ---VFVHGEslqaFLIAIVVP---DVETLRPWAQKR 615
Cdd:cd17653 357 EIEEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
263-604 |
5.54e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 123.88 E-value: 5.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 263 KPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDcsafVKATENSVNPCPDDTLISFLPLAHMFERVVECVM-LCHGAKI 341
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFHSFGLTVTLWLpLLEGIKV 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 GFFQGDirllMDDLKVLQ-------------PTVFpvvprllnRMFDRifgqaNTTLKRwlLDFASkrkeaelrsgiirn 408
Cdd:PRK08633 853 VYHPDP----TDALGIAKlvakhratillgtPTFL--------RLYLR-----NKKLHP--LMFAS-------------- 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 409 nslwdrlifhkvqsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMP-----GDWT-----AG 478
Cdd:PRK08633 900 -------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFKRqtgskEG 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 479 HVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL---DKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PRK08633 961 SVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDEDGFLTITDR 1040
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622942221 556 KKHIFKLAqGEYIAPEKIEniyirsEAIAQVFvHGESLQafLIAIVVPD 604
Cdd:PRK08633 1041 YSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD 1079
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-557 |
7.81e-29 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 121.14 E-value: 7.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAVT-----YIVNKAEL 195
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVK--PGDRVAVQVEKSPEALALYLATLRAGAVFLPL-----NTAYTlaeldYFIGDAEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 196 SLVFVDkPEKAKLLLEGVENKLTPSLKIivlMDAYGS-ELVERGQkcgveiislkamedlGRANRRKPKPPAPEDLAVVC 274
Cdd:PRK07514 102 ALVVCD-PANFAWLSKIAAAAGAPHVET---LDADGTgSLLEAAA---------------AAPDDFETVPRGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 275 FTSGTTGNPKGALITHRNIVSDCSAFVKA---TensvnpcPDDTLISFLPLAH---MFerVVECVMLCHGAKIGFFQG-D 347
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNALTLVDYwrfT-------PDDVLIHALPIFHthgLF--VATNVALLAGASMIFLPKfD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 348 IRLLMDDLKvlQPTVFPVVP----RLL-NRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqs 422
Cdd:PRK07514 234 PDAVLALMP--RATVMMGVPtfytRLLqEPRLTR---------------------------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 423 SLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSMP--GDWTAGHVGAPMPCNLIKLVDVEEMNYM 500
Cdd:PRK07514 266 EAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE--TNMNTSNPydGERRAGTVGFPLPGVSLRVTDPETGAEL 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942221 501 AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:PRK07514 344 PPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-694 |
9.24e-29 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 123.43 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 89 VTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEWLSYKQVAEMSECLGSALIQKGFtaTPDQFIGIFAQNRPEWVIIEQGCF 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGV--RPGDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 169 AYSMVIVPLYDTlgNEAVTYIVNKAELSLVFVDKPEKAKLLlegveNKLTPSLKIIVLMDA-YGSELVERGQKCGVEIIS 247
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAIL-----TCRSRKLETVVYTHSfYDEDDHAVARDLNITLIP 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 248 LKAMEDLGRANRRKPKPPAPED----LAVVCFTSGTTGNPKGALITHRNIVSDCSAFVkATENSVNPCPDDTLISFLPLA 323
Cdd:PTZ00297 577 YEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVHFTPFA 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 324 HMFERVVECVMLCHGAKIGffQGDIRLLMDDLKVLQPTVFPVVPRLlnrmfdriFGQANTTLKR----------WLLDfa 393
Cdd:PTZ00297 656 MLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE-- 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 394 skrKEAELRSGII---RNNSLWDRLIFHK-VQSSLGGKVRLMVTGAAPVSATvltflraalgcqfyegYGQTECTAGCCl 469
Cdd:PTZ00297 724 ---RAFQLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTS----------------FSLLEHISVCY- 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 470 smpgdwtaghvgapMPCnliklvdVEEMNYMAAegEGEVCVKG---PNVfQGYLK---DPAKTAE----ALDKDGWL-HT 538
Cdd:PTZ00297 784 --------------VPC-------LREVFFLPS--EGVFCVDGtpaPSL-QVDLEpfdEPSDGAGigqlVLAKKGEPrRT 839
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 539 GDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYIRSEAIAQVFVHGESLQAfLIAIVVPDVETLR-PWAQKRG 616
Cdd:PTZ00297 840 LPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVEfEWRQSHC 918
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 617 F---DGSFEELCRNKDVKKA---ILEDMVRLGKDSGLKPFEQVKGIALHPELFSIDNGLLTPTMKAKRPELRNYFRSQID 690
Cdd:PTZ00297 919 MgegGGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIE 998
|
....
gi 1622942221 691 ELYS 694
Cdd:PTZ00297 999 RFYS 1002
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
268-591 |
6.21e-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: 116.68 E-value: 6.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 268 EDLAVVCFTSGTTGNPKGALITHRNIvsdcSAFVKATENSVNPCPDDTLISFLPLAH------MFERVVE-CVMLCHGAk 340
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH----WWSAIGSALNLGLTEDDNWLCALPLFHisglsiLMRSVIYgMTVYLVDK- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 341 igFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLkrwlldfaskrkeaelrsgiirnnslwdrlifhkv 420
Cdd:cd05912 152 --FDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL----------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 qsslggkvRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTE-CTAGCCLSmPGDWTA--GHVGAPMPCNLIKLVDveem 497
Cdd:cd05912 192 --------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtCSQIVTLS-PEDALNkiGSAGKPLFPVELKIED---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:cd05912 258 DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
330
....*....|....
gi 1622942221 578 IRSEAIAQVFVHGE 591
Cdd:cd05912 336 LSHPAIKEAGVVGI 349
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-588 |
7.18e-28 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 118.54 E-value: 7.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVSD-CSAFVKATENSVNPCpddTLISFLPLAHMFERVVEC--VMLCHGAKIGFFQ 345
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMIGQV---VTLGLIPFFHIYGITGICcaTLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 346 GDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRLIFHKVqsslg 425
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 426 gKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTagcCLSMP-GDWTAGH-------VGAPMPCNLIKLVDVEE 496
Cdd:PLN02330 304 -KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 1622942221 577 YIRSEAIAQVFV 588
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-609 |
1.33e-27 |
|
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: 116.33 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELslvfv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALG--VGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 dkpekaklllegvenkltpslKIIVLMDAYGselvergqkcgveiislkamedlgranRRKPKPpAPEDLAVVCFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERFR---------------------------QFDPAA-MPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSDCSAFVKatenSVNPCPDDTLISFLPLAHMFERVvecvmlcHGAKIGFFQGDIRLLMDdlkVLQP 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAE----RLGLGPGDVFLVASPMAHQTGFV-------YGFTLPLLLGAPVVLQD---IWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 361 TVfpvVPRLLNRmfDRI-FGQANTTLKRWLLDfaskrkeAELRSGiirnnslwdrlifhKVQSSLggkvRLMVTGAAPVS 439
Cdd:cd05903 172 DK---ALALMRE--HGVtFMMGATPFLTDLLN-------AVEEAG--------------EPLSRL----RTFVCGGATVP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 440 ATVLTFLRAALGCQFYEGYGQTEC--TAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQ 517
Cdd:cd05903 222 RSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 518 GYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFVHG---ESLQ 594
Cdd:cd05903 301 GYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLG 378
|
490 500
....*....|....*....|.
gi 1622942221 595 AFLIAIVV------PDVETLR 609
Cdd:cd05903 379 ERACAVVVtksgalLTFDELV 399
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
262-590 |
1.56e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 117.64 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 262 PKPP-APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKaTENSV--NPCPDDTLISFLPLAHMFERVVECV-MLCH 337
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVR-FEASQyeYPGSDNVYLAALPMFHIYGLSLFVVgLLSL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 338 GAKI----GFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLKrwlldfaskrkeaelrsgiirnnslwd 413
Cdd:PLN02574 270 GSTIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK--------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 414 rlifhkvqsslggKVRLMVTGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTA----GCCLSMPGDWTAghVGAPMPCNL 488
Cdd:PLN02574 320 -------------SLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQ 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 489 IKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:PLN02574 385 AKVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQI 463
|
330 340
....*....|....*....|..
gi 1622942221 569 APEKIENIYIRSEAIAQVFVHG 590
Cdd:PLN02574 464 APADLEAVLISHPEIIDAAVTA 485
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
242-557 |
1.71e-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: 117.38 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 242 GVEIISLKAMEDLGRANRRKPKPPA-PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAfvKATENSVNPcpDDTLISFL 320
Cdd:cd05906 140 GLPGIRVLSIEELLDTAADHDLPQSrPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWV 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 321 PLAHmferVVECVMlCHGAkigffqgDIRLLMDDLKVLQPTVFPVVPRLLnRMFDRIfgQANTTlkrWLLDFA-SKRKEA 399
Cdd:cd05906 216 PLDH----VGGLVE-LHLR-------AVYLGCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPNFAfALLNDL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 400 ELRsgiiRNNSLWDrlifhkvQSSLggkvRLMVTGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGC--CLSM 471
Cdd:cd05906 278 LEE----IEDGTWD-------LSSL----RYLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGViySRSF 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 472 P-GDWTAGH----VGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLP 546
Cdd:cd05906 343 PtYDHSQALefvsLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLD 420
|
330
....*....|.
gi 1622942221 547 NGTLKIIDRKK 557
Cdd:cd05906 421 NGNLTITGRTK 431
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-603 |
1.71e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 116.96 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLK--KGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DkPEKAKLLLEGVEnkLTPSLKIIVLMDAYGSELVErgqkcgveiiSLKAMEDLGRANRRKPKPPAP--EDLAVVCFTSG 278
Cdd:PRK08316 115 D-PALAPTAEAALA--LLPVDTLILSLVLGGREAPG----------GWLDFADWAEAGSVAEPDVELadDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 279 TTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMFERVVecvmlchgakigffqgdirLLMDDLKVL 358
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDMS----ADDIPLHALPLYHCAQLDV-------------------FLGPYLYVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 359 QPTVFPVVPRLlNRMFDRIFGQANTTLkrwlldFASKrkeaelrsgiirnnSLWDRLIFHKV-----QSSLggkvRLMVT 433
Cdd:PRK08316 239 ATNVILDAPDP-ELILRTIEAERITSF------FAPP--------------TVWISLLRHPDfdtrdLSSL----RKGYY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 434 GAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAgccLSM---PGDwTAGHVG-APMPC-NL-IKLVDvEEMNYMAAeGE- 505
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTEIAP---LATvlgPEE-HLRRPGsAGRPVlNVeTRVVD-DDGNDVAP-GEv 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 506 GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSEAIAQ 585
Cdd:PRK08316 368 GEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAE 445
|
490 500
....*....|....*....|..
gi 1622942221 586 VFV----HGESLQAfLIAIVVP 603
Cdd:PRK08316 446 VAViglpDPKWIEA-VTAVVVP 466
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-604 |
2.99e-27 |
|
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: 115.85 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 119 EWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLV 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 199 FVDkpekaklllegvenkltpslkiivlmdaygSELVERGQKCGVEIisLKAMEDLGRANRRKPKPPAPEDLAVVCFTSG 278
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLPVL--LLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 279 TTGNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFFQGDI----RLLM 352
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 353 DDLKVLQPTVFpvvprllnrmfdrifgQANTTLKRWLLDfaskrkeaelrSGiirnnslWDRLifhkvqsslgGKVRLMV 432
Cdd:cd12116 211 RLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR----------AGLTALC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 433 TGAA--PVSATVLTflraALGCQFYEGYGQTECT--AGCCLSMPGDwTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 508
Cdd:cd12116 247 GGEAlpPDLAARLL----SRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGEL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 509 CVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSE 581
Cdd:cd12116 321 YIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHP 399
|
490 500
....*....|....*....|....*
gi 1622942221 582 AIAQ--VFVHGESLQAFLIAIVVPD 604
Cdd:cd12116 400 GVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
119-615 |
3.50e-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: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 119 EWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCF----AYsmviVPLYDTLGNEAVTYIVNKAE 194
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALG--VGPGDLVGVCLERSLEMVVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 195 LSLVfvdkpekaklllegvenkLTPSlkiivlmdaygsELVERGQKCGVEIISLKAMEDLGRANRRKPKPPAPEDLAVVC 274
Cdd:COG1020 574 ARLV------------------LTQS------------ALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 275 FTSGTTGNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAH------MFervvecVMLCHGAKIGFFQGDI 348
Cdd:COG1020 624 YTSGSTGRPKGVMVEHRALVN----LLAWMQRRYGLGPGDRVLQFASLSFdasvweIF------GALLSGATLVLAPPEA 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 349 RLLMDDLKVL----QPTVFPVVPRLLNRMFDrifgqanttlkrwlldfaskrkeaelrsgiirnnSLWDRLifhkvqSSL 424
Cdd:COG1020 694 RRDPAALAELlarhRVTVLNLTPSLLRALLD----------------------------------AAPEAL------PSL 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 ggkvRLMVTG--AAPVsATVLTFLRAALGCQFYEGYGQTECTAGCCLS--MPGDWTAGHV--GAPMPCNLIKLVDvEEMN 498
Cdd:COG1020 734 ----RLVLVGgeALPP-ELVRRWRARLPGARLVNLYGPTETTVDSTYYevTPPDADGGSVpiGRPIANTRVYVLD-AHLQ 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 499 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 571
Cdd:COG1020 808 PVPVGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELG 886
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1622942221 572 KIENIYIRSEAIAQ--VFVHGESLQA-FLIAIVVPDVETLRPWAQKR 615
Cdd:COG1020 887 EIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAAAAAALLR 933
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-628 |
4.14e-27 |
|
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: 115.47 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 120 WLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVF 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGIS--RGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 200 VDKPekakLLLEgvenkltpslkiivlmdaygsELVERGQKcgveiislkamedlgranRRKPKPPAPE-DLAVVCFTSG 278
Cdd:cd12118 107 VDRE----FEYE---------------------DLLAEGDP------------------DFEWIPPADEwDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 279 TTGNPKGALITHRnivsdcSAFVKATENSV----NPCPddTLISFLPLAHmfervveCVMLCHGAKIGFFQG-------- 346
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANILewemKQHP--VYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrkv 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 347 DIRLLMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIRNNSlwdrlifHKVQSSLGG 426
Cdd:cd12118 209 DAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAP-------PSDARPLPH 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 427 KVRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLSMPgDWTAGHV----------GAPMPCNL-IKLV 492
Cdd:cd12118 249 RVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAWKP-EWDELPTeerarlkarqGVRYVGLEeVDVL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 493 DVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 570
Cdd:cd12118 325 DPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISS 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942221 571 EKIENIYIRSEAIAQVFVH-------GESLQAFLiaivvpdveTLRPwaqkrGFDGSFEEL---CRNK 628
Cdd:cd12118 403 VEVEGVLYKHPAVLEAAVVarpdekwGEVPCAFV---------ELKE-----GAKVTEEEIiafCREH 456
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
264-598 |
4.91e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 116.29 E-value: 4.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 264 PPAPE-DLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPcpDDTLISFLPLAHMF-ERVVECVMLCHGAKI 341
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEG--EEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 GFF-QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqaNTTLkrwlldfaskRKEAELRSgiirnnslwdrlifhkv 420
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 qsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPgdW---TAGHVGAPMPCNLIKLVDVEEM 497
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFL--WekrVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 1622942221 578 IRSEAIAQVFV-------HGESLQAFLI 598
Cdd:PRK06710 474 YEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
219-584 |
6.70e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 116.21 E-value: 6.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 219 PSLKIIVLMDayGSELVERGQKCGVEIISLKAME---DLGRANRRKP-------KPPAPEDLAVVCFTSGTTGNPKGALI 288
Cdd:PRK07529 156 PELRTVVEVD--LARYLPGPKRLAVPLIRRKAHArilDFDAELARQPgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQH 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 289 THRNIVSDC---SAFVKATensvnpcPDDTLISFLPLAHMFERVVEC-VMLCHGAKIGFF--QG--DIRLLMDDLKVL-- 358
Cdd:PRK07529 234 THGNEVANAwlgALLLGLG-------PGDTVFCGLPLFHVNALLVTGlAPLARGAHVVLAtpQGyrGPGVIANFWKIVer 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 359 -QPTVFPVVPRLLNRMFDRIFGQANTtlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqSSLggkvRLMVTGAAP 437
Cdd:PRK07529 307 yRINFLSGVPTVYAALLQVPVDGHDI--------------------------------------SSL----RYALCGAAP 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 438 VSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMP-GDWTAGHVGAPMPCNLIKLVDVEEMNYM---AAEGE-GEVCVKG 512
Cdd:PRK07529 345 LPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAGRYlrdCAVDEvGVLCIAG 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622942221 513 PNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIA 584
Cdd:PRK07529 425 PNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
267-604 |
6.80e-27 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 114.95 E-value: 6.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLplAHMFE-RVVECVM-LCHGAKIGff 344
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT----SESRVLQFA--SYTFDvSILEIFTtLAAGGCLC-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 qgdI---RLLMDDLkvlqptvfpvvPRLLNRMfdrifgQANTtlkrwlldfaskrkeAELRSGIIRnnslwdrLIFHKVQ 421
Cdd:cd05918 177 ---IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLDPEDV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 SSLggkvRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLSMPG-DWTAGHVGAPMPCNLIkLVDVEEMNYM 500
Cdd:cd05918 215 PSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW-VVDPDNHDRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 501 AAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:cd05918 288 VPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQ 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622942221 567 YIAPEKIENiYIRS------EAIAQVFVH-GESLQAFLIAIVVPD 604
Cdd:cd05918 367 RVELGEIEH-HLRQslpgakEVVVEVVKPkDGSSSPQLVAFVVLD 410
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-614 |
7.56e-27 |
|
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: 114.73 E-value: 7.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 111 SRKPDQPY-----EWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTL 181
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKG--VGPDTIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 182 GNEAVTYIVNKAELSLVFVDKPEKAKLLLEGvenkltpslkIIVLMDAygselvergqkcgvEIISLKAMEDLGRANRrk 261
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENLEPVSK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 262 pkppaPEDLAVVCFTSGTTGNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAhmFERVVECVM--LCHGA 339
Cdd:cd17655 136 -----SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASIS--FDASVTEIFasLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 340 KIgffqgdirllmddLKVLQPTVFPVVPrllnrmFDRIFGQANTTLkrwlldfaSKRKEAELRsgiirnnslwdrlIFHK 419
Cdd:cd17655 205 TL-------------YIVRKETVLDGQA------LTQYIRQNRITI--------IDLTPAHLK-------------LLDA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 420 VQSSLGGKVRLMVTGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCCLSM--PGDWTAGHV--GAPMPCNLIKLVD 493
Cdd:cd17655 245 ADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASIYQyePETDQQVSVpiGKPLGNTRIYILD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 494 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:cd17655 325 -QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYR 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1622942221 568 IAPEKIENIYIRSEAIAQ--VFVH-GESLQAFLIAIVVPD----VETLRPWAQK 614
Cdd:cd17655 403 IELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSEkelpVAQLREFLAR 456
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
121-588 |
1.26e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 114.82 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSAL----IQKGftatpDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELS 196
Cdd:COG0365 40 LTYAELRREVNRFANALralgVKKG-----DR-VAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 197 LVFVD----KPEKAKLLLEGVEN--KLTPSLKIIVLMDAYGSELVERGQkcgveiISLkamEDLgRANRRKPKPPAP--- 267
Cdd:COG0365 114 VLITAdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEGD------LDW---DEL-LAAASAEFEPEPtda 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 268 EDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKateNSVNPCPDDTLISFLPLA----HMFervveCVM--LCHGAKI 341
Cdd:COG0365 184 DDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVFWCTADIGwatgHSY-----IVYgpLLNGATV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 GFFQGDI------RL--LMDDLKVlqpTVFPVVPRLLnRMfdrifgqanttLKRWLLDFASKrkeaelrsgiirnnslWD 413
Cdd:COG0365 256 VLYEGRPdfpdpgRLweLIEKYGV---TVFFTAPTAI-RA-----------LMKAGDEPLKK----------------YD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 414 RlifhkvqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWT-AGHVGAPMPCNLIKLV 492
Cdd:COG0365 305 L-------SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 493 DvEEMNYMAAEGEGEVCVKG--PNVFQGYLKDPAKTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 568
Cdd:COG0365 374 D-EDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRI 451
|
490 500
....*....|....*....|
gi 1622942221 569 APEKIENIYIRSEAIAQVFV 588
Cdd:COG0365 452 GTAEIESALVSHPAVAEAAV 471
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
113-615 |
1.46e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 114.49 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 113 KPDQPY-----EWLSYKQVAEMSECLGSALIQKGFTATpDQFIgIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVT 187
Cdd:PRK07786 30 QPDAPAlrflgNTTTWRELDDRVAALAGALSRRGVGFG-DRVL-ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 188 YIVNKAELSLVFVDKPEKAklLLEGVENkLTPSLKIIVLMDAYGSELVergqkcgveiislKAMEDLGRANRrKPKPPA- 266
Cdd:PRK07786 108 FLVSDCGAHVVVTEAALAP--VATAVRD-IVPLLSTVVVAGGSSDDSV-------------LGYEDLLAEAG-PAHAPVd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 -PEDL-AVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNpcpDDtlISFL--PLAHM--FERVVECVMLchGAK 340
Cdd:PRK07786 171 iPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADIN---SD--VGFVgvPLFHIagIGSMLPGLLL--GAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 341 IgffqgdirllmddlkVLQPTvfpvvprllnRMFDrifgqANTTLKRWlldfaskrkEAELRSGIIRNNSLWDRLIFHKV 420
Cdd:PRK07786 244 T---------------VIYPL----------GAFD-----PGQLLDVL---------EAEKVTGIFLVPAQWQAVCAEQQ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 QSSLGGKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLSMPGDWTA--GHVGAPMPCNLIKLVDvEEM 497
Cdd:PRK07786 285 ARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:PRK07786 364 NDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVL 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622942221 578 IRSEAIAQVFVHGESLQAF---LIAIVVPD-------VETLRPWAQKR 615
Cdd:PRK07786 442 ASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEFLTDR 489
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-671 |
1.70e-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: 114.45 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 107 PCLGSRKPDQPYEWLSYKQVAEMSECLGSALIQKGFTAtpDQFIGIFAQNRPEWVIIEQGCF---AYSMVIVPLYDTLGN 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSA--ERPLLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 184 EAV--TYIVNKAELSLVFVDKPEKAKLLLEGVENKLTPSlkIIVLMDAYGSELVERGqkcgveiiSLKAMEDLGRANRRK 261
Cdd:cd05921 90 DLAklKHLFELLKPGLVFAQDAAPFARALAAIFPLGTPL--VVSRNAVAGRGAISFA--------ELAATPPTAAVDAAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 262 PKPpAPEDLAVVCFTSGTTGNPKGALITHRNIVSdcsafVKATENSVNPCPDD---TLISFLPLAHMFervvecvmlchG 338
Cdd:cd05921 160 AAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCA-----NQAMLEQTYPFFGEeppVLVDWLPWNHTF-----------G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 339 AKIGF-----------------FQGDIRLLMDDLKVLQPTVFPVVPR----LLNRMfdrifgQANTTLKRWLLdfasKRK 397
Cdd:cd05921 223 GNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVPAgwemLVAAL------EKDEALRRRFF----KRL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 398 EAELRSGIIRNNSLWDRLIFHKVQSSlGGKVRlmvtgaapvsatvltflraalgcqFYEGYGQTEcTAGCCLSMPGDWT- 476
Cdd:cd05921 293 KLMFYAGAGLSQDVWDRLQALAVATV-GERIP------------------------MMAGLGATE-TAPTATFTHWPTEr 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 477 AGHVGAPMPCNLIKLVdveemnymAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKI 552
Cdd:cd05921 347 SGLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 553 IDRKKHIFKLAQGEYIA--PEKIENIYIRSEAIAQVFVHGESlQAFLIAIVVPDVETLRpwAQKRGFDGSFEELCRNKDV 630
Cdd:cd05921 419 DGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLACR--RLVGLQEASDAEVLRHAKV 495
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1622942221 631 KKAILEDMVRLGKDSGLKPfEQVKGIALHPELFSIDNGLLT 671
Cdd:cd05921 496 RAAFRDRLAALNGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-575 |
2.05e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 112.92 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 173 VIVPLYDTLGNEAVTYIVNKAELSLVFVDkpekaklllEGVENKLTPSLkiIVLMDAygselvergqkcgVEIISLKAME 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLAD---------AGAADRLRDAL--PASPDP-------------GTVLDADGIR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 253 DLGRAnrRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMFERVVEC 332
Cdd:cd05922 104 AARAS--APAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT----ADDRALTVLPLSYDYGLSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 333 VMLCHGAKIgFFQGDIRL---LMDDLKVLQPTVFPVVPRLLNrMFDRIfgqanttlkrwlldfasKRKEAELrsgiirnN 409
Cdd:cd05922 178 THLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKL-------P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 410 SLwdRLIfhkvqSSLGGKVRlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCCLsMPGDWTA---GHVGAPMPC 486
Cdd:cd05922 232 SL--RYL-----TQAGGRLP---------QETIARLRELLPGAQVYVMYGQTEATRRMTY-LPPERILekpGSIGLAIPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 487 NLIKLVDVEEMNYmaAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 565
Cdd:cd05922 295 GEFEILDDDGTPT--PPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-G 371
|
410
....*....|
gi 1622942221 566 EYIAPEKIEN 575
Cdd:cd05922 372 NRISPTEIEA 381
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
267-646 |
4.01e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 113.82 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVS------DCSAFVkATENSVnpcpddtLISFLPLAHMFERVVEC-VMLCHGA 339
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFL-AEEPPV-------LVDWLPWNHTFGGNHNLgIVLYNGG 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 340 KI---------GFFQGDIRllmdDLKVLQPTVFPVVPR--------------LLNRMFDRifgqanttLKrwLLDFASkr 396
Cdd:PRK08180 280 TLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemlvpalerdaaLRRRFFSR--------LK--LLFYAG-- 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 397 keAELRSgiirnnSLWDRLifHKV-QSSLGGKVRLMVtgaapvsatvltflraalgcqfyeGYGQTEcTAGCCLSM--PG 473
Cdd:PRK08180 344 --AALSQ------DVWDRL--DRVaEATCGERIRMMT------------------------GLGMTE-TAPSATFTtgPL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 474 DwTAGHVGAPMPCNLIKLVDVEemnymaaeGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGT 549
Cdd:PRK08180 389 S-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERG 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 550 LKIIDRKKHIFKLAQGEYIA--PEKIENIYIRSEAIAQVFVHGESlQAFLIAIVVPDVETLRPWAQKRGfDGSFEELCRN 627
Cdd:PRK08180 460 LMFDGRIAEDFKLSSGTWVSvgPLRARAVSAGAPLVQDVVITGHD-RDEIGLLVFPNLDACRRLAGLLA-DASLAEVLAH 537
|
410
....*....|....*....
gi 1622942221 628 KDVKKAILEDMVRLGKDSG 646
Cdd:PRK08180 538 PAVRAAFRERLARLNAQAT 556
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-598 |
9.05e-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: 110.65 E-value: 9.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTAtpDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRK--GDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 dkpekaklllegvenkltpslkiivlmdayGSELvergqkcgveiislkamedlgranrrkpkppapEDLAVVCFTSGTT 280
Cdd:cd05935 80 ------------------------------GSEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSDCSAFVKATensvNPCPDDTLISFLPLAHM--FERVVECVMLCHGAKIGFFQGDIRLLMDDLKVL 358
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWT----GLTPSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 359 QPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslggkVRLMVTGAAPV 438
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--------ATPEFKTRDLSS---------------------------------LKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 439 SATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQG 518
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 519 YLKDPAKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSEAIAQVFV------- 588
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|
gi 1622942221 589 HGESLQAFLI 598
Cdd:cd05935 371 VGEEVKAFIV 380
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
127-590 |
2.61e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 110.28 E-value: 2.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 127 AEMSECLG-SALIQKGFTATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFvdkpek 205
Cdd:PRK09088 26 AELDALVGrLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 206 aklllegvenkltpslkiivlmdayGSELVERGQKCGVEIISLKAMEDLGRANRRKPKPPapEDLAVVCFTSGTTGNPKG 285
Cdd:PRK09088 100 -------------------------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 286 ALITHRNIVSDCSAFVKATENsvnpcpdDTLISFLPLAHMFERV--VECV--MLCHGAKIGFFQGdirllmddlkvLQPT 361
Cdd:PRK09088 153 VMLSERNLQQTAHNFGVLGRV-------DAHSSFLCDAPMFHIIglITSVrpVLAVGGSILVSNG-----------FEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 362 vfpvvpRLLNRMFDRIFGQANTtlkrwlldFASKRKEAELRSGIIRNNSLWDRLIfhkvqsslggkvrLMVTGAAP-VSA 440
Cdd:PRK09088 215 ------RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhAAE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 441 TVLTFLraALGCQFYEGYGQTEctAGCCLSMPGDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCVKGPNV 515
Cdd:PRK09088 268 DILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPAGV-PGELLLRGPNL 342
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622942221 516 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:PRK09088 343 SPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHPGIRECAVVG 416
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
121-626 |
4.25e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 110.14 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAElSLVFV 200
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLG--VGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 --------DKPEkaklLLEGVENKLtPSLKIIVLMDAYGSELVERgqkcgveIISLKAME---DLGR--ANRRkpkpPAP 267
Cdd:PRK13295 133 vpktfrgfDHAA----MARRLRPEL-PALRHVVVVGGDGADSFEA-------LLITPAWEqepDAPAilARLR----PGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 268 EDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMfervvecvmlchgakIGFFQGD 347
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLG----ADDVILMASPMAHQ---------------TGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 348 IRLLMDDLK-VLQPTVFPVvprllnRMFDRI------FGQANTTlkrWLLDFASKRKEAElrsgiirnnslwdrlifhKV 420
Cdd:PRK13295 258 MMPVMLGATaVLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESG------------------RP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 QSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMN 498
Cdd:PRK13295 311 VSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAvtLTKLDDPDERASTTDGCPLPGVEVRVVDADGAP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 499 YMAAEgEGEVCVKGPNVFQGYLKDPAKTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYI 578
Cdd:PRK13295 387 LPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLY 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1622942221 579 RSEAIAQVFVHG---ESLQAFLIAIVVPdvetlRPwaqKRGFDgsFEELCR 626
Cdd:PRK13295 463 RHPAIAQVAIVAypdERLGERACAFVVP-----RP---GQSLD--FEEMVE 503
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-590 |
5.12e-25 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 109.18 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 119 EWLSYKQVAEMSECLGSALIQKgFTATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAVTyivnKAELSLV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYE-LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL-----NIRLT----ENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 199 FVDKpekaklllegvenkltpSLKIIVLMDAYGSELVERGQKCGVE-IISLKAMEDLGRANRRKPKPPAPEDLAVVCFTS 277
Cdd:PRK06839 96 LKDS-----------------GTTVLFVEKTFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEKNESASFIICYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 278 GTTGNPKGALITHRNIvsdcsaFVKATEN--SVNPCPDDTLISFLPLAHMfervvecvmlchgAKIGFFQgdirllmddl 355
Cdd:PRK06839 159 GTTGKPKGAVLTQENM------FWNALNNtfAIDLTMHDRSIVLLPLFHI-------------GGIGLFA---------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 356 kvlQPTVFP----VVPRLLN-----RMFDR-----IFGQAntTLKRWLLDfASKRKEAELRSgiirnnslwdrlifhkvq 421
Cdd:PRK06839 210 ---FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS------------------ 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 sslggkVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLSMPGDW--TAGHVGAPMPCNLIKLVDvEEMNY 499
Cdd:PRK06839 266 ------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNK 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIR 579
Cdd:PRK06839 338 VEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINK 415
|
490
....*....|.
gi 1622942221 580 SEAIAQVFVHG 590
Cdd:PRK06839 416 LSDVYEVAVVG 426
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-615 |
1.17e-24 |
|
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: 105.49 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVSdcSAfvKATENSVNPCPDDTLISFLPLAHM--FERVVECVMLchGAKIGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--AGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 347 DiRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 427 kVRLMVTGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEG 506
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 507 EVCVKGPNVFQGYLKDPakTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQV 586
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622942221 587 FVHG---ESLQAFLIAIVV----PDVETLRPWAQKR 615
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVgrgpADPAELRAWLKDK 292
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
1.41e-24 |
|
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: 105.43 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATensvNPCPDDTLISFLPLAHMFERVVECVMLCHGAK---IGFFQ 345
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAM----GLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 346 GDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiIRNnslwdrlifhkvqssl 424
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 ggkvrlmVTGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 503
Cdd:cd17637 119 -------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 504 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYIRSE 581
Cdd:cd17637 187 ETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1622942221 582 AIAQVFVHGeslqafliaivVPDVE 606
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
123-615 |
2.71e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 103.89 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 123 YKQVAEMSECLGSALIQKGftatpdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVDk 202
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 203 pekaklllEGVENKLTPSLKIIVlmdaygSELvergQKCGVEIISLKAMEDLgranrrkpkppapEDLAVVCFTSGTTGN 282
Cdd:PRK03640 107 --------DDFEAKLIPGISVKF------AEL----MNGPKEEAEIQEEFDL-------------DEVATIMYTSGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 283 PKGALITHRNivsdcsAFVKATENSVNP--CPDDTLISFLPLAH------MFERVVE-CVMLCH----GAKIgffqgdIR 349
Cdd:PRK03640 156 PKGVIQTYGN------HWWSAVGSALNLglTEDDCWLAAVPIFHisglsiLMRSVIYgMRVVLVekfdAEKI------NK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 350 LLMDDlKVlqpTVFPVVPRLLNRMFDRIfGQANTtlkrwlldfaskrkeaelrsgiirNNSLwdrlifhkvqsslggkvR 429
Cdd:PRK03640 224 LLQTG-GV---TIISVVSTMLQRLLERL-GEGTY------------------------PSSF-----------------R 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 430 LMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCCLSMPGDWTA---GHVGAPM-PCNlIKLVDveEMNYMAAEGE 505
Cdd:PRK03640 258 CMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFEE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 506 GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQ 585
Cdd:PRK03640 333 GEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVAE 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622942221 586 VFVHGESLQ-------AFLIAIVVPDVETLRPWAQKR 615
Cdd:PRK03640 411 AGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
121-610 |
5.58e-23 |
|
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: 103.32 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALiqKGFTATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVfV 200
Cdd:TIGR03098 26 LTYAALSERVLALASGL--RGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKPEKAKLLLEGVENklTPSLKIIVLMDAYGSElveRGQKCGVEIISLKAMEDLGRANRrkPKPPAPEDLAVVCFTSGTT 280
Cdd:TIGR03098 103 TSSERLDLLHPALPG--CHDLRTLIIVGDPAHA---SEGHPGEEPASWPKLLALGDADP--PHPVIDSDMAAILYTSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAhmfervvecvmlchgakigffqgdirllmddlkvlqp 360
Cdd:TIGR03098 176 GRPKGVVLSHRNLVAGAQSVATYLENR----PDDRLLAVLPLS------------------------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 361 tvfpvvprllnrmFDRIFGQANTTL----KRWLLDFASKRK-----EAELRSGIIRNNSLWDRLIFHKVQSSLGGKVRLM 431
Cdd:TIGR03098 215 -------------FDYGFNQLTTAFyvgaTVVLHDYLLPRDvlkalEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 432 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLSmPG--DWTAGHVGAPMPcNLIKLVDVEEMNYMAAEGEGEV 508
Cdd:TIGR03098 282 TNSGGAMPRATLSRLRSFLPnARLFLMYGLTEAFRSTYLP-PEevDRRPDSIGKAIP-NAEVLVLREDGSECAPGEEGEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 509 CVKGPNVFQGYLKDPAKTAEALDK----DGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 577
Cdd:TIGR03098 360 VHRGALVAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA 438
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622942221 578 IRSEAIAQVFVHG----ESLQAFLIAIVVPDVETLRP 610
Cdd:TIGR03098 439 YATGLVAEAVAFGvpdpTLGQAIVLVVTPPGGEELDR 475
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
266-610 |
7.59e-23 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 101.94 E-value: 7.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAHMFervveCVM-----LCHGAk 340
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFSFDL-----SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 341 igffqgdirllmddlkvlqpTVFPVvPRLLNRMFDRIF-GQANTTLKRWLldfaskrkeaelrsgiiRNNSLWDRLIFHK 419
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVWV-----------------STPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 420 --VQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-----SMPGDWTAGHVGAPMPCNLIKLV 492
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYievtpEVLDGYDRLPIGYAKPGAKLVIL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 493 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 569
Cdd:cd05945 287 D-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIE 364
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622942221 570 PEKIENIYIRSEAIAQVFV----HGESLQAfLIAIVVPDVETLRP 610
Cdd:cd05945 365 LEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGAEAG 408
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-682 |
1.53e-22 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 101.68 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DkPEKAKLLLEGVEnKLTPSLKIIVLMDAYGSELVErgqkcgveiislKAMEDL--GRANRRKPKPPAPEDLAVVCFTSG 278
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGPEAGA------------LLLAELvaAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 279 TTGNPKGALITHRNIVSDCSAFVKateNSVNPCPDDTLISFLPLAHMFErvvecvmLCHGAKIGFFQGDIRLLM------ 352
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 353 ----DDLKVLQPTVFPVVPRLLNRMfdrifgqanttlkrwlldfaskrkeaelrsgiIRNNSLWDRLifhkvQSSLggkv 428
Cdd:cd05959 244 aavfKRIRRYRPTVFFGVPTLYAAM--------------------------------LAAPNLPSRD-----LSSL---- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 429 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 508
Cdd:cd05959 283 RLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 509 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSEAIAQVFV 588
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 589 HGESLQAFLI---AIVVPdvetlrpwaqKRGFDGSfeelcrnkdvkkAILEDMVRLGKDSGLKPFEQVKGIALHPELFSi 665
Cdd:cd05959 440 VGVEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRLAPYKYPRWIVFVDELPK- 496
|
570
....*....|....*..
gi 1622942221 666 dngllTPTMKAKRPELR 682
Cdd:cd05959 497 -----TATGKIQRFKLR 508
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
264-615 |
1.79e-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: 101.51 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 264 PPAPEDLAVVCFTSGTTGNPKGALITHRNIVSdcsaFVKATeNSVNPCPDDTLISFLPL---AHMFERVVEcvmLCHGAK 340
Cdd:cd12117 132 PVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR----LVKNT-NYVTLGPDDRVLQTSPLafdASTFEIWGA---LLNGAR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 341 IgffqgdirllmddlkVLQPtvfPVVPRLLNRMFDRIFGQANTTLkrWLldfaskrkeaelrsgiirNNSLWdRLIFHKV 420
Cdd:cd12117 204 L---------------VLAP---KGTLLDPDALGALIAEEGVTVL--WL------------------TAALF-NQLADED 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 QSSLGGkVRLMVTGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCCLSMPGDWTAGHV--GAPMPcNLIKLVdVE 495
Cdd:cd12117 245 PECFAG-LRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIA-NTRVYV-LD 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 496 EMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd12117 322 EDGRPVPPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRI 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1622942221 569 APEKIENIYIRSEAIAQVFV---HGESLQAFLIAIVVP----DVETLRPWAQKR 615
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVvvrEDAGGDKRLVAYVVAegalDAAELRAFLRER 454
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-591 |
1.89e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 99.48 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDcsAFVKATENSVNPcpDDTLISFLPLAHMFERVVECVMLchgakigFFQG 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYN--AWMLALNSLFDP--DDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 347 DIRLLMDDLKVLQPTVFPVVPRLLNRMfdRIfgQANTTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLgg 426
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 427 kvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMP-GDWTAGHVGAPMPCNLIKLVDVE-EMNYM--AA 502
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 503 EGE-GEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSE 581
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330
....*....|
gi 1622942221 582 AIAQVFVHGE 591
Cdd:cd05944 280 AVAFAGAVGQ 289
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
266-682 |
1.95e-22 |
|
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: 100.58 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHR----NIVSDCSAFvkatensvNPCPDDTLISFLPlahmfervvecvmlchgAKI 341
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRvllgHLPGVQFPF--------NLFPRDGDLYWTP-----------------ADW 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 GFFQGdirlLMDdlkVLQPTVFPVVPRLLNRM--FDRifGQANTTLKRWLLDFASKRKEAeLRsgIIRnnslwdrliFHK 419
Cdd:cd05971 141 AWIGG----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 420 VQSSLGG-KVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLSMpGDWTAGHVGAPMPCNLIKLVDvEE 496
Cdd:cd05971 200 EQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLviGNCSAL-FPIKPGSMGKPIPGHRVAIVD-DN 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 497 MNYMAAEGEGEVCVKGPN--VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 574
Cdd:cd05971 278 GTPLPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 575 NIYIRSEAIAQVFV-------HGESLQAFLIaivvpdvetLRPwaqkrGFDGSfEELCRNkdvkkaiLEDMVRlgkdSGL 647
Cdd:cd05971 356 ECLLKHPAVLMAAVvgipdpiRGEIVKAFVV---------LNP-----GETPS-DALARE-------IQELVK----TRL 409
|
410 420 430
....*....|....*....|....*....|....*
gi 1622942221 648 KPFEQVKGIALHPELfsidngLLTPTMKAKRPELR 682
Cdd:cd05971 410 AAHEYPREIEFVNEL------PRTATGKIRRRELR 438
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-576 |
2.12e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 103.12 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGsALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKNTP--PGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKP--EKAKL--LLEGVENkltpSLKIIVLMDaygselVERGQKCGVEIISLKAmedlGRANRRKPKPPAPEDLAVVCFT 276
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 SGTTGNPKGALITHRNIVSDCsafvkATENSVNPC-PDDTLISFLPLAHMFervvecvmlchgakiGFFQGDIRLLMDDL 355
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLANR-----AQVAARIDFsPEDKVFNALPVFHSF---------------GLTGGLVLPLLSGV 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 356 KVL---QPTVFPVVPRLlnrmfdrIFgQANTTL----KRWLLDFASKRKEAELRSgiirnnslwdrlifhkvqsslggkV 428
Cdd:PRK06814 862 KVFlypSPLHYRIIPEL-------IY-DTNATIlfgtDTFLNGYARYAHPYDFRS------------------------L 909
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 429 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNymaaEGeGEV 508
Cdd:PRK06814 910 RYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-GRL 984
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622942221 509 CVKGPNVFQGYLK-DPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:PRK06814 985 FVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-682 |
2.60e-22 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 100.10 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSAL----IQKGftatpDQFIGIFAqNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELS 196
Cdd:cd05972 1 WSFRELKRESAKAANVLaklgLRKG-----DRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 197 LVFVDKpekaklllegvenkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkppapEDLAVVCFT 276
Cdd:cd05972 75 AIVTDA-----------------------------------------------------------------EDPALIYFT 89
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 SGTTGNPKGALITHRNIVS---DCSAFVKATENSVNPCPDDT------LISFL-PLAHMFervveCVMLCHGAKIgffqg 346
Cdd:cd05972 90 SGTTGLPKGVLHTHSYPLGhipTAAYWLGLRPDDIHWNIADPgwakgaWSSFFgPWLLGA-----TVFVYEGPRF----- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 347 DIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqanTTLKRWLldfaskrkEAELRSGiirnnslwdrlifhkVQSSLgg 426
Cdd:cd05972 160 DAERILELLERYGVTSFCGPP---------------TAYRMLI--------KQDLSSY---------------KFSHL-- 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 427 kvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEG 506
Cdd:cd05972 200 --RLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEEG 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 507 EVCVKGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSEAIA 584
Cdd:cd05972 277 DIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVA 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 585 QVFV-------HGESLQAFLIaivvpdvetLRPwaqkrGFDGSfEELcrnkdvkkaiLEDMVRLGKdSGLKPFEQVKGIA 657
Cdd:cd05972 355 EAAVvgspdpvRGEVVKAFVV---------LTS-----GYEPS-EEL----------AEELQGHVK-KVLAPYKYPREIE 408
|
570 580
....*....|....*....|....*
gi 1622942221 658 LHPELfsidngLLTPTMKAKRPELR 682
Cdd:cd05972 409 FVEEL------PKTISGKIRRVELR 427
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
70-604 |
2.80e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.11 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 70 ARRS----ALLDSDEplvyfYEDVTTLY----EGFQRGIQVSNNGPCLGSRKPDQPY-----EWLSYKQVAEMSECLGSA 136
Cdd:PRK12316 1970 AQAAlgelALLDAGE-----RQRILADWdrtpEAYPRGPGVHQRIAEQAARAPEAIAvvfgdQHLSYAELDSRANRLAHR 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 137 LIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFVDKPEKAKLLLEGvenk 216
Cdd:PRK12316 2045 LRARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA---- 2118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 217 ltpslkiivlmdaygselvergqkcGVEIISLKAMEDLGRANRRKPKPP-APEDLAVVCFTSGTTGNPKGALITHRNIVS 295
Cdd:PRK12316 2119 -------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 296 DCSAFVKATENSvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDLKVLQPtvfpvvprllNRM 373
Cdd:PRK12316 2174 HCQAAGERYELS----PADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWDP----------EQL 2228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 374 FDRIFGQANTtlkrwLLDFASkrkeaelrsgiirnnSLWDRLIFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQ 453
Cdd:PRK12316 2229 YDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 454 F-YEGYGQTECTA-----GCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTA 527
Cdd:PRK12316 2289 YlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTA 2367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 528 EALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHI-----FKLAQGEyIAPEKIENIYIRSEA-IAQVFVHGESLQ 594
Cdd:PRK12316 2368 ERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQvkirgFRIELGE-IEARLQAHPAVREAVvVAQDGASGKQLV 2446
|
570
....*....|
gi 1622942221 595 AFliaiVVPD 604
Cdd:PRK12316 2447 AY----VVPD 2452
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-590 |
3.93e-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: 100.28 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 dkpekaklllegvenkltpslkiivlmdAYGSELVERGQKCGVEIISLKAMEDLGRANRR----KPKPPAPEDLAVVCFT 276
Cdd:cd05923 107 ----------------------------AVDAQVMDAIFQSGVRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVFYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 SGTTGNPKGALITHRNIVSdcSAFVKATENSVNPCPDDTLISFLPLAHMfervvecvmlchgakIGFFQgdirLLMDDLk 356
Cdd:cd05923 159 SGTTGLPKGAVIPQRAAES--RVLFMSTQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 357 VLQPTVFPVvprllnRMFDRIFgqanttlkrwlldfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGK-VRLMVTGA 435
Cdd:cd05923 217 ALDGTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTFAG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 436 APVSATVLTFLRAALGCQFYEGYGQTEctAGCCLSMPgDWTAGHVGAPMPCNLIKLVDV-EEMNYMAAEG-EGEVCVK-- 511
Cdd:cd05923 277 ATMPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaa 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622942221 512 GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:cd05923 354 ADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIG 430
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
228-574 |
1.13e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 99.30 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 228 DAYGSELVERGqkcgveiISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENS 307
Cdd:PRK07768 119 LAAAPVLEEKG-------IRVLTVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 308 VNpcpDDTLISFLPLAH-MfervvecvmlchgAKIGFFQGDIRLLMDDLKVlQPTVFPVVPRLLNRMFDRIFGQ------ 380
Cdd:PRK07768 192 VE---TDVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELISKYRGTmtaapn 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 381 -ANTTLKRwLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLggkvRLMVTGAAPVS-ATVLTFLRA---------A 449
Cdd:PRK07768 255 fAYALLAR-RLRRQAKPGAFDL--------------------SSL----RFALNGAEPIDpADVEDLLDAgarfglrpeA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 450 LGCqfyeGYGQTECTAGCCLSMPGD--------------------WTAGHV------GAPMPCNLIKLVDvEEMNYMAAE 503
Cdd:PRK07768 310 ILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPR 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622942221 504 GEGEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 574
Cdd:PRK07768 385 GVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
268-640 |
1.47e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 96.56 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 268 EDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNpcpDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGD 347
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVV---GDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 348 IRL--LMDDLKVLQPTVFPVVPRLLNRMfdrifgqanttlkrwLLDFASKRKEAElrsgiirnnslwdrlifhkvqsslg 425
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKL---------------VSELKSANATVP------------------------- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 426 gKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWT-AGHVGAPMPCNLIKLVDVEEMNYMAAeG 504
Cdd:cd17635 118 -SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 505 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY-----IR 579
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERIAegvsgVQ 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942221 580 SEAIAQVF--VHGESLQAFLIAIVVPDVETLRpwAQKRGFDGSFEELCRNKDVKkaILEDMVR 640
Cdd:cd17635 274 ECACYEISdeEFGELVGLAVVASAELDENAIR--ALKHTIRRELEPYARPSTIV--IVTDIPR 332
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
119-609 |
1.87e-21 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 98.85 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 119 EWLSYKQVAEMSECLGSALIQKGFTATPdqfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVtyivnkAELSLV 198
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVGKPGDR---VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHA------ERLAAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 199 FVDKpeKAKLLLegvenkLTPSLKIIVLMDAYGSELVERGQKCGVEIIslkameDLGRANRRKPKPPAPEDLAVVCFTSG 278
Cdd:cd05931 94 LADA--GPRVVL------TTAAALAAVRAFAASRPAAGTPRLLVVDLL------PDTSAADWPPPSPDPDDIAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 279 TTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAH-MfervvecvmlchgakiGFFQGdirllmddlkV 357
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLD----PGDVVVSWLPLYHdM----------------GLIGG----------L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 358 LQPTV--FPVV---PR-LLNRMFdrifgqanttlkRWL-----------------LDFASKRKEAELRSGIirnnslwdR 414
Cdd:cd05931 210 LTPLYsgGPSVlmsPAaFLRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL--------D 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 415 LifhkvqsslgGKVRLMVTGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT----------AGCCLSMPGDWTAG 478
Cdd:cd05931 270 L----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDALAG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 479 HV----------------GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE------ALDKDGWL 536
Cdd:cd05931 340 RAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEGGWL 419
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942221 537 HTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIeniyirsEAIAQVfVHGESLQAFLIAIVVPDVETLR 609
Cdd:cd05931 420 RTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDI-------EATAEE-AHPALRPGCVAAFSVPDDGEER 482
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-606 |
1.92e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 98.49 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 112 RKPDQPYEW-----LSYKQVAEMSECLGSAL-----IQKGftatpDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTL 181
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLqqecgVRKG-----DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 182 GNEAVTYIVNKAELSLVFVdkpekAKLLLEGVEnKLTPSLKI-IVLMDAYGSELVERGQ-----KCGVEIiSLKAMEDLG 255
Cdd:PRK08314 96 REEELAHYVTDSGARVAIV-----GSELAPKVA-PAVGNLRLrHVIVAQYSDYLPAEPEiavpaWLRAEP-PLQALAPGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 256 -------RANRRKPKP--PAPEDLAVVCFTSGTTGNPKGALITHRNIVsdCSAFVKATENSVNPcpDDTLISFLPLAHmf 326
Cdd:PRK08314 169 vvawkeaLAAGLAPPPhtAGPDDLAVLPYTSGTTGVPKGCMHTHRTVM--ANAVGSVLWSNSTP--ESVVLAVLPLFH-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 327 erVVECVMLCHGAkigFFQGDIRLLMddlkvlqptvfpvvPR----LLNRMFDR---IFGQANTTLkrwLLDFaskrkea 399
Cdd:PRK08314 243 --VTGMVHSMNAP---IYAGATVVLM--------------PRwdreAAARLIERyrvTHWTNIPTM---VVDF------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 400 eLRSGIIRNNSLwdrlifhkvqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG-----------CC 468
Cdd:PRK08314 294 -LASPGLAERDL----------SSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpklQC 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 469 LSMPgdwTAGhVGApmpcnliKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA---LDKDGWLHTGDIGKWL 545
Cdd:PRK08314 359 LGIP---TFG-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMD 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942221 546 PNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSEAIAQVFV-------HGESLQAFliaiVVPDVE 606
Cdd:PRK08314 428 EEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
268-599 |
2.86e-21 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 97.15 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 268 EDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKateNSVNPCPDDTLISflpLAHMFErvveCVMLCHGAKIGFFQGD 347
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 348 IRLLMDD----------LKVLQPTVFPVVPRLlnrmfdrifgqanttlkrwlldFASKRKEAELRSGIIRNnslwdrlif 417
Cdd:cd05919 161 SAVLNPGwptaervlatLARFRPTVLYGVPTF----------------------YANLLDSCAGSPDALRS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 418 hkvqsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEM 497
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 577
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*....
gi 1622942221 578 IRSEAIAQVFV------HGES-LQAFLIA 599
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
264-615 |
3.33e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 98.19 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 264 PPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATensVNPCPDDTLISFLPlahMFervvecvmlchgakigF 343
Cdd:PRK06178 205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVA---VVGGEDSVFLSFLP---EF----------------W 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 344 FQGDirllmdDLKVLQPTVF--PVVprLLNRmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnslWDRLIF---- 417
Cdd:PRK06178 263 IAGE------NFGLLFPLFSgaTLV--LLAR---------------------------------------WDAVAFmaav 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 418 --HKVQSSLG---GKVRLMVTGAapVSATVLTFL--------------------RAALGCQFYEG-YGQTEcTAGCclsm 471
Cdd:PRK06178 296 erYRVTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdyrqrwRALTGSVLAEAaWGMTE-THTC---- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 472 pGDWTAG-------------HVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHT 538
Cdd:PRK06178 369 -DTFTAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 539 GDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFVHG---ESLQAFLIAIVVP------DVETLR 609
Cdd:PRK06178 447 GDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAVVGrpdPDKGQVPVAFVQLkpgadlTAAALQ 525
|
....*.
gi 1622942221 610 PWAQKR 615
Cdd:PRK06178 526 AWCREN 531
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
213-696 |
4.12e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 97.56 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 213 VENKLTPSLKIIVLMDAYGSELvergqkcGVEIISLKAMEDLGRANRRKPKPP---APEDLAVVCFTSGTTGNPKGALIT 289
Cdd:PLN02860 121 LQNDRLPSLMWQVFLESPSSSV-------FIFLNSFLTTEMLKQRALGTTELDyawAPDDAVLICFTSGTTGRPKGVTIS 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 290 HRNIVSDCSAFVKAtensVNPCPDDTLISFLPLAHM--FERVVECVML--CHGAKIGFfqgDIRLLMDDLKVLQPTVFPV 365
Cdd:PLN02860 194 HSALIVQSLAKIAI----VGYGEDDVYLHTAPLCHIggLSSALAMLMVgaCHVLLPKF---DAKAALQAIKQHNVTSMIT 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 366 VPRLL------NRMfdRIFGQANTTLKRWLldfaskrkeaelrSGiirNNSLWDRLIfhKVQSSLGGKVRLMVTGAAPVS 439
Cdd:PLN02860 267 VPAMMadlislTRK--SMTWKVFPSVRKIL-------------NG---GGSLSSRLL--PDAKKLFPNAKLFSAYGMTEA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 440 ATVLTFLRaaLGCQFYEGYGQTECTAGCCLSMPGDWTAGH-VGAPMPcnliklvDVEEMNYM-AAEGEGEVCVKGPNVFQ 517
Cdd:PLN02860 327 CSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP-------HVELKIGLdESSRVGRILTRGPHVML 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 518 GYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRSEAIAQVFVHGeSLQAFL 597
Cdd:PLN02860 398 GYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEVEAVLSQHPGVASVVVVG-VPDSRL 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 598 IAIVVPDVETLRPWaqkRGFDGSFEELCRNKDVKKAILEDMVRLGKDSGLKPfeqvkgialhPELFSI--DNGLLTPTMK 675
Cdd:PLN02860 476 TEMVVACVRLRDGW---IWSDNEKENAKKNLTLSSETLRHHCREKNLSRFKI----------PKLFVQwrKPFPLTTTGK 542
|
490 500
....*....|....*....|.
gi 1622942221 676 AKRPELRNYFRSQIDELYSTI 696
Cdd:PLN02860 543 IRRDEVRREVLSHLQSLPSNL 563
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-628 |
7.10e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 96.88 E-value: 7.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLL--PGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKpekaklllEGVENKLTPSLKIIVLMDAYGSElveRGQKCGVEIIslkameDLGRANRRKPKPPAPEDL----AVVCFT 276
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGD---SGPSGGTLSV------HLDAATEPTPATSTPEGLrpddAMIMFT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 SGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMFERVVECV-MLCHGAKI-----GFFQGdiRL 350
Cdd:PRK05852 185 GGTTGLPKMVPWTHANIASSVRAIITGYRLS----PRDATVAVMPLYHGHGLIAALLaTLASGGAVllparGRFSA--HT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 351 LMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFA----SKRKEAELRsgIIRNNSlwdrlifhkvqsslgg 426
Cdd:PRK05852 259 FWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKPAALR--FIRSCS---------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 427 kvrlmvtgaAPVSATVLTFLRAALGCQFYEGYGQTECT---------AGCCLSMPGDWT--AGHVGAPMpcnlIKLVDVE 495
Cdd:PRK05852 305 ---------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqieGIGQTENPVVSTglVGRSTGAQ----IRIVGSD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 496 EMNYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 575
Cdd:PRK05852 372 GLPLPAGA-VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERVEG 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622942221 576 IYIRSEAIAQVFVHGESLQAF---LIAIVVPDvETLRPWAQKrgfdgsFEELCRNK 628
Cdd:PRK05852 449 VLASHPNVMEAAVFGVPDQLYgeaVAAVIVPR-ESAPPTAEE------LVQFCRER 497
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
250-610 |
1.15e-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: 95.98 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 250 AMEDLGRANRRKPKP-PAPEDLAVVCFTSGTTGNPKgaLI--THRNIVsdCSAfvkatENSVNPC---PDDTLISFLPLA 323
Cdd:COG1021 165 SLDALLAAPADLSEPrPDPDDVAFFQLSGGTTGLPK--LIprTHDDYL--YSV-----RASAEICgldADTVYLAALPAA 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 324 HMFervvecVMLCHGAkIGFFQ--GDIRL-----------LMDDLKVlqpTVFPVVPRLLNRMfdrifgqanttlkrwlL 390
Cdd:COG1021 236 HNF------PLSSPGV-LGVLYagGTVVLapdpspdtafpLIERERV---TVTALVPPLALLW----------------L 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 391 DFASKRKeAELrsgiirnnslwdrlifhkvqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE----CTAg 466
Cdd:COG1021 290 DAAERSR-YDL--------------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEglvnYTR- 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 467 ccLSMPGDWTAGHVGAPM-PCNLIKLVDVEEMNymAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKW 544
Cdd:COG1021 344 --LDDPEEVILTTQGRPIsPDDEVRIVDEDGNP--VPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRR 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942221 545 LPNGTLKIIDRKK-HIFKlaQGEYIAPEKIENIYIRSEAIAQVFV-------HGESLQAFliaiVVPDVETLRP 610
Cdd:COG1021 420 TPDGYLVVEGRAKdQINR--GGEKIAAEEVENLLLAHPAVHDAAVvampdeyLGERSCAF----VVPRGEPLTL 487
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
121-609 |
2.33e-20 |
|
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: 94.72 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVfv 200
Cdd:cd17651 21 LTYAELDRRANRLAHRLRARG--VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 dkpekakLLLEGVENKLTPSLKIIVLMDAYGSElvergqkcgveiislkameDLGRANRRKPkpPAPEDLAVVCFTSGTT 280
Cdd:cd17651 97 -------LTHPALAGELAVELVAVTLLDQPGAA-------------------AGADAEPDPA--LDADDLAYVIYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKIGFFQGDIRllMDDlkvl 358
Cdd:cd17651 149 GRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATLVLPPEEVR--TDP---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 359 qptvfpvvprllnrmfdrifgqanTTLKRWLldfaskrkeAELR-SGIIRNNSLWDRLIFH-KVQSSLGGKVRLMVTGAA 436
Cdd:cd17651 217 ------------------------PALAAWL---------DEQRiSRVFLPTVALRALAEHgRPLGVRLAALRYLLTGGE 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 437 PVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLSMPGD---WTA-GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCV 510
Cdd:cd17651 264 QLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD-AALRPVPPGVPGELYI 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 511 KGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIA 584
Cdd:cd17651 343 GGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIELGEIEAALARHPGVR 421
|
490 500 510
....*....|....*....|....*....|....
gi 1622942221 585 QVFV-------HGESLQAFLI--AIVVPDVETLR 609
Cdd:cd17651 422 EAVVlaredrpGEKRLVAYVVgdPEAPVDAAELR 455
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-671 |
2.80e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 95.50 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 107 PCLGSRKPDQ-PYEWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---YDTLG 182
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLG--LDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 183 NE--AVTYIVNKAELSLVFVDKPEK-----AKLLLEGVEnkltpslKIIVLMDAYGS------ELVERGQKCGVEiislK 249
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVT-------VVHVTGPGEGIasiafaDLAATPPTAAVA----A 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 250 AMEDLGranrrkpkppaPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPCPDDTLiSFLPLAHMFerv 329
Cdd:PRK12582 213 AIAAIT-----------PDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSL-DWMPWNHTM--- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 330 vecvmlchGAKIGFfQGDIR----LLMDDLKVLqPTVFPVVPRLLNRMFDRIFGQANTTLKrwLLDFASKRKEAELRSgi 405
Cdd:PRK12582 278 --------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDALRRS-- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 406 irnnslwdrliFHKvqsslggKVRLMVTGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGCCLSMpgDWTA-- 477
Cdd:PRK12582 344 -----------FFK-------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAPTTTGT--HWDTer 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 478 -GHVGAPMPCNLIKLVDVEEmNYmaaegegEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKI 552
Cdd:PRK12582 403 vGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 553 IDRKKHIFKLAQGEY--IAPEKIENIYIRSEAIAQVFVHGESlQAFLIAIVVPDVETLRPWAQKRgfDGSFEELCRNKDV 630
Cdd:PRK12582 475 DGRVAEDFKLSTGTWvsVGTLRPDAVAACSPVIHDAVVAGQD-RAFIGLLAWPNPAACRQLAGDP--DAAPEDVVKHPAV 551
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1622942221 631 KKAILEDMVRLGKDSGlKPFEQVKGIALHPELFSIDNGLLT 671
Cdd:PRK12582 552 LAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
112-610 |
1.23e-19 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 92.90 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 112 RKPDQPY-----EWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAV 186
Cdd:PRK06155 33 RYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVK--RGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 187 TYIVNKAELSLVFVDkpekAKLL--LEGVENKLTPsLKIIVLMDAYGSELVERGqkcgVEIISLKAMedlgrANRRKPKP 264
Cdd:PRK06155 111 EHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAG----WSTAPLPPL-----DAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 265 PAPEDLAVVCFTSGTTGNPKGALITH-------RNIVSDcsafvkatensVNPCPDDTLISFLPLAH-----MFERVvec 332
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAED-----------LEIGADDVLYTTLPLFHtnalnAFFQA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 333 vmLCHGAKI---------GFFqgdirllmDDLKVLQPTVF----PVVPRLLnrmfdrifgqanttlkrwlldfaSKRKEA 399
Cdd:PRK06155 243 --LLAGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL-----------------------SQPARE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 400 ELRSgiirnnslwdrlifHKVQSSLGGKVrlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDwTAGH 479
Cdd:PRK06155 290 SDRA--------------HRVRVALGPGV----------PAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 480 VGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKG--PNVF-QGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK 556
Cdd:PRK06155 345 MGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRI 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 557 KHIFKlAQGEYIAPEKIENIYIRSEAIAQVFVH------GESlqAFLIAIVVPDVETLRP 610
Cdd:PRK06155 423 KDAIR-RRGENISSFEVEQVLLSHPAVAAAAVFpvpselGED--EVMAAVVLRDGTALEP 479
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
173-610 |
3.74e-19 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 91.28 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 173 VIVPLYDTLGNEAVTYIVNKAELSLVFVDkpEKAKLLLEGVENKLTPSLKIIVLMDAYGSElvERGqkcgveIISLKAME 252
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTS--AQFYPMYRQIQQEDATPLRHICLTRVALPA--DDG------VSSFTQLK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 253 DLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSdcSAFVKATENSVNPcpDDTLISFLPLAHM-FERVVE 331
Cdd:PRK08008 158 AQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF--AGYYSAWQCALRD--DDVYLTVMPAFHIdCQCTAA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 332 CVMLCHGAKIGF--------FQGDIRLLmddlkvlQPTVFPVVPRLLNRM-------FDRifgqaNTTLKRWL--LDFAS 394
Cdd:PRK08008 234 MAAFSAGATFVLlekysaraFWGQVCKY-------RATITECIPMMIRTLmvqppsaNDR-----QHCLREVMfyLNLSD 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 395 KRKEA-ELRSGiirnnslwdrlifhkvqsslggkVRLMVTgaapvsatvltflraalgcqfyegYGQTECTAGCCLSMPG 473
Cdd:PRK08008 302 QEKDAfEERFG-----------------------VRLLTS------------------------YGMTETIVGIIGDRPG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 474 D---WTAghVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKG---PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 546
Cdd:PRK08008 335 DkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDE 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622942221 547 NGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSEAIAQVFVHG-------ESLQAFliaIVVPDVETLRP 610
Cdd:PRK08008 411 EGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGikdsirdEAIKAF---VVLNEGETLSE 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-605 |
9.25e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 91.76 E-value: 9.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAVTYIVNKAELS 196
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVgllaVLKAGGAY----VPLDPEYPQDRLAYMLDDSGVR 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 197 LVFVDkPEKAKLLLEGVenkltpslkiivlmdaygselvergqkcGVEIISLKAMEDL--GRANRRKPKPPAPEDLAVVC 274
Cdd:PRK12467 612 LLLTQ-SHLLAQLPVPA----------------------------GLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVI 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 275 FTSGTTGNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqgdirLLMDD 354
Cdd:PRK12467 663 YTSGSTGQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPP 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 355 LKVLQPTVFpvvprllnrmFDRIFGQANTTLKrwlldfaskrkeaelrsgiiRNNSLWDRLIFHKVQSSLGGKVRLMVTG 434
Cdd:PRK12467 731 DCARDAEAF----------AALMADQGVTVLK--------------------IVPSHLQALLQASRVALPRPQRALVCGG 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 435 AA-PVSATVLTFlRAALGCQFYEGYGQTECTAGC----CLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVC 509
Cdd:PRK12467 781 EAlQVDLLARVR-ALGPGARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELY 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 510 VKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEA 582
Cdd:PRK12467 859 IGGAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPG 937
|
490 500
....*....|....*....|....*
gi 1622942221 583 IAQVFV--HGESLQAFLIAIVVPDV 605
Cdd:PRK12467 938 VREAVVlaQPGDAGLQLVAYLVPAA 962
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-585 |
3.33e-18 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 89.00 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 259 RRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVsdcsAFVKATENSVNPCPDDTLISFLPLAHMFervvecvmlchG 338
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALPLFHSF-----------G 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 339 AKIGFFQGdirlLMDDLKVL---QPTVFPVVPRLLnrmFDR----IFGQAnTTLKRWL-----LDFAskrkeaelrsgii 406
Cdd:PRK08043 421 LTVGLFTP----LLTGAEVFlypSPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 407 rnnslwdrlifhkvqsslggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPC 486
Cdd:PRK08043 480 --------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 487 NLIKLVDVEEMnymaaEGEGEVCVKGPNVFQGYLK--DP-------AKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:PRK08043 540 MDARLLSVPGI-----EQGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAK 614
|
330 340
....*....|....*....|....*...
gi 1622942221 558 HIFKLAqGEYIAPEKIENIYIRSEAIAQ 585
Cdd:PRK08043 615 RFAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
122-588 |
1.22e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 86.54 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 122 SYKQVAEMSECLGSAL----IQKGFTatpdqfIGIFAQNRPEWViieQGCFAYSM---VIVPLYDTLGNEAVTYIVNKAE 194
Cdd:PRK08162 45 TWAETYARCRRLASALarrgIGRGDT------VAVLLPNIPAMV---EAHFGVPMagaVLNTLNTRLDAASIAFMLRHGE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 195 LSLVFVDkPEKAKLLLEGVEnkLTPSLKIIVL---MDAYGselveRGQKCG-VEIISLKAMEDLGRAnrrkPKPPAPE-D 269
Cdd:PRK08162 116 AKVLIVD-TEFAEVAREALA--LLPGPKPLVIdvdDPEYP-----GGRFIGaLDYEAFLASGDPDFA----WTLPADEwD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 270 LAVVCFTSGTTGNPKGALITHRnivsdcSAFVKATEN--SVNPCPDDTLISFLPLAHmfervveCVMLCH--------GA 339
Cdd:PRK08162 184 AIALNYTSGTTGNPKGVVYHHR------GAYLNALSNilAWGMPKHPVYLWTLPMFH-------CNGWCFpwtvaaraGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 340 KIGFFQGDIRLLMDDLKVLQPTVF---PVVPRLLnrmfdrifgqANTtlkrwlldfaskrkEAELRSGIirnnslwdrli 416
Cdd:PRK08162 251 NVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEWRAGI----------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 417 fhkvqsslGGKVRLMVTGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLSMPGdWTA----------GHVGAPM 484
Cdd:PRK08162 296 --------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAlplderaqlkARQGVRY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 485 PC-NLIKLVDVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFk 561
Cdd:PRK08162 365 PLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII- 442
|
490 500
....*....|....*....|....*..
gi 1622942221 562 LAQGEYIAPEKIENIYIRSEAIAQVFV 588
Cdd:PRK08162 443 ISGGENISSIEVEDVLYRHPAVLVAAV 469
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-617 |
1.28e-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: 86.21 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVsdcsAFVKATENSVNPCPDDTLISFLPLAHMFErVVEcvM---LCHGAKIGF 343
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWE--IwgaLLHGGRLVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 344 FQGDIRLLMDDLkvlqptvfpvvPRLLNRMFDRIFGQANTTLKRWLldfaskrkEAELRsgiirnnslwdrliFHKVQSS 423
Cdd:cd17643 165 VPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 424 LggkvRLMVTGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCL-----SMPGDWTAGHVGAPMPCNLIKLVDvE 495
Cdd:cd17643 212 L----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaADLPAAAASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622942221 569 APEKIENIYIRSEAIAQVFV---HGESLQAFLIAIVVPDVETLRPWAQKRGF 617
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGAAADIAELRAL 417
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
173-590 |
1.76e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 86.09 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 173 VIVPLYDTLGNEAVTYIVNKAELSLVFVDKPEKAKLLLEGvenkltpslKIIVLmDAYGSELVERGQKCGVEIISLKame 252
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDAGAKLLLVDEEFDAIVALET---------PKIVI-DAAAQADSRRLAQGGLEIPPQA--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 253 dlgranrrkpkPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVnpcpDDTLISFLPLAHmferVVEC 332
Cdd:PRK06145 145 -----------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTA----SERLLVVGPLYH----VGAF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 333 -----VMLCHGAKIGFFQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASKRkeaelrsgii 406
Cdd:PRK06145 206 dlpgiAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLA---------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 407 rnnslWdrlifhkvqsSLGGkvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDW--TAGHVGAPM 484
Cdd:PRK06145 268 -----W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRAL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 485 PCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 564
Cdd:PRK06145 326 AHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISG 402
|
410 420
....*....|....*....|....*.
gi 1622942221 565 GEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:PRK06145 403 GENIASSEVERVIYELPEVAEAAVIG 428
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-617 |
3.56e-17 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 84.83 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPcpddtlISFLPLAHMFERVVE---CVMLCHGAKIGF 343
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASFSFDVFAgdfARSLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 344 FQGDIRL----LMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKE--AELRSGIIRNNSLWDRLiF 417
Cdd:cd17650 166 CPDEVKLdpaaLYDLILKSRITLMESTP----------------ALIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD-F 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 418 HKVQSSLGGKVRLmvtgaapVSATVLTflRAALGCQFYEGYGQTECTAGcclSMPgdwtaghVGAPMPCNLIKLVDvEEM 497
Cdd:cd17650 229 KTLAARFGQGMRI-------INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 571
Cdd:cd17650 289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELG 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1622942221 572 KIENIYIRSEAIAQVFV---HGESLQAFLIAIVVPDvETLRpWAQKRGF 617
Cdd:cd17650 368 EIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAA-ATLN-TAELRAF 414
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
266-615 |
4.03e-17 |
|
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: 84.34 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigf 343
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT----PGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 344 fqgdiRLLMDDLKVLQPtvfpvvPRLLNRMFDR----IFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhk 419
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADR------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 420 VQSSLGGKVRLMVTGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLSMPGDWTAGH---VGAPMPCNLIKLV 492
Cdd:cd17649 206 TGDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 493 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 565
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 566 EYIAPEKIENIYIRSEAIAQVFVHGES--LQAFLIAIVVP--------DVETLRPWAQKR 615
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLraaaaqpeLRAQLRTALRAS 420
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-615 |
5.25e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 84.79 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 dKPEKAKL----LLEGVENKLTPSLKIIVLMDAYGSELVERGQKCGVEIISLKAMEDLGRAnrrkPKPPAPEDLAVVCFT 276
Cdd:PRK06164 114 -WPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 -SGTTGNPK------GALITHRNIVSDCSAFVkatensvnpcPDDTLISFLPLahmfervveCVMLCHGAKIGFFQGDIR 349
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGYD----------PGAVLLAALPF---------CGVFGFSTLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 350 LLMDDlkvlqptVF--PVVPRLL-----------NRMFDRIFGQANTTLkrwllDFASKRkeaelrsgiirnnslwdRLI 416
Cdd:PRK06164 250 LVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----------------LFG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 417 FHKVQSSLGGKVRLMVTGAAPvsatvLTFLraalgcqfyegYGQTECTA-GCCLSMPGDWTAGHV--GAPM-PCNLIKLV 492
Cdd:PRK06164 301 FASFAPALGELAALARARGVP-----LTGL-----------YGSSEVQAlVALQPATDPVSVRIEggGRPAsPEARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 493 DVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 572
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAE 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1622942221 573 IENIYIRSEAIAQVFVHGESLQ------AFLIAI--VVPDVETLRPWAQKR 615
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
267-583 |
5.71e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 84.46 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVnpcpDDTLISFLPLAHMFErvvecVMLCHGAKIgfFQG 346
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKT----KDRILSWMPLTHDMG-----LIAFHLAPL--IAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 347 DIRLLMddlkvlqPT-VFPVVPRLlnrmfdrifgqanttlkrWLLDfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLG 425
Cdd:cd05908 174 MNQYLM-------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 426 GKVRLMVTGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCCLSMPGD------------------------- 474
Cdd:cd05908 228 SSIRMILNGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLPKAQSpfktitlgrrhvthgepepevdkkd 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 475 ---WTAGHVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTL 550
Cdd:cd05908 308 secLTFVEVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRL 384
|
330 340 350
....*....|....*....|....*....|...
gi 1622942221 551 KIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAI 583
Cdd:cd05908 385 VITGREKDII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
119-590 |
6.36e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 84.45 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 119 EWLSYKQVAEMSECLGSALiQKGFTATPDQFIGIFAQNRPEW--VIIEQGCFAysMVIVPLYDTLGNEAVTYIVNKAELS 196
Cdd:PRK05620 37 EQTTFAAIGARAAALAHAL-HDELGITGDQRVGSMMYNCAEHleVLFAVACMG--AVFNPLNKQLMNDQIVHIINHAEDE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 197 LVFVDkPEKAKLLLEGVENklTPSLKIIVLMDAYGSELVERGQKCGVEIISLKAMEDlGRANRRkPKPPAPEDLAV-VCF 275
Cdd:PRK05620 114 VIVAD-PRLAEQLGEILKE--CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDETTAAaICY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 276 TSGTTGNPKGALITHRNIVSDCSAFvkATENSVNPCPDDTLISFLPLAHmfervvecvMLCHGAKIGFFQGDIRLLMDDL 355
Cdd:PRK05620 189 STGTTGAPKGVVYSHRSLYLQSLSL--RTTDSLAVTHGESFLCCVPIYH---------VLSWGVPLAAFMSGTPLVFPGP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 356 KVLQPTVFPVVprllnrmfdrifgqaNTTLKRwlldfaskrkeaeLRSGIirnNSLWDRLIFHKVQS-----SLggkvRL 430
Cdd:PRK05620 258 DLSAPTLAKII---------------ATAMPR-------------VAHGV---PTLWIQLMVHYLKNppermSL----QE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 431 MVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAP-------MPCNLIKLVdVEEMNYMAA- 502
Cdd:PRK05620 303 IYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWAyrvsqgrFPASLEYRI-VNDGQVMESt 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 503 -EGEGEVCVKGPNVFQGYLKDPAKT----------------AEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQG 565
Cdd:PRK05620 382 dRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGG 460
|
490 500
....*....|....*....|....*
gi 1622942221 566 EYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:PRK05620 461 EWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-604 |
6.51e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 84.24 E-value: 6.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAG--VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKPekakllleGVENKLTPSLKIIVLMDAygselvergqkcgveiislkamedLGRANRRKPKPPAPEDLAVVCFTSGTT 280
Cdd:cd12114 91 DGP--------DAQLDVAVFDVLILDLDA------------------------LAAPAPPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAH------MFErvvecvMLCHGAKIGFFQGDIR----L 350
Cdd:cd12114 139 GTPKGVMISHRAALNTILDINRRFAVG----PDDRVLALSSLSFdlsvydIFG------ALSAGATLVLPDEARRrdpaH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 351 LMDDLKVLQPTVFPVVPRLLNrMfdrifgqanttlkrwLLDfaskrkeaELRSGIIRNNSLwdRLIFHK---VQSSLGGK 427
Cdd:cd12114 209 WAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL--RLVLLSgdwIPLDLPAR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 428 VRLMVTGAAPVSatvltflraaLGcqfyegyGQTEctaGCCLS-------MPGDWTAGHVGAPMPCNLIKLVDveemnym 500
Cdd:cd12114 263 LRALAPDARLIS----------LG-------GATE---ASIWSiyhpideVPPDWRSIPYGRPLANQRYRVLD------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 501 aAEGE-------GEVCVKGPNVFQGYLKDPAKTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 569
Cdd:cd12114 316 -PRGRdcpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIE 393
|
490 500 510
....*....|....*....|....*....|....*..
gi 1622942221 570 PEKIENIYIRSEAIAQ--VFVHGESLQAFLIAIVVPD 604
Cdd:cd12114 394 LGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-615 |
1.28e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 82.75 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DkpekaklllegvenkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkppaPEDLAVVCFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVsdcsAFVKATENSvnpCPDD--------TLISF-LPLAHMFervvecVMLCHGAKIgffqgdirll 351
Cdd:cd12115 118 GRPKGVAIEHRNAA----AFLQWAAAA---FSAEelagvlasTSICFdLSVFELF------GPLATGGKV---------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 352 mddlkVLQPTVFPvvprllnrmfdrifgqanttlkrwLLDFASkRKEAELrsgIIRNNSLWDRLIFHkvqSSLGGKVRLM 431
Cdd:cd12115 175 -----VLADNVLA------------------------LPDLPA-AAEVTL---INTVPSAAAELLRH---DALPASVRVV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 432 VTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 508
Cdd:cd12115 219 NLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGEL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 509 CVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEA 582
Cdd:cd12115 298 YIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPG 376
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622942221 583 IAQ--VFVHGESL-QAFLIAIVVPD------VETLRPWAQKR 615
Cdd:cd12115 377 VREavVVAIGDAAgERRLVAYIVAEpgaaglVEDLRRHLGTR 418
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
267-615 |
1.34e-16 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 82.69 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKAtensVNPCPDDTLISFLPLAhmFERVV-ECVM-LCHGAkigff 344
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAA----FDVGPGSRVLQFASPS--FDASVwELLMaLLAGA----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 qgdiRLLMDDLKVLQPtvfpvvprllnrmfdrifGQAnttlkrwLLDFaskrkeaelrsgiirnnsLWDRLIFHKVQS-- 422
Cdd:cd17652 161 ----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPpa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 423 --------SLGGKVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAGCCLSMP-GDWTAGHVGAPMPCNLIKLVD 493
Cdd:cd17652 194 alaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 494 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:cd17652 271 -ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGF 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942221 567 YIAPEKIENIYIRSEAIAQ--VFVHGESL-QAFLIAIVV------PDVETLRPWAQKR 615
Cdd:cd17652 349 RIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVpapgaaPTAAELRAHLAER 406
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
269-599 |
1.70e-16 |
|
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: 82.76 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKgaLI--THRnivsDCSAFVKAtenSVNPC---PDDTLISFLPLAHMFerVVEC-----VMLChG 338
Cdd:cd05920 140 EVALFLLSGGTTGTPK--LIprTHN----DYAYNVRA---SAEVCgldQDTVYLAVLPAAHNF--PLACpgvlgTLLA-G 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 339 AKIGFFQ----GDIRLLMDDLKVlqpTVFPVVPRLLnrmfdrifgqanttlKRWLlDFASKRKEAElrsgiirnnslwdr 414
Cdd:cd05920 208 GRVVLAPdpspDAAFPLIEREGV---TVTALVPALV---------------SLWL-DAAASRRADL-------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 415 lifhkvqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE----CTAgccLSMPGDWTAGHVGAPM-PCNLI 489
Cdd:cd05920 255 -------SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 490 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 569
Cdd:cd05920 321 RVVD-EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIA 398
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622942221 570 PEKIENIYIRSEAIAQVFV-------HGESLQAFLIA 599
Cdd:cd05920 399 AEEVENLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
427-590 |
1.95e-16 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 82.93 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 427 KVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLSMPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMAAEgE 505
Cdd:cd05970 302 SLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-E 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 506 GEVCV---KGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYIRS 580
Cdd:cd05970 380 GEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQH 457
|
170
....*....|
gi 1622942221 581 EAIAQVFVHG 590
Cdd:cd05970 458 PAVLECAVTG 467
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
421-603 |
5.18e-16 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 81.60 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 QSSLGGKVRLMVTGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCLSMPGD-WT------AGHVGAPMPCNLIKLVD 493
Cdd:PLN03102 296 LSPRSGPVHVLTGGSPPPAALVKKVQR--LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLAD 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 494 VEEMNYMAAEGE-------GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 566
Cdd:PLN03102 374 VDVKNKETQESVprdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGE 451
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622942221 567 YIAPEKIENIyirseaiaqVFVHGESLQAFLIAIVVP 603
Cdd:PLN03102 452 NISSVEVENV---------LYKYPKVLETAVVAMPHP 479
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-604 |
6.40e-16 |
|
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: 81.17 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKPEKAKLLLEGVenkltpslkiivlmdaygselvergqkcgveIISLKAMEDLGRANRRKPKPPAPEDLAVVCFTSGTT 280
Cdd:cd17646 102 TADLAARLPAGGD-------------------------------VALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSD----CSAFVKATENSV---NPCPDDTLIS--FLPLAHMfERVVECVMLCHGaKIGFFQGdirlL 351
Cdd:cd17646 151 GRPKGVMVTHAGIVNRllwmQDEYPLGPGDRVlqkTPLSFDVSVWelFWPLVAG-ARLVVARPGGHR-DPAYLAA----L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 352 MDDLKVlqpTVFPVVPRLLnrmfdRIFGQanttlkrwlldfaskrkeaELRSGIIRNnslwdrlifhkvqsslggkVRLM 431
Cdd:cd17646 225 IREHGV---TTCHFVPSML-----RVFLA-------------------EPAAGSCAS-------------------LRRV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 432 VTGAAPVSATVLTFLRAALGCQFYEGYGQTEC----TAGCClsmPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGE 505
Cdd:cd17646 259 FCSGEALPPELAARFLALPGAELHNLYGPTEAaidvTHWPV---RGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVP 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 506 GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIR 579
Cdd:cd17646 335 GELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAA 413
|
490 500
....*....|....*....|....*...
gi 1622942221 580 SEAIAQVFV---HGESLQAFLIAIVVPD 604
Cdd:cd17646 414 HPAVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
184-658 |
4.08e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 78.59 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 184 EAVTYIVNKAELSLVFVD---KPekaklLLEGVENKLtPSLKIIVLM-DAygselvergQKCGVEIISLKAMEDL-GRAN 258
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMtDA---------AHLPAGSTPLLCYETLvGAQD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 259 RRKPKPPAPEDLAV-VCFTSGTTGNPKGALITHRNIVsdCSAFVKATENSVNPCPDDTLisfLPLAHMFErvVECVMLCH 337
Cdd:PRK07008 166 GDYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 338 -----GAKIgffqgdirllmddlkvlqptVFPvvprllnrmfdrifGQAnttlkrwlLDFASKRK--EAELRSGIIRNNS 410
Cdd:PRK07008 239 sapltGAKL--------------------VLP--------------GPD--------LDGKSLYEliEAERVTFSAGVPT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 411 LWDRLIFHKVQSSLG-GKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE-------CT-AGCCLSMPGD------W 475
Cdd:PRK07008 277 VWLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEmsplgtlCKlKWKHSQLPLDeqrkllE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 476 TAGHV--GAPMpcnliKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDkDGWLHTGDIGKWLPNGTLK 551
Cdd:PRK07008 357 KQGRViyGVDM-----KIVG-DDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 552 IIDRKKHIFKlAQGEYIAPEKIENIyirseAIAQVFVHgeslQAFLIAIVVP--DVETLRPWAQKRGFDGSFEELCRNKD 629
Cdd:PRK07008 427 ITDRSKDVIK-SGGEWISSIDIENV-----AVAHPAVA----EAACIACAHPkwDERPLLVVVKRPGAEVTREELLAFYE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1622942221 630 VKKA---ILEDMVRL--------GKDSGLKPFEQVKGIAL 658
Cdd:PRK07008 497 GKVAkwwIPDDVVFVdaiphtatGKLQKLKLREQFRDYVL 536
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-614 |
8.93e-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: 77.21 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNpcpDDTLI--SFLPLAHMFErvvecvMLCH---GAKI 341
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPA---DKSLVyaSFSFDASAWE------IFPHltaGAAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 342 GFFQGDIRLLMDDLkvlqptvfpvvprllnrmfDRIFGQANTTLKRWLLDFASKRKEAElrsgiirNNSLwdrlifhkvq 421
Cdd:cd17645 174 HVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL---------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 sslggkvRLMVTGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLSMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMA 501
Cdd:cd17645 218 -------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 502 AEG-EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 574
Cdd:cd17645 284 PIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIE 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622942221 575 NIYIRSEAIAQVFV-------HGESLQAFLIAIVVPDVETLRPWAQK 614
Cdd:cd17645 363 PFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
224-607 |
9.95e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.41 E-value: 9.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 224 IVLMDAYGSELVErGQKCGVEIISLKAME--DLGRANRRKPKPPA---PEDLAVVCFTSGTTGNPKGALITHRNIVSDCS 298
Cdd:PRK07867 104 LVLTESAHAELLD-GLDPGVRVINVDSPAwaDELAAHRDAEPPFRvadPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 299 AFVKatenSVNPCPDDTLISFLPLAHMFERVVE-CVMLCHGAKI---------GFfqgdirllMDDLKVLQPTVFPVVPR 368
Cdd:PRK07867 183 MLAQ----RFGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 369 LLNrmfdrifgqanttlkrWLLDFASKRKEAElrsgiirnNSLwdRLIFhkvqsslGGKvrlmvtGAAPVSATvltfLRA 448
Cdd:PRK07867 251 PLS----------------YVLATPERPDDAD--------NPL--RIVY-------GNE------GAPGDIAR----FAR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 449 ALGCQFYEGYGQTEctAGCCLSMPGDWTAGHVGAPMPCnlIKLVDVE--------------EMNYMAAEGEgEVCVKGPN 514
Cdd:PRK07867 288 RFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGPG 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 515 VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFVHGeslq 594
Cdd:PRK07867 363 GFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA---- 436
|
410
....*....|...
gi 1622942221 595 afliaivVPDVET 607
Cdd:PRK07867 437 -------VPDPVV 442
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
121-608 |
1.62e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.89 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAVTYIVNKAELS 196
Cdd:PRK12467 1600 LTYGELNRRANRLAHRLIALG--VGPEVLVGIAVERSLEMVVgllaILKAGGAY----VPLDPEYPRERLAYMIEDSGIE 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 197 LVFVDKPEKAKL-LLEGVEnkltpslkiIVLMDAYGSELVERGqkcgveiislkaMEDLGRAnrrkpkpPAPEDLAVVCF 275
Cdd:PRK12467 1674 LLLTQSHLQARLpLPDGLR---------SLVLDQEDDWLEGYS------------DSNPAVN-------LAPQNLAYVIY 1725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 276 TSGTTGNPKGALITHRNIVsdcsAFVKATENSVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKIgffqgdirllmd 353
Cdd:PRK12467 1726 TSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARL------------ 1787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 354 dlkVLQPtvfPVVPRLLNRMFDRIFGQANTTlkrwlLDFASkrkeaelrsgiirnnSLWDRLIFHKVQSSLGGKVRLMVT 433
Cdd:PRK12467 1788 ---VIAP---PGAHRDPEQLIQLIERQQVTT-----LHFVP---------------SMLQQLLQMDEQVEHPLSLRRVVC 1841
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 434 G--AAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CCLSMPGDWTAGHVGAPMPcNLIKLVDVEEMNYMAAEGE 505
Cdd:PRK12467 1842 GgeALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIA-NLSTYILDASLNPVPIGVA 1918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 506 GEVCVKGPNVFQGYLKDPAKTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 578
Cdd:PRK12467 1919 GELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLR 1997
|
490 500 510
....*....|....*....|....*....|..
gi 1622942221 579 RSEAIAQ--VFVHGESLQAFLIAIVVPDVETL 608
Cdd:PRK12467 1998 EQGGVREavVIAQDGANGKQLVAYVVPTDPGL 2029
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-613 |
3.64e-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: 74.26 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 457 GYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGW 535
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942221 536 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSEAIAQVFVhgeslqafliaIVVPDVEtlrpWAQ 613
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERCLRQHPAVADAAV-----------IGVPDPR----WAQ 280
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-609 |
3.91e-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: 75.16 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAhmFERVVE--CVMLCHGAKIgff 344
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVN----LSHGLIKEYGITSSDRVLQFASIA--FDVAAEeiYVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 qgdirllmddlkVLQPtvfpvvprllNRMFdrifgqanttlkRWLLDFASKRKEAELRSGIIrNNSLWDRLIFHKVQSSL 424
Cdd:cd17644 176 ------------VLRP----------EEMR------------SSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 GG--KVRLMVTGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCCLSMPGDWTAGH-----VGAPMPCNLIKLVDvE 495
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622942221 568 IAPEKIENIYIRSEAIAQVFV---HGESLQAFLIAIVVP------DVETLR 609
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPhyeespSTVELR 429
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
410-609 |
4.51e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 74.91 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 410 SLWdRLIFHKVQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLI 489
Cdd:cd05974 185 TVW-RMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRV 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 490 KLVDVEEmnymAAEGEGEVCV-----KGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 564
Cdd:cd05974 264 ALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SS 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622942221 565 GEYIAPEKIENIYIRSEAIAQvfvhgeslqafliAIVVPDVETLR 609
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAE-------------AAVVPSPDPVR 369
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
242-615 |
4.97e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 4.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 242 GVEIISLKAMEDL-GRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVsdcsAFVKATENSVNPCPDDTLISFL 320
Cdd:PRK12316 4667 GLASLALDRDEDWeGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFM 4742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 321 PLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDLKVLQPtvfpvvprllNRMFDRIFGQANTTlkrwlLDFASkrke 398
Cdd:PRK12316 4743 SFS--FDGSHEGLYhpLINGA---------SVVIRDDSLWDP----------ERLYAEIHEHRVTV-----LVFPP---- 4792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 399 aelrsgiirnnSLWDRLIFHKVQSSLGGKVRLMVTG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLSMPGDW 475
Cdd:PRK12316 4793 -----------VYLQQLAEHAERDGEPPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGD 4860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 476 TAG----HVGAPMPCNLIKLVDVeEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKW 544
Cdd:PRK12316 4861 ACGaaymPIGTPLGNRSGYVLDG-QLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARY 4939
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942221 545 LPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFVHGE--SLQAFLIAIVVPDVETLRPWAQKR 615
Cdd:PRK12316 4940 RADGVIDYLGRVDHQVKI-RGFRIELGEIEARLREHPAVREAVVIAQegAVGKQLVGYVVPQDPALADADEAQ 5011
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-578 |
4.98e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 75.24 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKAtensVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQG 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 347 DIRLLMDDLkvlqPTVF---PVVPRLLNRMFDR----IFGQANTTLKrWLLDFASKRKEA--ELRSGIIRNNSLWDRLiF 417
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFD-YILKTAKKQESClpSLRFVVIGGDAFKDSL-Y 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 418 HKVQSslggkvrlmvtgaapvsatvlTFLRAALgcqfYEGYGQTECTA------------GCCLSMPgdwtaghvgapmp 485
Cdd:PRK06334 317 QEALK---------------------TFPHIQL----RQGYGTTECSPvitintvnspkhESCVGMP------------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 486 cnlIKLVDV----EEMNYMAAEGE-GEVCVKGPNVFQGYL-KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK06334 359 ---IRGMDVlivsEETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRF 435
|
330
....*....|....*....
gi 1622942221 560 FKLAqGEYIAPEKIENIYI 578
Cdd:PRK06334 436 VKIG-AEMVSLEALESILM 453
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
252-604 |
7.28e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 74.69 E-value: 7.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 252 EDLGRANRRKPKPPAPEDLAVVC---FTSGTTGNPKGALITHRNIvsdcsAFVKATENS-VNP--CPDDTLISFLPLAHM 325
Cdd:PRK07470 144 EALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQM-----AFVITNHLAdLMPgtTEQDASLVVAPLSHG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 326 fERVVECVMLCHGAKigffqgDIRLLMDDLKVlqPTVFPVVPRL-LNRMFdrifgQANTTLKRWLLDFASKRKEaelrsg 404
Cdd:PRK07470 219 -AGIHQLCQVARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD------ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 405 iirnnslwdrlifhkvQSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGC------CLSMPGDWTAG 478
Cdd:PRK07470 279 ----------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNitvlppALHDAEDGPDA 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 479 HVGapmPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKI 552
Cdd:PRK07470 338 RIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLYI 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622942221 553 IDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFVHGeslqafliaivVPD 604
Cdd:PRK07470 413 TGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD 452
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
432-598 |
7.70e-14 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 74.81 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 432 VTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVK 511
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 512 -GPN----VFQGYLKDPAKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQV 586
Cdd:cd05928 376 vKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170
....*....|....*....
gi 1622942221 587 FV-------HGESLQAFLI 598
Cdd:cd05928 454 AVvsspdpiRGEVVKAFVV 472
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
249-575 |
7.87e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 74.55 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 249 KAMEDLGRANRRKPKPPA---PEDLAVVCFTSGTTGNPKGALITHRNIVsdcsAFVKATENSVNPCPDDTLISFLPLahm 325
Cdd:PRK09274 152 TTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGIEPGEIDLPTFPL--- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 326 fervvecvMLCHGAKIGFfqGDIRLLMDDLKVLQptvfpVVPRllnRMFDRIFGQANTTLkrwlldFASKrkeaelrsgi 405
Cdd:PRK09274 225 --------FALFGPALGM--TSVIPDMDPTRPAT-----VDPA---KLFAAIERYGVTNL------FGSP---------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 406 irnnSLWDRLIFHKVQS--SLGGkVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC------TAGCCLSMPGDW 475
Cdd:PRK09274 271 ----ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpissiESREILFATRAA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 476 T---AGH-VGAPMPCNLIKLVDVEEM-------NYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEA--LDKDG--WLHTG 539
Cdd:PRK09274 346 TdngAGIcVGRPVDGVEVRIIAISDApipewddALRLATGEiGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGdvWHRMG 425
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622942221 540 DIGkWL-PNGTLKIIDRKKHIFKLAQGEY--IAPEKIEN 575
Cdd:PRK09274 426 DLG-YLdAQGRLWFCGRKAHRVETAGGTLytIPCERIFN 463
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
248-682 |
1.02e-13 |
|
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: 73.95 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 248 LKAMEDLGRANRRKPKPPAPEDLA--VVCFTSGTTGNPKGALITHrnivsdcsafvkatenSVNPCPDDTLISF-LPLAH 324
Cdd:cd05929 103 LDGLEDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGL----------------PGGPPDNDTLMAAaLGFGP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 325 MFERVVECVM-LCHGAKIGFFQGDIRL-----LM---DDLKVLQP------TVFPVVPRLLNRMfdrifgqanttLK--- 386
Cdd:cd05929 167 GADSVYLSPApLYHAAPFRWSMTALFMggtlvLMekfDPEEFLRLieryrvTFAQFVPTMFVRL-----------LKlpe 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 387 --RWLLDFASkrkeaeLRSgiirnnslwdrlIFHkvqsslggkvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECT 464
Cdd:cd05929 236 avRNAYDLSS------LKR------------VIH---------------AAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 465 AGCCLSmPGDWTA--GHVGAPMPCNLiKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDGWLHTGDIG 542
Cdd:cd05929 283 GLTIIN-GEEWLThpGSVGRAVLGKV-HILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 543 KWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFVHGeslqafliaivVPDVET-LRPWAQKRGFDGSf 621
Cdd:cd05929 359 YLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVG-----------VPDEELgQRVHAVVQPAPGA- 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622942221 622 eelcrnkDVKKAILEDMVRLGKDSgLKPFEQVKGIALHPELFSIDNGlltptmKAKRPELR 682
Cdd:cd05929 426 -------DAGTALAEELIAFLRDR-LSRYKCPRSIEFVAELPRDDTG------KLYRRLLR 472
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
266-603 |
2.28e-13 |
|
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: 72.90 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKateNSVNPCPDDTLISFLPLAHMFER-VVECVMLCHGAKIGFF 344
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 QGDI-RLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfASKRKEAELRSGiirnnslwdrlifhkvqss 423
Cdd:cd05958 172 EEATpDLLLSAIARYKPTVLFTAPTAYRAML------------------AHPDAAGPDLSS------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 424 lggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 503
Cdd:cd05958 215 ----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 504 GEGEVCVKGPNvfqGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYIRSEAI 583
Cdd:cd05958 290 TIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340
....*....|....*....|...
gi 1622942221 584 AQVFVHGESLQAFLI---AIVVP 603
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVL 388
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
264-606 |
3.37e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.21 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 264 PPAPEDLAVVCFTSGTTGNPKGALITHRNI------VSDCSAFvkaTENsvnpcpDDTLISfLPLAHmfervvecV---- 333
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQAHlasaegVLSLMPF---TAQ------DSWLLS-LPLFH--------Vsgqg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 334 ----MLCHGAKIGFfqGDIRLLMDDLkvLQPTVFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnn 409
Cdd:PRK09029 193 ivwrWLYAGATLVV--RDKQPLEQAL--AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 410 slwdrlifhkvqsslGGkvrlmvtGAAPVSatvLTFLRAALGCQFYEGYGQTECTAGCClSMPGDWTAGhVGAPMPCNLI 489
Cdd:PRK09029 248 ---------------GG-------AAIPVE---LTEQAEQQGIRCWCGYGLTEMASTVC-AKRADGLAG-VGSPLPGREV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 490 KLVDveemnymaaegeGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:PRK09029 301 KLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQ 365
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622942221 570 PEKIENIYIRSEAIAQVFVhgeslqafliaIVVPDVE 606
Cdd:PRK09029 366 PEEIERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-574 |
5.65e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 71.84 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL-YDTLGNEaVTYIVNKAELSLVF 199
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQG--LGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 200 VDK---PEKAKLLLEgvenklTPSLKIIVLMDAYGSELVERGqkcGVEIISLKAMEDLGRAnrrkPKPPAPEDLAVVCfT 276
Cdd:PRK07798 106 YERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-T 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 277 SGTTGNPKGALITHRNIVSdcSAFVKATENSVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK-----IGFFQGdirll 351
Cdd:PRK07798 172 GGTTGMPKGVMWRQEDIFR--VLLGGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSG----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 352 mddlkvlQPTVFPVVPRL-------------LNRMFdrIFGQAnttLKRWLLDFASKRKEAELrsgiirnnslwdrlifh 418
Cdd:PRK07798 245 -------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL----------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 419 kvqSSLggkvRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLSMPGDWTAGHVGAP--MPCNLIKLVDVE 495
Cdd:PRK07798 296 ---SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGPRTVVLDED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 572
Cdd:PRK07798 367 GNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEE 445
|
..
gi 1622942221 573 IE 574
Cdd:PRK07798 446 VE 447
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
428-628 |
1.17e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 71.03 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 428 VRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLSMPgDW------TAGHVGAPMPCNLIKL-----VD 493
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstVCAWKP-EWdslppeEQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 494 VEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 571
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942221 572 KIENIYIRSEAIAQVFV-------HGESLQAFLiaivvpdveTLRPWAQK---RGFDGSFEELCRNK 628
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV---------TLKPGVDKsdeAALAEDIMKFCRER 524
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
261-586 |
2.67e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 69.65 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 261 KPKPPAPEDLAVVcFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPCPDDTLISFLPLAHM--FERVVECVMlcHG 338
Cdd:PRK05857 163 NADQGSEDPLAMI-FTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIggLWWILTCLM--HG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 339 AKI---GFFQGDIRLLMDDLKVLQPTVfpvVPRLLNRMFdrifgqanttlkrwlldfaskrkeAELRSGIIRNNSLwdrl 415
Cdd:PRK05857 240 GLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPSL---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 416 ifhkvqsslggkvRLMVTGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCclsMPGD------WTAGHVGAPMPCN 487
Cdd:PRK05857 289 -------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALC---LPTDdgsivkIEAGAVGRPYPGV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 488 LIKLVDVEEMNYMAAEGE-----GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 562
Cdd:PRK05857 352 DVYLAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-I 429
|
330 340
....*....|....*....|....
gi 1622942221 563 AQGEYIAPEKIENIyirSEAIAQV 586
Cdd:PRK05857 430 CGGVNIAPDEVDRI---AEGVSGV 450
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-558 |
3.80e-12 |
|
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: 69.03 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 265 PAPEDLAVVCFTSGTTGNPKGALITHRNIVsdcsAFVKATENSVNPCPDDTLISFLPLAHMFervvecvmlchGAKIGff 344
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFA----AQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 qgdirllmddLKVLQPTVFPVVPrllnrmfdrifGQANttlKRWLLDFASKRKEaelrSGIIRNNSLWDRLIFHKVQSSL 424
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 G-GKVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LSMPGDWTAGH----VGAPMPCNLIKL 491
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622942221 492 VDVEEMNYMAAEGE--------GEVCVKGPNVFQGYLKDPAKTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:cd05910 277 IEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAH 355
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-604 |
5.51e-12 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 68.86 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 429 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE----------------CTAGCCLSmPGD--WTAGHVGAPMPcnlik 490
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEglvnytrlddsderifTTQGRPMS-PDDevWVADADGNPLP----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 491 lvdveemnymaaEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----G 565
Cdd:PRK10946 377 ------------QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgG 439
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622942221 566 EYIAPEKIENIYIRSEAIaqvfvhgesLQAFLIAIvvPD 604
Cdd:PRK10946 440 EKIAAEEIENLLLRHPAV---------IHAALVSM--ED 467
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-598 |
6.19e-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: 68.31 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTATpDQFIGIFAQNrPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPG-DVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKPEKAKLllegvenkltpslkiivlmdaygselvergqkcgveiislkamedlgranrrkpkppaPEDLAVVCFTSGTT 280
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVsdcsAFVKATENSVNPCPDDtliSFLPLAH------MFERVVECVMLCHGAKI---GFFQGDIRLL 351
Cdd:cd05973 101 GLPKGVPVPLRALA----AFGAYLRDAVDLRPED---SFWNAADpgwaygLYYAITGPLALGHPTILlegGFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 352 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkeaeLRSGIirnnslwdrlifhKVQSSLGGKVRLM 431
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLL------------------------------MAAGA-------------EVPARPKGRLRRV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 432 VTGAAPVSATVLTFLRAALGCQFYEGYGQTEctagccLSMP--GDWTAGHV------GAPMP---CNLIKLVDVEemnym 500
Cdd:cd05973 211 SSAGEPLTPEVIRWFDAALGVPIHDHYGQTE------LGMVlaNHHALEHPvhagsaGRAMPgwrVAVLDDDGDE----- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 501 AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 575
Cdd:cd05973 280 LGPGEpGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
490 500 510
....*....|....*....|....*....|
gi 1622942221 576 IYIRSEAIAQVFV-------HGESLQAFLI 598
Cdd:cd05973 355 ALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
184-590 |
1.37e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 67.47 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 184 EAVTYIVNKAELSLVFVDK---PekaklLLEGVENKLtPSLK-IIVLMDAygSELVERGQKcgveiiSLKAMED-LGRAN 258
Cdd:PRK06018 101 EQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVErYVVLTDA--AHMPQTTLK------NAVAYEEwIAEAD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 259 RRKPKPPAPEDLAV-VCFTSGTTGNPKGALITHRNIVsdCSAFVKATENSVNPCPDDTLISFLPLAH-------MFERVV 330
Cdd:PRK06018 167 GDFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHRSNV--LHALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAPSM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 331 ECVMLCHGAKIGffQGDIRLLMDDLKVlqpTVFPVVPrllnrmfdrifgqantTLKRWLLDF--ASKRKEAELRSGIIrn 408
Cdd:PRK06018 245 GTKLVMPGAKLD--GASVYELLDTEKV---TFTAGVP----------------TVWLMLLQYmeKEGLKLPHLKMVVC-- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 409 nslwdrlifhkvqsslGGkvrlmvtgaapvSATVLTFLRA--ALGCQFYEGYGQTECTAGCCLS--------MPGD---- 474
Cdd:PRK06018 302 ----------------GG------------SAMPRSMIKAfeDMGVEVRHAWGMTEMSPLGTLAalkppfskLPGDarld 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 475 WTAGHVGAPMPCNLiKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDKDGWLHTGDIGKWLPNGTLKI 552
Cdd:PRK06018 354 VLQKQGYPPFGVEM-KITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRI 428
|
410 420 430
....*....|....*....|....*....|....*...
gi 1622942221 553 IDRKKHIFKlAQGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:PRK06018 429 TDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-608 |
2.06e-11 |
|
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: 66.65 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpCPDDTLISFLPlAHMFERVVE--CVMLCHGAKIGFF 344
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGR---DNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 QGDIRL-------LMDDLKVlqpTVFPVVPRLLNRM-FDRIfgqanTTLKRWLL---DFASKRkeaelrsgiirnnslwd 413
Cdd:cd17648 169 PDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV----------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 414 rliFHKVQSSLGGkvrLMVTGAAPVSATVLTFLRaalgcqFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIklvd 493
Cdd:cd17648 224 ---FEKLRSRFAG---LIINAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 494 veemnymaaegeGEVCVKGPNVFQGYLKDPAKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd17648 288 ------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQ 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942221 560 FKLaQGEYIAPEKIENIYIRSEAIAQVFV--------HGESLQAFLIAIVVPDVETL 608
Cdd:cd17648 356 VKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
112-606 |
3.42e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 67.29 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 112 RKPDQPY-----EWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAV 186
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 187 TYIVNKAelslvfvdkpeKAKLLLEGVENKLTPSLKIIVLMdaygselVERGQkcgveiislkamEDLGRANrrKPKPPA 266
Cdd:PRK12316 3147 AYMLEDS-----------GAQLLLSQSHLRLPLAQGVQVLD-------LDRGD------------ENYAEAN--PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHrnivSDCSAFVKATENSVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqg 346
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRH----SALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV----- 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 347 dirllmddlkVLQPTVFPVVPRLLNRMFDRifGQANTTLKRWlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGG 426
Cdd:PRK12316 3266 ----------VLAGPEDWRDPALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTS 3312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 427 KVRLMVTGAAPVSATVltfLRAALGCQFYEGYGQTECTAGCCLSMPGDWTAGH--VGAPMPCNLIKLVDVeEMNYMAAEG 504
Cdd:PRK12316 3313 LKRIVCGGEALPADLQ---QQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGA 3388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 505 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYI 578
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLL 3467
|
490 500
....*....|....*....|....*...
gi 1622942221 579 RSEAIAQVFVHGESLQAfLIAIVVPDVE 606
Cdd:PRK12316 3468 EHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
422-606 |
6.68e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 65.31 E-value: 6.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 SSLggkvRLMVTGAAPVSATVLtflRAAL---GCQFYEGYGQTEcTAGCCLSMPGDWTA--GHVGAPMPCNlIKLVDvEE 496
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-ED 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK08276 332 GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
170 180 190
....*....|....*....|....*....|.
gi 1622942221 576 IYIRSEAIAQVFVHGeslqafliaivVPDVE 606
Cdd:PRK08276 410 LLVTHPKVADVAVFG-----------VPDEE 429
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-590 |
8.39e-11 |
|
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: 64.68 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 269 DLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMFERVVE-CVMLCHGAKIGF---F 344
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL----PSDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 QGdiRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfASKRKEAELRsgiirnnslwdrlifHKVQSSL 424
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 GGKVRLMVTGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGcCLSMPG-DWTAGHVGA----PMPCNLIKlVDVEEMN 498
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSG-FINFFGkPGAIGRNPSllrkVAPLALVK-YDLESGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 499 -------YMAAEGEGEV--CV-----KGPnvFQGYLkDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKH 558
Cdd:cd05940 271 pirdaegRCIKVPRGEPglLIsrinpLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
330 340 350
....*....|....*....|....*....|..
gi 1622942221 559 IFKLaQGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:cd05940 348 TFRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-590 |
1.94e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.94 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 112 RKPDQPY-------EWLSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNE 184
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLG--LKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 185 AVTYIVNKAELSLVF--VDKPEKAKLLLegvenKLTPSLKIIVLMDAYGSelvergqkcgveiisLKAMEDLGRANRRKP 262
Cdd:PRK13391 87 EAAYIVDDSGARALItsAAKLDVARALL-----KQCPGVRHRLVLDGDGE---------------LEGFVGYAEAVAGLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 263 KPPAPEDL--AVVCFTSGTTGNPKGalithrnivsdcsafVKAtensvnPCPDDTLISFLPLAHMFERVV----ECVMLC 336
Cdd:PRK13391 147 ATPIADESlgTDMLYSSGTTGRPKG---------------IKR------PLPEQPPDTPLPLTAFLQRLWgfrsDMVYLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 337 -----HGAKIGFFQGDIRL-----LMDD------LKVLQP---TVFPVVPRllnrMFDRIFGQANTTLKRWLLdfaskrk 397
Cdd:PRK13391 206 paplyHSAPQRAVMLVIRLggtviVMEHfdaeqyLALIEEygvTHTQLVPT----MFSRMLKLPEEVRDKYDL------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 398 eaelrsgiirnnslwdrlifhkvqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLSMPGDWTA 477
Cdd:PRK13391 275 ------------------------SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 478 --GHVGAPMpCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDG-WLHTGDIGKWLPNGTLKIID 554
Cdd:PRK13391 326 hpGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTD 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 1622942221 555 RKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:PRK13391 403 RAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
266-574 |
2.20e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNpcPDDTLISFLPLAHmfervvecvmlchgaKIGFFQ 345
Cdd:PRK05691 164 QPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLN--PDDVIVSWLPLYH---------------DMGLIG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 346 GdirllmddlkVLQPtVFPVVPRLLnrMFDRIFGQANTtlkRWLldfaskrkEA--ELRSGIIRNNSLWDRLIFHKV-QS 422
Cdd:PRK05691 227 G----------LLQP-IFSGVPCVL--MSPAYFLERPL---RWL--------EAisEYGGTISGGPDFAYRLCSERVsES 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 423 SLGG----KVRLMVTGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECTAGCCLSMPG--------DWTA------- 477
Cdd:PRK05691 283 ALERldlsRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATLFVSGGRRGqgipalelDAEAlarnrae 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 478 ---GHV----GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-LDKDG--WLHTGDIGkWLPN 547
Cdd:PRK05691 363 pgtGSVlmscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRD 441
|
330 340
....*....|....*....|....*..
gi 1622942221 548 GTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK05691 442 GELFVTGRLKDML-IVRGHNLYPQDIE 467
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-640 |
1.73e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 60.71 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRpEWVIIEQGCFAYSMVIVPLYDT-LGNEAVTYIVNKAELSLVF 199
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVR--AGDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 200 VDKpEKAKLLlEGVENKLtPSLKIIVlmdaygsELVERGQKCGVEIISLkamEDLGRANRRKPKPPAPEDLAVVCFTSGT 279
Cdd:PRK07788 152 YDD-EFTDLL-SALPPDL-GRLRAWG-------GNPDDDEPSGSTDETL---DDLIAGSSTAPLPKPPKPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 280 TGNPKGAlithrnivsdcsafvkatensvnpcPDDTLISFLPLAHMFERV---VECVMLC-----HG-----AKIGFFQG 346
Cdd:PRK07788 219 TGTPKGA-------------------------PRPEPSPLAPLAGLLSRVpfrAGETTLLpapmfHAtgwahLTLAMALG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 347 ---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwLLDFASKRKEAelrsgiirnnslwdrlif 417
Cdd:PRK07788 274 stvvlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPEVLAKYDT------------------ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 418 hkvqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECtAGCCLSMPGDWTA--GHVGAPMPCNLIKLVDvE 495
Cdd:PRK07788 323 ----SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-E 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK07788 393 NGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVED 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942221 576 IYIRSEAIAQVFVHGeslqafliaivVPDVET---LRPWAQKRgfDGSfeelcrnkdvkkAILEDMVR 640
Cdd:PRK07788 468 LLAGHPDVVEAAVIG-----------VDDEEFgqrLRAFVVKA--PGA------------ALDEDAIK 510
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
264-609 |
2.15e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 60.48 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 264 PPAPEDLAVVcFTSGTTGNPKGalithrnivsdcsafVKATensvNPCPDDTL--ISFLPLAHMFERVVECVM---LCHG 338
Cdd:PRK12406 149 PPVPQPQSMI-YTSGTTGHPKG---------------VRRA----APTPEQAAaaEQMRALIYGLKPGIRALLtgpLYHS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 339 AKIGFFQGDIRLlmDDLKVLQP-----------------TVFpVVPRllnrMFDRifgqanttlkrwLLDFASKRKEAel 401
Cdd:PRK12406 209 APNAYGLRAGRL--GGVLVLQPrfdpeellqlierhritHMH-MVPT----MFIR------------LLKLPEEVRAK-- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 402 rsgiirnnslWDrlifhkvQSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE------CTAGCCLSMPGDw 475
Cdd:PRK12406 268 ----------YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTEsgavtfATSEDALSHPGT- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 476 taghVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNV--FQgYLKDPAKTAEaLDKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PRK12406 326 ----VGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLC 398
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 554 DRKKHIFkLAQGEYIAPEKIEniyirSEAIAQVFVH------------GESLQAFL--IAIVVPDVETLR 609
Cdd:PRK12406 399 DRKRDMV-ISGGVNIYPAEIE-----AVLHAVPGVHdcavfgipdaefGEALMAVVepQPGATLDEADIR 462
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
101-610 |
2.97e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 60.04 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 101 QVSNNGPCLGSRkpDQPYEWlsyKQVAEMSECLGSALIQKgftATPDQ--FIGIFAQNRPEWVIIEQGCFAYSMVIVPLY 178
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTW---REVLAEAAARAAALIAL---ADPDRplHVGVLLGNTPEMLFWLAAAALGGYVLVGLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 179 DTLGNEAVTYIVNKAELSLVFVDKPEKAklLLEGVEnklTPSLKIIVLMDAYGSELVergqkcgveiislkamedlGRAN 258
Cdd:PRK13388 84 TTRRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTPAYAELV-------------------AAAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 259 RRKP-KPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSvnpcPDDTLISFLPLAHMfervvECVM--- 334
Cdd:PRK13388 140 ALTPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT----RDDVCYVSMPLFHS-----NAVMagw 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 335 ---LCHGAKI---------GFfqgdirllMDDLKVLQPTVFPVVPRLL-------NRMFDrifgqANTTLKRWLLDFASK 395
Cdd:PRK13388 211 apaVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 396 RKEAElrsgiirnnslwdrlifhkvqsslggkvrlmvtgaapvsatvltFLRAaLGCQFYEGYGQTEctAGCCLSMPGDW 475
Cdd:PRK13388 278 RDIAE--------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 476 TAGHVGAPMPCnlIKLVDVEEM---------------NymAAEGEGE-VCVKGPNVFQGYLKDPAKTAEALdKDGWLHTG 539
Cdd:PRK13388 311 PPGSIGRGAPG--VAIYNPETLtecavarfdahgallN--ADEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSG 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622942221 540 DIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFVHG----ESLQAFLIAIVVPDVETLRP 610
Cdd:PRK13388 386 DLAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATFDP 459
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
250-576 |
4.18e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.39 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 250 AMEDL---GRANRRKPKPPAP-EDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATenSVNPcPDDTLISFLPLAH- 324
Cdd:PRK05851 130 TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARV--GLDA-ATDVGCSWLPLYHd 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 325 MFERVVECVMLChGAKIGffqgdirllmddlkvLQPT-VFPVVP-RLLNrmfdrifgqanttlkrWLLDF-ASKRKEAEL 401
Cdd:PRK05851 207 MGLAFLLTAALA-GAPLW---------------LAPTtAFSASPfRWLS----------------WLSDSrATLTAAPNF 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 402 RSGIIRNNSlwdrlifHKVQSSLGGKVRLMVTGAAPVSATVLT-FLRAALGCQFYEG-----YGQTECTagCCLSMP--- 472
Cdd:PRK05851 255 AYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaapsYGLAEST--CAVTVPvpg 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 473 ------------GDWTAGH--VGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAktaeaLDKDGWLHT 538
Cdd:PRK05851 326 iglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDDWFPT 400
|
330 340 350
....*....|....*....|....*....|....*...
gi 1622942221 539 GDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:PRK05851 401 GDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV 436
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
264-574 |
4.64e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.63 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 264 PPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFvkaTENSVNPCPDDTLISFLPLAH-MfervvecvmlchgAKIG 342
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI---SHDGLKVRPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 343 FFQGDI--RLLMDDLKVLQptvFPVVPRLLNRMFDR---------IFGqanttlkrwlLDFASKRKEAELRSGIirNNSL 411
Cdd:PRK09192 236 FLLTPVatQLSVDYLPTRD---FARRPLQWLDLISRnrgtisyspPFG----------YELCARRVNSKDLAEL--DLSC 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 412 WdrlifhkvqsslggkvRLMVTGAAPVSATVL-----TFlrAALGCQ---FYEGYGQTECTAGCCLSMPG--------DW 475
Cdd:PRK09192 301 W----------------RVAGIGADMIRPDVLhqfaeAF--APAGFDdkaFMPSYGLAEATLAVSFSPLGsgivveevDR 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 476 TA----GHV----------------GAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAkTAEALDKDGW 535
Cdd:PRK09192 363 DRleyqGKAvapgaetrrvrtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGW 440
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622942221 536 LHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09192 441 LDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
113-638 |
4.85e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 59.14 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 113 KPDQP-YEWL----SYKQVAEMSECLGSALIQKGFTA-TPdqfIGIFAQNRPEWVI-----IEQGCfAYsmviVPLYDTL 181
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSLKLPDkSP---IIVFGHMSPEMLAtflgaVKAGH-AY----IPVDVSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 182 GNEAVTYIVNKAELSLVFvdkpEKAKLLLEGVenkltpslkiivlmdaygselvergqkcGVEIISLKAMEDLGRAnrrk 261
Cdd:PRK04813 87 PAERIEMIIEVAKPSLII----ATEELPLEIL----------------------------GIPVITLDELKDIFAT---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 262 pKPPAPEDLAV-------VCFTSGTTGNPKGALITHRNIVSdcsaFVKaTENSVNPCPDDTlisflplahmfervvecVM 334
Cdd:PRK04813 131 -GNPYDFDHAVkgddnyyIIFTSGTTGKPKGVQISHDNLVS----FTN-WMLEDFALPEGP-----------------QF 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 335 LCHgAKIGFfqgdirllmdDLKV--LQP------TVFPVVPRLLNRmfdriFGQANTTLKR-----W----------LLD 391
Cdd:PRK04813 188 LNQ-APYSF----------DLSVmdLYPtlasggTLVALPKDMTAN-----FKQLFETLPQlpinvWvstpsfadmcLLD 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 392 --FASKrKEAELRsgiirnnslwdRLIF------HKVQSSLggKVRLmvtgaaPvSATVltflraalgcqfYEGYGQTEC 463
Cdd:PRK04813 252 psFNEE-HLPNLT-----------HFLFcgeelpHKTAKKL--LERF------P-SATI------------YNTYGPTEA 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 464 TAGC------------CLSMPgdwtaghVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL- 530
Cdd:PRK04813 299 TVAVtsieitdemldqYKRLP-------IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFf 370
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 531 DKDGW--LHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI-----YIRSeAIAQVFVHGESLQAfLIAIVVP 603
Cdd:PRK04813 371 TFDGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GYRIELEEIEQNlrqssYVES-AVVVPYNKDHKVQY-LIAYVVP 446
|
570 580 590
....*....|....*....|....*....|....*
gi 1622942221 604 DvetlrpwaqkrgfDGSFEelcRNKDVKKAILEDM 638
Cdd:PRK04813 447 K-------------EEDFE---REFELTKAIKKEL 465
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
267-606 |
7.91e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 59.40 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNpcpdDTLISFLPLAhmFERVVECVM--LCHGAKIGFF 344
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN----DRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 QGDIRllmDDLKVLQptvfpvvprLLNRmfDRIfgqanTTlkrwlLDFASkrkeaelrsgiirnNSLWDRLIFHKVQSsl 424
Cdd:PRK12467 3310 DNDLW---DPEELWQ---------AIHA--HRI-----SI-----ACFPP--------------AYLQQFAEDAGGAD-- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 425 GGKVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCL-SMPGDWTAGHVGAPMPCNLIKL---VDVEEMNY 499
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLDGQLNP 3429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:PRK12467 3430 VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGE 3508
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622942221 573 IENIYIRSEAIAQVFVHGESLQA--FLIAIVVPDVE 606
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADP 3544
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
275-604 |
8.91e-09 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 57.42 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 275 FTSGTTGNPKGALITHRNIVsdcsAFVKATENSVNPCPDDTLISFLPLAH-MFERVVECVMLCHGAKIGFFQGDIRLLMD 353
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSWIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 354 DLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkEAELRSGIIRNnslwdrlifhkvqsslggKVRLMVT 433
Cdd:cd17633 83 KINQYNATVIYLVPTML---------------------------QALARTLEPES------------------KIKSIFS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 434 GAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCnliklVDVEEMNymAAEGE-GEVCVK 511
Cdd:cd17633 118 SGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRN--ADGGEiGKIFVK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 512 GPNVFQGYLKdpaktAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFVHGE 591
Cdd:cd17633 191 SEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
330
....*....|....*.
gi 1622942221 592 SLQAF---LIAIVVPD 604
Cdd:cd17633 265 PDARFgeiAVALYSGD 280
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
121-606 |
1.85e-08 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 57.48 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTYIVNKAELSLVFV 200
Cdd:cd17656 14 LTYRELNERSNQLARFLREKG--VKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 201 DKPEKAKLLLEGVenkltpslkIIVLMDaygselvergqkcgvEIISLKAMEDLGRANrrkpkppAPEDLAVVCFTSGTT 280
Cdd:cd17656 92 QRHLKSKLSFNKS---------TILLED---------------PSISQEDTSNIDYIN-------NSDDLLYIIYTSGTT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 281 GNPKGALITHRNIVSdcsaFVKATENSVNPCPDDTLISFLPLAH--MFERVVECvmLCHGAKIGFFQGDIRLLMDDLKVL 358
Cdd:cd17656 141 GKPKGVQLEHKNMVN----LLHFEREKTNINFSDKVLQFATCSFdvCYQEIFST--LLSGGTLYIIREETKRDVEQLFDL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 359 ------QPTVFPVVprLLNRMFDrifgqanttLKRWLLDFASKRKEAeLRSG--IIRNNSLWDRLIFHkvqsslggkvrl 430
Cdd:cd17656 215 vkrhniEVVFLPVA--FLKFIFS---------EREFINRFPTCVKHI-ITAGeqLVITNEFKEMLHEH------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 431 mvtgaapvsatvltflraalGCQFYEGYG--QTECTAGCCLSMPGDWTA-GHVGAPMPCNLIKLVDvEEMNYMAAEGEGE 507
Cdd:cd17656 271 --------------------NVHLHNHYGpsETHVVTTYTINPEAEIPElPPIGKPISNTWIYILD-QEQQLQPQGIVGE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 508 VCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSE 581
Cdd:cd17656 330 LYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRIELGEIEAQLLNHP 408
|
490 500
....*....|....*....|....*...
gi 1622942221 582 AIAQ--VFVHGESL-QAFLIAIVVPDVE 606
Cdd:cd17656 409 GVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
105-608 |
2.11e-08 |
|
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: 57.10 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 105 NGPCLGSRKPDQPYewlSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQ---NRPEWVIieqGCFAYSMVIVPLYDTL 181
Cdd:cd17654 4 PALIIDQTTSDTTV---SYADLAEKISNLSNFLRKKF--QTEERAIGLRCDrgtESPVAIL---AILFLGAAYAPIDPAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 182 GNEAVTYIVNKAELSLVfvdkpekaklllegVENKLTPSLKIIVLMDAygselvergqkcgveiislkamedlgranrRK 261
Cdd:cd17654 76 PEQRSLTVMKKCHVSYL--------------LQNKELDNAPLSFTPEH------------------------------RH 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 262 PKPPAPEDLAVVCFTSGTTGNPKGALITHR----NIVSDCSAFvkatensvNPCPDDTLIsFLPLAHMFERVVECVM-LC 336
Cdd:cd17654 112 FNIRTDECLAYVIHTSGTTGTPKIVAVPHKcilpNIQHFRSLF--------NITSEDILF-LTSPLTFDPSVVEIFLsLS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 337 HGAKIgffqgdirllmddlkVLQPTVFPVVPRLLNRMFDRIFG----QANTTLKRwllDFASKRKEAELRSGIirnnslw 412
Cdd:cd17654 183 SGATL---------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT------- 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 413 drlifhkvqSSLggkvRLMVTGAAP-VSATVLTFLRAA-LGCQFYEGYGQTECtagCCLS----MPGDWTAGHVGAPMPC 486
Cdd:cd17654 238 ---------SSL----RVLALGGEPfPSLVILSSWRGKgNRTRIFNIYGITEV---SCWAlaykVPEEDSPVQLGSPLLG 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 487 NLIKLVDVEemnymAAEGEGEVCVKGPNVfQGYLKDPAKTAEALdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGE 566
Cdd:cd17654 302 TVIEVRDQN-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GK 369
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1622942221 567 YIAPEKIENIYIRSEAIAQVFVHGESLQAFLIAIVVPDVETL 608
Cdd:cd17654 370 RINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSR 411
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
114-626 |
6.76e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 55.79 E-value: 6.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 114 PDQPY-------EWLSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAV 186
Cdd:PRK13390 11 PDRPAvivaetgEQVSYRQLDDDSAALARVLYDAGLR--TGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 187 TYIV-NKAELSLVfvdkpekAKLLLEGVENKLTPSLKIIVlmdAYGSELVERGqkcgveiiSLKAMedLGRANRRKPKPP 265
Cdd:PRK13390 89 DYIVgDSGARVLV-------ASAALDGLAAKVGADLPLRL---SFGGEIDGFG--------SFEAA--LAGAGPRLTEQP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APedlAVVCFTSGTTGNPKGAL--ITHRNIVSDCSAFVKATENSVNPCPDDTLISFLPLAHMFE-RVVECVMLCHGAKIG 342
Cdd:PRK13390 149 CG---AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHALGGTVVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 343 FFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskRKEAELRSGiirnnslwdrlifHKVQS 422
Cdd:PRK13390 226 AKRFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR-------------YDVSS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 423 slggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLSMPGDWTA--GHVGAPMPCNLiKLVDvEEMNYM 500
Cdd:PRK13390 272 -----LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDL-HICD-DDGNEL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 501 AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYI 578
Cdd:PRK13390 344 PAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENALT 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1622942221 579 RSEAIAQVFVHGeslqafliaivVPDVET---LRPWAQ-KRGFDGSfEELCR 626
Cdd:PRK13390 423 MHPAVHDVAVIG-----------VPDPEMgeqVKAVIQlVEGIRGS-DELAR 462
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-609 |
7.89e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.33 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 268 EDLAVVCFTSGTTGNPKGALITHRNIVSDCsAFVKATEnSVNPcpDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFF- 344
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERL-QWMQATY-ALDD--SDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 345 ---QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlLDFASKRKEAELRsgiirnnslwDRlifhkvq 421
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELR----------NR------- 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 422 sslggkvrlmvtgaapvsatVLTFLRAAlgcQFYEGYGQTE----CTAGCCLSMPGDWTAghVGAPMPCNLIKLVDvEEM 497
Cdd:PRK05691 1408 --------------------VLQRLPQV---QLHNRYGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD-AEL 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 570
Cdd:PRK05691 1462 NLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEP 1540
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1622942221 571 EKIENIYIRSEAIAQ--VFVH----GESLQAFLIAIVVPDVETLR 609
Cdd:PRK05691 1541 EEIQARLLAQPGVAQaaVLVRegaaGAQLVGYYTGEAGQEAEAER 1585
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
1.06e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 55.27 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGFTatPDQFIGIFAQNRPEWVIIEQGcFAYSMVIVPLYDT-LGNEAVTYIVNKAELSLVF 199
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVG--KGDVVALLMENRPEYLAAWLG-LAKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 200 VDkPEKAKLLlEGVENKLTPSLKIIVLMDAYGselvergqkcgveiISLKAMEDLGRANRRKPKPPAP-------EDLAV 272
Cdd:PRK08279 140 VG-EELVEAF-EEARADLARPPRLWVAGGDTL--------------DDPEGYEDLAAAAAGAPTTNPAsrsgvtaKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622942221 273 VCFTSGTTGNPKGALITHRNIVSDCSAFVkateNSVNPCPDDTLISFLPLAH 324
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFG----GLLRLTPDDVLYCCLPLYH 251
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-615 |
1.36e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 121 LSYKQVAEMSECLGSALIQKGftATPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAVTYIVNKAELS 196
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERG--VGPDVLVGVAMERSIEMVVallaILKAGGAY----VPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 197 LVFVDKPEKAKL-LLEGVENkltpslkiiVLMDAYGSELveRGQKCGVEIISLkamedlgranrrkpkppAPEDLAVVCF 275
Cdd:PRK12316 611 LLLSQSHLGRKLpLAAGVQV---------LDLDRPAAWL--EGYSEENPGTEL-----------------NPENLAYVIY 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 276 TSGTTGNPKGALITHRNIVSDCSAFVKATEnsvnpcpddtlisfLPLAhmfERVVECVMLCHGAKIGFFQGDirlLMDDL 355
Cdd:PRK12316 663 TSGSTGKPKGAGNRHRALSNRLCWMQQAYG--------------LGVG---DTVLQKTPFSFDVSVWEFFWP---LMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 356 KVLqptvfpVVPRLLNRMFDRIFGQANTTLKRwLLDFASKRKEAELRSGiirnnslwdrlifhKVQSSLggKVRLMVTGA 435
Cdd:PRK12316 723 RLV------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE--------------DVASCT--SLRRIVCSG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 436 APVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLSMPGDWTAGHV--GAPMPCNLIKLVDVeEMNYMAAEGEGEVCVKG 512
Cdd:PRK12316 780 EALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGGDSVpiGRPIANLACYILDA-NLEPVPVGVLGELYLAG 858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 513 PNVFQGYLKDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQV 586
Cdd:PRK12316 859 RGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHPWVREA 937
|
490 500 510
....*....|....*....|....*....|....*
gi 1622942221 587 FVHGESLQAfLIAIVVPD------VETLRPWAQKR 615
Cdd:PRK12316 938 AVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
248-601 |
1.74e-07 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 54.65 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 248 LKAMEDLGRANRRKP---KPPAPEDLAVVCFTSGTTGNPKGALitHRNivSDCSAFVKAT-ENSVNPCPDDtlisflpla 323
Cdd:PRK06060 122 AEAAELMSEAARVAPggyEPMGGDALAYATYTSGTTGPPKAAI--HRH--ADPLTFVDAMcRKALRLTPED--------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 324 hmfervvecVMLChGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPrllnrmfdrIFGQANTTLkrwlldfaSKRKEAELRS 403
Cdd:PRK06060 189 ---------TGLC-SARMYFAYGLGNSVWFPLATGGSAVINSAP---------VTPEAAAIL--------SARFGPSVLY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 404 GIirnNSLWDRLIFHKVQSSLGgKVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLSMPGDWTAGHVGA 482
Cdd:PRK06060 242 GV---PNFFARVIDSCSPDSFR-SLRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWRLGTLGR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 483 PMPCNLIKLVdVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTaeaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKL 562
Cdd:PRK06060 318 VLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDT-EV 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622942221 563 AQGEYIAPEKIENIYIRSEAIAQVFVHG-------ESLQAFLIAIV 601
Cdd:PRK06060 393 IGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
113-290 |
3.17e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 53.75 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 113 KPDQPYEWLSYKQVAEMSECLGSAL----IQKGftatpDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAVTY 188
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLkelgVEKG-----DR-VFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 189 IVNKAElSLVFVDKPEkaklLLEGVENKLTPSLKIIVLMDAYGSElvergqkcGVEIISL-KAMEDlgrANRRKPKPP-A 266
Cdd:PRK04319 140 RLEDSE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDVEE--------GPGTLDFnALMEQ---ASDEFDIEWtD 203
|
170 180
....*....|....*....|....
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITH 290
Cdd:PRK04319 204 REDGAILHYTSGSTGKPKGVLHVH 227
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
261-597 |
3.21e-07 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 53.59 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 261 KPKPPAPE-DLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNPCPddTLISFLPLAHmfervveCVMLCHGA 339
Cdd:cd05915 145 ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH-------VNAWCLPY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 340 KIGFFQGDIRLLMDdlkVLQPTVfpvvprllnrMFDRIFGQANTTL--KRWLLDFASKRKEAelrsgiirnnslwdrlif 417
Cdd:cd05915 216 AATLVGAKQVLPGP---RLDPAS----------LVELFDGEGVTFTagVPTVWLALADYLES------------------ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 418 hkVQSSLGGKVRLMVTGAAPvsATVLTFLRAALGCQFYEGYGQTEC--TAGCCLSMPgDWT------AGHVGAPMPCN-L 488
Cdd:cd05915 265 --TGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspVVVQNFVKS-HLEslseeeKLTLKAKTGLPiP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 489 IKLVDVEEMNYMAAEGEGE----VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 564
Cdd:cd05915 340 LVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG- 418
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622942221 565 GEYIAPEKIENIYIRSEAIAQVFV-------HGESLQAFL 597
Cdd:cd05915 419 GEWISSVDLENALMGHPKVKEAAVvaiphpkWQERPLAVV 458
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
243-324 |
1.17e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 51.87 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 243 VEIISLkameDLGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDC----SAFVKATENSvnPCPDDTLIS 318
Cdd:PRK05850 139 IEVDLL----DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVS 212
|
....*.
gi 1622942221 319 FLPLAH 324
Cdd:PRK05850 213 WLPFYH 218
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
251-325 |
4.88e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.60 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 251 MEDLGRANRRKPKPPAPEDL---------AVVCFTSGTTGNPKGALITHRNIVSdCSAFVKatenSVNPCPDDTLISFLP 321
Cdd:cd05938 118 VISLLDKVDAASDEPVPASLrahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGFLS----LCGVTADDVIYITLP 192
|
....
gi 1622942221 322 LAHM 325
Cdd:cd05938 193 LYHS 196
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
266-599 |
8.51e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.40 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 266 APEDLAVVCFTSGTTGNPKGALITHRNIVSDCSA---FVKATENSV-----NPCPDDTLISFLPlAHMFERVVECV--ML 335
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSkvpYLALSEADViaqtaSQSFDISVWQFLA-APLFGARVEIVpnAI 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 336 CHgakigffqgDIRLLMDDLKVLQPTVFPVVPRLLNRMF--DRifgQANTTLkRWLLDfaskrkeaelrsgiirnnslwd 413
Cdd:PRK05691 3946 AH---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLP---------------------- 3990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 414 rlifhkvqsslggkvrlmvTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-SMPGDWTAGH---VGAPMPCNLI 489
Cdd:PRK05691 3991 -------------------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfRVDLASTRGSylpIGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 490 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHI--- 559
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQvki 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622942221 560 --FKLAQGEyIAPEKIENIYIRSEAIA-QVFVHGESLQAFLIA 599
Cdd:PRK05691 4131 rgYRIELGE-IEARLHEQAEVREAAVAvQEGVNGKHLVGYLVP 4172
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
254-294 |
1.02e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 49.27 E-value: 1.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1622942221 254 LGRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIV 294
Cdd:PRK10252 584 LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
275-590 |
2.39e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 47.47 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 275 FTSGTTGNPKGALITHRNIVSdcsafvkatensvnpcpddtliSFLPLAHMFERVVECVMLCHGAKIG--FFQGDIR-LL 351
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLH----------------------SFDCNVHDFHMKREDSVLIAGTLVHslFLYGAIStLY 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 352 MDDLKVLQPTVFPvvprllNRMFDRIFGQANTTLKRwlldfASKRKEAELRSGIIRNNSLwdrlifhKVQSSlGGKvrlm 431
Cdd:PRK07638 208 VGQTVHLMRKFIP------NQVLDKLETENISVMYT-----VPTMLESLYKENRVIENKM-------KIISS-GAK---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 432 vTGAAPVSATVLTFLRAalgcQFYEGYGQTECTAGCCLSmPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGE-GEVCV 510
Cdd:PRK07638 265 -WEAEAKEKIKNIFPYA----KLYEFYGASELSFVTALV-DEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEiGTVYV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 511 KGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:PRK07638 339 KSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-590 |
3.22e-05 |
|
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: 46.61 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 265 PAPEDLAVVCfTSGTTGNPKGALITHRNIVSdcSAFVKATENSVNPCPDD---------TLISFLPLAHmfervvecvmL 335
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFR--MLMGGADFGTGEFTPSEdahkaaaaaAGTVMFPAPP----------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 336 CHGAK-----IGFFQGDiRLLMDDLKVLQPTVFPVVPR-LLNRMFdrIFGQAnttLKRWLLDfaskrkeaELRSGiiRNN 409
Cdd:cd05924 68 MHGTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 410 SLwdrlifhkvqSSLggkvRLMVTGAAPVSATVLT-FLRAALGCQFYEGYGQTECTA-GCCLSMPGDWTAGHVGAPMPcn 487
Cdd:cd05924 132 DL----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 488 LIKLVDvEEMNYM--AAEGEGEVCVKGpNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:cd05924 196 DTVVLD-DDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINT 273
|
330 340
....*....|....*....|....*...
gi 1622942221 563 AqGEYIAPEKIENIYIRSEAIAQVFVHG 590
Cdd:cd05924 274 G-GEKVFPEEVEEALKSHPAVYDVLVVG 300
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
261-615 |
3.26e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 46.58 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 261 KPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSdcSAfvKATENSVNPcPDDTLISfLPLAHmfervvecvmlchgak 340
Cdd:PRK07824 28 RVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTA--SA--DATHDRLGG-PGQWLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 341 IGFFQGDIRLLM---DDLKVLQPTVF--PVVPRLLNRM-FDRIF-GQANTTLKRWLLDFASKRKEAELRSGIIrnnslwd 413
Cdd:PRK07824 86 IAGLQVLVRSVIagsEPVELDVSAGFdpTALPRAVAELgGGRRYtSLVPMQLAKALDDPAATAALAELDAVLV------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 414 rlifhkvqsslggkvrlmvtGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLsmpgdwtagHVGAPMPCNLIKLV 492
Cdd:PRK07824 159 --------------------GGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 493 DveemnymaaegeGEVCVKGPNVFQGY--LKDPAKTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAP 570
Cdd:PRK07824 207 D------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLP 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622942221 571 EKIENIYIRSEAIAQVFVHG---ESLQAFLIAIVVPD--------------VETLRPWAQKR 615
Cdd:PRK07824 269 QVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGDggpaptlealrahvARTLDRTAAPR 330
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-594 |
5.05e-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: 46.27 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 267 PEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFvkatENSVNPCPDDTLISFLPLAH---MFERVVECVMlcHGAKIGF 343
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLL----SHDLNLKNGDRTYTCMPLYHgtaAFLGACNCLM--SGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 344 ---FQgdIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfaskrkeaelrSGIIrnnSLWDRLifHKV 420
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLL------------STPP---SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 421 QSSLGGKVRLMVTGAapvsatvltfLRAALGC-QFYEGYGQTECTAGCCLSMPGDWTAGHVGAPMPCNLIKLVDVE---- 495
Cdd:cd05937 205 RVAWGNGLRPDIWER----------FRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 496 -----EMNYM---------AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEALDK------DGWLHTGDIGKWLPNGTL 550
Cdd:cd05937 275 mdpetDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622942221 551 KIIDRKKHIFKLaQGEYIAPEKIENIYIRSEAIAQVFVHGESLQ 594
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
71-290 |
1.82e-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: 41.41 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 71 RRSALLDSDEPLVYFYEDVT--TLYEGFQRGIQvsNNGPCLG----SRKPDQPYEWlSYKQVAEMSECLGSALIQKGFTA 144
Cdd:cd17634 32 VKNTSFAPGAPSIKWFEDATlnLAANALDRHLR--ENGDRTAiiyeGDDTSQSRTI-SYRELHREVCRFAGTLLDLGVKK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942221 145 tpDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAV-TYIVNKAELSLVFVD---KPEKAKLLLEGVENKLT-- 218
Cdd:cd17634 109 --GDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVaGRIIDSSSRLLITADggvRAGRSVPLKKNVDDALNpn 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942221 219 -PSLKIIVLMDAYGSELverGQKCGVEIISLKAMEDlgRANRRKPKPPAPEDLAVVCFTSGTTGNPKGALITH 290
Cdd:cd17634 187 vTSVEHVIVLKRTGSDI---DWQEGRDLWWRDLIAK--ASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT 254
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
261-324 |
2.21e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 41.25 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942221 261 KPKPPAPEDLAVVCFTSGTTGNPKGALITHRNIVSDCSAFVKATENSVNpcpdDTLISFLPLAH 324
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEG----DRGVSWLPFFH 232
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