|
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: 980.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 116 QPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 196 SLVFVDKpekaklllegvenklipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICF 275
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 355
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 356 KVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVT 433
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 434 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA--EGEGEVCVK 511
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 512 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGE 591
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 592 SLQAFLIAIVVPDVETLCSWA-QKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLL 670
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1034638914 671 TPTMKAKRPELRNYFRSQIDDLYS 694
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
86-696 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 714.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 86 YDDVTTLYEGFQRGIQVSNNGPCLGSR-KPDQ---PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWV 161
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRiRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 162 IIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVdKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQRC 241
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 242 GVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENtvnpCPDDTLISFLP 321
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF----YPSDVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 322 LAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEA 399
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 400 ELRSGiiRNNS-LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAG 478
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 479 HVGAPMPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 555
Cdd:PLN02736 429 HVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 556 KKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAI 634
Cdd:PLN02736 509 KKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAV 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034638914 635 LEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 696
Cdd:PLN02736 589 LADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
86-694 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 542.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 86 YDDVTTLYEGFQRGIQVSNNGPCLgSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQ 165
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVK--PGDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 166 GCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENklIPGLKIIVVMDaygselvERGQRCGVEV 245
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 246 TSMKAMEDLGRANR------RKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISF 319
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 320 LPLAHMFERVVECVMLCHGAKIGFfQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLDFA---S 394
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 395 KRKEAELRSGiiRNNSLW--------DRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAG 466
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 467 CCLTMPGDWTAGHVGAPMPCNLIKLvdveemnymaAEgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 546
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI----------AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 547 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRG-FEGSFEELC 625
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGlPYTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638914 626 RNKDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 694
Cdd:COG1022 535 QDPEVRALIQEEVDRANA--GLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
116-681 |
1.48e-174 |
|
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: 505.98 E-value: 1.48e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 116 QPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVE--PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 196 SLVFVDKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDLAVICF 275
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIGFFQgDIRLLMDD 354
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 355 LKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslGGRVRLMVTG 434
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 435 AAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPN 514
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 515 VFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESlQ 594
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 595 AFLIAIVVPDVETLCSWAQKRG-FEGSFEELCRNKDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNGLLTPT 673
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1034638914 674 MKAKRPEL 681
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
117-678 |
1.47e-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: 467.46 E-value: 1.47e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 117 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 196
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 197 LVFVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpPAPEDLAVICFT 276
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 277 SGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD--- 353
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPELL--GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 354 -----DLKVLQPTVFPVVPRLLNRMFDRIFGQANT--TLKRWLLDFASKRKEAELRSGIirNNSLWDRLIFHKVQSSLGG 426
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 427 RVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYM--AAEG 504
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYStdKPPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 505 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA 584
Cdd:cd17639 330 RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 585 QVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-EGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELF 663
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 1034638914 664 SIDNGLLTPTMKAKR 678
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
117-698 |
3.85e-158 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 471.63 E-value: 3.85e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 117 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 196
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVN--PGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 197 LVFVDKPEKAKLLleGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPkPPAPEDLAVICFT 276
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 277 SGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCP-DDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 355
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATeEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 356 KVLQPTVFPVVPRLlnrmFDRIFG------QANTTLKRWLLDFASKRKEAELRSGIIRNNS--LWDRLIFHKVQSSLGGR 427
Cdd:PLN02861 309 QALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGR 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 428 VRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT-AGHVGAPMPCNLIKLVDVEEMNYMAAEG-- 504
Cdd:PLN02861 385 VRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYDALSDvp 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 505 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA 584
Cdd:PLN02861 465 RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIA 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 585 QVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFS 664
Cdd:PLN02861 544 SIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFD 623
|
570 580 590
....*....|....*....|....*....|....
gi 1034638914 665 IDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV 698
Cdd:PLN02861 624 IERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
88-696 |
4.98e-158 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 471.61 E-value: 4.98e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 88 DVTTLYEGFQRGIQVSNNGPCLGSRKPDQ----PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVII 163
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAE--PGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 164 EQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV-DKpeKAKLLLEGvENKLIPGLKIIVVMDAYGSELVERGQRCG 242
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 243 VEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRN---IVSDCSAFVKATENTVNPcpDDTLISF 319
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFEDKMTH--DDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 320 LPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRK 397
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 398 EAELRSGIIRNNS--LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW 475
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 476 TA-GHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKI 552
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 553 IDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKK 632
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034638914 633 AILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 696
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
87-697 |
9.72e-155 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 463.34 E-value: 9.72e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 87 DDVTTLYEGFQRGIQVSNNGPCLGSR-----KPDQpYEWLSYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWV 161
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 162 IIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLlegvenKLIPG----LKIIVVMDAYGSELVER 237
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF------KTCPNsteyMKTVVSFGGVSREQKEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 238 GQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENtVNPC--PDDT 315
Cdd:PLN02614 193 AETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKS-ANAAltVKDV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 316 LISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFA 393
Cdd:PLN02614 272 YLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 394 SKRKEAELRSGI--IRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTM 471
Cdd:PLN02614 352 FSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 472 PGDW-TAGHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNG 548
Cdd:PLN02614 432 PDELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNG 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 549 TLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNK 628
Cdd:PLN02614 511 SMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNE 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638914 629 DVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIK 697
Cdd:PLN02614 591 KAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
62-694 |
3.45e-137 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 419.14 E-value: 3.45e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 62 VEVAGSGG-ARRSALLDsdEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRK---------PDQ---------PYEWLS 122
Cdd:PLN02387 31 VDVGGEPGyAIRNARFP--ELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisrefetsSDGrkfeklhlgEYEWIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 123 YKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDK 202
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 203 PEKAKLLleGVENKLiPGLKIIVVMDAYGSELVERG-QRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTG 281
Cdd:PLN02387 187 KQLKKLI--DISSQL-ETVKRVIYMDDEGVDSDSSLsGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 282 NPKGAMVTHRNIVSDCSAFVkatenTVNP--CPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD------ 353
Cdd:PLN02387 264 LPKGVMMTHGNIVATVAGVM-----TVVPklGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkik 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 354 -----DLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKEAELR------SGIIRnnSLWDRLIFHKV 420
Cdd:PLN02387 337 kgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 421 QSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYM 500
Cdd:PLN02387 415 RAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYL 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 501 AAEG---EGEVCVKGPNVFQGYLKDPAKTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKI 573
Cdd:PLN02387 495 ISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKV 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 574 ENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQ 652
Cdd:PLN02387 575 EAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEI 654
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1034638914 653 VKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 694
Cdd:PLN02387 655 PAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
112-563 |
1.73e-129 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 389.36 E-value: 1.73e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 112 RKPDQP------YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 185
Cdd:pfam00501 7 RTPDKTalevgeGRRLTYRELDERANRLAAGLRALGVG--KGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 186 ITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVergqrcgvevtsMKAMEDLGRANRRKPKPP 265
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVEC-VMLCHGAKIGFF 344
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 QGDIRL----LMDDLKVLQPTVFPVVPRLLNRMFDrifgqaNTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkv 420
Cdd:pfam00501 233 PGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------AGAPKRALL------------------------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 421 qsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW---TAGHVGAPMPCNLIKLVDVEEM 497
Cdd:pfam00501 277 -----SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETG 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638914 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
121-693 |
2.77e-103 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 330.79 E-value: 2.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfV 200
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLT--KGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI-V 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKPEKAKLLLEGVENKLIPGLKIIvvmdaYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPE---DLAVICFTS 277
Cdd:PTZ00216 199 CNGKNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 278 GTTGNPKGAMVTHRNIVSDCSAFV-KATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD--- 353
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALEdRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 354 ----DLKVLQPTVFPVVPRLlnrmFDRI----------FGqantTLKRWLLDFASKRKEAELRSGiiRNNSLWDRLIFHK 419
Cdd:PTZ00216 352 rphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 420 VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCqFYEGYGQTECTagCC--LTMPGDWTAGHVGAPMPCNLIKLVDVEEM 497
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTGDLEPNAVGQLLKGVEMKLLDTEEY 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 NYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENI 576
Cdd:PTZ00216 499 KHTdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEAL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 577 YMRSEPVAQ----VFVHgeSLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQ 652
Cdd:PTZ00216 579 YGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1034638914 653 VKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 693
Cdd:PTZ00216 657 VRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
116-679 |
6.35e-96 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 304.28 E-value: 6.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 116 QPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 196 SLVFVdkpekaklllegvENklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppAPEDLAVICF 275
Cdd:cd17640 79 VALVV-------------EN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMDDL 355
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSD----IVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 356 KVLQPTVFPVVPRLlnrmfdrifgqanttlkrWlldfaskrkEAeLRSGI---IRNNSLWDRLIFHKVQSslGGRVRLMV 432
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 433 TGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKG 512
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 513 PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGES 592
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 593 lQAFLIAIVVPDVETLCSWAQKRG--FEGSFEELCRNKDVKKAI-LEDMVRLGKDSGLKPFEQVKGITLHPELFsIDNGL 669
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGE 456
|
570
....*....|
gi 1034638914 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 |
3.76e-81 |
|
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: 266.64 E-value: 3.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 118 YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSL 197
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLE--PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 198 VFVDKPEKAKLLLEGVenkliPGlKIIVVMDAYGSELvergqRCGVEVTSMKAMedlGRANRRKPkPPAPEDLAVICFTS 277
Cdd:cd05932 82 LFVGKLDDWKAMAPGV-----PE-GLISISLPPPSAA-----NCQYQWDDLIAQ---HPPLEERP-TRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 278 GTTGNPKGAMVTHRNIVSDCSAFVkateNTVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIgFFQGDIRLLMDDLK 356
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQAGI----EHIGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 357 VLQPTVFPVVPRLLNRMFDRIFgqanttlkrwlldfaSKRKEAELRsgIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGA 435
Cdd:cd05932 222 RARPTLFFSVPRLWTKFQQGVQ---------------DKIPQQKLN--LLLKIPVVNSLVKRKVLKGLGlDQCRLAGCGS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 436 APVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPNV 515
Cdd:cd05932 285 APVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 516 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQA 595
Cdd:cd05932 353 MMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 596 FLIAIVVPDVETLCSWAQKRG-FEGSFeelcrnkdvkKAILEDMvrlgkDSGLKPFEQVKGITLHPELFSIDNGLLTPTM 674
Cdd:cd05932 433 PLALVVLSEEARLRADAFARAeLEASL----------RAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTL 497
|
....
gi 1034638914 675 KAKR 678
Cdd:cd05932 498 KIKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
112-615 |
8.17e-75 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 248.19 E-value: 8.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 112 RKPDQP-----YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 186
Cdd:COG0318 11 RHPDRPalvfgGRRLTYAELDARARRLAAALRALGVG--PGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 187 TYIVNKAELSLVFVdkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppa 266
Cdd:COG0318 89 AYILEDSGARALVT------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 pedlAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI---- 341
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT----PGDVVLVALPLFHVFGLTVGLLApLLAGATLvllp 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 342 GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELRSgiirnnslwdrlifhkvq 421
Cdd:COG0318 175 RF---DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------ 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 422 sslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNY 499
Cdd:COG0318 217 ------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMR 579
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAA 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1034638914 580 SEPVAQVFV-------HGESLQAFLI--AIVVPDVETLCSWAQKR 615
Cdd:COG0318 368 HPGVAEAAVvgvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
122-678 |
1.96e-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: 1.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 122 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIE---QGCFAYSMvivPLYDTLGNEAITYIVNKAELSLV 198
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAElaaQAIGALSL---GIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 199 FVDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQrcgveVTSMKAMEDLGRA-NRRKPK-------PPAPEDL 270
Cdd:cd17641 88 IAEDEEQVDKLLEIADR--IPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 271 AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQgDIR 349
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLG----PGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 350 LLMDDLKVLQPTVFPVVPRLLNRM--FDRIFGQANTTLKRWLLDF--------ASKRKEAELRSGIIRNNS-LWDRLIFH 418
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 419 KVQSSLG-GRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVeem 497
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 nymaaegeGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIY 577
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 578 MRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDsgLKPFEQV-KG 655
Cdd:cd17641 464 KFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRIrRF 540
|
570 580
....*....|....*....|...
gi 1034638914 656 ITLHPELfSIDNGLLTPTMKAKR 678
Cdd:cd17641 541 LLLYKEL-DADDGELTRTRKVRR 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
113-693 |
2.03e-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: 246.11 E-value: 2.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 113 KPDQPYEWLSYKQVAELseCIGSAliqKGF-KTAPDQF--IGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYI 189
Cdd:cd05933 1 KRGDKWHTLTYKEYYEA--CRQAA---KAFlKLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 190 VNKAELSLVFVDKPEKAKLLLEgVENKLiPGLKIIVvmdAYGSELVERGQRcgveVTSMKAMEDLGR-----ANRRKPKP 264
Cdd:cd05933 76 AETSEANILVVENQKQLQKILQ-IQDKL-PHLKAII---QYKEPLKEKEPN----LYSWDEFMELGRsipdeQLDAIISS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 265 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVEcVMLC--HGAKIG 342
Cdd:cd05933 147 QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPikVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 343 FFQGDIR--LLMDDLKVLQPTVFPVVPRLLNRMFDRI--FGQANTTLKRWLLDFAsKRKEAE-------LRSGIIRNNSL 411
Cdd:cd05933 226 FAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSPLFYRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 412 WDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIK 490
Cdd:cd05933 305 AKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 491 LVDVEemnymaAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 570
Cdd:cd05933 384 IHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 571 EKIEN-IYMRSEPVAQVFVHGESLQaFLIAIVV----PDVET----------LCSWAQKRGFEGS-FEELCRNKD--VKK 632
Cdd:cd05933 458 VPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTlkceVNPETgepldelteeAIEFCRKLGSQATrVSEIAGGKDpkVYE 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034638914 633 AILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 693
Cdd:cd05933 537 AIEEGIKRVNKKAISNA-QKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
89-671 |
1.44e-68 |
|
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: 235.43 E-value: 1.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 89 VTTLYEGF-QRgiqvsnngPCLGSRK---PDQPYE-WLSYKQVAELSECIGSALIQKGFKTA----------PDQFIGIF 153
Cdd:cd17632 28 IATVMTGYaDR--------PALGQRAtelVTDPATgRTTLRLLPRFETITYAELWERVGAVAaahdpeqpvrPGDFVAVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 154 AQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDK---PEKAKLLLEGvenkliPGLKIIVVMDaY 230
Cdd:cd17632 100 GFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAehlDLAVEAVLEG------GTPPRLVVFD-H 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 231 GSEL----------VERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPED---LAVICFTSGTTGNPKGAMVTHRNIVSdc 297
Cdd:cd17632 173 RPEVdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTERLVAT-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 298 sAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTVFPVVPRLLNRMFD 375
Cdd:cd17632 251 -FWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 376 RIfgQAntTLKRWLLDFA-----SKRKEAELRsgiirnnslwdrlifhkvQSSLGGRVRLMVTGAAPVSATVLTFLRAAL 450
Cdd:cd17632 329 RY--QA--ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 451 GCQFYEGYGQTEctAGCCLTmpgdwtAGHVGAPmPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTA 527
Cdd:cd17632 387 DLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 528 EALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVET 607
Cdd:cd17632 458 EVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDA 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034638914 608 LCSWAQKRgfegsfeelcrnkdVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLT 671
Cdd:cd17632 538 LAGEDTAR--------------LRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
121-678 |
2.09e-67 |
|
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: 228.87 E-value: 2.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKTAPDqfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDLAVICFTSGTT 280
Cdd:cd05914 86 SDED----------------------------------------------------------------DVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVSD---CSAFVKATENtvnpcpdDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQGDIRLLMDDLK 356
Cdd:cd05914 102 GNSKGVMLTYRNIVSNvdgVKEVVLLGKG-------DKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 357 VLQPTVFPVVPRLLNRMFDRIFGQAN-TTLKRWLLDFASKRKEAELRSgiirnnslwdrLIFHKVQSSLGGRVRLMVTGA 435
Cdd:cd05914 175 FAQVTPTLGVPVPLVIEKIFKMDIIPkLTLKKFKFKLAKKINNRKIRK-----------LAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 436 APVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPmpcnlIKLVDVEEMNYMAAEGEGEVCVKGPNV 515
Cdd:cd05914 244 AKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 516 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA--QVFVHGESL 593
Cdd:cd05914 318 MKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKL 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 594 QAflIAIVVPDvetlcswaqkrgFEGSFEELCRNKdvKKAILEDmVRLGKDSGLKPFEQVKGITLHPELFSidnglLTPT 673
Cdd:cd05914 398 VA--LAYIDPD------------FLDVKALKQRNI--IDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFE-----KTPK 455
|
....*
gi 1034638914 674 MKAKR 678
Cdd:cd05914 456 GKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
269-615 |
3.09e-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: 216.38 E-value: 3.09e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKI----GFF 344
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 QGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiirnnslwdrlifhkvqssl 424
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 425 ggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT--AGHVGAPMPCNLIKLVDVEEmNYMAA 502
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 503 EGEGEVCVKGPNVFQGYLKDPAKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEP 582
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034638914 583 VAQVFVHG---ESLQAFLIAIVVP------DVETLCSWAQKR 615
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
121-590 |
3.74e-64 |
|
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: 220.55 E-value: 3.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKPEKAKLLleGVENKLIPGLKIIVvMDAYGSELVERGQrcGVEVTSMKAMEDlgranRRKPKPPAPEDLAVICFTSGTT 280
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKIIV-LDDKPDGVLSIED--LLSPTLGEEDED-----LPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVSDCSaFVKATEnTVNPCPDDTLISFLPLAHMFervveCVMLCHGAKIgffQG---------DIRLL 351
Cdd:cd05911 159 GLPKGVCLSHRNLIANLS-QVQTFL-YGNDGSNDVILGFLPLYHIY-----GLFTTLASLL---NGatviimpkfDSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 352 MDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRlifHKVQSslggrVRLM 431
Cdd:cd05911 229 LDLIEKYKITFLYLVPPIAAALA---------------------------------KSPLLDK---YDLSS-----LRVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 432 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCV 510
Cdd:cd05911 268 LSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 511 KGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd05911 348 RGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
110-615 |
2.05e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 214.00 E-value: 2.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 110 GSRKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIieqGCFAYSM---VIVPLYDTL 181
Cdd:PRK07656 15 ARRFGDKEAyvfgdQRLTYAELNARVRRAAAALAALGIG--KGDRVAIWAPNSPHWVI---AALGALKagaVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 182 GNEAITYIVNKAELSLVFVdkpekAKLLLeGVENKL---IPGLKIIVVMDaygselVERGQRCGVEVTSMKAMedLGRAN 258
Cdd:PRK07656 90 TADEAAYILARGDAKALFV-----LGLFL-GVDYSAttrLPALEHVVICE------TEEDDPHTEKMKTFTDF--LAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 259 RRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMF---ERVVECVM 334
Cdd:PRK07656 156 PAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLT----EGDRYLAANPFFHVFgykAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 335 lcHGAKIgffqgDIRLLMDDLKVLQ------PTVFPVVPrllnrmfdrifgqantTLKRWLLDFAsKRKEAELRSgiirn 408
Cdd:PRK07656 232 --RGATI-----LPLPVFDPDEVFRlieterITVLPGPP----------------TMYNSLLQHP-DRSAEDLSS----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 409 nslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLTMPGD---WTAGHVGAPM 484
Cdd:PRK07656 283 -------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 485 PCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 563
Cdd:PRK07656 344 AGVENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638914 564 QGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVP------DVETLCSWAQKR 615
Cdd:PRK07656 421 GGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
112-603 |
1.23e-60 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 210.50 E-value: 1.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 112 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 186
Cdd:cd05936 11 RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 187 TYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkaMEDLGRANRRKPKPPA 266
Cdd:cd05936 89 EHILNDSGAKALIVAVS-----------------------------------------------FTDLLAAGAPLGERVA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 --PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAfVKATENTVNPcPDDTLISFLPLAHMFERVVECV-MLCHGAKIGF 343
Cdd:cd05936 122 ltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWLEDLLE-GDDVVLAALPLFHVFGLTVALLlPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 344 FQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiirnnslwdrlifhkvqs 422
Cdd:cd05936 200 IPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 423 slggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMA 501
Cdd:cd05936 244 -----LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 581
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHP 395
|
490 500
....*....|....*....|....*....
gi 1034638914 582 PVAQVFV-------HGESLQAFliaiVVP 603
Cdd:cd05936 396 AVAEAAVvgvpdpySGEAVKAF----VVL 420
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
122-591 |
3.38e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 210.81 E-value: 3.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 122 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIieqgC-FAYSM---VIVPLYDTLGNEAITYIVNKAELSL 197
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVK--KGDRVAVFDWNSHEYLE----AyFAVPKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 198 VFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSElvergqRCGVEVTSMKAMedLGRANRRKPKPPAPE-DLAVICFT 276
Cdd:PRK06187 107 VLVD-SEFVPLL-AAILPQL-PTVRTVIVEGDGPAA------PLAPEVGEYEEL--LAAASDTFDFPDIDEnDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 277 SGTTGNPKGAMVTHRNIVSD---CSAFVKATentvnpcPDDTLISFLPLAHMFERVVECVMLCHGAKI---GFFqgDIRL 350
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHslaVCAWLKLS-------RDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPEN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 351 LMDDLKVLQPTVFPVVPRLLNRMFdrifgQANTTLKRWLldfaskrkeaelrsgiirnnslwdrlifhkvqsslgGRVRL 430
Cdd:PRK06187 247 LLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF------------------------------------SSLRL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 431 MVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLT----MPGDWT-AGHVGAPMPCNLIKLVDvEEMNYMAAEG 504
Cdd:PRK06187 286 VIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 505 E--GEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEP 582
Cdd:PRK06187 365 GevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPA 442
|
....*....
gi 1034638914 583 VAQVFVHGE 591
Cdd:PRK06187 443 VAEVAVIGV 451
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
269-615 |
3.53e-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: 167.47 E-value: 3.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVV----------ECVMLchg 338
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGLVNallcplfagaSVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 339 akiGFF---QGDIRLLMDDLkvlqpTVFPVVPRllnrMFDRIFGQANTTLKrwllDFASKRKEAElrsgiirnnslwdrl 415
Cdd:cd05941 163 ---PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 416 ifhkvqsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMP--GDWTAGHVGAPMPCNLIKLVD 493
Cdd:cd05941 212 ----------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEK 572
Cdd:cd05941 280 EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALE 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034638914 573 IENIYMRSEPVAQVFVHGESLQAF---LIAIVVP-------DVETLCSWAQKR 615
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
121-616 |
4.40e-41 |
|
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: 156.72 E-value: 4.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAeLSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05909 8 LTYRKLL-TGAIALARKLAKM--TKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKP--EKAKLL-------------LEGVENKLIPGLKIIVVMDAYgselvergqrcgveVTSMKAMEDLGRANRRkpkpp 265
Cdd:cd05909 85 SKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFLAGK--------------FPPKWLLRIFGVAPVQ----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 aPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQ 345
Cdd:cd05909 146 -PDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFHSF---------------GLTG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 346 GDIRLLMDDLKVLQ---PTVFPVVPRLLNRMFDRIFGQANTTLKRWLldfasKRKEAELRSGIirnnslwdrlifhkvqs 422
Cdd:cd05909 206 CLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPTFLRGYA-----RAAHPEDFSSL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 423 slggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMA 501
Cdd:cd05909 264 ------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 502 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSE 581
Cdd:cd05909 338 IGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEIL 415
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1034638914 582 P----VAQVFV----HGESLQAFLIAIvVPDVETLCSWAQKRG 616
Cdd:cd05909 416 PedneVAVVSVpdgrKGEKIVLLTTTT-DTDPSSLNDILKNAG 457
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
232-576 |
1.30e-40 |
|
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: 155.86 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 232 SELVERGQRCGVEVTSMKAMEDLGRANRR------KPKPPAPE----DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV 301
Cdd:cd05904 112 AELAEKLASLALPVVLLDSAEFDSLSFSDllfeadEAEPPVVVikqdDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 302 KATENtvNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMfdr 376
Cdd:cd05904 192 AGEGS--NSDSEDVFLCVLPMFHIYGLSSFALgLLRLGATVvvmpRF---DLEELLAAIERYKVTHLPVVPPIVLAL--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 377 ifgqanttlkrwlldfaskrkeaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFY 455
Cdd:cd05904 264 ------------------------VKSPIVDKYDL----------SSL----RQIMSGAAPLGKELIEAFRAKFpNVDLG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 456 EGYGQTECTAGCCLTMPGDWTAGHVG-----APMPCnlIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL 530
Cdd:cd05904 306 QGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNVE--AKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034638914 531 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:cd05904 384 DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
111-604 |
2.71e-40 |
|
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: 153.53 E-value: 2.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 111 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 185
Cdd:cd17631 6 RRHPDRTaLVFggrsLTYAELDERVNRLAHALRALGVA--KGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 186 ITYIVNKAElslvfvdkpekAKLLLEgvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpp 265
Cdd:cd17631 84 VAYILADSG-----------AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 apeDLAVICFTSGTTGNPKGAMVTHRNIvsdcsafvkaTENTVN------PCPDDTLISFLPLAHMFERVVECVM-LCHG 338
Cdd:cd17631 99 ---DLALLMYTSGTTGRPKGAMLTHRNL----------LWNAVNalaaldLGPDDVLLVVAPLFHIGGLGVFTLPtLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 339 AKI----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTlkrwllDFASkrkeaelrsgiirnnslwdr 414
Cdd:cd17631 166 GTVvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS-------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 415 lifhkvqsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLV 492
Cdd:cd17631 215 -------------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 493 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEK 572
Cdd:cd17631 281 D-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAE 357
|
490 500 510
....*....|....*....|....*....|....*....
gi 1034638914 573 IENIYMRSEPVAQVFV-------HGESlqafLIAIVVPD 604
Cdd:cd17631 358 VEDVLYEHPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
267-691 |
1.75e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 152.57 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFVKatentVNPcpdDTLISFLPLAHMFERVVECVMLCHGAK 340
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK-----YNP---KTHLSYLPISHIYERVIAYLSFMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 341 IGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLdfaskRKEAELRSGiiRNNSLWDRL--- 415
Cdd:PTZ00342 375 INIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLV-----KKILSLRKS--NNNGGFSKFleg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 416 IFH---KVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPM-PCNLIKL 491
Cdd:PTZ00342 448 ITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 492 VDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 571
Cdd:PTZ00342 528 RTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 572 KIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-------EGSFEELCRNKDVKKAILEDMVR---- 640
Cdd:PTZ00342 608 MLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlestginEKNYLEKLTDETINNNIYVDYVKgkml 687
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034638914 641 -LGKDSGLKPFEQVKGITLHPELFSIDNgLLTPTMKAKRPELRNYFRSQIDD 691
Cdd:PTZ00342 688 eVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKDYAFFIDQ 738
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
254-608 |
3.23e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 149.91 E-value: 3.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 254 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKAteNTVNPCpdDTLISFLPLAHMFERVV 330
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGS--NLNEGC--EILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 331 ECVMLchgakigffqgdirLLMDDLKVLQPTvfpvvPRLLNRMFdrifgqanTTLKRWLLdfaskrkeaelrSGIIRNNS 410
Cdd:PRK05677 269 HCMAM--------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 411 LWDRLI----FHKVQSSlggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 486
Cdd:PRK05677 310 LFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 487 NLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 566
Cdd:PRK05677 387 TLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGF 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1034638914 567 YIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaIVVPDVETL 608
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
115-615 |
5.66e-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: 147.84 E-value: 5.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 115 DQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVI-----IEQGCfaysmVIVPLYDTLGNEAITYI 189
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIK--KGDRVAIALPNGLEFVVaflaaARAGA-----VVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 190 VNKAELSLVFVDKPEkaklLLEGVENKLIPGLKII-VVMDAYGSELVERGQRCGVEvtsmkameDLGRANRRKPKPPAPE 268
Cdd:cd05926 82 LADLGSKLVLTPKGE----LGPASRAASKLGLAILeLALDVGVLIRAPSAESLSNL--------LADKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----GF 343
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLsTLAAGGSVvlppRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 344 fqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqss 423
Cdd:cd05926 226 ---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEPNPESPP---------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 424 lgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgcclTM------PGDWTAGHVGAPMPcNLIKLVDvEEM 497
Cdd:cd05926 265 --PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH----QMtsnplpPGPRKPGSVGKPVG-VEVRILD-EDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 577
Cdd:cd05926 337 EILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVL 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1034638914 578 MRSEPVAQ--VF-----VHGESLQAFliaiVVP------DVETLCSWAQKR 615
Cdd:cd05926 416 LSHPAVLEavAFgvpdeKYGEEVAAA----VVLregasvTEEELRAFCRKH 462
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
267-599 |
2.09e-37 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 147.51 E-value: 2.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcPDDTLISFLPLAHMFERVVECVMLCH-GAKigffq 345
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHP-GKELVVTALPLYHIFALTVNCLLFIElGGQ----- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 346 gdirllmdDLKVLQPTVFP-VVPRLLNRMFDRIFGqANTTLKRWLldfaskrkeaelrsgiirNNSLwdrliFHKVQSSl 424
Cdd:PRK08974 279 --------NLLITNPRDIPgFVKELKKYPFTAITG-VNTLFNALL------------------NNEE-----FQELDFS- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 425 ggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCcltmPGDWT--AGHVGAPMPCNLIKLVDvEEMNY 499
Cdd:PRK08974 326 --SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVN----PYDLDyySGSIGLPVPSTEIKLVD-DDGNE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMR 579
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVML 476
|
330 340
....*....|....*....|....*..
gi 1034638914 580 SEPVAQVF-------VHGESLQAFLIA 599
Cdd:PRK08974 477 HPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
122-576 |
7.80e-37 |
|
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: 145.36 E-value: 7.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 122 SYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVD 201
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 202 KPEKAKLLleGVENKLiPGLKIIVVMDaygSELVERGQRCgveVTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSG 278
Cdd:cd17642 124 KKGLQKVL--NVQKKL-KIIKTIIILD---SKEDYKGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 279 TTGNPKGAMVTHRNIvsdCSAFVKATENTV--NPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGF---FQGDIRL-LM 352
Cdd:cd17642 195 STGLPKGVQLTHKNI---VARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 353 DDLKV----LQPTVFPVVPRllnrmfdrifgqanttlkrwlldfaskrkeaelrSGIIRNNSLwdrlifhkvqSSLggrv 428
Cdd:cd17642 272 QDYKVqsalLVPTLFAFFAK----------------------------------STLVDKYDL----------SNL---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 429 RLMVTGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGE 507
Cdd:cd17642 304 HEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638914 508 VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESI 451
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-628 |
1.48e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 140.49 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFV----KATENTVNPCPddtlisfLPLAHMFERVVEcVMLC--HGAK 340
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIgerlGLTEQDRLCIP-------VPLFHCFGSVLG-VLACltHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 341 IGFfqgdIRLLMDDLKVLQP------TVFPVVPRllnrMFDRIFGQAnttlKRWLLDFASkrkeaeLRSGIIrnnslwdr 414
Cdd:cd05917 72 MVF----PSPSFDPLAVLEAiekekcTALHGVPT----MFIAELEHP----DFDKFDLSS------LRTGIM-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 415 lifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 490
Cdd:cd05917 126 -------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 491 LVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:cd05917 187 IVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIY 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638914 570 PEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQ-KRGFEGSFEEL---CRNK 628
Cdd:cd05917 265 PREIEEFLHTHPKVSDVQVVG-----------VPDErygEEVCAWIRlKEGAELTEEDIkayCKGK 319
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
269-615 |
4.53e-36 |
|
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: 138.79 E-value: 4.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI---GFF 344
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLT----EDDRYLIINPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 qgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELrsgiirnnslwdrlifhkvqSSL 424
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 425 ggrvRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTagcCLTM--PGD---WTAGHVGAPMPcnliklvDVEemn 498
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG---VATMcrPGDdaeTVATTCGRACP-------GFE--- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 499 yMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 578
Cdd:cd17638 181 -VRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALA 258
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034638914 579 RSEPVAQVFV-------HGESLQAFLIA--IVVPDVETLCSWAQKR 615
Cdd:cd17638 259 EHPGVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRER 304
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
123-615 |
4.90e-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: 4.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 123 YKQVAELSECIGSALIQKGfktapdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDk 202
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 203 pekAKLLLEGVENKLIPGLKiivvmdAYGselvergqRCGVEVTSMKAMEDLgranrrkpkppapedlAVICFTSGTTGN 282
Cdd:TIGR01923 79 ---SLLEEKDFQADSLDRIE------AAG--------RYETSLSASFNMDQI----------------ATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 283 PKGAMVTHRNIvsdcSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLmDDLKVLQPTV 362
Cdd:TIGR01923 126 PKAVPHTFRNH----YASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 363 FPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkvqsslggrvrlmvtGAAPVSATV 442
Cdd:TIGR01923 201 ISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGSAIPAPL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 443 LTFLRAaLGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHVGAPMPCNLIKL-VDveemnymAAEGEGEVCVKGPNVFQGYL 520
Cdd:TIGR01923 236 IEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVD-------NKEGHGEIMVKGANLMKGYL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 521 kDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESL 593
Cdd:TIGR01923 308 -YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQVP 385
|
490 500
....*....|....*....|..
gi 1034638914 594 QAFLIAIVVPDVETLCSWAQKR 615
Cdd:TIGR01923 386 VAYIVSESDISQAKLIAYLTEK 407
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
111-590 |
7.97e-36 |
|
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: 142.00 E-value: 7.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 111 SRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIV 190
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVK--PGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 191 NKAELSLVFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSELVERGQRCGvevtsmkAMEDL-GRANRRKPKPPAPE- 268
Cdd:cd12119 94 NHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAGVGVL-------AYEELlAAESPEYDWPDFDEn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTlisFLPLAHMFErvVE-------CVMLchGAKI 341
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVL--HAMAALLTDGLGLSESDV---VLPVVPMFH--VNawglpyaAAMV--GAKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 342 ----GFFQGDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRifgqanttLKRWLLDFASKRkeaelrsgiirnnslwdrli 416
Cdd:cd12119 235 vlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLDH--------LEANGRDLSSLR-------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 417 fhkvqsslggrvRLMVTGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHV----------GAPMP 485
Cdd:cd12119 284 ------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPVP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 486 CNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 563
Cdd:cd12119 350 GVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG 427
|
490 500
....*....|....*....|....*..
gi 1034638914 564 qGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd12119 428 -GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
254-559 |
9.41e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 142.83 E-value: 9.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 254 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCS---AFVKATentvnPCPDDTLISFLPLAHMF--ER 328
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGL-----GDGPERVLAALPMFHAYglTL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 329 VVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLlnrmFDRIfgqanttlkrwlldfaskRKEAELRsGIirn 408
Cdd:PRK05605 280 CLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 409 nslwdrlifhkvqsSLGGrVRLMVTGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMP 485
Cdd:PRK05605 334 --------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFP 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638914 486 CNLIKLVDVEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:PRK05605 397 DTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
247-599 |
9.38e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 139.57 E-value: 9.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 247 SMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD------CSAFVKATENTVNPCPDDTLISFL 320
Cdd:PRK12492 186 PFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAPL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 321 PLAHMFERVVECVMLchgakigFFQGDIRLLMDDlkvlqptvfpvvPRLLNRMFDRifgqanttLKRWLLdfaskrkeae 400
Cdd:PRK12492 266 PLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF---------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 401 lrSGIIRNNSLWDRLIFHKVQSSLGGRvRLMVT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCLTMPGDWTA 477
Cdd:PRK12492 309 --SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELAR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 478 -GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 556
Cdd:PRK12492 385 lGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRK 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034638914 557 KHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFLIA 599
Cdd:PRK12492 464 KDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
114-628 |
1.33e-34 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 139.18 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 114 PDQPYEWlSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEqgcFAYS-----MV-IVPLYDTlgNEaIT 187
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIE--KGDRVGIWAPNVPEWVLTQ---FATAkigaiLVtINPAYRL--SE-LE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 188 YIVNKAELS-LVFVDK--------------PEKAKLLLEGVENKLIPGLKIIVVMDAYGSelveRGQRCGVEVTSMKAME 252
Cdd:PRK08315 109 YALNQSGCKaLIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGDEKH----PGMLNFDELLALGRAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 253 DLGRANRRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFVkaTENtVNPCPDDTLISFLPLAHMFErvveC 332
Cdd:PRK08315 185 DDAELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNILNN-GYFI--GEA-MKLTEEDRLCIPVPLYHCFG----M 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 333 VM-----LCHGAKI-----GFfqgdirllmDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwl 389
Cdd:PRK08315 256 VLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 390 LDFASkrkeaeLRSGI-------IRnnslwdrlIFHKVQSSLGgrvrlM--VTGAapvsatvltflraalgcqfyegYGQ 460
Cdd:PRK08315 312 FDLSS------LRTGImagspcpIE--------VMKRVIDKMH-----MseVTIA----------------------YGM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 461 TECTAGCCLTMPGD------WTaghVGAPMPCNLIKLVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD 533
Cdd:PRK08315 351 TETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 534 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCS 610
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG-----------VPDEkygEEVCA 494
|
570 580
....*....|....*....|..
gi 1034638914 611 WAQKR-GFEGSFEEL---CRNK 628
Cdd:PRK08315 495 WIILRpGATLTEEDVrdfCRGK 516
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
254-683 |
4.65e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 137.32 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 254 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKATENTVNPCpdDTLISFLPLAHMFERVV 330
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKLEEGC--EVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 331 ECVMLchgAKIGFFQG------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsg 404
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 405 iirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT-MPGDWTAGHVGAP 483
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 484 MPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 562
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 563 AQGEYIAPEKIENIYMRSEPVAQVfvhgeslqaflIAIVVPDvetlcswaQKRGfegsfeELCRNKDVKK--AILEDMVR 640
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1034638914 641 LGKDSGLKPFEQVKGITLHPELFSIDNGlltptmKAKRPELRN 683
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
255-637 |
1.80e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 134.35 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 255 GRANRRKPKPPaPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvecvm 334
Cdd:PRK07787 116 ARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHV--------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 335 lcHGAKIGffqgdirllmddlkVLQPTvfpvvprllnrmfdRIFGQANTTLKrwlldFASKRKEAELRSGiirnNSL--- 411
Cdd:PRK07787 182 --HGLVLG--------------VLGPL--------------RIGNRFVHTGR-----PTPEAYAQALSEG----GTLyfg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 412 ----WDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCN 487
Cdd:PRK07787 223 vptvWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 488 LIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHI 559
Cdd:PRK07787 303 ETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 560 FKLAQGEyiapekIENIYMRSEPVAQVFVHGE---SLQAFLIAIVVPD-----------VETLCSwAQKRGFEGSF-EEL 624
Cdd:PRK07787 382 YRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGAddvaadelidfVAQQLS-VHKRPREVRFvDAL 454
|
410
....*....|....*.
gi 1034638914 625 CRN---KDVKKAILED 637
Cdd:PRK07787 455 PRNamgKVLKKQLLSE 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
121-628 |
4.22e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 134.52 E-value: 4.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEqgcFAYSMV------IVPLYDTlgnEAITYIVNKAE 194
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQ--PGDRVGIWAPNCAEWLLTQ---FATARIgailvnINPAYRA---SELEYALGQSG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 195 LSLVFVDK---------------PEKAKLLLEGVENKLIPGLKIIVVMDAYGS-------ELVERGqrcgvEVTSMKAME 252
Cdd:PRK12583 118 VRWVICADafktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAPAPPpgflawhELQARG-----ETVSREALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 253 DLGRANRRkpkppapEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFV----KATENtvnpcpdDTLISFLPLAHMFER 328
Cdd:PRK12583 193 ERQASLDR-------DDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVaeslGLTEH-------DRLCVPVPLYHCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 329 VVeCVMLC--HGAKIgFFQGDirlLMDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwlLDFA 393
Cdd:PRK12583 258 VL-ANLGCmtVGACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 394 SkrkeaeLRSGIIrnnslwdrlifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMP 472
Cdd:PRK12583 318 S------LRTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 473 GD---WTAGHVGAPMPCNLIKLVDVEemNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNG 548
Cdd:PRK12583 365 ADdleRRVETVGRTQPHLEVKVVDPD--GATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 549 TLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQKR-GFEGSFEEL 624
Cdd:PRK12583 443 YVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEEL 510
|
....*..
gi 1034638914 625 ---CRNK 628
Cdd:PRK12583 511 refCKAR 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
122-608 |
5.73e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 132.03 E-value: 5.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 122 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVD 201
Cdd:cd05934 5 TYAELLRESARIAAALAALGIR--PGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 202 kpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapedLAVICFTSGTTG 281
Cdd:cd05934 83 --------------------------------------------------------------------PASILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 282 NPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVEC-VMLCHGAKI--------GFFQGDIRllm 352
Cdd:cd05934 95 PPKGVVITHANLTFAGYYSARRFGLG----EDDVYLTVLPLFHINAQAVSVlAALSVGATLvllprfsaSRFWSDVR--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 353 ddlkVLQPTVF---PVVPRLLNRMFDRIFGQANttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslggRVR 429
Cdd:cd05934 168 ----RYGATVTnylGAMLSYLLAQPPSPDDRAH--------------------------------------------RLR 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 430 LmVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVC 509
Cdd:cd05934 200 A-AYGAPNPPELHEEFEER-FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGELV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 510 VK---GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQV 586
Cdd:cd05934 277 IRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREA 354
|
490 500
....*....|....*....|....*.
gi 1034638914 587 FVHG----ESLQAFLIAIVVPDVETL 608
Cdd:cd05934 355 AVVAvpdeVGEDEVKAVVVLRPGETL 380
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
266-574 |
1.06e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 133.18 E-value: 1.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFErvVECVMLCH---GAKIG 342
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 343 FFQG-DIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlLDFAskrkeaelRSGIIRNNSLwdrlifhkvq 421
Cdd:PLN02246 255 IMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL---------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 422 SSlggrVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTM-------PGDWTAGHVGAPMPCNLIKLVD 493
Cdd:PLN02246 298 SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:PLN02246 372 PETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAEL 450
|
.
gi 1034638914 574 E 574
Cdd:PLN02246 451 E 451
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
121-607 |
1.12e-32 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 131.50 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWV-----IIEQGCfAYsmviVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVG--PGDLVAVLLERSLEMVvailaVLKAGA-AY----VPLDPSYPAERLAYILEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 196 SLVFVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICF 275
Cdd:cd05930 86 KLVLTD-----------------------------------------------------------------PDDLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 276 TSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAH-MFerVVE-CVMLCHGAKI----GFFQGDIR 349
Cdd:cd05930 101 TSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEiFGALLAGATLvvlpEEVRKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 350 LLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslggrvr 429
Cdd:cd05930 175 ALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL------------------------------------------ 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 430 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT--MPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGE 505
Cdd:cd05930 213 VLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 506 GEVCVKGPNVFQGYLKDPAKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMR 579
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLA 370
|
490 500 510
....*....|....*....|....*....|.
gi 1034638914 580 SEPVAQVFV---HGESLQAFLIAIVVPDVET 607
Cdd:cd05930 371 HPGVREAAVvarEDGDGEKRLVAYVVPDEGG 401
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
121-557 |
1.18e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 132.31 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAIT-----YIVNKAEL 195
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVK--PGDRVAVQVEKSPEALALYLATLRAGAVFLPL-----NTAYTlaeldYFIGDAEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 196 SLVFVDkPEKAKLLLEGVENKlipGLKIIVVMDAYGS-ELVERGQrcgvevtsmkamedlGRANRRKPKPPAPEDLAVIC 274
Cdd:PRK07514 102 ALVVCD-PANFAWLSKIAAAA---GAPHVETLDADGTgSLLEAAA---------------AAPDDFETVPRGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 275 FTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH---MFerVVECVMLCHGAKIGFFQG-DIRL 350
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFT----PDDVLIHALPIFHthgLF--VATNVALLAGASMIFLPKfDPDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 351 LMDDLKvlQPTVFPVVP----RLL-NRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqsSLG 425
Cdd:PRK07514 237 VLALMP--RATVMMGVPtfytRLLqEPRLTR----------------------------------------------EAA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 426 GRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaGCCLTM-P--GDWTAGHVGAPMPCNLIKLVDVEEMNYMAA 502
Cdd:PRK07514 269 AHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TNMNTSnPydGERRAGTVGFPLPGVSLRVTDPETGAELPP 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1034638914 503 EGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:PRK07514 346 GEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
220-588 |
2.54e-32 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 129.69 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 220 GLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSA 299
Cdd:TIGR01733 72 GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 300 FVKATENTvnpcPDDTLISFLPLAHMFervveCVM-----LCHGAK--------IGFFQGDIRLLMDDLKVlqpTVFPVV 366
Cdd:TIGR01733 152 LARRYGLD----PDDRVLQFASLSFDA-----SVEeifgaLLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 367 PrllnrmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGgrVRLMVTGA-APVSATVLTF 445
Cdd:TIGR01733 220 P------------------------------------------SLLALLAAALPPALAS--LRLVILGGeALTPALVDRW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 446 LRAALGCQFYEGYGQTECTAGCCLT-----MPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYL 520
Cdd:TIGR01733 256 RARGPGARLINLYGPTETTVWSTATlvdpdDAPRESPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638914 521 KDPAKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:TIGR01733 335 NRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
111-603 |
1.09e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 129.72 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 111 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPE-WVIIEQGCFAySMVIVPLYDTLGNE 184
Cdd:PRK06188 23 KRYPDRPaLVLgdtrLTYGQLADRISRYIQAFEALGL--GTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 185 AITYIVNKAELSLVFVDK---PEKAKLLLEGVenkliPGLKIIVVMDA--YGSELvergqrcgvevtsmkamedLGRANR 259
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDL-------------------LAAAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 260 RKPKPP----APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEntvnpCPDDtlISFL---PLAHMFERVVEC 332
Cdd:PRK06188 156 FGPAPLvaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE-----WPAD--PRFLmctPLSHAGGAFFLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 333 VMLCHGAKI---GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFASKRKeAELrsgiirnn 409
Cdd:PRK06188 229 TLLRGGTVIvlaKF---DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDL-------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 410 slwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV------GAP 483
Cdd:PRK06188 281 ------------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 484 MPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 562
Cdd:PRK06188 345 TPGLRVALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-V 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1034638914 563 AQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQafliAIVVP 603
Cdd:PRK06188 421 TGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
113-578 |
2.00e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 129.48 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 113 KPDQPYEWlSYKQVAELSECIGSALIQKGFKTApdqfiGIFAQNRPEW---VIIEQGCFAYSMVIVPLYDTLGNEAITYI 189
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPG-----DRVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 190 VNKAElSLVF-----VDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVErgqrcgveVTSMKAMEDLGRANrrKPKP 264
Cdd:PRK06087 117 LNKCQ-AKMFfaptlFKQTRPVDLILPLQNQ--LPQLQQIVGVDKLAPATSS--------LSLSQIIADYEPLT--TAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 265 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHmfervvecvmlchgaKIGFF 344
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH---------------ATGFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 QGDIR-LLMDDLKVLQPTVFPVVP-RLLNRmfDRIFGQANTTlkRWLLDFASKRKEAELRSgiirnnslwdrlifhkvqS 422
Cdd:PRK06087 245 HGVTApFLIGARSVLLDIFTPDAClALLEQ--QRCTCMLGAT--PFIYDLLNLLEKQPADL------------------S 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 423 SLggrvRLMVTGAAPVSATVLtflRAAL--GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMN 498
Cdd:PRK06087 303 AL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-EARK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 499 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 578
Cdd:PRK06087 375 TLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILL 453
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
264-615 |
2.43e-31 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 127.43 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 341
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIFstLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 342 gFFQGDIRLLMDDLKVLqpTVFPVVPRLLnrmfdrifgqanTTLKRWLLDfaskrkeaelrsgiirnnslwdrlifhkvq 421
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSIL------------STLSPQDFP------------------------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 422 sslggRVRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLT--MPGDWTagHVGAPMPCNLIKLVDVEEMNY 499
Cdd:cd17653 210 -----NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQPV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 500 MAAEgEGEVCVKGPNVFQGYLKDPAKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 573
Cdd:cd17653 281 PEGV-VGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034638914 574 ENIYMRSEPVAQ---VFVHGEslqaFLIAIVVP---DVETLCSWAQKR 615
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
119-604 |
3.42e-31 |
|
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: 127.41 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 119 EWLSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLV 198
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 199 FVDkpekaklllegvenklipglkiivvmdaygSELVERGQRCGVevTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSG 278
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLP--VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 279 TTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFFQGDI----RLLM 352
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 353 DDLKVLQPTVFpvvprllnrmfdrifgQANTTLKRWLLDfaskrkeaelrSGiirnnslWDRLifhkvqsslgGRVRLMV 432
Cdd:cd12116 211 RLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR----------AGLTALC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 433 TGAA--PVSATVLTflraALGCQFYEGYGQTECT--AGCCLTMPGDwTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 508
Cdd:cd12116 247 GGEAlpPDLAARLL----SRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGEL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 509 CVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSE 581
Cdd:cd12116 321 YIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHP 399
|
490 500
....*....|....*....|....*
gi 1034638914 582 PVAQ--VFVHGESLQAFLIAIVVPD 604
Cdd:cd12116 400 GVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
255-598 |
1.97e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 126.29 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 255 GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC--------SAFVKatentvnPCPDDTLISF--LPLAH 324
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYH 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 325 MFERVVECVMlchGAKIGffqG---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfask 395
Cdd:PRK07059 264 IFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL--------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 396 rkeaelrsgiirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYG--QTECTAGCCLTMPG 473
Cdd:PRK07059 317 ------------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVDAT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 474 DWTaGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKII 553
Cdd:PRK07059 377 EFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIV 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034638914 554 DRKKHIFkLAQGEYIAPEKIENIyMRSEP----VAQVFVH----GESLQAFLI 598
Cdd:PRK07059 455 DRKKDMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
121-616 |
1.34e-29 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 122.10 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELslvfv 200
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVG--PGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 dkpekaklllegvenklipglKIIVVMDAYGSelvergqrcgvevTSMKAMedlgranrrkpkppaPEDLAVICFTSGTT 280
Cdd:cd05903 75 ---------------------KVFVVPERFRQ-------------FDPAAM---------------PDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVvecvmlcHGAKIGFFQGDIRLLMDdlkVLQP 360
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAERLGLG----PGDVFLVASPMAHQTGFV-------YGFTLPLLLGAPVVLQD---IWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 361 TVfpvVPRLLNRmfDRI-FGQANTTLKRWLLDfaskrkeAELRSGiirnnslwDRLifhkvqsslgGRVRLMVTGAAPVS 439
Cdd:cd05903 172 DK---ALALMRE--HGVtFMMGATPFLTDLLN-------AVEEAG--------EPL----------SRLRTFVCGGATVP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 440 ATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQ 517
Cdd:cd05903 222 RSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 518 GYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQ 594
Cdd:cd05903 301 GYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLG 378
|
490 500
....*....|....*....|....*...
gi 1034638914 595 AFLIAIVV------PDVETLCSWAQKRG 616
Cdd:cd05903 379 ERACAVVVtksgalLTFDELVAYLDRQG 406
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
173-604 |
2.61e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 125.04 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 173 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDaygseLVERgqrcgveVTSMKAME 252
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLED-----LKAK-------ISKVDKLT 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 253 DLGRA--------NRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAH 324
Cdd:PRK08633 759 ALLAArllparllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFH 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 325 MFERVVECVM-LCHGAKIGFFQGDirllMDDLKVLQ-------------PTVFpvvprllnRMFDRifgqaNTTLKRwlL 390
Cdd:PRK08633 835 SFGLTVTLWLpLLEGIKVVYHPDP----TDALGIAKlvakhratillgtPTFL--------RLYLR-----NKKLHP--L 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 391 DFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT 470
Cdd:PRK08633 896 MFAS---------------------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVN 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 471 MP-----GDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL---DKDGWLH 537
Cdd:PRK08633 943 LPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYV 1022
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638914 538 TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniymrsEPVAQVFvHGESLQafLIAIVVPD 604
Cdd:PRK08633 1023 TGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD 1079
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
120-628 |
4.33e-29 |
|
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: 121.64 E-value: 4.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 120 WLSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVF 199
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 200 VDKPekakLLLEgvenklipglkiivvmdaygsELVERGQRcgvevtsmkamedlgranRRKPKPPAPE-DLAVICFTSG 278
Cdd:cd12118 107 VDRE----FEYE---------------------DLLAEGDP------------------DFEWIPPADEwDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 279 TTGNPKGAMVTHRnivsdcSAFVKATENTV----NPCPddTLISFLPLAHmfervveCVMLCHGAKIGFFQG-------- 346
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANILewemKQHP--VYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrkv 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 347 DIRLLMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIRNNSlwdrlifHKVQSSLGG 426
Cdd:cd12118 209 DAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAP-------PSDARPLPH 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 427 RVRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDWTAGHV----------GAPMPCNL-IKLV 492
Cdd:cd12118 249 RVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAWKP-EWDELPTeerarlkarqGVRYVGLEeVDVL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 493 DVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 570
Cdd:cd12118 325 DPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISS 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638914 571 EKIENIymrsepvaqVFVHGESLQAFLIAivVPD---VETLCSW-AQKRGFEGSFEEL---CRNK 628
Cdd:cd12118 403 VEVEGV---------LYKHPAVLEAAVVA--RPDekwGEVPCAFvELKEGAKVTEEEIiafCREH 456
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
269-588 |
7.73e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 121.62 E-value: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVSD-CSAFVKATENTVNPCpddTLISFLPLAHMFERVVEC--VMLCHGAKIGFFQ 345
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMIGQV---VTLGLIPFFHIYGITGICcaTLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 346 GDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRLIFHKVqsslg 425
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 426 gRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTagcCLTMP-GDWTAGH-------VGAPMPCNLIKLVDVEE 496
Cdd:PLN02330 304 -KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 1034638914 577 YMRSEPVAQVFV 588
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
121-603 |
1.16e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 120.81 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLK--KGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DkPEKAKLLLEGVENKlipglkiivVMDAYGSELVERGQrcgVEVTSMKAMEDLGRANRRKPKPPAP--EDLAVICFTSG 278
Cdd:PRK08316 115 D-PALAPTAEAALALL---------PVDTLILSLVLGGR---EAPGGWLDFADWAEAGSVAEPDVELadDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 279 TTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVecvmlchgakigffqgdirLLMDDLKVL 358
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDMS----ADDIPLHALPLYHCAQLDV-------------------FLGPYLYVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 359 QPTVFPVVPRLlNRMFDRIFGQANTTLkrwlldFASKrkeaelrsgiirnnSLWDRLIFHKV-----QSSLggrvRLMVT 433
Cdd:PRK08316 239 ATNVILDAPDP-ELILRTIEAERITSF------FAPP--------------TVWISLLRHPDfdtrdLSSL----RKGYY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 434 GAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLTMPGDwTAGHVG-APMPC-NL-IKLVDvEEMNYMAAeGE-GEV 508
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAGRPVlNVeTRVVD-DDGNDVAP-GEvGEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 509 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:PRK08316 371 VHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAV 448
|
490
....*....|....*....
gi 1034638914 589 ----HGESLQAfLIAIVVP 603
Cdd:PRK08316 449 iglpDPKWIEA-VTAVVVP 466
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
173-575 |
2.15e-28 |
|
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: 119.08 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 173 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaYGSELVERGQRCGVEVTSMKAME 252
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG--------------------------AADRLRDALPASPDPGTVLDADG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 253 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVEC 332
Cdd:cd05922 102 IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT----ADDRALTVLPLSYDYGLSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 333 VMLCHGAKIgFFQGDIRL---LMDDLKVLQPTVFPVVPRLLNrMFDRIfgqanttlkrwlldfasKRKEAELrsgiirnN 409
Cdd:cd05922 178 THLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKL-------P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 410 SLwdRLIfhkvqSSLGGRVRlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTA---GHVGAPMPC 486
Cdd:cd05922 232 SL--RYL-----TQAGGRLP---------QETIARLRELLPGAQVYVMYGQTEATRRMT-YLPPERILekpGSIGLAIPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 487 NLIKLVDVEEMNYmaAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 565
Cdd:cd05922 295 GEFEILDDDGTPT--PPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-G 371
|
410
....*....|
gi 1034638914 566 EYIAPEKIEN 575
Cdd:cd05922 372 NRISPTEIEA 381
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
114-557 |
4.05e-28 |
|
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: 119.31 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 114 PDQPYEWLSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAQNRpEWVIIEQGC----FAYSMVIVPLYDTLGNEAITYI 189
Cdd:cd05906 33 ADGSEEFQSYQDLLEDARRLAAGLRQLGLR-PGDSVILQFDDNE-DFIPAFWACvlagFVPAPLTVPPTYDEPNARLRKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 190 VNKAELslvfVDKPekakLLLegVENKLIPGLKiivvmdaygsELVERGQRCGVEVTSMkamEDLGRANRRKPKPPA-PE 268
Cdd:cd05906 111 RHIWQL----LGSP----VVL--TDAELVAEFA----------GLETLSGLPGIRVLSI---EELLDTAADHDLPQSrPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHmferVVECVMlCHGAkigffqgDI 348
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLT----PQDVFLNWVPLDH----VGGLVE-LHLR-------AV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 349 RLLMDDLKVLQPTVFPVVPRLLnRMFDRIfgQANTTlkrWLLDFA-SKRKEAELRsgiiRNNSLWDrlifhkvQSSLggr 427
Cdd:cd05906 232 YLGCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPNFAfALLNDLLEE----IEDGTWD-------LSSL--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 428 vRLMVTGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGC--CLTMP-GDWTAGH----VGAPMPCNLIKLVDv 494
Cdd:cd05906 292 -RYLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVD- 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638914 495 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 557
Cdd:cd05906 370 DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
127-574 |
8.50e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 117.60 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 127 AELSECIG-SALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFvdkpek 205
Cdd:PRK09088 26 AELDALVGrLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 206 aklllegvenklipglkiivvmdayGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPapEDLAVICFTSGTTGNPKG 285
Cdd:PRK09088 100 -------------------------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 286 AMVTHRNIVSDCSAFVKATENTVNPcpddtliSFLPLAHMFERV--VECV--MLCHGAKIGFFQGdirllmddlkvLQPT 361
Cdd:PRK09088 153 VMLSERNLQQTAHNFGVLGRVDAHS-------SFLCDAPMFHIIglITSVrpVLAVGGSILVSNG-----------FEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 362 vfpvvpRLLNRMFDRIFGQANTtlkrwlldFASKRKEAELRSGIIRNNSLWDRLIfhkvqsslggrvrLMVTGAAP-VSA 440
Cdd:PRK09088 215 ------RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhAAE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 441 TVLTFLraALGCQFYEGYGQTEctAGCCLTMPGDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCVKGPNV 515
Cdd:PRK09088 268 DILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPAGV-PGELLLRGPNL 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638914 516 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09088 343 SPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
264-598 |
1.07e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.21 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 264 PPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpDDTLISFLPLAHMF-ERVVECVMLCHGAKI 341
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEG--EEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 342 GFF-QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqaNTTLkrwlldfaskRKEAELRSgiirnnslwdrlifhkv 420
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 421 qsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPgdW---TAGHVGAPMPCNLIKLVDVEEM 497
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFL--WekrVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 1034638914 578 MRSEPVAQVFV-------HGESLQAFLI 598
Cdd:PRK06710 474 YEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
89-694 |
1.46e-27 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 119.57 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 89 VTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCF 168
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVR--PGDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 169 AYSMVIVPLYDTlgNEAITYIVNKAELSLVFVDKPEKAKLL------LEGVENklipglkiivVMDAYGSELVERGQRCG 242
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILtcrsrkLETVVY----------THSFYDEDDHAVARDLN 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 243 VEVTSMKAMEDLGRANRRKPKPPAPED----LAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVkATENTVNPCPDDTLIS 318
Cdd:PTZ00297 572 ITLIPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVH 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 319 FLPLAHMFERVVECVMLCHGAKIGffQGDIRLLMDDLKVLQPTVFPVVPRLlnrmfdriFGQANTTLKR----------W 388
Cdd:PTZ00297 651 FTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysW 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 389 LLDfaskrKEAELRSGII---RNNSLWDRLIFHK-VQSSLGGRVRLMVTGAAPVSATvltflraalgcqfyegYGQTECT 464
Cdd:PTZ00297 721 LFE-----RAFQLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTS----------------FSLLEHI 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 465 AGCCltmpgdwtaghvgapMPCnliklvdVEEMNYMAAegEGEVCVKG---PNVfQGYLK---DPAKTAE----ALDKDG 534
Cdd:PTZ00297 780 SVCY---------------VPC-------LREVFFLPS--EGVFCVDGtpaPSL-QVDLEpfdEPSDGAGigqlVLAKKG 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 535 WL-HTGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAfLIAIVVPDVETL-CSW 611
Cdd:PTZ00297 835 EPrRTLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVeFEW 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 612 AQKRGFE---GSFEELCRNKDVKKA---ILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYF 685
Cdd:PTZ00297 914 RQSHCMGeggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYF 993
|
....*....
gi 1034638914 686 RSQIDDLYS 694
Cdd:PTZ00297 994 SSVIERFYS 1002
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
184-584 |
1.49e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 184 EAITYIVNKAELSLVFVDKPE-------KAKLLLEGVenkliPGLKIIVVMDayGSELVERGQRCGVEVTSMKAME---D 253
Cdd:PRK07529 119 EQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL-----PELRTVVEVD--LARYLPGPKRLAVPLIRRKAHArilD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 254 LGRANRRKP-------KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC---SAFVKATentvnpcPDDTLISFLPLA 323
Cdd:PRK07529 192 FDAELARQPgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLG-------PGDTVFCGLPLF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 324 HMFERVVEC-VMLCHGAKIGFF--QG--DIRLLMDDLKVL---QPTVFPVVPRLLNRMFDRIFGQANTtlkrwlldfask 395
Cdd:PRK07529 265 HVNALLVTGlAPLARGAHVVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDI------------ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 396 rkeaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GD 474
Cdd:PRK07529 333 --------------------------SSL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 475 WTAGHVGAPMPCNLIKLVDVEEM-NYM--AAEGE-GEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTL 550
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYF 461
|
410 420 430
....*....|....*....|....*....|....
gi 1034638914 551 KIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 584
Cdd:PRK07529 462 WLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
267-604 |
2.62e-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: 116.10 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLplAHMFE-RVVECVM-LCHGAKIGff 344
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT----SESRVLQFA--SYTFDvSILEIFTtLAAGGCLC-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 qgdI---RLLMDDLkvlqptvfpvvPRLLNRMfdrifgQANTtlkrwlldfaskrkeAELRSGIIRnnslwdrLIFHKVQ 421
Cdd:cd05918 177 ---IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLDPEDV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 422 SSLggrvRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIkLVDVEEMNYM 500
Cdd:cd05918 215 PSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW-VVDPDNHDRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 501 AAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:cd05918 288 VPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQ 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034638914 567 YIAPEKIENIYMRSEP-----VAQVFVH-GESLQAFLIAIVVPD 604
Cdd:cd05918 367 RVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLD 410
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
107-671 |
3.02e-27 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 116.76 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 107 PCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCF---AYSMVIVPLYDTLGN 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLS--AERPLLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 184 E--AITYIVNKAELSLVFVDKPEKAKLLLEGVenkLIPGLKIIVVmdaygselveRGQRCGVEVTSMK---AMEDLGRAN 258
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVVS----------RNAVAGRGAISFAelaATPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 259 RRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchG 338
Cdd:cd05921 157 AAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCA--NQAMLEQTYPFFGEEPPVLVDWLPWNHTF-----------G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 339 AKIGF-----------------FQGDIRLLMDDLKVLQPTVFPVVPR----LLNRMfdrifgQANTTLKRWLLdfasKRK 397
Cdd:cd05921 223 GNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVPAgwemLVAAL------EKDEALRRRFF----KRL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 398 EAELRSGIIRNNSLWDRLIFHKVQSSlGGRVRlmvtgaapvsatvltflraalgcqFYEGYGQTECTAGCCLTMPGDWTA 477
Cdd:cd05921 293 KLMFYAGAGLSQDVWDRLQALAVATV-GERIP------------------------MMAGLGATETAPTATFTHWPTERS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 478 GHVGAPMPCNLIKLVdveemnymAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKII 553
Cdd:cd05921 348 GLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 554 DRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLcsWAQKRGFEGSFEELCRNKDVK 631
Cdd:cd05921 420 GRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLAC--RRLVGLQEASDAEVLRHAKVR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1034638914 632 KAILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLT 671
Cdd:cd05921 497 AAFRDRLAALNGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
268-591 |
4.72e-27 |
|
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: 114.37 E-value: 4.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 268 EDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATENTVNPCPDDTLISFLPLAH------MFERVVE-CVMLCHGAk 340
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH----WWSAIGSALNLGLTEDDNWLCALPLFHisglsiLMRSVIYgMTVYLVDK- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 341 igFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLkrwlldfaskrkeaelrsgiirnnslwdrlifhkv 420
Cdd:cd05912 152 --FDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL----------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 421 qsslggrvRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPMPCNLIKLVDveem 497
Cdd:cd05912 192 --------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIED---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:cd05912 258 DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
330
....*....|....
gi 1034638914 578 MRSEPVAQVFVHGE 591
Cdd:cd05912 336 LSHPAIKEAGVVGI 349
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
262-576 |
7.73e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 115.71 E-value: 7.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 262 PKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVK-ATENTVNPCPDDTLISFLPLAHMFERVVECV-MLCHG 338
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfEASQYEYPGSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 339 AKI----GFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLKrwlldfaskrkeaelrsgiirnnslwdr 414
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 415 lifhkvqsSLggrvRLMVTGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTA----GCCLTMPGDWTAghVGAPMPCNLI 489
Cdd:PLN02574 320 --------SL----KQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 490 KLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 569
Cdd:PLN02574 386 KVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIA 464
|
....*..
gi 1034638914 570 PEKIENI 576
Cdd:PLN02574 465 PADLEAV 471
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
119-590 |
1.09e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.57 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 119 EWLSYKQVAELSECIGSALIQKgFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAITyivnKAELSLV 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYE-LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL-----NIRLT----ENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 199 FVDKpekaklllegvenklipGLKIIVVMDAYGSELVERGQRCGVE----VTSMKAMEDLGRANRrkpKPPAPEDLAVIC 274
Cdd:PRK06839 96 LKDS-----------------GTTVLFVEKTFQNMALSMQKVSYVQrvisITSLKEIEDRKIDNF---VEKNESASFIIC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 275 FTSGTTGNPKGAMVTHRNIvsdcsaFVKATEN--TVNPCPDDTLISFLPLAHMfervvecvmlchgAKIGFFQgdirllm 352
Cdd:PRK06839 156 YTSGTTGKPKGAVLTQENM------FWNALNNtfAIDLTMHDRSIVLLPLFHI-------------GGIGLFA------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 353 ddlkvlQPTVFP----VVPRLLN-----RMFDR-----IFGQAntTLKRWLLDfASKRKEAELRSgiirnnslwdrlifh 418
Cdd:PRK06839 210 ------FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS--------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 419 kvqsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLVDvEE 496
Cdd:PRK06839 266 ---------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-EN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 576
Cdd:PRK06839 335 KNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV 412
|
490
....*....|....
gi 1034638914 577 YMRSEPVAQVFVHG 590
Cdd:PRK06839 413 INKLSDVYEVAVVG 426
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
121-598 |
1.57e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 112.96 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKTApdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAelslvfv 200
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 dkpekaklllegvenklipGLKIIVVmdayGSELvergqrcgvevtsmkamedlgranrrkpkppapEDLAVICFTSGTT 280
Cdd:cd05935 73 -------------------GAKVAVV----GSEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHM--FERVVECVMLCHGAKIGFFQGDIRLLMDDLKVL 358
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 359 QPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPV 438
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--------ATPEFKTRDLSS---------------------------------LKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 439 SATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQG 518
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 519 YLKDPAKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV------- 588
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|
gi 1034638914 589 HGESLQAFLI 598
Cdd:cd05935 371 VGEEVKAFIV 380
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
121-624 |
1.77e-26 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 114.44 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVK--KGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 D----KPEKAKLLLEGVEN--KLIPGLKIIVVMDAYGSELVERGQRcgvevtsmkAMEDLgRANRRKPKPPAP---EDLA 271
Cdd:COG0365 118 AdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEGDL---------DWDEL-LAAASAEFEPEPtdaDDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 272 VICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLA----HMFervveCVM--LCHGAKIGFFQ 345
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVFWCTADIGwatgHSY-----IVYgpLLNGATVVLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 346 GDI------RL--LMDDLKVlqpTVFPVVPRLLnRMfdrifgqanttLKRWLLDFASKrkeaelrsgiirnnslWDRlif 417
Cdd:COG0365 260 GRPdfpdpgRLweLIEKYGV---TVFFTAPTAI-RA-----------LMKAGDEPLKK----------------YDL--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 418 hkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT-AGHVGAPMPCNLIKLVDvEE 496
Cdd:COG0365 306 ----SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD-ED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 497 MNYMAAEGEGEVCVKG--PNVFQGYLKDPAKTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 572
Cdd:COG0365 377 GNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAE 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638914 573 IENIYMRSEPVAQVFV----HGESLQAfLIAIVVPdvetlcswaqKRGFEGSfEEL 624
Cdd:COG0365 456 IESALVSHPAVAEAAVvgvpDEIRGQV-VKAFVVL----------KPGVEPS-DEL 499
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
112-646 |
2.99e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 114.21 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 112 RKPDQPY--------EW--LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---Y 178
Cdd:PRK08180 51 EAPDRVFlaergadgGWrrLTYAEALERVRAIAQALLDRGL--SAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 179 DTLGN--EAITYIVNKAELSLVFVDKPEKAKLLLEGVEnklIPGLKIIVVmdaygselveRGQRCGVEVTSMKAMEDLGR 256
Cdd:PRK08180 129 SLVSQdfGKLRHVLELLTPGLVFADDGAAFARALAAVV---PADVEVVAV----------RGAVPGRAATPFAALLATPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 257 ANRRKPKPPA--PEDLAVICFTSGTTGNPKGAMVTHRNIVS------DCSAFVKATEntvnpcPddTLISFLPLAHMFER 328
Cdd:PRK08180 196 TAAVDAAHAAvgPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEP------P--VLVDWLPWNHTFGG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 329 VVEC-VMLCHGAKI---------GFFQGDIRllmdDLKVLQPTVFPVVPR--------------LLNRMFDRifgqantt 384
Cdd:PRK08180 268 NHNLgIVLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemlvpalerdaaLRRRFFSR-------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 385 LKrwLLDFASkrkeAELRSgiirnnSLWDRLifHKV-QSSLGGRVRLMVtgaapvsatvltflraalgcqfyeGYGQTEc 463
Cdd:PRK08180 336 LK--LLFYAG----AALSQ------DVWDRL--DRVaEATCGERIRMMT------------------------GLGMTE- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 464 TAGCCL--TMPGDwTAGHVGAPMPCNLIKLVDVEemnymaaeGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDI 541
Cdd:PRK08180 377 TAPSATftTGPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 542 GKWL----PNGTLKIIDRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVEtLCSWAQKR 615
Cdd:PRK08180 448 VRFVdpadPERGLMFDGRIAEDFKLSSGTWVSvgPLRARAVSAGAPLVQDVVITGHD-RDEIGLLVFPNLD-ACRRLAGL 525
|
570 580 590
....*....|....*....|....*....|.
gi 1034638914 616 GFEGSFEELCRNKDVKKAILEDMVRLGKDSG 646
Cdd:PRK08180 526 LADASLAEVLAHPAVRAAFRERLARLNAQAT 556
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
152-615 |
3.40e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 113.33 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 152 IFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAklLLEGVENkLIPGLKIIVVMDAYG 231
Cdd:PRK07786 72 ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRD-IVPLLSTVVVAGGSS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 232 SELVergqrcgvevtsmKAMEDLGRANRrKPKPPA--PEDL-AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTV 308
Cdd:PRK07786 149 DDSV-------------LGYEDLLAEAG-PAHAPVdiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 309 NpcpDDtlISFL--PLAHM--FERVVECVMLchGAKIgffqgdirllmddlkVLQPTvfpvvprllnRMFDrifgqANTT 384
Cdd:PRK07786 215 N---SD--VGFVgvPLFHIagIGSMLPGLLL--GAPT---------------VIYPL----------GAFD-----PGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 385 LKRWlldfaskrkEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEC 463
Cdd:PRK07786 258 LDVL---------EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 464 TAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDI 541
Cdd:PRK07786 329 SPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 542 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAF---LIAIVVPD-------VETLCSW 611
Cdd:PRK07786 407 VRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEF 485
|
....
gi 1034638914 612 AQKR 615
Cdd:PRK07786 486 LTDR 489
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
121-603 |
5.15e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.84 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAElSLVFV 200
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLG--VGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 --------DKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERgqrcgveVTSMKAME---DLGR--ANRRkpkpPAP 267
Cdd:PRK13295 133 vpktfrgfDHAAMARRLRPE-----LPALRHVVVVGGDGADSFEA-------LLITPAWEqepDAPAilARLR----PGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvecvmlchgakIGFFQGD 347
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLG----ADDVILMASPMAHQ---------------TGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 348 IRLLMDDLK-VLQPTVFPVvprllnRMFDRI------FGQANTTlkrWLLDFASKRKEAElrsgiirnnslwdrlifhKV 420
Cdd:PRK13295 258 MMPVMLGATaVLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESG------------------RP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 421 QSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLTMPGD---WTAGHVGAPMPCNLIKLVDVEEM 497
Cdd:PRK13295 311 VSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDADGA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 NYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 577
Cdd:PRK13295 386 PLPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALL 461
|
490 500
....*....|....*....|....*....
gi 1034638914 578 MRSEPVAQVFVHG---ESLQAFLIAIVVP 603
Cdd:PRK13295 462 YRHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-608 |
1.81e-25 |
|
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: 113.03 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 86 YDDVTTLYEGFQRgiQVSnngpclgsRKPDQP-----YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEW 160
Cdd:COG1020 472 YPADATLHELFEA--QAA--------RTPDAVavvfgDQSLTYAELNARANRLAHHLRALGVG--PGDLVGVCLERSLEM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 161 VIIEQGCF----AYsmviVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVEnklipglkiIVVMDAygselve 236
Cdd:COG1020 540 VVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVP---------VLALDA------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 237 rgqrcgvevtsmkamEDLGRANRRKPKPPA-PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDT 315
Cdd:COG1020 600 ---------------LALAAEPATNPPVPVtPDDLAYVIYTSGSTGRPKGVMVEHRALV----NLLAWMQRRYGLGPGDR 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 316 LISFLPLAH------MFervvecVMLCHGAKIGFFQGDIRLLMDDLKVL----QPTVFPVVPRLLNRMFDrifgqanttl 385
Cdd:COG1020 661 VLQFASLSFdasvweIF------GALLSGATLVLAPPEARRDPAALAELlarhRVTVLNLTPSLLRALLD---------- 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 386 krwlldfaskrkeaelrsgiirnnSLWDRLifhkvqsslgGRVRLMVTG--AAPVsATVLTFLRAALGCQFYEGYGQTEC 463
Cdd:COG1020 725 ------------------------AAPEAL----------PSLRLVLVGgeALPP-ELVRRWRARLPGARLVNLYGPTET 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 464 TAGCCL--TMPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDG 534
Cdd:COG1020 770 TVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPG 848
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638914 535 --WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQ--VFVHGESLQA-FLIAIVVPDVETL 608
Cdd:COG1020 849 arLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAA 926
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
269-606 |
7.32e-25 |
|
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: 106.20 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFvkATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK---IGFFQ 345
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 346 GDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiIRNnslwdrlifhkvqssl 424
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 425 ggrvrlmVTGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 503
Cdd:cd17637 119 -------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 504 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYMRSE 581
Cdd:cd17637 187 ETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1034638914 582 PVAQVFVHGeslqafliaivVPDVE 606
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
111-604 |
7.74e-25 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 108.57 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 111 SRKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTL 181
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVG--PDTIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 182 GNEAITYIVNKAELSLVFVDKPEKAKLLLEGvenklipglkIIVVMDAygselvergqrcgvEVTSMKAMEDLGRANRrk 261
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENLEPVSK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 262 pkppaPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGA 339
Cdd:cd17655 136 -----SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASIS--FDASVTEIFasLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 340 KIgffqgdirllmddLKVLQPTVFPVVPrllnrmFDRIFGQANTTLkrwlldfaSKRKEAELRsgiirnnslwdrlIFHK 419
Cdd:cd17655 205 TL-------------YIVRKETVLDGQA------LTQYIRQNRITI--------IDLTPAHLK-------------LLDA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 420 VQSSLGGRVRLMVTGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCC--LTMPGDWTAGHV--GAPMPCNLIKLVD 493
Cdd:cd17655 245 ADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYEPETDQQVSVpiGKPLGNTRIYILD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:cd17655 325 -QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYR 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034638914 568 IAPEKIENIYMRSEPVAQ--VFVH-GESLQAFLIAIVVPD 604
Cdd:cd17655 403 IELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE 442
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
119-583 |
7.85e-25 |
|
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: 109.25 E-value: 7.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 119 EWLSYKQVAELSECIGSALIQKGfktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA---ITYIVNKAEL 195
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG---KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 196 SLVFVDKPEKAKLLLEGVENKLIPGLKIIVVmDAYGSELVERGQrcgvevtsmkamedlgranrrkPKPPAPEDLAVICF 275
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLLVV-DLLPDTSAADWP----------------------PPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH-MfervvecvmlchgakiGFFQGdirllmdd 354
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLD----PGDVVVSWLPLYHdM----------------GLIGG-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 355 lkVLQPTV--FPVV---PR-LLNRMFdrifgqanttlkRWL-----------------LDFASKRKEAELRSGIirnnsl 411
Cdd:cd05931 209 --LLTPLYsgGPSVlmsPAaFLRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL------ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 412 wdRLifhkvqsslgGRVRLMVTGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT----------AGCCLTMPGDW 475
Cdd:cd05931 269 --DL----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 476 TAGHV----------------GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE------ALDKD 533
Cdd:cd05931 337 LAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEG 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1034638914 534 GWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 583
Cdd:cd05931 417 GWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
121-682 |
6.69e-24 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 105.11 E-value: 6.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAqNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLR-KGDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapEDLAVICFTSGTT 280
Cdd:cd05972 79 DA-----------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVS---DCSAFVKATENTVNPCPDDT------LISFL-PLAHMFervveCVMLCHGAKIgffqgDIRL 350
Cdd:cd05972 94 GLPKGVLHTHSYPLGhipTAAYWLGLRPDDIHWNIADPgwakgaWSSFFgPWLLGA-----TVFVYEGPRF-----DAER 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 351 LMDDLKVLQPTVFPVVPrllnrmfdrifgqanTTLKRWL-LDFASKRKeaelrsgiirnnslwdrlifhkvqsslgGRVR 429
Cdd:cd05972 164 ILELLERYGVTSFCGPP---------------TAYRMLIkQDLSSYKF----------------------------SHLR 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 430 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLTMPgdWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGE 507
Cdd:cd05972 201 LVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLtvGNFPDMP--VKPGSMGRPTPGYDVAIID-DDGRELPPGEEGD 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 508 VCVKGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQ 585
Cdd:cd05972 278 IAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAE 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 586 VFV-------HGESLQAFLIAivvpdvetlcswaqKRGFEGSfEELcrnkdvkkaiLEDMVRLGKdSGLKPFEQVKGITL 658
Cdd:cd05972 356 AAVvgspdpvRGEVVKAFVVL--------------TSGYEPS-EEL----------AEELQGHVK-KVLAPYKYPREIEF 409
|
570 580
....*....|....*....|....
gi 1034638914 659 HPELfsidngLLTPTMKAKRPELR 682
Cdd:cd05972 410 VEEL------PKTISGKIRRVELR 427
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
266-607 |
1.41e-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: 104.25 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAHMFervveCVM-----LCHGAk 340
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFSFDL-----SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 341 igffqgdirllmddlkvlqpTVFPVvPRLLNRMFDRIF-GQANTTLKRWLldfaskrkeaelrsgiiRNNSLWDRLIFHK 419
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVWV-----------------STPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 420 --VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTmpgDWT----AGH----VGAPMPCNLI 489
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYI---EVTpevlDGYdrlpIGYAKPGAKL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 490 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 566
Cdd:cd05945 284 VILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGY 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034638914 567 YIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDVET 607
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGA 405
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
121-682 |
1.58e-23 |
|
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: 104.76 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DkPEKAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgqrcgvevtsmKAMEDL--GRANRRKPKPPAPEDLAVICFTSG 278
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGPEAGA------------LLLAELvaAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 279 TTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLAHMFErvvecvmLCHGAKIGFFQGDIRLLM------ 352
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 353 ----DDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWdrlifhkvQSSLGGRV 428
Cdd:cd05959 244 aavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAPNL--------PSRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 429 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 508
Cdd:cd05959 283 RLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 509 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 589 HGESLQAFLI---AIVVPdvetlcswaqKRGFEGSfeelcrnkdvkkAILEDMVRLGKDSGLKPFEQVKGITLHPELFSi 665
Cdd:cd05959 440 VGVEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRLAPYKYPRWIVFVDELPK- 496
|
570
....*....|....*..
gi 1034638914 666 dngllTPTMKAKRPELR 682
Cdd:cd05959 497 -----TATGKIQRFKLR 508
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
111-615 |
3.20e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 104.35 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 111 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPlydtlgnea 185
Cdd:PRK06178 44 RERPQRPaIIFyghvITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVP--------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 186 ITYIVNKAELSLVFVDKpekaklllegvenklipGLKIIVVMDAYgSELVER-GQRCGVE---VTSMKAM---------- 251
Cdd:PRK06178 113 VSPLFREHELSYELNDA-----------------GAEVLLALDQL-APVVEQvRAETSLRhviVTSLADVlpaeptlplp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 252 -------------EDLGRANRRKPKP-----PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATentVNPCPD 313
Cdd:PRK06178 175 dslraprlaaagaIDLLPALRACTAPvplppPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVA---VVGGED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 314 DTLISFLPlahMFervvecvmlchgakigFFQGDirllmdDLKVLQPTVF--PVVprLLNRmfdrifgqanttlkrwlld 391
Cdd:PRK06178 252 SVFLSFLP---EF----------------WIAGE------NFGLLFPLFSgaTLV--LLAR------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 392 faskrkeaelrsgiirnnslWDRLIF------HKVQSSLG---GRVRLMVTGAapVSATVLTFL---------------- 446
Cdd:PRK06178 286 --------------------WDAVAFmaaverYRVTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdy 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 447 ----RAALGCQFYEG-YGQTEcTAGCcltmpGDWTAG-------------HVGAPMPCNLIKLVDVEEMNYMAAEGEGEV 508
Cdd:PRK06178 344 rqrwRALTGSVLAEAaWGMTE-THTC-----DTFTAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEI 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 509 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAV 495
|
570 580 590
....*....|....*....|....*....|....*.
gi 1034638914 589 HG---ESLQAFLIAIVVP------DVETLCSWAQKR 615
Cdd:PRK06178 496 VGrpdPDKGQVPVAFVQLkpgadlTAAALQAWCREN 531
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
123-615 |
3.37e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 103.50 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 123 YKQVAELSECIGSALIQKGfktapdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDk 202
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 203 pekaklllEGVENKLIPGLKIIVvmdaygSELVErgqrcgvevtsmkamedlGRANRRKPKPPAPED-LAVICFTSGTTG 281
Cdd:PRK03640 107 --------DDFEAKLIPGISVKF------AELMN------------------GPKEEAEIQEEFDLDeVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 282 NPKGAMVTHRNivsdcsAFVKATENTVNP--CPDDTLISFLPLAH------MFERVVE-CVMLCH----GAKIgffqgdI 348
Cdd:PRK03640 155 KPKGVIQTYGN------HWWSAVGSALNLglTEDDCWLAAVPIFHisglsiLMRSVIYgMRVVLVekfdAEKI------N 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 349 RLLMDDlKVlqpTVFPVVPRLLNRMFDRIfGQANTtlkrwlldfaskrkeaelrsgiirNNSLwdrlifhkvqsslggrv 428
Cdd:PRK03640 223 KLLQTG-GV---TIISVVSTMLQRLLERL-GEGTY------------------------PSSF----------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 429 RLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPM-PCNlIKLVDveEMNYMAAEG 504
Cdd:PRK03640 257 RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 505 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 584
Cdd:PRK03640 332 EGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVA 409
|
490 500 510
....*....|....*....|....*....|....*...
gi 1034638914 585 QVFVHGESLQ-------AFLIAIVVPDVETLCSWAQKR 615
Cdd:PRK03640 410 EAGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
121-603 |
3.69e-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: 103.71 E-value: 3.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALiqKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfV 200
Cdd:TIGR03098 26 LTYAALSERVLALASGL--RGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRrkPKPPAPEDLAVICFTSGTT 280
Cdd:TIGR03098 103 TSSERLDLLHPA-----LPGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADP--PHPVIDSDMAAILYTSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmfervvecvmlchgakigffqgdirllmddlkvlqp 360
Cdd:TIGR03098 176 GRPKGVVLSHRNLVAGAQSVATYLENR----PDDRLLAVLPLS------------------------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 361 tvfpvvprllnrmFDRIFGQANTTL----KRWLLDFASKRK-----EAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLM 431
Cdd:TIGR03098 215 -------------FDYGFNQLTTAFyvgaTVVLHDYLLPRDvlkalEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 432 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTmPG--DWTAGHVGAPMPcNLIKLVDVEEMNYMAAEGEGEV 508
Cdd:TIGR03098 282 TNSGGAMPRATLSRLRSFLPnARLFLMYGLTEAFRSTYLP-PEevDRRPDSIGKAIP-NAEVLVLREDGSECAPGEEGEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 509 CVKGPNVFQGYLKDPAKTAEALDK----DGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 577
Cdd:TIGR03098 360 VHRGALVAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA 438
|
490 500 510
....*....|....*....|....*....|
gi 1034638914 578 MRSEPVAQVFVHG----ESLQAfLIAIVVP 603
Cdd:TIGR03098 439 YATGLVAEAVAFGvpdpTLGQA-IVLVVTP 467
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
269-615 |
3.77e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 100.87 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATENTVNPCPDDTLISFLPLAHM--FERVVECVMLchGAKIGFFQG 346
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--AGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 347 DiRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslgg 426
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 427 rVRLMVTGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEG 506
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 507 EVCVKGPNVFQGYLKDPakTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQV 586
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350
....*....|....*....|....*....|....*.
gi 1034638914 587 FVHG---ESLQAFLIAIVV----PDVETLCSWAQKR 615
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVgrgpADPAELRAWLKDK 292
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
121-604 |
5.66e-23 |
|
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: 103.05 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWV-----IIEQGCfAYsmviVPLYDTLGNEAITYIVNKAEL 195
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGV--GPGDVVGVLAERSPELVvallaVLKAGA-AY----VPLDPELPAERLAFMLADAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 196 SLVFVDKPEKAklllegvenkLIPGLKIIVVMDAYGSELVERGQRCgvevtsmkamedlgranrrkpkPPAPEDLAVICF 275
Cdd:cd12117 96 KVLLTDRSLAG----------RAGGLEVAVVIDEALDAGPAGNPAV----------------------PVSPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 276 TSGTTGNPKGAMVTHRNIVSdcsaFVKATeNTVNPCPDDTLISFLPL---AHMFERVVEcvmLCHGAKIgffqgdirllm 352
Cdd:cd12117 144 TSGSTGRPKGVAVTHRGVVR----LVKNT-NYVTLGPDDRVLQTSPLafdASTFEIWGA---LLNGARL----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 353 ddlkVLQPtvfPVVPRLLNRMFDRIFGQANTTLkrWLldfaskrkeaelrsgiirNNSLWdRLIFHKVQSSLGGrVRLMV 432
Cdd:cd12117 205 ----VLAP---KGTLLDPDALGALIAEEGVTVL--WL------------------TAALF-NQLADEDPECFAG-LRELL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 433 TGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCCLTMPGDWTAGHV--GAPMPcNLIKLVdVEEMNYMAAEGE-G 506
Cdd:cd12117 256 TGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIA-NTRVYV-LDEDGRPVPPGVpG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 507 EVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRS 580
Cdd:cd12117 334 ELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAH 412
|
490 500
....*....|....*....|....*..
gi 1034638914 581 EPVAQVFV---HGESLQAFLIAIVVPD 604
Cdd:cd12117 413 PGVREAVVvvrEDAGGDKRLVAYVVAE 439
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
267-624 |
1.35e-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: 99.86 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVMLchgakigFFQG 346
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 347 DIRLLMDDLKVLQPTVFPVVPRLLNRMfdRIfgQANTTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLgg 426
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 427 rvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GDWTAGHVGAPMPCNLIKLVDVE-EMNYM--AA 502
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 503 EGE-GEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 581
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034638914 582 PVaqvfvhgeslqAFLIAIVVPDV---ETLCSWAQ-KRGFEGSFEEL 624
Cdd:cd05944 280 AV-----------AFAGAVGQPDAhagELPVAYVQlKPGAVVEEEEL 315
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
112-606 |
7.24e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 100.03 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 112 RKPDQPYEW-----LSYKQVAELSECIGSAL-----IQKGfktapDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTL 181
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLqqecgVRKG-----DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 182 GNEAITYIVNKAELSLVFVdkpekAKLLLEGVEnKLI--PGLKIIVV------MDAYGSE-----LVERGQRCGVEVTSM 248
Cdd:PRK08314 96 REEELAHYVTDSGARVAIV-----GSELAPKVA-PAVgnLRLRHVIVaqysdyLPAEPEIavpawLRAEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 249 KAMEDLGRANRRkpkPPA----PEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPcpDDTLISFLPLAH 324
Cdd:PRK08314 170 VAWKEALAAGLA---PPPhtagPDDLAVLPYTSGTTGVPKGCMHTHRTVM--ANAVGSVLWSNSTP--ESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 325 mferVVECVMLCHGAkigFFQGDIRLLMddlkvlqptvfpvvPR----LLNRMFDR---IFGQANTTLkrwLLDFaskrk 397
Cdd:PRK08314 243 ----VTGMVHSMNAP---IYAGATVVLM--------------PRwdreAAARLIERyrvTHWTNIPTM---VVDF----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 398 eaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG----------- 466
Cdd:PRK08314 294 ---LASPGLAERDL----------SSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpkl 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 467 CCLTMPgdwTAGhVGApmpcnliKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA---LDKDGWLHTGDIGK 543
Cdd:PRK08314 357 QCLGIP---TFG-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGR 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 544 WLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVPDVE 606
Cdd:PRK08314 426 MDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
121-576 |
1.22e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 100.43 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGsALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKN--TPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKP--EKAKL--LLEGVENklipGLKIIVVMDaygselVERGQRCGVEVTSMKAmedlGRANRRKPKPPAPEDLAVICFT 276
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 277 SGTTGNPKGAMVTHRNIVSDC---SAFVKATentvnpcPDDTLISFLPLAHMFervvecvmlchgakiGFFQGDIRLLMD 353
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLANRaqvAARIDFS-------PEDKVFNALPVFHSF---------------GLTGGLVLPLLS 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 354 DLKVL---QPTVFPVVPRLlnrmfdrIFgQANTTL----KRWLLDFASKRKEAELRSgiirnnslwdrlifhkvqsslgg 426
Cdd:PRK06814 860 GVKVFlypSPLHYRIIPEL-------IY-DTNATIlfgtDTFLNGYARYAHPYDFRS----------------------- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 427 rVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNymaaEGeG 506
Cdd:PRK06814 909 -LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-G 982
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034638914 507 EVCVKGPNVFQGYLK-DPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:PRK06814 983 RLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEEL 1051
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
268-599 |
1.30e-21 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 98.30 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISflpLAHMFErvveCVMLCHGAKIGFFQGD 347
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 348 IRLLMDD----------LKVLQPTVFPVVPRLlnrmfdrifgqanttlkrwlldFASKRKEAELRSGIIRNnslwdrlif 417
Cdd:cd05919 161 SAVLNPGwptaervlatLARFRPTVLYGVPTF----------------------YANLLDSCAGSPDALRS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 418 hkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEM 497
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 577
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*....
gi 1034638914 578 MRSEPVAQVFV------HGES-LQAFLIA 599
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
121-626 |
1.36e-21 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 98.74 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVF- 199
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 200 -VDKPekakllleGVENKLIPGLKIIVVMDAYGSelvergqrcGVEVTSMKAMEDlgranrrkpKPPAPEDLAVICFTSG 278
Cdd:cd05923 107 aVDAQ--------VMDAIFQSGVRVLALSDLVGL---------GEPESAGPLIED---------PPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 279 TTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMfervvecvmlchgakIGFFQgdirLLMDDLkVL 358
Cdd:cd05923 161 TTGLPKGAVIPQRAAES--RVLFMSTQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-AL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 359 QPTVFPVvprllnRMFDRIFgqanttlkrwlldfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGAAP 437
Cdd:cd05923 219 DGTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 438 VSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMPgDWTAGHVGAPMPCNLIKLVDV-EEMNYMAAEG-EGEVCVK--GP 513
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 514 NVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG--- 590
Cdd:cd05923 356 AAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvad 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 1034638914 591 ESLQAFLIAIVVPDVETLCswaqkrgfEGSFEELCR 626
Cdd:cd05923 434 ERWGQSVTACVVPREGTLS--------ADELDQFCR 461
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
266-696 |
1.56e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 99.10 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHM--FERVVECVML--CHGAKI 341
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAI----VGYGEDDVYLHTAPLCHIggLSSALAMLMVgaCHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 342 GFfqgDIRLLMDDLKVLQPTVFPVVPRLL------NRMfdRIFGQANTTLKRWLldfaskrkeaelrSGiirNNSLWDRL 415
Cdd:PLN02860 246 KF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRKIL-------------NG---GGSLSSRL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 416 IfhKVQSSLGGRVRLMVTGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCLTMPGDWTAGH-VGAPMPcnliklvDV 494
Cdd:PLN02860 305 L--PDAKKLFPNAKLFSAYGMTEACSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP-------HV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 495 EEMNYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 573
Cdd:PLN02860 374 ELKIGLdESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 574 ENIYMRSEPVAQVFVHGeSLQAFLIAIVVPDVETLCSW--------AQKRGFEGSFEEL---CRNKdvkkailedmvrlg 642
Cdd:PLN02860 453 EAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK-------------- 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1034638914 643 kdsGLKPFEQVKGITLHPELFSidnglLTPTMKAKRPELRNYFRSQIDDLYSTI 696
Cdd:PLN02860 518 ---NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
266-682 |
1.84e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 97.89 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPlahmfervvecvmlchgAKIGFFQ 345
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLGH----LPGVQFPFNLFPRDGDLYWTP-----------------ADWAWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 346 GdirlLMDdlkVLQPTVFPVVPRLLNRM--FDRifGQANTTLKRWLLDFASKRKEAeLRsgIIRnnslwdrliFHKVQSS 423
Cdd:cd05971 145 G----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 424 LGG-RVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC---TAGCCLTMPGDwtAGHVGAPMPCNLIKLVDvEEMNY 499
Cdd:cd05971 204 HAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 500 MAAEGEGEVCVKGPN--VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 577
Cdd:cd05971 281 LPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 578 MRSEPVAQVFV-------HGESLQAFliaIVVpdvetlcswaqKRGFEGSfEELCRNkdvkkaiLEDMVRlgkdSGLKPF 650
Cdd:cd05971 359 LKHPAVLMAAVvgipdpiRGEIVKAF---VVL-----------NPGETPS-DALARE-------IQELVK----TRLAAH 412
|
410 420 430
....*....|....*....|....*....|..
gi 1034638914 651 EQVKGITLHPELfsidngLLTPTMKAKRPELR 682
Cdd:cd05971 413 EYPREIEFVNEL------PRTATGKIRRRELR 438
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
121-603 |
3.25e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.03 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGL--LPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKpekaklllEGVENKLIPGLKIIVVMDAYGSElveRGQRCG-VEVTsmkamedLGRANRRKPKPPAPEDL----AVICF 275
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGD---SGPSGGtLSVH-------LDAATEPTPATSTPEGLrpddAMIMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECV-MLCHGAKI-----GFFQGdiR 349
Cdd:PRK05852 184 TGGTTGLPKMVPWTHANIASSVRAIITGYRLS----PRDATVAVMPLYHGHGLIAALLaTLASGGAVllparGRFSA--H 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 350 LLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFA----SKRKEAELRsgIIRNNSlwdrlifhkvqsslg 425
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKPAALR--FIRSCS--------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 426 grvrlmvtgaAPVSATVLTFLRAALGCQFYEGYGQTECT----------AGCCLTmPGDWT--AGHVGAPMpcnlIKLVD 493
Cdd:PRK05852 305 ----------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQTEN-PVVSTglVGRSTGAQ----IRIVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 VEEMNYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 573
Cdd:PRK05852 370 SDGLPLPAGA-VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERV 446
|
490 500 510
....*....|....*....|....*....|...
gi 1034638914 574 ENIYMRSEPVAQVFVHGESLQAF---LIAIVVP 603
Cdd:PRK05852 447 EGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
264-604 |
3.92e-21 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 97.41 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 341
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 342 GFFQGDIRllMDDlkvlqptvfpvvprllnrmfdrifgqanTTLKRWLldfaskrkeAELR-SGIIRNNSLWDRLIFH-K 419
Cdd:cd17651 206 VLPPEEVR--TDP----------------------------PALAAWL---------DEQRiSRVFLPTVALRALAEHgR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 420 VQSSLGGRVRLMVTGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLTMPGD---WTA-GHVGAPMPCNLIKLVD 493
Cdd:cd17651 247 PLGVRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:cd17651 327 -AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034638914 568 IAPEKIENIYMRSEPVAQ--VFVHGE-SLQAFLIAIVVPD 604
Cdd:cd17651 405 IELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGD 444
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
268-576 |
8.27e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 94.25 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGD 347
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVV---GDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 348 IRL--LMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfaskrkeaELRSGIIRNNSLwdRLIfhkvqsslg 425
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKLVS------------------------ELKSANATVPSL--RLI--------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 426 grvrlMVTGAAPVSATVLTFLRAALgCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAeG 504
Cdd:cd17635 123 -----GYGGSRAIAADVRFIEATGL-TNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034638914 505 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 576
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
70-604 |
1.27e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.72 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 70 ARRS----ALLDSDEplvyfYDDVTTLY----EGFQRGIQVSNNGPCLGSRKPDQPY-----EWLSYKQVAELSECIGSA 136
Cdd:PRK12316 1970 AQAAlgelALLDAGE-----RQRILADWdrtpEAYPRGPGVHQRIAEQAARAPEAIAvvfgdQHLSYAELDSRANRLAHR 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 137 LIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGvenk 216
Cdd:PRK12316 2045 LRARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA---- 2118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 217 lipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVS 295
Cdd:PRK12316 2119 -------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 296 DCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDLKVLQPtvfpvvprllNRM 373
Cdd:PRK12316 2174 HCQAAGERYELS----PADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWDP----------EQL 2228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 374 FDRIFGQANTtlkrwLLDFASkrkeaelrsgiirnnSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQ 453
Cdd:PRK12316 2229 YDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 454 F-YEGYGQTECTA-----GCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTA 527
Cdd:PRK12316 2289 YlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTA 2367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 528 EALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV---HGESLQAfL 597
Cdd:PRK12316 2368 ERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVvaqDGASGKQ-L 2445
|
....*..
gi 1034638914 598 IAIVVPD 604
Cdd:PRK12316 2446 VAYVVPD 2452
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
259-585 |
2.65e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 95.55 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 259 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchG 338
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALPLFHSF-----------G 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 339 AKIGFFQGdirlLMDDLKVL---QPTVFPVVPRLLnrmFDR----IFGQAnTTLKRWL-----LDFAskrkeaelrsgii 406
Cdd:PRK08043 421 LTVGLFTP----LLTGAEVFlypSPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 407 rnnslwdrlifhkvqsslggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 486
Cdd:PRK08043 480 --------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 487 NLIKLVDVEEMnymaaEGEGEVCVKGPNVFQGYLK--DP-------AKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 557
Cdd:PRK08043 540 MDARLLSVPGI-----EQGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAK 614
|
330 340
....*....|....*....|....*...
gi 1034638914 558 HIFKLAqGEYIAPEKIENIYMRSEPVAQ 585
Cdd:PRK08043 615 RFAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
220-583 |
2.76e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.06 E-value: 2.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 220 GLKIIVV---MDAYGSELVERGQRcGVEVTSMKAMEDLgranrrKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD 296
Cdd:PRK07768 108 GAKAVVVgepFLAAAPVLEEKGIR-VLTVADLLAADPI------DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 297 CSAFVKATENTVNpcpDDTLISFLPLAH-MfervvecvmlchgAKIGFFQGDIRLLMDDLKVlQPTVFPVVPRLLNRMFD 375
Cdd:PRK07768 181 AEAMFVAAEFDVE---TDVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELIS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 376 RIFGQ-------ANTTLKRwLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVS-ATVLTFLR 447
Cdd:PRK07768 244 KYRGTmtaapnfAYALLAR-RLRRQAKPGAFDL--------------------SSL----RFALNGAEPIDpADVEDLLD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 448 A---------ALGCqfyeGYGQTECTAGCCLTMPGD--------------------WTAGHV------GAPMPCNLIKLV 492
Cdd:PRK07768 299 AgarfglrpeAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 493 DvEEMNYMAAEGEGEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 572
Cdd:PRK07768 375 D-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTD 451
|
410
....*....|.
gi 1034638914 573 IENIYMRSEPV 583
Cdd:PRK07768 452 IERAAARVEGV 462
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
173-590 |
3.03e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.57 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 173 VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekaklllegvENKLIPGLKI-IVVMDAYGSELVERGQRCGVEVTSMKam 251
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDAGAKLLLVDE-----------EFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 252 edlgranrrkpkPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpcpDDTLISFLPLAHmferVVE 331
Cdd:PRK06145 145 ------------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTA----SERLLVVGPLYH----VGA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 332 C-----VMLCHGAKIGFFQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASKRkeaelrsgi 405
Cdd:PRK06145 205 FdlpgiAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLA--------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 406 irnnslWdrlifhkvqsSLGGrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAP 483
Cdd:PRK06145 268 ------W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 484 MPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 563
Cdd:PRK06145 325 LAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-IS 401
|
410 420
....*....|....*....|....*..
gi 1034638914 564 QGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:PRK06145 402 GGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
112-588 |
3.51e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 94.83 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 112 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 186
Cdd:PRK06155 33 RYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVK--RGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 187 TYIVNKAELSLVFVDkpekAKLL--LEGVENKLIPgLKIIVVMDAYGSELVERGQRcgveVTSMKAMedlgrANRRKPKP 264
Cdd:PRK06155 111 EHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAGWS----TAPLPPL-----DAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 265 PAPEDLAVICFTSGTTGNPKGAMVTH-------RNIVSDcsafvkatentVNPCPDDTLISFLPLAH-----MFERVvec 332
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAED-----------LEIGADDVLYTTLPLFHtnalnAFFQA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 333 vmLCHGAKI---------GFFqgdirllmDDLKVLQPTVF----PVVPRLLnrmfdrifgqanttlkrwlldfaSKRKEA 399
Cdd:PRK06155 243 --LLAGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL-----------------------SQPARE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 400 ELRSgiirnnslwdrlifHKVQSSLGGrvrlmvtgaaPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDwTAGH 479
Cdd:PRK06155 290 SDRA--------------HRVRVALGP----------GVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 480 VGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKG--PNVF-QGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK 556
Cdd:PRK06155 345 MGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRI 422
|
490 500 510
....*....|....*....|....*....|...
gi 1034638914 557 KHIFKlAQGEYIAPEKIENIyMRSEP-VAQVFV 588
Cdd:PRK06155 423 KDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
184-626 |
1.04e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 93.09 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 184 EAITYIVNKAELSLVFVDkPEKAKLLLEGVEnkLIPGLKIIVV---MDAYGselveRGQRCG-VEVTSMKAMEDLGRAnr 259
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVIdvdDPEYP-----GGRFIGaLDYEAFLASGDPDFA-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 260 rkPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRnivsdcSAFVKATENTV--NPCPDDTLISFLPLAHmfervveCVMLC 336
Cdd:PRK08162 175 --WTLPADEwDAIALNYTSGTTGNPKGVVYHHR------GAYLNALSNILawGMPKHPVYLWTLPMFH-------CNGWC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 337 H--------GAKIGFFQGDIRLLMDDLKVLQPTVF---PVVPRLLnrmfdrifgqANTtlkrwlldfaskrkEAELRSGI 405
Cdd:PRK08162 240 FpwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEWRAGI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 406 irnnslwdrlifhkvqsslGGRVRLMVTGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLTMPGdWTA------ 477
Cdd:PRK08162 296 -------------------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAlplder 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 478 ----GHVGAPMPC-NLIKLVDVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTL 550
Cdd:PRK08162 354 aqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 551 KIIDRKKHIFkLAQGEYIAPEKIENIYMRsepvaqvfvHgeslQAFLIAIVV--PDV---ETLCSWAQ-KRGFEGSFEEL 624
Cdd:PRK08162 433 KIKDRSKDII-ISGGENISSIEVEDVLYR---------H----PAVLVAAVVakPDPkwgEVPCAFVElKDGASATEEEI 498
|
....*
gi 1034638914 625 ---CR 626
Cdd:PRK08162 499 iahCR 503
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
121-626 |
2.72e-19 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 91.75 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKTA-------PdqfigifaqNRPEWVIIeqgCFAYSMV-IVPLYdTL----GNEaITY 188
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGdrvvvqlP---------NVAEFVIV---FFALFRAgAIPVF-ALpahrRAE-ISH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 189 IVNKAELS-LVFVDKPEK------AKLLLEGVenkliPGLKIIVVMDAYGSELvergqrcgvevtsmkAMEDLGRANRRK 261
Cdd:COG1021 117 FAEQSEAVaYIIPDRHRGfdyralARELQAEV-----PSLRHVLVVGDAGEFT---------------SLDALLAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 262 PKP-PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPcpDDTLISFLPLAHMFervvecVMLCHGAk 340
Cdd:COG1021 177 SEPrPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL--YSVRASAEICGLDA--DTVYLAALPAAHNF------PLSSPGV- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 341 IGFFQ--GDIRL-----------LMDDLKVlqpTVFPVVPRLLNRMfdrifgqanttlkrwlLDFASKRKeAELrsgiir 407
Cdd:COG1021 246 LGVLYagGTVVLapdpspdtafpLIERERV---TVTALVPPLALLW----------------LDAAERSR-YDL------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 408 nnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGD---WTAGHVGAP 483
Cdd:COG1021 300 --------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeeVILTTQGRP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 484 M-PCNLIKLVDVEEMNymAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIF 560
Cdd:COG1021 359 IsPDDEVRIVDEDGNP--VPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQIN 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 561 KlaQGEYIAPEKIENIYMRSEPVAQVfvhgeslqafliAIV-VPDV---ETLCSWAQKRGFEGSFEELCR 626
Cdd:COG1021 437 R--GGEKIAAEEVENLLLAHPAVHDA------------AVVaMPDEylgERSCAFVVPRGEPLTLAELRR 492
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
55-605 |
5.78e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 92.53 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 55 CDLSMQSVEvagsggARRSALLDSD-EPLVYFYDDVTTLyegFQRGIQVSNNGPCLGSRKpdqpyEWLSYKQVAELSECI 133
Cdd:PRK12467 485 GELPLLDAE------ERARELVRWNaPATEYAPDCVHQL---IEAQARQHPERPALVFGE-----QVLSYAELNRQANRL 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 134 GSALIQKGfkTAPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLL 209
Cdd:PRK12467 551 AHVLIAAG--VGPDVLVGIAVERSIEMVVgllaVLKAGGAY----VPLDPEYPQDRLAYMLDDSGVRLLLTQ-SHLLAQL 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 210 legvenKLIPGLKIIVvMDAYGSELVergqrcgvevtsmkamedlGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVT 289
Cdd:PRK12467 624 ------PVPAGLRSLC-LDEPADLLC-------------------GYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 290 HRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqgdirLLMDDLKVLQPTVFpvvprl 369
Cdd:PRK12467 678 HGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF------ 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 370 lnrmFDRIFGQANTTLKRwlldfaskrkeaelrsgiirNNSLWDRLIFHKVQSSLGGRVRLMVTGAA-PVSATVLTFlRA 448
Cdd:PRK12467 740 ----AALMADQGVTVLKI--------------------VPSHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR-AL 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 449 ALGCQFYEGYGQTECTAGC----CLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPA 524
Cdd:PRK12467 795 GPGARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHRRPA 873
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 525 KTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV--HGESLQA 595
Cdd:PRK12467 874 LTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGDAGL 952
|
570
....*....|
gi 1034638914 596 FLIAIVVPDV 605
Cdd:PRK12467 953 QLVAYLVPAA 962
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
115-583 |
1.09e-18 |
|
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: 89.85 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 115 DQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPlydtlgneaityivnkae 194
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIK--PGQEVVFQITHNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 195 lslVFVDKPEKAKLLLEGVENKLI-PGLkiivvmdaygselvergqrcgveVTSMKAMEDLgranrrkpkppaPEDLAVI 273
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWNTLKnPYL-----------------------ITEEEVLCEL------------ADELAFI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 274 CFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpcpDDTLISFLPLAHMFErvvecVMLCHGAKIgfFQGDIRLLMd 353
Cdd:cd05908 112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKT----KDRILSWMPLTHDMG-----LIAFHLAPL--IAGMNQYLM- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 354 dlkvlqPT-VFPVVPRLlnrmfdrifgqanttlkrWLLDfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMV 432
Cdd:cd05908 180 ------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMIL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 433 TGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCCL----------------------------TMPGDWTAG 478
Cdd:cd05908 235 NGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKDSECLTFV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 479 HVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 557
Cdd:cd05908 315 EVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREK 391
|
490 500
....*....|....*....|....*.
gi 1034638914 558 HIFkLAQGEYIAPEKIENIYMRSEPV 583
Cdd:cd05908 392 DII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
107-671 |
1.13e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 90.11 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 107 PCLGSRKPDQ-PYEWLSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---YDTLG 182
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 183 NE--AITYIVNKAELSLVFVDKPEK-----AKLLLEGVEnklipglkiIVVMDAYG--------SELVERGQRCGVEvts 247
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVT---------VVHVTGPGegiasiafADLAATPPTAAVA--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 248 mKAMEDLGranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRNIvsdCSAfVKATENTVNPCPDD---TLISFLPLAH 324
Cdd:PRK12582 212 -AAIAAIT-----------PDTVAKYLFTSGSTGMPKAVINTQRMM---CAN-IAMQEQLRPREPDPpppVSLDWMPWNH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 325 MFervvecvmlchGAKIGFfQGDIR----LLMDDLKVLqPTVFPVVPRLLNRMFDRIFGQANTTLKrwLLDFASKRKEAE 400
Cdd:PRK12582 276 TM-----------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 401 LRSgiirnnslwdrliFHKvqsslggRVRLMVTGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGccLTMPGD 474
Cdd:PRK12582 341 RRS-------------FFK-------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAP--TTTGTH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 475 WTA---GHVGAPMPCNLIKLVDVEEmNYmaaegegEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PN 547
Cdd:PRK12582 398 WDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 548 GTLKIIDRKKHIFKLAQGEYIAPEKIE-NIYMRSEPVAQ-VFVHGESlQAFLIAIVVPDVETLCSWAQKRGfeGSFEELC 625
Cdd:PRK12582 470 KGLIFDGRVAEDFKLSTGTWVSVGTLRpDAVAACSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVV 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1034638914 626 RNKDVKKAILEDMVRLGKDSGlKPFEQVKGITLHPELFSIDNGLLT 671
Cdd:PRK12582 547 KHPAVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
138-598 |
2.94e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 88.59 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 138 IQKGFKTApdqfigIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfVDKPEKAKLLLEGVENKL 217
Cdd:PRK08008 59 IRKGDKVA------LHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLL-VTSAQFYPMYRQIQQEDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 218 IPgLKIIVVMDAYGSElvERGqrcgveVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdc 297
Cdd:PRK08008 132 TP-LRHICLTRVALPA--DDG------VSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 298 SAFVKATENTVNPcpDDTLISFLPLAHM-FERVVECVMLCHGAKIGF--------FQGDIRLLmddlkvlQPTVFPVVPR 368
Cdd:PRK08008 201 AGYYSAWQCALRD--DDVYLTVMPAFHIdCQCTAAMAAFSAGATFVLlekysaraFWGQVCKY-------RATITECIPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 369 LLNRM-------FDRifgqaNTTLKRWL--LDFASKRKEA-ELRSGiirnnslwdrlifhkvqsslggrVRLMVTgaapv 438
Cdd:PRK08008 272 MIRTLmvqppsaNDR-----QHCLREVMfyLNLSDQEKDAfEERFG-----------------------VRLLTS----- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 439 satvltflraalgcqfyegYGQTECTAGCCLTMPGD---WTAghVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKG-- 512
Cdd:PRK08008 319 -------------------YGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 513 -PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHG- 590
Cdd:PRK08008 376 gKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGi 454
|
490
....*....|....
gi 1034638914 591 ------ESLQAFLI 598
Cdd:PRK08008 455 kdsirdEAIKAFVV 468
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
121-604 |
3.43e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 88.10 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd12114 13 LTYGELAERARRVAGALKAAG--VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKPekakllleGVENKLIPGLKIIVVMDAygselvergqrcgvevtsmkamedLGRANRRKPKPPAPEDLAVICFTSGTT 280
Cdd:cd12114 91 DGP--------DAQLDVAVFDVLILDLDA------------------------LAAPAPPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH------MFErvvecvMLCHGAKIGFFQGDIR----L 350
Cdd:cd12114 139 GTPKGVMISHRAALNTILDINRRFAVG----PDDRVLALSSLSFdlsvydIFG------ALSAGATLVLPDEARRrdpaH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 351 LMDDLKVLQPTVFPVVPRLLNrMfdrifgqanttlkrwLLDfaskrkeaELRSGIIRNNSLwdRLIFHK---VQSSLGGR 427
Cdd:cd12114 209 WAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL--RLVLLSgdwIPLDLPAR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 428 VRLMVTGAAPVSatvltflraaLGcqfyegyGQTECTAGCCL----TMPGDWTAGHVGAPMPCNLIKLVDveemnymaAE 503
Cdd:cd12114 263 LRALAPDARLIS----------LG-------GATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLD--------PR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 504 GE-------GEVCVKGPNVFQGYLKDPAKTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:cd12114 318 GRdcpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGE 396
|
490 500 510
....*....|....*....|....*....|....
gi 1034638914 573 IENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPD 604
Cdd:cd12114 397 IEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
267-617 |
9.56e-18 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 86.37 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpddtlISFLPLAHMFERVVE---CVMLCHGAKIGF 343
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASFSFDVFAgdfARSLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 344 FQGDIRL----LMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKE--AELRSGIIRNNSLWDRLiF 417
Cdd:cd17650 166 CPDEVKLdpaaLYDLILKSRITLMESTP----------------ALIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD-F 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 418 HKVQSSLGGRVRLmvtgaapVSATVLTflRAALGCQFYEGYGQTECTAGcclTMPgdwtaghVGAPMPCNLIKLVDvEEM 497
Cdd:cd17650 229 KTLAARFGQGMRI-------INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 571
Cdd:cd17650 289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELG 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1034638914 572 KIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETlcSWAQKRGF 617
Cdd:cd17650 368 EIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAELRAF 414
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
121-615 |
1.01e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.11 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 dKPEKAKL----LLEGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICFT 276
Cdd:PRK06164 114 -WPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 277 -SGTTGNPK------GAMVTHRNIVSDCSAFVkatentvnpcPDDTLISFLPLahmfervveCVMLCHGAKIGFFQGDIR 349
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGYD----------PGAVLLAALPF---------CGVFGFSTLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 350 LLMDDlkvlqptVF--PVVPRLL-----------NRMFDRIFGQANTTLkrwllDFASKRkeaelrsgiirnnslwdRLI 416
Cdd:PRK06164 250 LVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----------------LFG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 417 FHKVQSSLGGRVRLMVTGAAPvsatvLTFLraalgcqfyegYGQTECTA-GCCLTMPGDWTAGHV--GAPM-PCNLIKLV 492
Cdd:PRK06164 301 FASFAPALGELAALARARGVP-----LTGL-----------YGSSEVQAlVALQPATDPVSVRIEggGRPAsPEARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 493 DVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 572
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAE 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1034638914 573 IENIYMRSEPVAQVFVHGESLQ------AFLIAI--VVPDVETLCSWAQKR 615
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
168-590 |
1.22e-17 |
|
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: 86.78 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 168 FAYSM--------VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgQ 239
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIE-KAAPECPSKPKLVWVGDPVPE--G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 240 RCGVEVTSMKAMEDLGRanRRKPKPPAPEDLAVICFTSGTTGNPKgaMVTHRNIvsdcsafvkatentvnpcpddtlisf 319
Cdd:cd05970 159 WIDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFT-------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 320 LPLAHMFErvvecVMLCHGAKigffQGDIRLLMDDLKVLQPtvfpvvprllnrMFDRIFGQANTTLKRWLLDFasKRKEA 399
Cdd:cd05970 209 YPLGHIVT-----AKYWQNVR----EGGLHLTVADTGWGKA------------VWGKIYGQWIAGAAVFVYDY--DKFDP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 400 ELRSGIIRNN---------SLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLT 470
Cdd:cd05970 266 KALLEKLSKYgvttfcappTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 471 MPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCV---KGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKW 544
Cdd:cd05970 345 FPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWM 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1034638914 545 LPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd05970 423 DEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
147-590 |
2.00e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 85.99 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 147 DQFIGIFAQNRPEW--VIIEQGCFAysMVIVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLLLEGVENklIPGLKII 224
Cdd:PRK05620 64 DQRVGSMMYNCAEHleVLFAVACMG--AVFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 225 VVMDAYGSELVERGQRCGVEVTSMKAMEDlGRANRRkPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKA 303
Cdd:PRK05620 139 VFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLSLRTT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 304 TENTVNpcPDDTLISFLPLAHmfervvecvMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVprllnrmfdrifgqaNT 383
Cdd:PRK05620 217 DSLAVT--HGESFLCCVPIYH---------VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKII---------------AT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 384 TLKRwlldfaskrkeaeLRSGIirnNSLWDRLIFHKVQSSlGGRVRL--MVTGAAPVSATVLTFLRAALGCQFYEGYGQT 461
Cdd:PRK05620 271 AMPR-------------VAHGV---PTLWIQLMVHYLKNP-PERMSLqeIYVGGSAVPPILIKAWEERYGVDVVHVWGMT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 462 ECTAGCCLTMPGDWTAGHVGAP-------MPCNLIKLVdVEEMNYMAA--EGEGEVCVKGPNVFQGYLKDPAKT------ 526
Cdd:PRK05620 334 ETSPVGTVARPPSGVSGEARWAyrvsqgrFPASLEYRI-VNDGQVMEStdRNEGEIQVRGNWVTASYYHSPTEEgggaas 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034638914 527 ----------AEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:PRK05620 413 tfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
121-607 |
2.08e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 85.89 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKTAPDQFiGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:PRK07867 29 TSWREHIRGSAARAAALRARLDPTRPPHV-GVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKPEKAklLLEGVEnkliPGLKIIVVMDAYGSELVergqrcgvevtsmkameDLGRANRRKPKPPAPEDLAVICFTSGTT 280
Cdd:PRK07867 108 ESAHAE--LLDGLD----PGVRVINVDSPAWADEL-----------------AAHRDAEPPFRVADPDDLFMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDTLISFLPLAHMFERVVE-CVMLCHGAKI---------GFfqgdirl 350
Cdd:PRK07867 165 GDPKAVRCTHRKVASAGVMLAQ----RFGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 351 lMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrWLLDFASKRKEAElrsgiirnNSLwdRLIFhkvqsslggrvrl 430
Cdd:PRK07867 234 -LPDVRRYGATYANYVGKPLS----------------YVLATPERPDDAD--------NPL--RIVY------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 431 mvtGAAPVSATVLTFlRAALGCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAPMPCnlIKLVDVE--------------E 496
Cdd:PRK07867 274 ---GNEGAPGDIARF-ARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 497 MNYMAAEGEgEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 576
Cdd:PRK07867 346 LNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERI 422
|
490 500 510
....*....|....*....|....*....|.
gi 1034638914 577 YMRSEPVAQVFVHGeslqafliaivVPDVET 607
Cdd:PRK07867 423 LLRYPDATEVAVYA-----------VPDPVV 442
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
267-607 |
2.78e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 85.05 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFErVVEcvM---LCHGAKIGF 343
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWE--IwgaLLHGGRLVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 344 FQGDIRLLMDDLkvlqptvfpvvPRLLNRMFDRIFGQANTTLKRWLldfaskrkEAELRsgiirnnslwdrliFHKVQSS 423
Cdd:cd17643 165 VPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 424 LggrvRLMVTGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCL-----TMPGDWTAGHVGAPMPCNLIKLVDvE 495
Cdd:cd17643 212 L----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaADLPAAAASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034638914 569 APEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVET 607
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
121-604 |
4.75e-17 |
|
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: 84.63 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKPEKAKLllegvenklipglkiivvmdaygselvergqRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTT 280
Cdd:cd17646 102 TADLAARL-------------------------------PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVSD----CSAFVKATENTV---NPCPDDTLIS--FLPLAHMfERVVECVMLCHGaKIGFFQGdirlL 351
Cdd:cd17646 151 GRPKGVMVTHAGIVNRllwmQDEYPLGPGDRVlqkTPLSFDVSVWelFWPLVAG-ARLVVARPGGHR-DPAYLAA----L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 352 MDDLKVlqpTVFPVVPRLLnrmfdRIFGQanttlkrwlldfaskrkeaELRSGIIRNnslwdrlifhkvqsslggrVRLM 431
Cdd:cd17646 225 IREHGV---TTCHFVPSML-----RVFLA-------------------EPAAGSCAS-------------------LRRV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 432 VTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGEV 508
Cdd:cd17646 259 FCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGEL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 509 CVKGPNVFQGYLKDPAKTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEP 582
Cdd:cd17646 338 YLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPA 416
|
490 500
....*....|....*....|....*
gi 1034638914 583 VAQVFV---HGESLQAFLIAIVVPD 604
Cdd:cd17646 417 VTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
150-638 |
7.65e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.30 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 150 IGIFAQNRPEwviIEQGCFAYSM---VIVPLYDTLGNEAITYIVNKAELSLVFVDKP-----EKAKLLLEGVENKLIPGL 221
Cdd:PLN03102 67 VSVLAPNTPA---MYEMHFAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDRSfeplaREVLHLLSSEDSNLNLPV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 222 KIIVVMD----AYGSE-----LVERGQRCGVEVTSMKAMEDlgranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRN 292
Cdd:PLN03102 144 IFIHEIDfpkrPSSEEldyecLIQRGEPTPSLVARMFRIQD-------------EHDPISLNYTSGTTADPKGVVISHRG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 293 I-VSDCSAFVKATENTvnpCPddTLISFLPLAHmfervvecvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTVFPVVpr 368
Cdd:PLN03102 211 AyLSTLSAIIGWEMGT---CP--VYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 369 llnRMFDRIFGQANTTLKRWLLdfaskrkeaelrsgiiRNNSLwdrlifhkVQSSLGGRVRLMVTGAAPVSATVLTFLRa 448
Cdd:PLN03102 271 ---EMHNVTHMCCVPTVFNILL----------------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 449 aLGCQFYEGYGQTECTAGCCLTMPGD-WT------AGHVGAPMPCNLIKLVDVEEMNYMAAEGE-------GEVCVKGPN 514
Cdd:PLN03102 323 -LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLADVDVKNKETQESVprdgktmGEIVIKGSS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 515 VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIymrsepvaqVFVHGESLQ 594
Cdd:PLN03102 402 IMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLE 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1034638914 595 AFLIAIVVPDV-ETLCSW-AQKRGFEGSFEE----LCRNKDVKKAILEDM 638
Cdd:PLN03102 471 TAVVAMPHPTWgETPCAFvVLEKGETTKEDRvdklVTRERDLIEYCRENL 520
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
267-615 |
9.70e-17 |
|
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: 83.07 E-value: 9.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVV-ECVM-LCHGAkigff 344
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG----PGSRVLQFASPS--FDASVwELLMaLLAGA----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 qgdiRLLMDDLKVLQPtvfpvvprllnrmfdrifGQAnttlkrwLLDFaskrkeaelrsgiirnnsLWDRLIFHKVQS-- 422
Cdd:cd17652 161 ----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPpa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 423 --------SLGGRVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAgcCLTMPGDWTAGHV---GAPMPCNLIKL 491
Cdd:cd17652 194 alaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTV--CATMAGPLPGGGVppiGRPVPGTRVYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 492 VDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 564
Cdd:cd17652 269 LD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-R 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 565 GEYIAPEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVV------PDVETLCSWAQKR 615
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVpapgaaPTAAELRAHLAER 406
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
266-603 |
2.17e-16 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 82.42 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigf 343
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT----PGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 344 fqgdiRLLMDDLKVLQPtvfpvvPRLLNRMFDR----IFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhk 419
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADR------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 420 VQSSLGGRVRLMVTGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLTMPGDWTAGH---VGAPMPCNLIKLV 492
Cdd:cd17649 206 TGDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 493 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 565
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034638914 566 EYIAPEKIENIYMRSEPVAQVFVHGES--LQAFLIAIVVP 603
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVL 400
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
269-599 |
3.97e-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: 81.61 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRnivsDCSAFVKATENTVNPCPDDTLISFLPLAHMFerVVEC-----VMLChGAKIGF 343
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHN----DYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 344 FQ----GDIRLLMDDLKVlqpTVFPVVPRLLnrmfdrifgqanttlKRWLlDFASKRKEAElrsgiirnnslwdrlifhk 419
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPALV---------------SLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 420 vqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTM---PGDWTAGHVGAPM-PCNLIKLVDv 494
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE---GlLNYTRlddPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 495 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 574
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 1034638914 575 NIYMRSEPVAQVFV-------HGESLQAFLIA 599
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
121-590 |
3.12e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 79.16 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL-YDTLGNEaITYIVNKAELSLVF 199
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLG--PGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 200 VDK---PEKAKLLLEgvenklIPGLKIIVVMDAYGSELVERGqrcGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICfT 276
Cdd:PRK07798 106 YERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-T 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 277 SGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK-----IGFFQGdirll 351
Cdd:PRK07798 172 GGTTGMPKGVMWRQEDIFR--VLLGGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSG----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 352 mddlkvlQPTVFPVVPRL-------------LNRMFdrIFGQAnttLKRWLLDFASKRKEAELrsgiirnnslwdrlifh 418
Cdd:PRK07798 245 -------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL----------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 419 kvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAP--MPCNLIKLVDVE 495
Cdd:PRK07798 296 ---SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGPRTVVLDED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 572
Cdd:PRK07798 367 GNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEE 445
|
490
....*....|....*....
gi 1034638914 573 IENIyMRSEP-VAQVFVHG 590
Cdd:PRK07798 446 VEEA-LKAHPdVADALVVG 463
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
234-587 |
5.09e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.40 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 234 LVERGQRCGvevTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNP 310
Cdd:PRK09274 140 LVTVGGRLL---WGGTTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 311 CPDDTLISFLPLahmfervvecvMLCHGAKIGFfqGDIRLLMDDLKVLQptvfpVVPRllnRMFDRIFGQANTTLkrwll 390
Cdd:PRK09274 213 EPGEIDLPTFPL-----------FALFGPALGM--TSVIPDMDPTRPAT-----VDPA---KLFAAIERYGVTNL----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 391 dFASKrkeaelrsgiirnnSLWDRLIFHKVQS--SLGGrVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC--- 463
Cdd:PRK09274 267 -FGSP--------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpi 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 464 ---TAGCCLTMPGDWT---AGH-VGAPMPCNLIKLVDVEEM-------NYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAE 528
Cdd:PRK09274 331 ssiESREILFATRAATdngAGIcVGRPVDGVEVRIIAISDApipewddALRLATGEiGEIVVAGPMVTRSYYNRPEATRL 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034638914 529 A--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniymrSEPVAQVF 587
Cdd:PRK09274 411 AkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIF 462
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
267-614 |
8.46e-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: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDTLI--SFLPLAHMFErvvecvMLCH---GAKI 341
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPA---DKSLVyaSFSFDASAWE------IFPHltaGAAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 342 GFFQGDIRLLMDDLkvlqptvfpvvprllnrmfDRIFGQANTTLKRWLLDFASKRKEAElrsgiirNNSLwdrlifhkvq 421
Cdd:cd17645 174 HVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL---------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 422 sslggrvRLMVTGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMA 501
Cdd:cd17645 218 -------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 502 AEG-EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 574
Cdd:cd17645 284 PIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIE 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034638914 575 NIYMRSEPVAQVFV-------HGESLQAFLIAIVVPDVETLCSWAQK 614
Cdd:cd17645 363 PFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
266-603 |
1.97e-14 |
|
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: 75.98 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLAHMFER-VVECVMLCHGAKIGFF 344
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 QGDI-RLLMDDLKVLQPTVFPVVPRLLNRMfdrifgqanttlkrwlldFASKRKEAELRSGiirnnslwdrlifhkvqss 423
Cdd:cd05958 172 EEATpDLLLSAIARYKPTVLFTAPTAYRAM------------------LAHPDAAGPDLSS------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 424 lggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 503
Cdd:cd05958 215 ----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 504 GEGEVCVKGPNvfqGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 583
Cdd:cd05958 290 TIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340
....*....|....*....|...
gi 1034638914 584 AQVFVHGESLQAFLI---AIVVP 603
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVL 388
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
457-613 |
2.28e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 74.65 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 457 GYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGW 535
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638914 536 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyMRSEP-VAQVFVhgeslqafliaIVVPDVetlcSWAQ 613
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAV-----------IGVPDP----RWAQ 280
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
267-578 |
2.31e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQG 346
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 347 DIRLLMDDLkvlqPTVF---PVVPRLLNRMFDR----IFGQANTTLKrWLLDFASKRKEA--ELRSGIIRNNSLWDRLiF 417
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFD-YILKTAKKQESClpSLRFVVIGGDAFKDSL-Y 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 418 HKVQSslggrvrlmvtgaapvsatvlTFLRAALgcqfYEGYGQTECTAgcCLTMPGDWTAGH---VGAPMPCNLIKLVDv 494
Cdd:PRK06334 317 QEALK---------------------TFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGMPIRGMDVLIVS- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 495 EEMNYMAAEGE-GEVCVKGPNVFQGYL-KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 572
Cdd:PRK06334 369 EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEA 447
|
....*.
gi 1034638914 573 IENIYM 578
Cdd:PRK06334 448 LESILM 453
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
121-604 |
2.53e-14 |
|
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: 75.82 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICFTSGTT 280
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVsdcsAFVKATENTvnpCPDD--------TLISF-LPLAHMFervvecVMLCHGAKIgffqgdirll 351
Cdd:cd12115 118 GRPKGVAIEHRNAA----AFLQWAAAA---FSAEelagvlasTSICFdLSVFELF------GPLATGGKV---------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 352 mddlkVLQPTVFPvvprllnrmfdrifgqanttlkrwLLDFASkRKEAELrsgIIRNNSLWDRLIFHkvqSSLGGRVRLM 431
Cdd:cd12115 175 -----VLADNVLA------------------------LPDLPA-AAEVTL---INTVPSAAAELLRH---DALPASVRVV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 432 VTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 508
Cdd:cd12115 219 NLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGEL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 509 CVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEP 582
Cdd:cd12115 298 YIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPG 376
|
490 500
....*....|....*....|....*
gi 1034638914 583 VAQ--VFVHGESL-QAFLIAIVVPD 604
Cdd:cd12115 377 VREavVVAIGDAAgERRLVAYIVAE 401
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
267-617 |
2.61e-14 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 75.93 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpdDTLISFLPLAhmFERVVE--CVMLCHGAKIgff 344
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS----DRVLQFASIA--FDVAAEeiYVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 qgdirllmddlkVLQPtvfpvvprllNRMFdrifgqanttlkRWLLDFASKRKEAELRSGIIrNNSLWDRLIFHKVQSSL 424
Cdd:cd17644 176 ------------VLRP----------EEMR------------SSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 425 GG--RVRLMVTGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCCLTMPGDWTAGH-----VGAPMPCNLIKLVDvE 495
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 496 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034638914 568 IAPEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETLCSWAQKRGF 617
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
184-658 |
3.13e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.90 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 184 EAITYIVNKAELSLVFVD---KPekaklLLEGVENKLiPGLKIIVVM-DAygselvergQRCGVEVTSMKAMEDL-GRAN 258
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMtDA---------AHLPAGSTPLLCYETLvGAQD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 259 RRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPCPDDTLisfLPLAHMFErvVECVMLCH 337
Cdd:PRK07008 166 GDYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 338 -----GAKIgffqgdirllmddlkvlqptVFPvvprllnrmfdrifGQAnttlkrwlLDFASKRK--EAELRSGIIRNNS 410
Cdd:PRK07008 239 sapltGAKL--------------------VLP--------------GPD--------LDGKSLYEliEAERVTFSAGVPT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 411 LWDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLT-----MPGD------W 475
Cdd:PRK07008 277 VWLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKwkhsqLPLDeqrkllE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 476 TAGHV--GAPMpcnliKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDkDGWLHTGDIGKWLPNGTLK 551
Cdd:PRK07008 357 KQGRViyGVDM-----KIVG-DDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 552 IIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAqvfvhgeslQAFLIAIVVP--DVETLCSWAQKRGFEGSFEELCRNKD 629
Cdd:PRK07008 427 ITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA---------EAACIACAHPkwDERPLLVVVKRPGAEVTREELLAFYE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034638914 630 VKKA---ILEDMVRL--------GKDSGLKPFEQVKGITL 658
Cdd:PRK07008 497 GKVAkwwIPDDVVFVdaiphtatGKLQKLKLREQFRDYVL 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
264-608 |
4.05e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAki 341
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELT----PDDRVLQFMSFS--FDGSHEGLYhpLINGA-- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 342 gffqgdiRLLMDDLKVLQPtvfpvvprllNRMFDRIFGQANTTlkrwlLDFASkrkeaelrsgiirnnSLWDRLIFHKVQ 421
Cdd:PRK12316 4762 -------SVVIRDDSLWDP----------ERLYAEIHEHRVTV-----LVFPP---------------VYLQQLAEHAER 4804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 422 SSLGGRVRLMVTG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLTMPGDWTAG----HVGAPMPCNLIKLVDV 494
Cdd:PRK12316 4805 DGEPPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDG 4883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 495 eEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 567
Cdd:PRK12316 4884 -QLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFR 4961
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034638914 568 IAPEKIEnIYMRSEP-------VAQVFVHGeslqAFLIAIVVPDVETL 608
Cdd:PRK12316 4962 IELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPQDPAL 5004
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
268-598 |
8.85e-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: 74.42 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 268 EDLAVICFTSGTTGNPKgaMVTHrnivSDCSAFVKA----------TENTVNPCPDDTLISFLPLAHMFERVVE--CVML 335
Cdd:cd05928 174 QEPMAIYFTSGTTGSPK--MAEH----SHSSLGLGLkvngrywldlTASDIMWNTSDTGWIKSAWSSLFEPWIQgaCVFV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 336 CHGAKIgffqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLL--DFASkrkeaelrsgiirnnslwd 413
Cdd:cd05928 248 HHLPRF-----DPLVILKTLSSYPITTFCGAP----------------TVYRMLVqqDLSS------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 414 rlifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG-DWTAGHVGAPMPCNLIKLV 492
Cdd:cd05928 288 ----YKFPS-----LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGmKIKPGSMGKASPPYDVQII 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 493 DvEEMNYMAAEGEGEVCVK-GPN----VFQGYLKDPAKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 567
Cdd:cd05928 358 D-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYR 434
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034638914 568 IAPEKIENIYMRSEPVAQVFV-------HGESLQAFLI 598
Cdd:cd05928 435 IGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
264-606 |
1.88e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.98 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFvkatenTVNpcpDDTLISfLPLAHmfervvecV---- 333
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQAHlasaegVLSLMPF------TAQ---DSWLLS-LPLFH--------Vsgqg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 334 ----MLCHGAKIGFfqGDIRLLMDDLkvLQPTVFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnn 409
Cdd:PRK09029 193 ivwrWLYAGATLVV--RDKQPLEQAL--AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 410 slwdrlifhkvqsslGGrvrlmvtGAAPVSatvLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTAGhVGAPMPCNLI 489
Cdd:PRK09029 248 ---------------GG-------AAIPVE---LTEQAEQQGIRCWCGYGLTEMASTVC-AKRADGLAG-VGSPLPGREV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 490 KLVDveemnymaaegeGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIA 569
Cdd:PRK09029 301 KLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQ 365
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034638914 570 PEKIENIYMRSEPVAQVFVhgeslqafliaIVVPDVE 606
Cdd:PRK09029 366 PEEIERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
252-604 |
3.36e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.77 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 252 EDLGRANRRKPKPPAPEDLAVIC---FTSGTTGNPKGAMVTHRNIvsdcsAFVkATENTVNPCPD----DTLISFLPLAH 324
Cdd:PRK07470 144 EALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQM-----AFV-ITNHLADLMPGtteqDASLVVAPLSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 325 MfERVVECVMLCHGAKigffqgDIRLLMDDLKVlqPTVFPVVPRL-LNRMFdrifgQANTTLKRWLLDFASKRKEaelrs 403
Cdd:PRK07470 218 G-AGIHQLCQVARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD----- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 404 giirnnslwdrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGC------CLTMPGDWTA 477
Cdd:PRK07470 279 -----------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNitvlppALHDAEDGPD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 478 GHVGapmPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLK 551
Cdd:PRK07470 337 ARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLY 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034638914 552 IIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPD 604
Cdd:PRK07470 412 ITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD 452
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
265-639 |
6.15e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.89 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 265 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKIG 342
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 343 FFQGDIRL----LMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFAskrkEAELRSGIIRnnslwdRLIFh 418
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ----------------LLQMD----EQVEHPLSLR------RVVC- 1841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 419 kvqsslGGRvrlmvtgAAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CCLTMPGDWTAGHVGAPMPcNLIKLV 492
Cdd:PRK12467 1842 ------GGE-------ALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIA-NLSTYI 1905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 493 DVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQG 565
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RG 1984
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638914 566 EYIAPEKIENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPDVETLCSWAQKRGfeGSFEELcrnKDVKKAILED-MV 639
Cdd:PRK12467 1985 FRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV--ALRAIL---KNHLKASLPEyMV 2056
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-587 |
7.08e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 71.34 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 265 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchGAKIGff 344
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFA----AQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 qgdirllmddLKVLQPTVFPVVPrllnrmfdrifGQANttlKRWLLDFASKRKEaelrSGIIRNNSLWDRLIFHKVQSSL 424
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 425 G-GRVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LTMPGDWTAGH----VGAPMPCNLIKL 491
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 492 VDVEEMNYMAAEGE--------GEVCVKGPNVFQGYLKDPAKTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd05910 277 IEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*...
gi 1034638914 560 FKLAQGEYIapekieniymrSEPVAQVF 587
Cdd:cd05910 357 VITTGGTLY-----------TEPVERVF 373
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
410-588 |
1.52e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 70.29 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 410 SLWdRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLI 489
Cdd:cd05974 185 TVW-RMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRV 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 490 KLVDVEEmnymAAEGEGEVCV-----KGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 564
Cdd:cd05974 264 ALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SS 337
|
170 180
....*....|....*....|....
gi 1034638914 565 GEYIAPEKIENIYMRSEPVAQVFV 588
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAEAAV 361
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
261-586 |
1.76e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 261 KPKPPAPEDLAVIcFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHM--FERVVECVMlcHG 338
Cdd:PRK05857 163 NADQGSEDPLAMI-FTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIggLWWILTCLM--HG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 339 AKI---GFFQGDIRLLMDDLKVLQPTVfpvVPRLLNRMFdrifgqanttlkrwlldfaskrkeAELRSGIIRNNSLwdrl 415
Cdd:PRK05857 240 GLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPSL---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 416 ifhkvqsslggrvRLMVTGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 490
Cdd:PRK05857 289 -------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 491 LVDVEEMNYMAAEGE-----GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 565
Cdd:PRK05857 355 LAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGG 432
|
330 340
....*....|....*....|.
gi 1034638914 566 EYIAPEKIENIymrSEPVAQV 586
Cdd:PRK05857 433 VNIAPDEVDRI---AEGVSGV 450
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
121-598 |
2.06e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 69.85 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAQNrPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05973 1 LTFGELRALSARFANALQELGVG-PGDVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 DKPEKAKLllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICFTSGTT 280
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 281 GNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDtliSFLPLAH------MFERVVECVMLCHGAKI---GFFQGDIRLL 351
Cdd:cd05973 101 GLPKGVPVPLRALA----AFGAYLRDAVDLRPED---SFWNAADpgwaygLYYAITGPLALGHPTILlegGFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 352 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkeaeLRSGIirnnslwdrlifhKVQSSLGGRVRLM 431
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLL------------------------------MAAGA-------------EVPARPKGRLRRV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 432 VTGAAPVSATVLTFLRAALGCQFYEGYGQTEctagccLTMP--GDWTAGHV------GAPMP---CNLIKLVDVEemnym 500
Cdd:cd05973 211 SSAGEPLTPEVIRWFDAALGVPIHDHYGQTE------LGMVlaNHHALEHPvhagsaGRAMPgwrVAVLDDDGDE----- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 501 AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 575
Cdd:cd05973 280 LGPGEpGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
490 500 510
....*....|....*....|....*....|
gi 1034638914 576 IYMRSEPVAQVFV-------HGESLQAFLI 598
Cdd:cd05973 355 ALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
250-603 |
2.19e-12 |
|
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: 69.71 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 250 AMEDLGRANRRKPKPPAPEDLA--VICFTSGTTGNPKGAMVTHrnivsDCsafvkatentvNPCPDDTLISF-LPLAHMF 326
Cdd:cd05929 105 GLEDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGL-----PG-----------GPPDNDTLMAAaLGFGPGA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 327 ERVVECVM-LCHGAKIGFFQGDIRL-----LM---DDLKVLQP------TVFPVVPRLLNRMfdrifgqanttLK----- 386
Cdd:cd05929 169 DSVYLSPApLYHAAPFRWSMTALFMggtlvLMekfDPEEFLRLieryrvTFAQFVPTMFVRL-----------LKlpeav 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 387 RWLLDFASkrkeaeLRSgiirnnslwdrlIFHkvqsslggrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG 466
Cdd:cd05929 238 RNAYDLSS------LKR------------VIH---------------AAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 467 CCLTmPGDWTA--GHVGAPMPCNLiKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDGWLHTGDIGKW 544
Cdd:cd05929 285 TIIN-GEEWLThpGSVGRAVLGKV-HILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYL 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034638914 545 LPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVP 603
Cdd:cd05929 361 DEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
428-597 |
5.07e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 69.10 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 428 VRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDW------TAGHVGAPMPCNLIKL-----VD 493
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstVCAWKP-EWdslppeEQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 VEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 571
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190
....*....|....*....|....*....|...
gi 1034638914 572 KIENIYMRSEPVAQVFV-------HGESLQAFL 597
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
121-585 |
5.13e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 69.81 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNrPEWVIIEQGCFaYSMVI-VPLYDTLGN-----EAITYIVNKAE 194
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQARA--SFGDRAVLLFPSG-PDYVAAFFGCL-YAGVIaVPAYPPESArrhhqERLLSIIADAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 195 LSLVFVDkpekAKLL--LEGVENKLIPGLKIIVVMDAYGSELVERGQrcgvevtsmkamedlgranrrKPKPPaPEDLAV 272
Cdd:PRK05691 117 PRLLLTV----ADLRdsLLQMEELAAANAPELLCVDTLDPALAEAWQ---------------------EPALQ-PDDIAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 273 ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcPDDTLISFLPLAHmfervvecvmlchgaKIGFFQGdirllm 352
Cdd:PRK05691 171 LQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLN--PDDVIVSWLPLYH---------------DMGLIGG------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 353 ddlkVLQPtVFPVVPRLLnrMFDRIFGQANTtlkRWLldfaskrkEA--ELRSGIIRNNSLWDRLIFHKV-QSSLGG--- 426
Cdd:PRK05691 228 ----LLQP-IFSGVPCVL--MSPAYFLERPL---RWL--------EAisEYGGTISGGPDFAYRLCSERVsESALERldl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 427 -RVRLMVTGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECT---AGC-------CLTMPGDWTAGHV--------- 480
Cdd:PRK05691 290 sRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgipALELDAEALARNRaepgtgsvl 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 481 ---GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-LDKDG--WLHTGDIGkWLPNGTLKIID 554
Cdd:PRK05691 370 mscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTG 448
|
490 500 510
....*....|....*....|....*....|.
gi 1034638914 555 RKKHIFkLAQGEYIAPEKIENIYMRSEPVAQ 585
Cdd:PRK05691 449 RLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
112-590 |
6.00e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.56 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 112 RKPDQPY-------EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNE 184
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLK--RGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 185 AITYIVNKAELSLVF--VDKPEKAKLLLegvenKLIPGLKIIVVMDAYGSelvergqrcgvevtsMKAMEDLGRANRRKP 262
Cdd:PRK13391 87 EAAYIVDDSGARALItsAAKLDVARALL-----KQCPGVRHRLVLDGDGE---------------LEGFVGYAEAVAGLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 263 KPPAPEDL--AVICFTSGTTGNPKGamvthrnivsdcsafVKAtentvnPCPDDTLISFLPLAHMFERVV----ECVMLC 336
Cdd:PRK13391 147 ATPIADESlgTDMLYSSGTTGRPKG---------------IKR------PLPEQPPDTPLPLTAFLQRLWgfrsDMVYLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 337 -----HGAKIGFFQGDIRL-----LMDD------LKVLQP---TVFPVVPRllnrMFDRIFGQANTTLKRWLLdfaskrk 397
Cdd:PRK13391 206 paplyHSAPQRAVMLVIRLggtviVMEHfdaeqyLALIEEygvTHTQLVPT----MFSRMLKLPEEVRDKYDL------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 398 eaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDWTA 477
Cdd:PRK13391 275 ------------------------SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 478 --GHVGAPMpCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDG-WLHTGDIGKWLPNGTLKIID 554
Cdd:PRK13391 326 hpGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTD 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 1034638914 555 RKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:PRK13391 403 RAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
101-608 |
2.15e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 66.97 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 101 QVSNNGPCLGSRkpDQPYEWlsyKQVAELSECIGSALIQKGFKTAPDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT 180
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTW---REVLAEAAARAAALIALADPDRPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLNTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 181 LGNEAITYIVNKAELSLVFVDKPEKAklLLEGVEnklIPGLKIIVVMDAYGSELVERGQRCgvevtsmkamedlgranrr 260
Cdd:PRK13388 86 RRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTPAYAELVAAAGAL------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 261 KP-KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvECVM----- 334
Cdd:PRK13388 142 TPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT----RDDVCYVSMPLFHS-----NAVMagwap 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 335 -LCHGAKI---------GFfqgdirllMDDLKVLQPTVFPVVPRLL-------NRMFDrifgqANTTLKRWLLDFASKRK 397
Cdd:PRK13388 213 aVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPRD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 398 EAElrsgiirnnslwdrlifhkvqsslggrvrlmvtgaapvsatvltFLRAaLGCQFYEGYGQTEctAGCCLTMPGDWTA 477
Cdd:PRK13388 280 IAE--------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 478 GHVGAPMPCnlIKLVDVEEM---------------NymAAEGEGE-VCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDI 541
Cdd:PRK13388 313 GSIGRGAPG--VAIYNPETLtecavarfdahgallN--ADEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDL 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034638914 542 GKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG----ESLQAFLIAIVVPDVETL 608
Cdd:PRK13388 388 AYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATF 457
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
184-590 |
2.22e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 66.70 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 184 EAITYIVNKAELSLVFVDK---PekaklLLEGVENKLiPGLKIIVVMdaygselverGQRCGVEVTSMK---AMED-LGR 256
Cdd:PRK06018 101 EQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVVL----------TDAAHMPQTTLKnavAYEEwIAE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 257 ANRRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPCPDDTLISFLPLAH-------MFER 328
Cdd:PRK06018 165 ADGDFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHRSNV--LHALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 329 VVECVMLCHGAKIGffQGDIRLLMDDLKVlqpTVFPVVPrllnrmfdrifgqantTLKRWLLDF--ASKRKEAELRSGII 406
Cdd:PRK06018 243 SMGTKLVMPGAKLD--GASVYELLDTEKV---TFTAGVP----------------TVWLMLLQYmeKEGLKLPHLKMVVC 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 407 rnnslwdrlifhkvqsslGGrvrlmvtgaapvSATVLTFLRA--ALGCQFYEGYGQTECT---AGCCLTMPGDWTAGHV- 480
Cdd:PRK06018 302 ------------------GG------------SAMPRSMIKAfeDMGVEVRHAWGMTEMSplgTLAALKPPFSKLPGDAr 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 481 -------GAPMPCNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDKDGWLHTGDIGKWLPNGTLK 551
Cdd:PRK06018 352 ldvlqkqGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMR 427
|
410 420 430
....*....|....*....|....*....|....*....
gi 1034638914 552 IIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:PRK06018 428 ITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
267-608 |
3.70e-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: 65.88 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpCPDDTLISFLPlAHMFERVVE--CVMLCHGAKIGFF 344
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGR---DNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 QGDIRL-------LMDDLKVlqpTVFPVVPRLLNRM-FDRIfgqanTTLKRWLL---DFASKRkeaelrsgiirnnslwd 413
Cdd:cd17648 169 PDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV----------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 414 rliFHKVQSSLGGRVrlmVTGAAPVSATVLTFLRaalgcqFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIklvd 493
Cdd:cd17648 224 ---FEKLRSRFAGLI---INAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 veemnymaaegeGEVCVKGPNVFQGYLKDPAKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd17648 288 ------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQ 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638914 560 FKLaQGEYIAPEKIENIYMRSEPVAQVFV--------HGESLQAFLIAIVVPDVETL 608
Cdd:cd17648 356 VKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
429-604 |
6.90e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.40 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 429 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGDwTAGHV----GAPM-PCNLIKLVDvEEMNYMAa 502
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GlVNYTRLDD-SDERIfttqGRPMsPDDEVWVAD-ADGNPLP- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 503 EGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIY 577
Cdd:PRK10946 377 QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLL 451
|
170 180
....*....|....*....|....*..
gi 1034638914 578 MRsepvaqvfvHGESLQAFLIAIvvPD 604
Cdd:PRK10946 452 LR---------HPAVIHAALVSM--ED 467
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
269-590 |
9.40e-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: 9.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 269 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVE-CVMLCHGAKIGF---F 344
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL----PSDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 QGdiRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfASKRKEAELRsgiirnnslwdrlifHKVQSSL 424
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 425 GGRVRLMVTGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGCCLTMPGDWTAGHVGA----PMPCNLIKlVDVEEMN- 498
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSGFINFFGKPGAIGRNPSllrkVAPLALVK-YDLESGEp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 499 ------YMAAEGEGEV--CV-----KGPnvFQGYLkDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHI 559
Cdd:cd05940 272 irdaegRCIKVPRGEPglLIsrinpLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDT 348
|
330 340 350
....*....|....*....|....*....|.
gi 1034638914 560 FKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd05940 349 FRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
267-614 |
2.00e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.80 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpdDTLISFLPLAhmFERVVECVM--LCHGAKIGFF 344
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN----DRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 QGDIRllmDDLKVLQptvfpvvprLLNRmfDRIfgqanTTlkrwlLDFASkrkeaelrsgiirnNSLWDRLIFHKVQSsl 424
Cdd:PRK12467 3310 DNDLW---DPEELWQ---------AIHA--HRI-----SI-----ACFPP--------------AYLQQFAEDAGGAD-- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 425 GGRVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKL---VDVEEMNY 499
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLDGQLNP 3429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 500 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 572
Cdd:PRK12467 3430 VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGE 3508
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034638914 573 IENIYMRSEPVAQVFVHGESLQA--FLIAIVVPDVETlCSWAQK 614
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQ-GDWRET 3551
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
422-606 |
2.26e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 63.38 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 422 SSLggrvRLMVTGAAPVSATVLtflRAAL---GCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNlIKLVDvEE 496
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-ED 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 497 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 575
Cdd:PRK08276 332 GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
170 180 190
....*....|....*....|....*....|.
gi 1034638914 576 IYMRSEPVAQVFVHGeslqafliaivVPDVE 606
Cdd:PRK08276 410 LLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
112-606 |
2.58e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 112 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 186
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 187 TYIVNKAELsLVFVDKPEKAKLLLEGVENKLipglkiivvmdaygselVERGQrcgvevtsmkamEDLGRANrrKPKPPA 266
Cdd:PRK12316 3147 AYMLEDSGA-QLLLSQSHLRLPLAQGVQVLD-----------------LDRGD------------ENYAEAN--PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHrnivSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqg 346
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRH----SALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV----- 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 347 dirllmddlkVLQPTVFPVVPRLLNRMFDRifGQANTTLKRWlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGG 426
Cdd:PRK12316 3266 ----------VLAGPEDWRDPALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTS 3312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 427 RVRLMVTGAAPVSATVltfLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGH--VGAPMPCNLIKLVDVeEMNYMAAEG 504
Cdd:PRK12316 3313 LKRIVCGGEALPADLQ---QQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGA 3388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 505 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYM 578
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLL 3467
|
490 500
....*....|....*....|....*...
gi 1034638914 579 RSEPVAQVFVHGESLQAfLIAIVVPDVE 606
Cdd:PRK12316 3468 EHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
229-586 |
3.23e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.25 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 229 AYGSELvergQRCGVEVTSMkAMEDL---GRANRRKPKPPAP-EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAT 304
Cdd:PRK05851 114 SHGSHL----ERLRAVDSSV-TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 305 ENTVnpcPDDTLISFLPLAH-MFERVVECVMLChGAKIGffqgdirllmddlkvLQPT-VFPVVP-RLLNrmfdrifgqa 381
Cdd:PRK05851 189 GLDA---ATDVGCSWLPLYHdMGLAFLLTAALA-GAPLW---------------LAPTtAFSASPfRWLS---------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 382 nttlkrWLLDF-ASKRKEAELRSGIIRNNSlwdrlifHKVQSSLGGRVRLMVTGAAPVSATVLT-FLRAALGCQFYEG-- 457
Cdd:PRK05851 240 ------WLSDSrATLTAAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaa 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 458 ---YGQTECTagCCLTMP---------------GDWTAGH--VGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQ 517
Cdd:PRK05851 307 apsYGLAEST--CAVTVPvpgiglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMS 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638914 518 GYLKDPAktaeaLDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIymrsepVAQV 586
Cdd:PRK05851 385 GYLGQAP-----IDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
184-604 |
3.41e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 62.79 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 184 EAITYIVN--KAELSLVFVDkpekaklLLEGVENKLIPGLKIIVV------MDAYGSELVERGQRCGvevtsMKAMEDLG 255
Cdd:PRK12406 73 EEIAYILEdsGARVLIAHAD-------LLHGLASALPAGVTVLSVptppeiAAAYRISPALLTPPAG-----AIDWEGWL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 256 RANRRKPKPPAPEDLAVIcFTSGTTGNPKGamvthrnivsdcsafVKATentvNPCPDDTL--ISFLPLAHMFERVVECV 333
Cdd:PRK12406 141 AQQEPYDGPPVPQPQSMI-YTSGTTGHPKG---------------VRRA----APTPEQAAaaEQMRALIYGLKPGIRAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 334 M---LCHGAKIGFFQGDIRLlmDDLKVLQP-----------------TVFpVVPRllnrMFDRifgqanttlkrwLLDFA 393
Cdd:PRK12406 201 LtgpLYHSAPNAYGLRAGRL--GGVLVLQPrfdpeellqlierhritHMH-MVPT----MFIR------------LLKLP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 394 SKRKEAelrsgiirnnslWDrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG 473
Cdd:PRK12406 262 EEVRAK------------YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 474 DWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNV--FQgYLKDPAKTAEaLDKDGWLHTGDIGKWLPNGT 549
Cdd:PRK12406 318 DALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638914 550 LKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 604
Cdd:PRK12406 395 LFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
121-607 |
1.27e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 61.10 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRpEWVIIEQGCFAYSMVIVPLYDT-LGNEAITYIVNKAELSLVF 199
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVR--AGDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 200 VDKpEKAKLLlEGVENKLIPGLKIIVVMDAygselvERGQRCGVEVtsmkaMEDLGRANRRKPKPPAPEDLAVICFTSGT 279
Cdd:PRK07788 152 YDD-EFTDLL-SALPPDLGRLRAWGGNPDD------DEPSGSTDET-----LDDLIAGSSTAPLPKPPKPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 280 TGNPKGAMVTHRNIVSDCSAFV-----KATENTVNPCPddtlisflplahMFervvecvmlcHG-----AKIGFFQG--- 346
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLLsrvpfRAGETTLLPAP------------MF----------HAtgwahLTLAMALGstv 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 347 ------DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwLLDFASKRKEAelrsgiirnnslwdrlifhkv 420
Cdd:PRK07788 277 vlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPEVLAKYDT--------------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 421 qSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECtAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMN 498
Cdd:PRK07788 323 -SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-ENGN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 499 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 578
Cdd:PRK07788 396 EVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLA 470
|
490 500
....*....|....*....|....*....
gi 1034638914 579 RSEPVAQVFVHGeslqafliaivVPDVET 607
Cdd:PRK07788 471 GHPDVVEAAVIG-----------VDDEEF 488
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
113-638 |
1.44e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 61.06 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 113 KPDQP-YEWL----SYKQVAELSECIGSALIQKGF-KTAPdqfIGIFAQNRPEWVI-----IEQGCfAYsmviVPLYDTL 181
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSLKLpDKSP---IIVFGHMSPEMLAtflgaVKAGH-AY----IPVDVSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 182 GNEAITYIVNKAELSLVFvdkpEKAKLLLEGVENKLIpglkiivvmdayGSELVERGQRCGVEVTSMKAMEDlgranrrk 261
Cdd:PRK04813 87 PAERIEMIIEVAKPSLII----ATEELPLEILGIPVI------------TLDELKDIFATGNPYDFDHAVKG-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 262 pkppapEDLAVICFTSGTTGNPKGAMVTHRNIVS----DCSAFVKATENTV-NPCPddtlISFlplahmfervvecvmlc 336
Cdd:PRK04813 143 ------DDNYYIIFTSGTTGKPKGVQISHDNLVSftnwMLEDFALPEGPQFlNQAP----YSF----------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 337 hgakigffqgdirllmdDLKV--LQP------TVFPVVPRLLNRmfdriFGQANTTLKR-----W----------LLD-- 391
Cdd:PRK04813 196 -----------------DLSVmdLYPtlasggTLVALPKDMTAN-----FKQLFETLPQlpinvWvstpsfadmcLLDps 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 392 FASKrKEAELRsgiirnnslwdRLIF------HKVQSSLGGRVrlmvtgaaPvSATVltflraalgcqfYEGYGQTECTA 465
Cdd:PRK04813 254 FNEE-HLPNLT-----------HFLFcgeelpHKTAKKLLERF--------P-SATI------------YNTYGPTEATV 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 466 GC------------CLTMPgdwtaghVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DK 532
Cdd:PRK04813 301 AVtsieitdemldqYKRLP-------IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTF 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 533 DGW--LHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDve 606
Cdd:PRK04813 373 DGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GYRIELEEIEQNLRQSSYVESAVVvpynKDHKVQY-LIAYVVPK-- 447
|
570 580 590
....*....|....*....|....*....|..
gi 1034638914 607 tlcswaqkrgfEGSFEelcRNKDVKKAILEDM 638
Cdd:PRK04813 448 -----------EEDFE---REFELTKAIKKEL 465
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
268-606 |
3.58e-09 |
|
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: 59.80 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAH--MFERVVECvmLCHGAKIGFFQ 345
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVN----LLHFEREKTNINFSDKVLQFATCSFdvCYQEIFST--LLSGGTLYIIR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 346 GDIRLLMDDLKVL------QPTVFPVVprLLNRMFDrifgqanttLKRWLLDFASKRKEAeLRSG--IIRNNSLWDRLIF 417
Cdd:cd17656 202 EETKRDVEQLFDLvkrhniEVVFLPVA--FLKFIFS---------EREFINRFPTCVKHI-ITAGeqLVITNEFKEMLHE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 418 HkvqsslggrvrlmvtgaapvsatvltflraalGCQFYEGYGQTEC-TAGCCLTMPGDWTAGH--VGAPMPCNLIKLVDv 494
Cdd:cd17656 270 H--------------------------------NVHLHNHYGPSEThVVTTYTINPEAEIPELppIGKPISNTWIYILD- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 495 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 568
Cdd:cd17656 317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRI 395
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034638914 569 APEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVVPDVE 606
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
264-574 |
5.71e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.25 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 264 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkaTENTVNPCPDDTLISFLPLAH-MfervvecvmlchgAKIG 342
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI---SHDGLKVRPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 343 FFQGDI--RLLMDDLKVLQptvFPVVPRLLNRMFDR---------IFG------------QANTTLKRW----------- 388
Cdd:PRK09192 236 FLLTPVatQLSVDYLPTRD---FARRPLQWLDLISRnrgtisyspPFGyelcarrvnskdLAELDLSCWrvagigadmir 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 389 ---LLDFASKRKEA-----------------------ELRSGIIRNNSLWDRLIFHKVQSSLGGRVRlmvtgaaPVSATV 442
Cdd:PRK09192 313 pdvLHQFAEAFAPAgfddkafmpsyglaeatlavsfsPLGSGIVVEEVDRDRLEYQGKAVAPGAETR-------RVRTFV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 443 LtflraalgcqfyegygqtectagcCltmpgdwtaghvGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKD 522
Cdd:PRK09192 386 N------------------------C------------GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRD 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1034638914 523 PAkTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 574
Cdd:PRK09192 429 EE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
265-608 |
6.29e-09 |
|
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: 58.64 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 265 PAPEDLAVICFTSGTTGNPKGAMVTHR----NIVSDCSAFvkatentvNPCPDDTLIsFLPLAHMFERVVECVM-LCHGA 339
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKcilpNIQHFRSLF--------NITSEDILF-LTSPLTFDPSVVEIFLsLSSGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 340 KIgffqgdirllmddlkVLQPTVFPVVPRLLNRMFDRIFG----QANTTLKRwllDFASKRKEAELRSGIirnnslwdrl 415
Cdd:cd17654 186 TL---------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT---------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 416 ifhkvqSSLggRVrLMVTGAAPVSATVLTFLRAA-LGCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVD 493
Cdd:cd17654 238 ------SSL--RV-LALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAyKVPEEDSPVQLGSPLLGTVIEVRD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 VEemnymAAEGEGEVCVKGPNVfQGYLKDPAKTAEALdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 573
Cdd:cd17654 309 QN-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLI 376
|
330 340 350
....*....|....*....|....*....|....*
gi 1034638914 574 ENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETL 608
Cdd:cd17654 377 QQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSR 411
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
273-604 |
5.65e-08 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 55.10 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 273 ICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAH-MFERVVECVMLCHGAKIGFFQGDIRLL 351
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 352 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkEAELRSGIIRnnslwdrlifHKVQSSLGGrvrlm 431
Cdd:cd17633 81 IRKINQYNATVIYLVPTML---------------------------QALARTLEPE----------SKIKSIFSS----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 432 vtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCnliklVDVEEMNymAAEGE-GEVCV 510
Cdd:cd17633 119 --GQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRN--ADGGEiGKIFV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 511 KGPNVFQGYLKdpaktAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 590
Cdd:cd17633 190 KSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
330
....*....|....*..
gi 1034638914 591 ESLQAF---LIAIVVPD 604
Cdd:cd17633 264 IPDARFgeiAVALYSGD 280
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-599 |
6.38e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.33 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 268 EDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFF- 344
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 345 ---QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlLDFASKRKEAELRsgiirnnslwDRLIFHKVQ 421
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELR----------NRVLQRLPQ 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 422 SSLGGRvrlmvtgaapvsatvltflraalgcqfyegYGQTE----CTAGCCLTMPGDWTAghVGAPMPCNLIKLVDvEEM 497
Cdd:PRK05691 1415 VQLHNR------------------------------YGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD-AEL 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 498 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 570
Cdd:PRK05691 1462 NLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEP 1540
|
330 340 350
....*....|....*....|....*....|.
gi 1034638914 571 EKIENIYMRSEPVAQ--VFVHGESLQAFLIA 599
Cdd:PRK05691 1541 EEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
243-324 |
8.28e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.33 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 243 VEVTSMkameDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC----SAFVKATENTvnPCPDDTLIS 318
Cdd:PRK05850 139 IEVDLL----DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVS 212
|
....*.
gi 1034638914 319 FLPLAH 324
Cdd:PRK05850 213 WLPFYH 218
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
261-654 |
1.34e-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: 54.74 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 261 KPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPddTLISFLPLAHmfervveCVMLCHGA 339
Cdd:cd05915 145 ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH-------VNAWCLPY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 340 KIGFFQGDIRLLMDdlkVLQPTVfpvvprllnrMFDRIFGQANTTL--KRWLLDFASKRKEAelrsgiirnnslwdrlif 417
Cdd:cd05915 216 AATLVGAKQVLPGP---RLDPAS----------LVELFDGEGVTFTagVPTVWLALADYLES------------------ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 418 hkVQSSLGGRVRLMVTGAAPvsATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPgDWT------AGHVGAPMPCN-L 488
Cdd:cd05915 265 --TGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspVVVQNFVKS-HLEslseeeKLTLKAKTGLPiP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 489 IKLVDVEEMNYMAAEGEGE----VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 564
Cdd:cd05915 340 LVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG- 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 565 GEYIAPEKIENIYMRSEPVAQVFVHGEslqafliaivvPDV---ETLCSWAQKRGFEGSFEEL---CRNKDVKKAILEDM 638
Cdd:cd05915 419 GEWISSVDLENALMGHPKVKEAAVVAI-----------PHPkwqERPLAVVVPRGEKPTPEELnehLLKAGFAKWQLPDA 487
|
410
....*....|....*.
gi 1034638914 639 VRLGKDSGLKPFEQVK 654
Cdd:cd05915 488 YVFAEEIPRTSAGKFL 503
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
114-606 |
2.33e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 53.86 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 114 PDQPY-------EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPE-----WVIIEQGcfaysmvivpLYDTl 181
Cdd:PRK13390 11 PDRPAvivaetgEQVSYRQLDDDSAALARVLYDAGLR--TGDVVALLSDNSPEalvvlWAALRSG----------LYIT- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 182 gneAITYIVNKAELSLVFVDKPEK---AKLLLEGVENKLIPGLKIIVvmdAYGSELVERGQrcgVEVTsmkamedLGRAN 258
Cdd:PRK13390 78 ---AINHHLTAPEADYIVGDSGARvlvASAALDGLAAKVGADLPLRL---SFGGEIDGFGS---FEAA-------LAGAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 259 RRKPKPPAPedlAVICFTSGTTGNPKGAM--VTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFE-RVVECVML 335
Cdd:PRK13390 142 PRLTEQPCG---AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 336 CHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskRKEAELRSGiirnnslwdrl 415
Cdd:PRK13390 219 LGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR----------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 416 ifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNLiKLVD 493
Cdd:PRK13390 267 --YDVSS-----LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDL-HICD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 494 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 571
Cdd:PRK13390 338 -DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQ 415
|
490 500 510
....*....|....*....|....*....|....*
gi 1034638914 572 KIENIYMRSEPVAQVFVHGeslqafliaivVPDVE 606
Cdd:PRK13390 416 ETENALTMHPAVHDVAVIG-----------VPDPE 439
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
265-590 |
5.10e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 52.38 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 265 PAPEDLAVICfTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDD---------TLISFLPLAHmfervvecvmL 335
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFR--MLMGGADFGTGEFTPSEdahkaaaaaAGTVMFPAPP----------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 336 CHGAK-----IGFFQGDiRLLMDDLKVLQPTVFPVVPR-LLNRMFdrIFGQAnttLKRWLLDfaskrkeaELRSGiiRNN 409
Cdd:cd05924 68 MHGTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 410 SLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLT-FLRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMPcn 487
Cdd:cd05924 132 DL----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 488 LIKLVDvEEMNYM--AAEGEGEVCVKGpNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:cd05924 196 DTVVLD-DDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINT 273
|
330 340
....*....|....*....|....*....
gi 1034638914 563 AqGEYIAPEKIENIyMRSEP-VAQVFVHG 590
Cdd:cd05924 274 G-GEKVFPEEVEEA-LKSHPaVYDVLVVG 300
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
113-290 |
6.89e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.59 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 113 KPDQPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIgiFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNK 192
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 193 AElSLVFVDKPEkaklLLEGVENKLIPGLKIIVVMDAYGSELvergqrcGVEVTSMKAMEDlgrANRRKPKPP-APEDLA 271
Cdd:PRK04319 144 SE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDVEEG-------PGTLDFNALMEQ---ASDEFDIEWtDREDGA 208
|
170 180
....*....|....*....|....*
gi 1034638914 272 VICFTSGTTGNPKG------AMVTH 290
Cdd:PRK04319 209 ILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
254-589 |
7.19e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 52.74 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 254 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIV------------SDCSAFVKATentvnPCPDDtlIS--- 318
Cdd:PRK10252 584 LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllwmqnhyplTADDVVLQKT-----PCSFD--VSvwe 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 319 -FLPlahmfervvecvMLChGAKIGFFQGD-------IRLLMDDLKVlqpTVFPVVPRLL----NRMFDRIFGQANTTLK 386
Cdd:PRK10252 657 fFWP------------FIA-GAKLVMAEPEahrdplaMQQFFAEYGV---TTTHFVPSMLaafvASLTPEGARQSCASLR 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 387 RWlldFASKRK-EAELRsgiirnnSLWDRLIfhkvqsslggrvrlmvtgAAPVsatvltflraalgcqfYEGYGQTECT- 464
Cdd:PRK10252 721 QV---FCSGEAlPADLC-------REWQQLT------------------GAPL----------------HNLYGPTEAAv 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 465 ------AGccltmpGDWTAGHVGAPMPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDK 532
Cdd:PRK10252 757 dvswypAF------GEELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIA 829
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638914 533 DGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVH 589
Cdd:PRK10252 830 DPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
121-290 |
1.23e-06 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 51.72 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKTApDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 200
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKG-DR-VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 201 -------DKP-------EKAKLLLEGVEnklipglKIIVVmdaygselvergQRCGVEVTSMKAmEDLGRANRRKPKPPA 266
Cdd:cd05968 170 adgftrrGREvnlkeeaDKACAQCPTVE-------KVVVV------------RHLGNDFTPAKG-RDLSYDEEKETAGDG 229
|
170 180
....*....|....*....|....*....
gi 1034638914 267 -----PEDLAVICFTSGTTGNPKGAMVTH 290
Cdd:cd05968 230 aerteSEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
121-324 |
1.25e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.80 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGcFAYSMVIVPLYDT-LGNEAITYIVNKAELSLVF 199
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVG--KGDVVALLMENRPEYLAAWLG-LAKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 200 VDkPEKAKLLlEGVENKLIPGLKIIVVMDAYGSELVergqrcgvevtsmkAMEDLGRANRRKPKPPAP-------EDLAV 272
Cdd:PRK08279 140 VG-EELVEAF-EEARADLARPPRLWVAGGDTLDDPE--------------GYEDLAAAAAGAPTTNPAsrsgvtaKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034638914 273 ICFTSGTTGNPKGAMVTHRNIVSDCSAFVkateNTVNPCPDDTLISFLPLAH 324
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFG----GLLRLTPDDVLYCCLPLYH 251
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
246-601 |
2.40e-06 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 50.80 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 246 TSMKAMEDLGRANRRKP---KPPAPEDLAVICFTSGTTGNPKGAMvtHRNivSDCSAFVKAT-ENTVNPCPDDtlisflp 321
Cdd:PRK06060 120 RVAEAAELMSEAARVAPggyEPMGGDALAYATYTSGTTGPPKAAI--HRH--ADPLTFVDAMcRKALRLTPED------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 322 lahmfervvecVMLChGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPrllnrmfdrIFGQANTTLkrwlldfaSKRKEAEL 401
Cdd:PRK06060 189 -----------TGLC-SARMYFAYGLGNSVWFPLATGGSAVINSAP---------VTPEAAAIL--------SARFGPSV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 402 RSGIirnNSLWDRLIFHKVQSSLGGrVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHV 480
Cdd:PRK06060 240 LYGV---PNFFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWRLGTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 481 GAPMPCNLIKLVdVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTaeaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIf 560
Cdd:PRK06060 316 GRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDT- 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034638914 561 KLAQGEYIAPEKIENIYMRSEPVAQVFVHG-------ESLQAFLIAIV 601
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
266-599 |
3.18e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 266 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV--------KATENTVNPCPDDTLISFLPlAHMFERVVECV--ML 335
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVpylalseaDVIAQTASQSFDISVWQFLA-APLFGARVEIVpnAI 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 336 CHgakigffqgDIRLLMDDLKVLQPTVFPVVPRLLNRMF--DRifgQANTTLkRWLLDfaskrkeaelrsgiirnnslwd 413
Cdd:PRK05691 3946 AH---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLP---------------------- 3990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 414 rlifhkvqsslggrvrlmvTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGH---VGAPMPCNLI 489
Cdd:PRK05691 3991 -------------------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfRVDLASTRGSylpIGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 490 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHIFKL 562
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1034638914 563 aQGEYIAPEKIENIYMRSEPV------AQVFVHGESLQAFLIA 599
Cdd:PRK05691 4131 -RGYRIELGEIEARLHEQAEVreaavaVQEGVNGKHLVGYLVP 4172
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
121-615 |
3.70e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 121 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAITYIVNKAELS 196
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERG--VGPDVLVGVAMERSIEMVVallaILKAGGAY----VPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 197 LVFVDKPEKAKL-LLEGVENklipglkiiVVMDAYGSELveRGQRCGVEVTSMkamedlgranrrkpkppAPEDLAVICF 275
Cdd:PRK12316 611 LLLSQSHLGRKLpLAAGVQV---------LDLDRPAAWL--EGYSEENPGTEL-----------------NPENLAYVIY 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 276 TSGTTGNPKGAMVTHRNIVSDCSAFVKATEntvnpcpddtlisfLPLAhmfERVVECVMLCHGAKIGFFQGDirlLMDDL 355
Cdd:PRK12316 663 TSGSTGKPKGAGNRHRALSNRLCWMQQAYG--------------LGVG---DTVLQKTPFSFDVSVWEFFWP---LMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 356 KVLqptvfpVVPRLLNRMFDRIFGQANTTLKRwLLDFASKRKEAELRSGiirnnslwdrlifhKVQSSLGgrVRLMVTGA 435
Cdd:PRK12316 723 RLV------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE--------------DVASCTS--LRRIVCSG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 436 APVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCltmpgDWTAGH-------VGAPMPCNLIKLVDVeEMNYMAAEGEGE 507
Cdd:PRK12316 780 EALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVT-----HWTCVEeggdsvpIGRPIANLACYILDA-NLEPVPVGVLGE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 508 VCVKGPNVFQGYLKDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSE 581
Cdd:PRK12316 854 LYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHP 932
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034638914 582 PVAQVFVHGESLQAfLIAIVVPD------VETLCSWAQKR 615
Cdd:PRK12316 933 WVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
233-325 |
8.85e-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: 48.83 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 233 ELVERGQRCGV--EVTSMKAMEDLGRANRRKPKPPAPEDL---------AVICFTSGTTGNPKGAMVTHRNIVSdCSAFV 301
Cdd:cd05938 98 ALRADGVSVWYlsHTSNTEGVISLLDKVDAASDEPVPASLrahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGFL 176
|
90 100
....*....|....*....|....
gi 1034638914 302 KATentvNPCPDDTLISFLPLAHM 325
Cdd:cd05938 177 SLC----GVTADDVIYITLPLYHS 196
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
267-594 |
6.77e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 45.89 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkatENTVNPCPDDTLISFLPLAH---MFERVVECVMlcHGAKIGF 343
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLL----SHDLNLKNGDRTYTCMPLYHgtaAFLGACNCLM--SGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 344 ---FQgdIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfaskrkeaelrSGIIrnnSLWDRLifHKV 420
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLL------------STPP---SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 421 QSSLGGRVRLMVTGAapvsatvltfLRAALGC-QFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVE---- 495
Cdd:cd05937 205 RVAWGNGLRPDIWER----------FRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 496 -----EMNYM---------AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEALDK------DGWLHTGDIGKWLPNGTL 550
Cdd:cd05937 275 mdpetDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034638914 551 KIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHGESLQ 594
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
505-590 |
8.51e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 505 EGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 584
Cdd:PRK07638 333 IGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVD 410
|
....*.
gi 1034638914 585 QVFVHG 590
Cdd:PRK07638 411 EIVVIG 416
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
261-604 |
9.83e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 261 KPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATENTVNPcPDDTLISfLPLAHmfervvecvmlchgak 340
Cdd:PRK07824 28 RVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTA--SA--DATHDRLGG-PGQWLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 341 IGFFQGDIRLLM---DDLKVLQPTVF--PVVPRLLNRM-FDRIF-GQANTTLKRWLLDFASKRKEAELRSGIIrnnslwd 413
Cdd:PRK07824 86 IAGLQVLVRSVIagsEPVELDVSAGFdpTALPRAVAELgGGRRYtSLVPMQLAKALDDPAATAALAELDAVLV------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 414 rlifhkvqsslggrvrlmvtGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLtmpgdwtagHVGAPMPCNLIKLV 492
Cdd:PRK07824 159 --------------------GGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 493 DveemnymaaegeGEVCVKGPNVFQGY--LKDPAKTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAP 570
Cdd:PRK07824 207 D------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLP 268
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034638914 571 EKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 604
Cdd:PRK07824 269 QVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGD 305
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-562 |
1.22e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 267 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDtlisflplahmfervveCVMlcHGAKIGFFQG 346
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE----RFGMRADD-----------------CEL--HFYSINFDAA 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 347 DIRLLmddlkvlqptvfpvVPRLLN-RMFDRIFGQanttlkrWlldfaskrkEAELRSGIIRNNSLwDRLIFHKVQSS-- 423
Cdd:PRK05691 2389 SERLL--------------VPLLCGaRVVLRAQGQ-------W---------GAEEICQLIREQQV-SILGFTPSYGSql 2437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 424 ---LGGR-----VRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTE-------CTAGccLTMPGDWTAGHVGAPMPCN 487
Cdd:PRK05691 2438 aqwLAGQgeqlpVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGAR 2515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638914 488 LIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIF 560
Cdd:PRK05691 2516 VAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQV 2594
|
..
gi 1034638914 561 KL 562
Cdd:PRK05691 2595 KI 2596
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
259-290 |
1.75e-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: 1.75e-03
10 20 30
....*....|....*....|....*....|..
gi 1034638914 259 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTH 290
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT 254
|
|
| |
