|
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 ... |
52-630 |
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: 978.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 52 QPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 131
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 132 SLVFVDKpekaklllegvenklipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICF 211
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 212 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 291
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 292 KVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVT 369
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 370 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA--EGEGEVCVK 447
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 448 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGE 527
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 528 SLQAFLIAIVVPDVETLCSWA-QKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLL 606
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1832483362 607 TPTMKAKRPELRNYFRSQIDDLYS 630
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
22-632 |
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 1832483362 22 YDDVTTLYEGFQRGIQVSNNGPCLGSR-KPDQ---PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWV 97
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRiRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 98 IIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVdKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQRC 177
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 178 GVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENtvnpCPDDTLISFLP 257
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF----YPSDVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 258 LAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEA 335
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 336 ELRSGiiRNNS-LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAG 414
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 415 HVGAPMPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 491
Cdd:PLN02736 429 HVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 492 KKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAI 570
Cdd:PLN02736 509 KKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAV 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832483362 571 LEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 632
Cdd:PLN02736 589 LADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
22-630 |
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 1832483362 22 YDDVTTLYEGFQRGIQVSNNGPCLgSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQ 101
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVK--PGDRVAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 102 GCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENklIPGLKIIVVMDaygselvERGQRCGVEV 181
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 182 TSMKAMEDLGRANR------RKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISF 255
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 256 LPLAHMFERVVECVMLCHGAKIGFfQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLDFA---S 330
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 331 KRKEAELRSGiiRNNSLW--------DRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAG 402
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 403 CCLTMPGDWTAGHVGAPMPCNLIKLvdveemnymaAEgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 482
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKI----------AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 483 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRG-FEGSFEELC 561
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGlPYTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832483362 562 RNKDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 630
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 ... |
52-617 |
1.69e-175 |
|
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: 506.36 E-value: 1.69e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 52 QPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 131
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVE--PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 132 SLVFVDKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDLAVICF 211
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 212 TSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIGFFQgDIRLLMDD 290
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 291 LKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslGGRVRLMVTG 370
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 371 AAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPN 450
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 451 VFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESlQ 530
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 531 AFLIAIVVPDVETLCSWAQKRG-FEGSFEELCRNKDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNGLLTPT 609
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1832483362 610 MKAKRPEL 617
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
53-614 |
5.27e-159 |
|
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: 466.31 E-value: 5.27e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 53 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 132
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 133 LVFVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpPAPEDLAVICFT 212
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 213 SGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD--- 289
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPELL--GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 290 -----DLKVLQPTVFPVVPRLLNRMFDRIFGQANT--TLKRWLLDFASKRKEAELRSGIirNNSLWDRLIFHKVQSSLGG 362
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 363 RVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYM--AAEG 440
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYStdKPPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 441 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA 520
Cdd:cd17639 330 RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 521 QVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-EGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELF 599
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 1832483362 600 SIDNGLLTPTMKAKR 614
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
53-634 |
5.90e-159 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 471.63 E-value: 5.90e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 53 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 132
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVN--PGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 133 LVFVDKPEKAKLLleGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPkPPAPEDLAVICFT 212
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 213 SGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCP-DDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 291
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATeEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 292 KVLQPTVFPVVPRLlnrmFDRIFG------QANTTLKRWLLDFASKRKEAELRSGIIRNNS--LWDRLIFHKVQSSLGGR 363
Cdd:PLN02861 309 QALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGR 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 364 VRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT-AGHVGAPMPCNLIKLVDVEEMNYMAAEG-- 440
Cdd:PLN02861 385 VRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYDALSDvp 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 441 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA 520
Cdd:PLN02861 465 RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIA 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 521 QVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFS 600
Cdd:PLN02861 544 SIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFD 623
|
570 580 590
....*....|....*....|....*....|....
gi 1832483362 601 IDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV 634
Cdd:PLN02861 624 IERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
24-632 |
6.27e-159 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 471.61 E-value: 6.27e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 24 DVTTLYEGFQRGIQVSNNGPCLGSRKPDQ----PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVII 99
Cdd:PLN02430 40 DITTAWDIFSKSVEKYPDNKMLGWRRIVDgkvgPYMWKTYKEVYEEVLQIGSALRASGAE--PGSRVGIYGSNCPQWIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 100 EQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV-DKpeKAKLLLEGvENKLIPGLKIIVVMDAYGSELVERGQRCG 178
Cdd:PLN02430 118 MEACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 179 VEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRN---IVSDCSAFVKATENTVNPcpDDTLISF 255
Cdd:PLN02430 195 VKTYSWIDFLHMGKENPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFEDKMTH--DDVYLSF 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 256 LPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRK 333
Cdd:PLN02430 273 LPLAHILDRMIEEYFFRKGASVGYYHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYK 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 334 EAELRSGIIRNNS--LWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW 411
Cdd:PLN02430 353 LAWMNRGYSHKKAspMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEM 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 412 TA-GHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKI 488
Cdd:PLN02430 433 CMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKI 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 489 IDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKK 568
Cdd:PLN02430 512 IDRKKNLIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKE 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832483362 569 AILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 632
Cdd:PLN02430 592 HILSELKSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
23-633 |
1.24e-155 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 463.34 E-value: 1.24e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 23 DDVTTLYEGFQRGIQVSNNGPCLGSR-----KPDQpYEWLSYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWV 97
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 98 IIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLlegvenKLIPG----LKIIVVMDAYGSELVER 173
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF------KTCPNsteyMKTVVSFGGVSREQKEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 174 GQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENtVNPC--PDDT 251
Cdd:PLN02614 193 AETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKS-ANAAltVKDV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 252 LISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFA 329
Cdd:PLN02614 272 YLSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 330 SKRKEAELRSGI--IRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTM 407
Cdd:PLN02614 352 FSYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 408 PGDW-TAGHVGAPMPCNLIKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNG 484
Cdd:PLN02614 432 PDELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNG 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 485 TLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNK 564
Cdd:PLN02614 511 SMKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNE 590
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832483362 565 DVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIK 633
Cdd:PLN02614 591 KAKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
4-630 |
1.30e-136 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 415.28 E-value: 1.30e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 4 GGARRSALLDsdEPLVYFYDDVTTLYEGFQRGIQVSNNGPCLGSRK---------PDQ---------PYEWLSYKQVAEL 65
Cdd:PLN02387 38 GYAIRNARFP--ELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisrefetsSDGrkfeklhlgEYEWITYGQVFER 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 66 SECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLL 145
Cdd:PLN02387 116 VCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 146 leGVENKLiPGLKIIVVMDAYGSELVERG-QRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMV 224
Cdd:PLN02387 194 --DISSQL-ETVKRVIYMDDEGVDSDSSLsGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 225 THRNIVSDCSAFVkatenTVNP--CPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD-----------DL 291
Cdd:PLN02387 271 THGNIVATVAGVM-----TVVPklGKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 292 KVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKEAELR------SGIIRnnSLWDRLIFHKVQSSLGGR 363
Cdd:PLN02387 344 SALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGR 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 364 VRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEG--- 440
Cdd:PLN02387 422 IRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmp 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 441 EGEVCVKGPNVFQGYLKDPAKTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRS 516
Cdd:PLN02387 502 RGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVS 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 517 EPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLH 595
Cdd:PLN02387 582 PYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLL 661
|
650 660 670
....*....|....*....|....*....|....*
gi 1832483362 596 PELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 630
Cdd:PLN02387 662 PEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
48-499 |
1.35e-130 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 390.13 E-value: 1.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 48 RKPDQP------YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 121
Cdd:pfam00501 7 RTPDKTalevgeGRRLTYRELDERANRLAAGLRALGVG--KGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 122 ITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVergqrcgvevtsMKAMEDLGRANRRKPKPP 201
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVEC-VMLCHGAKIGFF 280
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 QGDIRL----LMDDLKVLQPTVFPVVPRLLNRMFDrifgqaNTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkv 356
Cdd:pfam00501 233 PGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------AGAPKRALL------------------------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 357 qsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW---TAGHVGAPMPCNLIKLVDVEEM 433
Cdd:pfam00501 277 -----SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETG 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832483362 434 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 499
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
57-629 |
4.87e-104 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 330.79 E-value: 4.87e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfV 136
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLT--KGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI-V 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKPEKAKLLLEGVENKLIPGLKIIvvmdaYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPE---DLAVICFTS 213
Cdd:PTZ00216 199 CNGKNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 214 GTTGNPKGAMVTHRNIVSDCSAFV-KATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD--- 289
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALEdRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 290 ----DLKVLQPTVFPVVPRLlnrmFDRI----------FGqantTLKRWLLDFASKRKEAELRSGiiRNNSLWDRLIFHK 355
Cdd:PTZ00216 352 rphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 356 VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCqFYEGYGQTECTagCC--LTMPGDWTAGHVGAPMPCNLIKLVDVEEM 433
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTGDLEPNAVGQLLKGVEMKLLDTEEY 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 NYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENI 512
Cdd:PTZ00216 499 KHTdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEAL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 513 YMRSEPVAQ----VFVHgeSLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQ 588
Cdd:PTZ00216 579 YGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1832483362 589 VKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 629
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 ... |
52-615 |
1.23e-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: 1.23e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 52 QPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 131
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 132 SLVFVdkpekaklllegvENklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppAPEDLAVICF 211
Cdd:cd17640 79 VALVV-------------EN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 212 TSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMDDL 291
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSD----IVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 292 KVLQPTVFPVVPRLlnrmfdrifgqanttlkrWlldfaskrkEAeLRSGI---IRNNSLWDRLIFHKVQSslGGRVRLMV 368
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 369 TGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKG 448
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 449 PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGES 528
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 529 lQAFLIAIVVPDVETLCSWAQKRG--FEGSFEELCRNKDVKKAI-LEDMVRLGKDSGLKPFEQVKGITLHPELFsIDNGL 605
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGE 456
|
570
....*....|
gi 1832483362 606 LTPTMKAKRP 615
Cdd:cd17640 457 MTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
54-614 |
8.64e-82 |
|
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: 8.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 54 YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSL 133
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLE--PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 134 VFVDKPEKAKLLLEGVenkliPGlKIIVVMDAYGSELvergqRCGVEVTSMKAMedlGRANRRKPkPPAPEDLAVICFTS 213
Cdd:cd05932 82 LFVGKLDDWKAMAPGV-----PE-GLISISLPPPSAA-----NCQYQWDDLIAQ---HPPLEERP-TRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 214 GTTGNPKGAMVTHRNIVSDCSAFVkateNTVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIgFFQGDIRLLMDDLK 292
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQAGI----EHIGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 293 VLQPTVFPVVPRLLNRMFDRIFgqanttlkrwlldfaSKRKEAELRsgIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGA 371
Cdd:cd05932 222 RARPTLFFSVPRLWTKFQQGVQ---------------DKIPQQKLN--LLLKIPVVNSLVKRKVLKGLGlDQCRLAGCGS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 372 APVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPNV 451
Cdd:cd05932 285 APVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 452 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQA 531
Cdd:cd05932 353 MMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 532 FLIAIVVPDVETLCSWAQKRG-FEGSFeelcrnkdvkKAILEDMvrlgkDSGLKPFEQVKGITLHPELFSIDNGLLTPTM 610
Cdd:cd05932 433 PLALVVLSEEARLRADAFARAeLEASL----------RAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTL 497
|
....
gi 1832483362 611 KAKR 614
Cdd:cd05932 498 KIKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
48-551 |
8.15e-76 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 249.34 E-value: 8.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 48 RKPDQP-----YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 122
Cdd:COG0318 11 RHPDRPalvfgGRRLTYAELDARARRLAAALRALGVG--PGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 123 TYIVNKAELSLVFVdkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppa 202
Cdd:COG0318 89 AYILEDSGARALVT------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 pedlAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI---- 277
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT----PGDVVLVALPLFHVFGLTVGLLApLLAGATLvllp 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 278 GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELRSgiirnnslwdrlifhkvq 357
Cdd:COG0318 175 RF---DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------ 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 358 sslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNY 435
Cdd:COG0318 217 ------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 436 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMR 515
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAA 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1832483362 516 SEPVAQVFV-------HGESLQAFLI--AIVVPDVETLCSWAQKR 551
Cdd:COG0318 368 HPGVAEAAVvgvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
58-614 |
5.07e-73 |
|
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: 5.07e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 58 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIE---QGCFAYSMvivPLYDTLGNEAITYIVNKAELSLV 134
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAElaaQAIGALSL---GIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 135 FVDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQrcgveVTSMKAMEDLGRA-NRRKPK-------PPAPEDL 206
Cdd:cd17641 88 IAEDEEQVDKLLEIADR--IPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 207 AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQgDIR 285
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLG----PGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 286 LLMDDLKVLQPTVFPVVPRLLNRM--FDRIFGQANTTLKRWLLDF--------ASKRKEAELRSGIIRNNS-LWDRLIFH 354
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 355 KVQSSLG-GRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVeem 433
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 nymaaegeGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIY 513
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 514 MRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDsgLKPFEQV-KG 591
Cdd:cd17641 464 KFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRIrRF 540
|
570 580
....*....|....*....|...
gi 1832483362 592 ITLHPELfSIDNGLLTPTMKAKR 614
Cdd:cd17641 541 LLLYKEL-DADDGELTRTRKVRR 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
49-629 |
5.22e-73 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 246.11 E-value: 5.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 49 KPDQPYEWLSYKQVAELseCIGSAliqKGF-KTAPDQF--IGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYI 125
Cdd:cd05933 1 KRGDKWHTLTYKEYYEA--CRQAA---KAFlKLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 126 VNKAELSLVFVDKPEKAKLLLEgVENKLiPGLKIIVvmdAYGSELVERGQRcgveVTSMKAMEDLGR-----ANRRKPKP 200
Cdd:cd05933 76 AETSEANILVVENQKQLQKILQ-IQDKL-PHLKAII---QYKEPLKEKEPN----LYSWDEFMELGRsipdeQLDAIISS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 201 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVEcVMLC--HGAKIG 278
Cdd:cd05933 147 QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPikVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 279 FFQGDIR--LLMDDLKVLQPTVFPVVPRLLNRMFDRI--FGQANTTLKRWLLDFAsKRKEAE-------LRSGIIRNNSL 347
Cdd:cd05933 226 FAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSPLFYRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 348 WDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIK 426
Cdd:cd05933 305 AKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 427 LVDVEemnymaAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 506
Cdd:cd05933 384 IHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 507 EKIEN-IYMRSEPVAQVFVHGESLQaFLIAIVV----PDVET----------LCSWAQKRGFEGS-FEELCRNKD--VKK 568
Cdd:cd05933 458 VPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTlkceVNPETgepldelteeAIEFCRKLGSQATrVSEIAGGKDpkVYE 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832483362 569 AILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 629
Cdd:cd05933 537 AIEEGIKRVNKKAISNA-QKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
25-607 |
3.97e-69 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 235.43 E-value: 3.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 25 VTTLYEGF-QRgiqvsnngPCLGSRK---PDQPYE-WLSYKQVAELSECIGSALIQKGFKTA----------PDQFIGIF 89
Cdd:cd17632 28 IATVMTGYaDR--------PALGQRAtelVTDPATgRTTLRLLPRFETITYAELWERVGAVAaahdpeqpvrPGDFVAVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 90 AQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDK---PEKAKLLLEGvenkliPGLKIIVVMDaY 166
Cdd:cd17632 100 GFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSAehlDLAVEAVLEG------GTPPRLVVFD-H 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 167 GSEL----------VERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPED---LAVICFTSGTTGNPKGAMVTHRNIVSdc 233
Cdd:cd17632 173 RPEVdahraalesaRERLAAVGIPVTTLTLIAVRGRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTERLVAT-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 234 sAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTVFPVVPRLLNRMFD 311
Cdd:cd17632 251 -FWLKVSSIQDIRPPASITLNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 312 RIfgQAntTLKRWLLDFA-----SKRKEAELRsgiirnnslwdrlifhkvQSSLGGRVRLMVTGAAPVSATVLTFLRAAL 386
Cdd:cd17632 329 RY--QA--ELDRRSVAGAdaetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 387 GCQFYEGYGQTEctAGCCLTmpgdwtAGHVGAPmPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTA 463
Cdd:cd17632 387 DLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 464 EALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVET 543
Cdd:cd17632 458 EVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDA 537
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832483362 544 LCSWAQKRgfegsfeelcrnkdVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLT 607
Cdd:cd17632 538 LAGEDTAR--------------LRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
57-614 |
6.01e-68 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 228.87 E-value: 6.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKTAPDqfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDLAVICFTSGTT 216
Cdd:cd05914 86 SDED----------------------------------------------------------------DVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVSD---CSAFVKATENtvnpcpdDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQGDIRLLMDDLK 292
Cdd:cd05914 102 GNSKGVMLTYRNIVSNvdgVKEVVLLGKG-------DKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 293 VLQPTVFPVVPRLLNRMFDRIFGQAN-TTLKRWLLDFASKRKEAELRSgiirnnslwdrLIFHKVQSSLGGRVRLMVTGA 371
Cdd:cd05914 175 FAQVTPTLGVPVPLVIEKIFKMDIIPkLTLKKFKFKLAKKINNRKIRK-----------LAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 372 APVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPmpcnlIKLVDVEEMNYMAAEGEGEVCVKGPNV 451
Cdd:cd05914 244 AKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 452 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA--QVFVHGESL 529
Cdd:cd05914 318 MKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKL 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 530 QAflIAIVVPDvetlcswaqkrgFEGSFEELCRNKdvKKAILEDmVRLGKDSGLKPFEQVKGITLHPELFSidnglLTPT 609
Cdd:cd05914 398 VA--LAYIDPD------------FLDVKALKQRNI--IDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFE-----KTPK 455
|
....*
gi 1832483362 610 MKAKR 614
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 ... |
205-551 |
7.56e-65 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 216.77 E-value: 7.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKI----GFF 280
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 QGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiirnnslwdrlifhkvqssl 360
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 361 ggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT--AGHVGAPMPCNLIKLVDVEEmNYMAA 438
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 439 EGEGEVCVKGPNVFQGYLKDPAKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEP 518
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832483362 519 VAQVFVHG---ESLQAFLIAIVVP------DVETLCSWAQKR 551
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
57-526 |
1.52e-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: 1.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKPEKAKLLleGVENKLIPGLKIIVvMDAYGSELVERGQrcGVEVTSMKAMEDlgranRRKPKPPAPEDLAVICFTSGTT 216
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKIIV-LDDKPDGVLSIED--LLSPTLGEEDED-----LPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVSDCSaFVKATEnTVNPCPDDTLISFLPLAHMFervveCVMLCHGAKIgffQG---------DIRLL 287
Cdd:cd05911 159 GLPKGVCLSHRNLIANLS-QVQTFL-YGNDGSNDVILGFLPLYHIY-----GLFTTLASLL---NGatviimpkfDSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 288 MDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRlifHKVQSslggrVRLM 367
Cdd:cd05911 229 LDLIEKYKITFLYLVPPIAAALA---------------------------------KSPLLDK---YDLSS-----LRVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 368 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCV 446
Cdd:cd05911 268 LSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 447 KGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 526
Cdd:cd05911 348 RGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
46-551 |
5.33e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 214.38 E-value: 5.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 46 GSRKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIieqGCFAYSM---VIVPLYDTL 117
Cdd:PRK07656 15 ARRFGDKEAyvfgdQRLTYAELNARVRRAAAALAALGIG--KGDRVAIWAPNSPHWVI---AALGALKagaVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 118 GNEAITYIVNKAELSLVFVdkpekAKLLLeGVENKL---IPGLKIIVVMDaygselVERGQRCGVEVTSMKAMedLGRAN 194
Cdd:PRK07656 90 TADEAAYILARGDAKALFV-----LGLFL-GVDYSAttrLPALEHVVICE------TEEDDPHTEKMKTFTDF--LAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 195 RRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMF---ERVVECVM 270
Cdd:PRK07656 156 PAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLT----EGDRYLAANPFFHVFgykAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 271 lcHGAKIgffqgDIRLLMDDLKVLQ------PTVFPVVPrllnrmfdrifgqantTLKRWLLDFAsKRKEAELRSgiirn 344
Cdd:PRK07656 232 --RGATI-----LPLPVFDPDEVFRlieterITVLPGPP----------------TMYNSLLQHP-DRSAEDLSS----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 345 nslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLTMPGD---WTAGHVGAPM 420
Cdd:PRK07656 283 -------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 421 PCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 499
Cdd:PRK07656 344 AGVENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832483362 500 QGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVP------DVETLCSWAQKR 551
Cdd:PRK07656 421 GGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
48-539 |
3.01e-61 |
|
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: 210.88 E-value: 3.01e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 48 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 122
Cdd:cd05936 11 RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 123 TYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkaMEDLGRANRRKPKPPA 202
Cdd:cd05936 89 EHILNDSGAKALIVAVS-----------------------------------------------FTDLLAAGAPLGERVA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 --PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAfVKATENTVNPcPDDTLISFLPLAHMFERVVECV-MLCHGAKIGF 279
Cdd:cd05936 122 ltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWLEDLLE-GDDVVLAALPLFHVFGLTVALLlPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 280 FQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiirnnslwdrlifhkvqs 358
Cdd:cd05936 200 IPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 359 slggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMA 437
Cdd:cd05936 244 -----LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 438 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 517
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHP 395
|
490 500
....*....|....*....|....*....
gi 1832483362 518 PVAQVFV-------HGESLQAFliaiVVP 539
Cdd:cd05936 396 AVAEAAVvgvpdpySGEAVKAF----VVL 420
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
58-527 |
8.36e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 211.20 E-value: 8.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 58 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIieqgC-FAYSM---VIVPLYDTLGNEAITYIVNKAELSL 133
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVK--KGDRVAVFDWNSHEYLE----AyFAVPKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 134 VFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSElvergqRCGVEVTSMKAMedLGRANRRKPKPPAPE-DLAVICFT 212
Cdd:PRK06187 107 VLVD-SEFVPLL-AAILPQL-PTVRTVIVEGDGPAA------PLAPEVGEYEEL--LAAASDTFDFPDIDEnDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 213 SGTTGNPKGAMVTHRNIVSD---CSAFVKATentvnpcPDDTLISFLPLAHMFERVVECVMLCHGAKI---GFFqgDIRL 286
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHslaVCAWLKLS-------RDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPEN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 287 LMDDLKVLQPTVFPVVPRLLNRMFdrifgQANTTLKRWLldfaskrkeaelrsgiirnnslwdrlifhkvqsslgGRVRL 366
Cdd:PRK06187 247 LLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF------------------------------------SSLRL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 367 MVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLT----MPGDWT-AGHVGAPMPCNLIKLVDvEEMNYMAAEG 440
Cdd:PRK06187 286 VIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 441 E--GEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEP 518
Cdd:PRK06187 365 GevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPA 442
|
....*....
gi 1832483362 519 VAQVFVHGE 527
Cdd:PRK06187 443 VAEVAVIGV 451
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
205-551 |
1.28e-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: 167.85 E-value: 1.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVV----------ECVMLchg 274
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGLVNallcplfagaSVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 275 akiGFF---QGDIRLLMDDLkvlqpTVFPVVPRllnrMFDRIFGQANTTLKrwllDFASKRKEAElrsgiirnnslwdrl 351
Cdd:cd05941 163 ---PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 352 ifhkvqsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMP--GDWTAGHVGAPMPCNLIKLVD 429
Cdd:cd05941 212 ----------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEK 508
Cdd:cd05941 280 EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALE 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832483362 509 IENIYMRSEPVAQVFVHGESLQAF---LIAIVVP-------DVETLCSWAQKR 551
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
57-552 |
2.57e-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: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAeLSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd05909 8 LTYRKLL-TGAIALARKLAKM--TKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKP--EKAKLL-------------LEGVENKLIPGLKIIVVMDAYgselvergqrcgveVTSMKAMEDLGRANRRkpkpp 201
Cdd:cd05909 85 SKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFLAGK--------------FPPKWLLRIFGVAPVQ----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 aPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQ 281
Cdd:cd05909 146 -PDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFHSF---------------GLTG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 282 GDIRLLMDDLKVLQ---PTVFPVVPRLLNRMFDRIFGQANTTLKRWLldfasKRKEAELRSGIirnnslwdrlifhkvqs 358
Cdd:cd05909 206 CLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPTFLRGYA-----RAAHPEDFSSL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 359 slggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMA 437
Cdd:cd05909 264 ------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 438 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSE 517
Cdd:cd05909 338 IGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEIL 415
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1832483362 518 P----VAQVFV----HGESLQAFLIAIvVPDVETLCSWAQKRG 552
Cdd:cd05909 416 PedneVAVVSVpdgrKGEKIVLLTTTT-DTDPSSLNDILKNAG 457
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
168-512 |
5.73e-41 |
|
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: 156.24 E-value: 5.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 168 SELVERGQRCGVEVTSMKAMEDLGRANRR------KPKPPAPE----DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV 237
Cdd:cd05904 112 AELAEKLASLALPVVLLDSAEFDSLSFSDllfeadEAEPPVVVikqdDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 238 KATENtvNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMfdr 312
Cdd:cd05904 192 AGEGS--NSDSEDVFLCVLPMFHIYGLSSFALgLLRLGATVvvmpRF---DLEELLAAIERYKVTHLPVVPPIVLAL--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 313 ifgqanttlkrwlldfaskrkeaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFY 391
Cdd:cd05904 264 ------------------------VKSPIVDKYDL----------SSL----RQIMSGAAPLGKELIEAFRAKFpNVDLG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 392 EGYGQTECTAGCCLTMPGDWTAGHVG-----APMPCnlIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL 466
Cdd:cd05904 306 QGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNVE--AKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832483362 467 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 512
Cdd:cd05904 384 DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
47-540 |
1.09e-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: 153.92 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 47 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 121
Cdd:cd17631 6 RRHPDRTaLVFggrsLTYAELDERVNRLAHALRALGVA--KGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 122 ITYIVNKAElslvfvdkpekAKLLLEgvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpp 201
Cdd:cd17631 84 VAYILADSG-----------AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 apeDLAVICFTSGTTGNPKGAMVTHRNIvsdcsafvkaTENTVN------PCPDDTLISFLPLAHMFERVVECVM-LCHG 274
Cdd:cd17631 99 ---DLALLMYTSGTTGRPKGAMLTHRNL----------LWNAVNalaaldLGPDDVLLVVAPLFHIGGLGVFTLPtLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 275 AKI----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTlkrwllDFASkrkeaelrsgiirnnslwdr 350
Cdd:cd17631 166 GTVvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS-------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 351 lifhkvqsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLV 428
Cdd:cd17631 215 -------------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 429 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEK 508
Cdd:cd17631 281 D-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAE 357
|
490 500 510
....*....|....*....|....*....|....*....
gi 1832483362 509 IENIYMRSEPVAQVFV-------HGESlqafLIAIVVPD 540
Cdd:cd17631 358 VEDVLYEHPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
203-627 |
9.50e-39 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 152.57 E-value: 9.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFVKatentVNPcpdDTLISFLPLAHMFERVVECVMLCHGAK 276
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK-----YNP---KTHLSYLPISHIYERVIAYLSFMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 277 IGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLdfaskRKEAELRSGiiRNNSLWDRL--- 351
Cdd:PTZ00342 375 INIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLV-----KKILSLRKS--NNNGGFSKFleg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 352 IFH---KVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPM-PCNLIKL 427
Cdd:PTZ00342 448 ITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 428 VDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 507
Cdd:PTZ00342 528 RTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 508 KIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-------EGSFEELCRNKDVKKAILEDMVR---- 576
Cdd:PTZ00342 608 MLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlestginEKNYLEKLTDETINNNIYVDYVKgkml 687
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1832483362 577 -LGKDSGLKPFEQVKGITLHPELFSIDNgLLTPTMKAKRPELRNYFRSQIDD 627
Cdd:PTZ00342 688 eVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKDYAFFIDQ 738
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
190-544 |
1.86e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 149.91 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 190 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKAteNTVNPCpdDTLISFLPLAHMFERVV 266
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGS--NLNEGC--EILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 267 ECVMLchgakigffqgdirLLMDDLKVLQPTvfpvvPRLLNRMFdrifgqanTTLKRWLLdfaskrkeaelrSGIIRNNS 346
Cdd:PRK05677 269 HCMAM--------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 347 LWDRLI----FHKVQSSlggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 422
Cdd:PRK05677 310 LFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 423 NLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 502
Cdd:PRK05677 387 TLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGF 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1832483362 503 YIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaIVVPDVETL 544
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
51-551 |
3.35e-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: 3.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 51 DQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVI-----IEQGCfaysmVIVPLYDTLGNEAITYI 125
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIK--KGDRVAIALPNGLEFVVaflaaARAGA-----VVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 126 VNKAELSLVFVDKPEkaklLLEGVENKLIPGLKII-VVMDAYGSELVERGQRCGVEvtsmkameDLGRANRRKPKPPAPE 204
Cdd:cd05926 82 LADLGSKLVLTPKGE----LGPASRAASKLGLAILeLALDVGVLIRAPSAESLSNL--------LADKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----GF 279
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLsTLAAGGSVvlppRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 280 fqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqss 359
Cdd:cd05926 226 ---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEPNPESPP---------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 360 lgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgcclTM------PGDWTAGHVGAPMPcNLIKLVDvEEM 433
Cdd:cd05926 265 --PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH----QMtsnplpPGPRKPGSVGKPVG-VEVRILD-EDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 513
Cdd:cd05926 337 EILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVL 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1832483362 514 MRSEPVAQ--VF-----VHGESLQAFliaiVVP------DVETLCSWAQKR 551
Cdd:cd05926 416 LSHPAVLEavAFgvpdeKYGEEVAAA----VVLregasvTEEELRAFCRKH 462
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
203-535 |
1.23e-37 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 147.51 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcPDDTLISFLPLAHMFERVVECVMLCH-GAKigffq 281
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHP-GKELVVTALPLYHIFALTVNCLLFIElGGQ----- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 282 gdirllmdDLKVLQPTVFP-VVPRLLNRMFDRIFGqANTTLKRWLldfaskrkeaelrsgiirNNSLwdrliFHKVQSSl 360
Cdd:PRK08974 279 --------NLLITNPRDIPgFVKELKKYPFTAITG-VNTLFNALL------------------NNEE-----FQELDFS- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 361 ggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCcltmPGDWT--AGHVGAPMPCNLIKLVDvEEMNY 435
Cdd:PRK08974 326 --SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVN----PYDLDyySGSIGLPVPSTEIKLVD-DDGNE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 436 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMR 515
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVML 476
|
330 340
....*....|....*....|....*..
gi 1832483362 516 SEPVAQVF-------VHGESLQAFLIA 535
Cdd:PRK08974 477 HPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
58-512 |
4.73e-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: 4.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 58 SYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVD 137
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 138 KPEKAKLLleGVENKLiPGLKIIVVMDaygSELVERGQRCgveVTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSG 214
Cdd:cd17642 124 KKGLQKVL--NVQKKL-KIIKTIIILD---SKEDYKGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 215 TTGNPKGAMVTHRNIvsdCSAFVKATENTV--NPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGF---FQGDIRL-LM 288
Cdd:cd17642 195 STGLPKGVQLTHKNI---VARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 289 DDLKV----LQPTVFPVVPRllnrmfdrifgqanttlkrwlldfaskrkeaelrSGIIRNNSLwdrlifhkvqSSLggrv 364
Cdd:cd17642 272 QDYKVqsalLVPTLFAFFAK----------------------------------STLVDKYDL----------SNL---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 365 RLMVTGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGE 443
Cdd:cd17642 304 HEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832483362 444 VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 512
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESI 451
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
203-564 |
1.22e-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: 140.11 E-value: 1.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFV----KATENTVNPCPddtlisfLPLAHMFERVVEcVMLC--HGAK 276
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIgerlGLTEQDRLCIP-------VPLFHCFGSVLG-VLACltHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 277 IGFfqgdIRLLMDDLKVLQP------TVFPVVPRllnrMFDRIFGQAnttlKRWLLDFASkrkeaeLRSGIIrnnslwdr 350
Cdd:cd05917 72 MVF----PSPSFDPLAVLEAiekekcTALHGVPT----MFIAELEHP----DFDKFDLSS------LRTGIM-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 351 lifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 426
Cdd:cd05917 126 -------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 427 LVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 505
Cdd:cd05917 187 IVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIY 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832483362 506 PEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQ-KRGFEGSFEEL---CRNK 564
Cdd:cd05917 265 PREIEEFLHTHPKVSDVQVVG-----------VPDErygEEVCAWIRlKEGAELTEEDIkayCKGK 319
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
205-551 |
2.62e-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: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI---GFF 280
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLT----EDDRYLIINPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 qgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELrsgiirnnslwdrlifhkvqSSL 360
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 361 ggrvRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTagcCLTM--PGD---WTAGHVGAPMPcnliklvDVEemn 434
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG---VATMcrPGDdaeTVATTCGRACP-------GFE--- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 435 yMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 514
Cdd:cd17638 181 -VRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALA 258
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832483362 515 RSEPVAQVFV-------HGESLQAFLIA--IVVPDVETLCSWAQKR 551
Cdd:cd17638 259 EHPGVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRER 304
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
59-551 |
3.13e-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: 3.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 59 YKQVAELSECIGSALIQKGfktapdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDk 138
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 139 pekAKLLLEGVENKLIPGLKiivvmdAYGselvergqRCGVEVTSMKAMEDLgranrrkpkppapedlAVICFTSGTTGN 218
Cdd:TIGR01923 79 ---SLLEEKDFQADSLDRIE------AAG--------RYETSLSASFNMDQI----------------ATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 219 PKGAMVTHRNIvsdcSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLmDDLKVLQPTV 298
Cdd:TIGR01923 126 PKAVPHTFRNH----YASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 299 FPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkvqsslggrvrlmvtGAAPVSATV 378
Cdd:TIGR01923 201 ISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGSAIPAPL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 379 LTFLRAaLGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHVGAPMPCNLIKL-VDveemnymAAEGEGEVCVKGPNVFQGYL 456
Cdd:TIGR01923 236 IEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVD-------NKEGHGEIMVKGANLMKGYL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 457 kDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESL 529
Cdd:TIGR01923 308 -YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQVP 385
|
490 500
....*....|....*....|..
gi 1832483362 530 QAFLIAIVVPDVETLCSWAQKR 551
Cdd:TIGR01923 386 VAYIVSESDISQAKLIAYLTEK 407
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
47-526 |
4.98e-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: 4.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 47 SRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIV 126
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVK--PGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 127 NKAELSLVFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSELVERGQRCGvevtsmkAMEDL-GRANRRKPKPPAPE- 204
Cdd:cd12119 94 NHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAGVGVL-------AYEELlAAESPEYDWPDFDEn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTlisFLPLAHMFErvVE-------CVMLchGAKI 277
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVL--HAMAALLTDGLGLSESDV---VLPVVPMFH--VNawglpyaAAMV--GAKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 278 ----GFFQGDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRifgqanttLKRWLLDFASKRkeaelrsgiirnnslwdrli 352
Cdd:cd12119 235 vlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLDH--------LEANGRDLSSLR-------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 353 fhkvqsslggrvRLMVTGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHV----------GAPMP 421
Cdd:cd12119 284 ------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPVP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 422 CNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 499
Cdd:cd12119 350 GVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG 427
|
490 500
....*....|....*....|....*..
gi 1832483362 500 qGEYIAPEKIENIYMRSEPVAQVFVHG 526
Cdd:cd12119 428 -GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
190-495 |
5.80e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 142.83 E-value: 5.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 190 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCS---AFVKATentvnPCPDDTLISFLPLAHMF--ER 264
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGL-----GDGPERVLAALPMFHAYglTL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 265 VVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLlnrmFDRIfgqanttlkrwlldfaskRKEAELRsGIirn 344
Cdd:PRK05605 280 CLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 345 nslwdrlifhkvqsSLGGrVRLMVTGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMP 421
Cdd:PRK05605 334 --------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFP 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832483362 422 CNLIKLVDVEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 495
Cdd:PRK05605 397 DTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
183-535 |
6.09e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 139.57 E-value: 6.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 183 SMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD------CSAFVKATENTVNPCPDDTLISFL 256
Cdd:PRK12492 186 PFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAPL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 257 PLAHMFERVVECVMLchgakigFFQGDIRLLMDDlkvlqptvfpvvPRLLNRMFDRifgqanttLKRWLLdfaskrkeae 336
Cdd:PRK12492 266 PLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF---------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 337 lrSGIIRNNSLWDRLIFHKVQSSLGGRvRLMVT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCLTMPGDWTA 413
Cdd:PRK12492 309 --SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELAR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 414 -GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 492
Cdd:PRK12492 385 lGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRK 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1832483362 493 KHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFLIA 535
Cdd:PRK12492 464 KDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
50-564 |
7.42e-35 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 139.18 E-value: 7.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 50 PDQPYEWlSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEqgcFAYS-----MV-IVPLYDTlgNEaIT 123
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIE--KGDRVGIWAPNVPEWVLTQ---FATAkigaiLVtINPAYRL--SE-LE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 124 YIVNKAELS-LVFVDK--------------PEKAKLLLEGVENKLIPGLKIIVVMDAYGSelveRGQRCGVEVTSMKAME 188
Cdd:PRK08315 109 YALNQSGCKaLIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGDEKH----PGMLNFDELLALGRAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 189 DLGRANRRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFVkaTENtVNPCPDDTLISFLPLAHMFErvveC 268
Cdd:PRK08315 185 DDAELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNILNN-GYFI--GEA-MKLTEEDRLCIPVPLYHCFG----M 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 269 VM-----LCHGAKI-----GFfqgdirllmDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwl 325
Cdd:PRK08315 256 VLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 326 LDFASkrkeaeLRSGI-------IRnnslwdrlIFHKVQSSLGgrvrlM--VTGAapvsatvltflraalgcqfyegYGQ 396
Cdd:PRK08315 312 FDLSS------LRTGImagspcpIE--------VMKRVIDKMH-----MseVTIA----------------------YGM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 397 TECTAGCCLTMPGD------WTaghVGAPMPCNLIKLVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD 469
Cdd:PRK08315 351 TETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 470 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCS 546
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG-----------VPDEkygEEVCA 494
|
570 580
....*....|....*....|..
gi 1832483362 547 WAQKR-GFEGSFEEL---CRNK 564
Cdd:PRK08315 495 WIILRpGATLTEEDVrdfCRGK 516
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
190-619 |
2.78e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 137.70 E-value: 2.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 190 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKATENTVNPCpdDTLISFLPLAHMFERVV 266
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKLEEGC--EVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 267 ECVMLchgAKIGFFQG------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsg 340
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 341 iirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT-MPGDWTAGHVGAP 419
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 420 MPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 498
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 499 AQGEYIAPEKIENIYMRSEPVAQVfvhgeslqaflIAIVVPDvetlcswaQKRGfegsfeELCRNKDVKK--AILEDMVR 576
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1832483362 577 LGKDSGLKPFEQVKGITLHPELFSIDNGlltptmKAKRPELRN 619
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
191-573 |
1.22e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 134.35 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 191 GRANRRKPKPPaPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvecvm 270
Cdd:PRK07787 116 ARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHV--------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 271 lcHGAKIGffqgdirllmddlkVLQPTvfpvvprllnrmfdRIFGQANTTLKrwlldFASKRKEAELRSGiirnNSL--- 347
Cdd:PRK07787 182 --HGLVLG--------------VLGPL--------------RIGNRFVHTGR-----PTPEAYAQALSEG----GTLyfg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 348 ----WDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCN 423
Cdd:PRK07787 223 vptvWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 424 LIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHI 495
Cdd:PRK07787 303 ETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 496 FKLAQGEyiapekIENIYMRSEPVAQVFVHGE---SLQAFLIAIVVPD-----------VETLCSwAQKRGFEGSF-EEL 560
Cdd:PRK07787 382 YRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGAddvaadelidfVAQQLS-VHKRPREVRFvDAL 454
|
410
....*....|....*.
gi 1832483362 561 CRN---KDVKKAILED 573
Cdd:PRK07787 455 PRNamgKVLKKQLLSE 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
57-564 |
1.55e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 135.29 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEqgcFAYSMV------IVPLYDTlgnEAITYIVNKAE 130
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQ--PGDRVGIWAPNCAEWLLTQ---FATARIgailvnINPAYRA---SELEYALGQSG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 131 LSLVFVDK---------------PEKAKLLLEGVENKLIPGLKIIVVMDAYGS-------ELVERGqrcgvEVTSMKAME 188
Cdd:PRK12583 118 VRWVICADafktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAPAPPpgflawhELQARG-----ETVSREALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 189 DLGRANRRkpkppapEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFV----KATENtvnpcpdDTLISFLPLAHMFER 264
Cdd:PRK12583 193 ERQASLDR-------DDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVaeslGLTEH-------DRLCVPVPLYHCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 265 VVeCVMLC--HGAKIgFFQGDirlLMDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwlLDFA 329
Cdd:PRK12583 258 VL-ANLGCmtVGACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 330 SkrkeaeLRSGIIrnnslwdrlifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMP 408
Cdd:PRK12583 318 S------LRTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 409 GD---WTAGHVGAPMPCNLIKLVDVEemNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNG 484
Cdd:PRK12583 365 ADdleRRVETVGRTQPHLEVKVVDPD--GATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 485 TLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQKR-GFEGSFEEL 560
Cdd:PRK12583 443 YVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEEL 510
|
....*..
gi 1832483362 561 ---CRNK 564
Cdd:PRK12583 511 refCKAR 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
58-544 |
2.81e-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: 132.42 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 58 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVD 137
Cdd:cd05934 5 TYAELLRESARIAAALAALGIR--PGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 138 kpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapedLAVICFTSGTTG 217
Cdd:cd05934 83 --------------------------------------------------------------------PASILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 218 NPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVEC-VMLCHGAKI--------GFFQGDIRllm 288
Cdd:cd05934 95 PPKGVVITHANLTFAGYYSARRFGLG----EDDVYLTVLPLFHINAQAVSVlAALSVGATLvllprfsaSRFWSDVR--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 289 ddlkVLQPTVF---PVVPRLLNRMFDRIFGQANttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslggRVR 365
Cdd:cd05934 168 ----RYGATVTnylGAMLSYLLAQPPSPDDRAH--------------------------------------------RLR 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 366 LmVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVC 445
Cdd:cd05934 200 A-AYGAPNPPELHEEFEER-FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGELV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 446 VK---GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQV 522
Cdd:cd05934 277 IRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREA 354
|
490 500
....*....|....*....|....*.
gi 1832483362 523 FVHG----ESLQAFLIAIVVPDVETL 544
Cdd:cd05934 355 AVVAvpdeVGEDEVKAVVVLRPGETL 380
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
57-493 |
5.18e-33 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 133.08 E-value: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAIT-----YIVNKAEL 131
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVK--PGDRVAVQVEKSPEALALYLATLRAGAVFLPL-----NTAYTlaeldYFIGDAEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 132 SLVFVDkPEKAKLLLEGVENKlipGLKIIVVMDAYGS-ELVERGQrcgvevtsmkamedlGRANRRKPKPPAPEDLAVIC 210
Cdd:PRK07514 102 ALVVCD-PANFAWLSKIAAAA---GAPHVETLDADGTgSLLEAAA---------------AAPDDFETVPRGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 211 FTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH---MFerVVECVMLCHGAKIGFFQG-DIRL 286
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFT----PDDVLIHALPIFHthgLF--VATNVALLAGASMIFLPKfDPDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 287 LMDDLKvlQPTVFPVVP----RLL-NRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqsSLG 361
Cdd:PRK07514 237 VLALMP--RATVMMGVPtfytRLLqEPRLTR----------------------------------------------EAA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 362 GRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaGCCLTM-P--GDWTAGHVGAPMPCNLIKLVDVEEMNYMAA 438
Cdd:PRK07514 269 AHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TNMNTSnPydGERRAGTVGFPLPGVSLRVTDPETGAELPP 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1832483362 439 EGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 493
Cdd:PRK07514 346 GEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
57-543 |
7.82e-33 |
|
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: 7.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWV-----IIEQGCfAYsmviVPLYDTLGNEAITYIVNKAEL 131
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVG--PGDLVAVLLERSLEMVvailaVLKAGA-AY----VPLDPSYPAERLAYILEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 132 SLVFVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICF 211
Cdd:cd05930 86 KLVLTD-----------------------------------------------------------------PDDLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 212 TSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAH-MFerVVE-CVMLCHGAKI----GFFQGDIR 285
Cdd:cd05930 101 TSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEiFGALLAGATLvvlpEEVRKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 286 LLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslggrvr 365
Cdd:cd05930 175 ALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL------------------------------------------ 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 366 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT--MPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGE 441
Cdd:cd05930 213 VLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 442 GEVCVKGPNVFQGYLKDPAKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMR 515
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLA 370
|
490 500 510
....*....|....*....|....*....|.
gi 1832483362 516 SEPVAQVFV---HGESLQAFLIAIVVPDVET 543
Cdd:cd05930 371 HPGVREAAVvarEDGDGEKRLVAYVVPDEGG 401
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
202-510 |
9.15e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 132.80 E-value: 9.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFErvVECVMLCH---GAKIG 278
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 279 FFQG-DIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlLDFAskrkeaelRSGIIRNNSLwdrlifhkvq 357
Cdd:PLN02246 255 IMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL---------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 358 SSlggrVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTM-------PGDWTAGHVGAPMPCNLIKLVD 429
Cdd:PLN02246 298 SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 509
Cdd:PLN02246 372 PETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAEL 450
|
.
gi 1832483362 510 E 510
Cdd:PLN02246 451 E 451
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
156-524 |
1.82e-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: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 156 GLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSA 235
Cdd:TIGR01733 72 GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 236 FVKATENTvnpcPDDTLISFLPLAHMFervveCVM-----LCHGAK--------IGFFQGDIRLLMDDLKVlqpTVFPVV 302
Cdd:TIGR01733 152 LARRYGLD----PDDRVLQFASLSFDA-----SVEeifgaLLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 303 PrllnrmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGgrVRLMVTGA-APVSATVLTF 381
Cdd:TIGR01733 220 P------------------------------------------SLLALLAAALPPALAS--LRLVILGGeALTPALVDRW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 382 LRAALGCQFYEGYGQTECTAGCCLT-----MPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYL 456
Cdd:TIGR01733 256 RARGPGARLINLYGPTETTVWSTATlvdpdDAPRESPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832483362 457 KDPAKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV 524
Cdd:TIGR01733 335 NRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
47-539 |
4.75e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 130.49 E-value: 4.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 47 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPE-WVIIEQGCFAySMVIVPLYDTLGNE 120
Cdd:PRK06188 23 KRYPDRPaLVLgdtrLTYGQLADRISRYIQAFEALGL--GTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHPLGSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 121 AITYIVNKAELSLVFVDK---PEKAKLLLEGVenkliPGLKIIVVMDA--YGSELvergqrcgvevtsmkamedLGRANR 195
Cdd:PRK06188 100 DHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDL-------------------LAAAAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 196 RKPKPP----APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEntvnpCPDDtlISFL---PLAHMFERVVEC 268
Cdd:PRK06188 156 FGPAPLvaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE-----WPAD--PRFLmctPLSHAGGAFFLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 269 VMLCHGAKI---GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFASKRKeAELrsgiirnn 345
Cdd:PRK06188 229 TLLRGGTVIvlaKF---DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDL-------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 346 slwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHV------GAP 419
Cdd:PRK06188 281 ------------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRP 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 420 MPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 498
Cdd:PRK06188 345 TPGLRVALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-V 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1832483362 499 AQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQafliAIVVP 539
Cdd:PRK06188 421 TGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
49-514 |
1.40e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 129.48 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 49 KPDQPYEWlSYKQVAELSECIGSALIQKGFKTApdqfiGIFAQNRPEW---VIIEQGCFAYSMVIVPLYDTLGNEAITYI 125
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPG-----DRVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 126 VNKAElSLVF-----VDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVErgqrcgveVTSMKAMEDLGRANrrKPKP 200
Cdd:PRK06087 117 LNKCQ-AKMFfaptlFKQTRPVDLILPLQNQ--LPQLQQIVGVDKLAPATSS--------LSLSQIIADYEPLT--TAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 201 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHmfervvecvmlchgaKIGFF 280
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH---------------ATGFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 QGDIR-LLMDDLKVLQPTVFPVVP-RLLNRmfDRIFGQANTTlkRWLLDFASKRKEAELRSgiirnnslwdrlifhkvqS 358
Cdd:PRK06087 245 HGVTApFLIGARSVLLDIFTPDAClALLEQ--QRCTCMLGAT--PFIYDLLNLLEKQPADL------------------S 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 359 SLggrvRLMVTGAAPVSATVLtflRAAL--GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMN 434
Cdd:PRK06087 303 AL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-EARK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 435 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 514
Cdd:PRK06087 375 TLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILL 453
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
200-551 |
1.76e-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: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 200 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 277
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIFstLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 278 gFFQGDIRLLMDDLKVLqpTVFPVVPRLLnrmfdrifgqanTTLKRWLLDfaskrkeaelrsgiirnnslwdrlifhkvq 357
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSIL------------STLSPQDFP------------------------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 358 sslggRVRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLT--MPGDWTagHVGAPMPCNLIKLVDVEEMNY 435
Cdd:cd17653 210 -----NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQPV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 436 MAAEgEGEVCVKGPNVFQGYLKDPAKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 509
Cdd:cd17653 281 PEGV-VGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1832483362 510 ENIYMRSEPVAQ---VFVHGEslqaFLIAIVVP---DVETLCSWAQKR 551
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
55-540 |
2.37e-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: 127.79 E-value: 2.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 55 EWLSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLV 134
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 135 FVDkpekaklllegvenklipglkiivvmdaygSELVERGQRCGVevTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSG 214
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLP--VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 215 TTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFFQGDI----RLLM 288
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 289 DDLKVLQPTVFpvvprllnrmfdrifgQANTTLKRWLLDfaskrkeaelrSGiirnnslWDRLifhkvqsslgGRVRLMV 368
Cdd:cd12116 211 RLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR----------AGLTALC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 369 TGAA--PVSATVLTflraALGCQFYEGYGQTECT--AGCCLTMPGDwTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 444
Cdd:cd12116 247 GGEAlpPDLAARLL----SRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGEL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 445 CVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSE 517
Cdd:cd12116 321 YIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHP 399
|
490 500
....*....|....*....|....*
gi 1832483362 518 PVAQ--VFVHGESLQAFLIAIVVPD 540
Cdd:cd12116 400 GVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
191-534 |
1.20e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 126.67 E-value: 1.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 191 GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC--------SAFVKatentvnPCPDDTLISF--LPLAH 260
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYH 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 261 MFERVVECVMlchGAKIGffqG---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfask 331
Cdd:PRK07059 264 IFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL--------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 332 rkeaelrsgiirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYG--QTECTAGCCLTMPG 409
Cdd:PRK07059 317 ------------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVDAT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 410 DWTaGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKII 489
Cdd:PRK07059 377 EFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIV 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832483362 490 DRKKHIFkLAQGEYIAPEKIENIyMRSEP----VAQVFVH----GESLQAFLI 534
Cdd:PRK07059 455 DRKKDMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
57-552 |
6.19e-30 |
|
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: 122.87 E-value: 6.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELslvfv 136
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVG--PGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 dkpekaklllegvenklipglKIIVVMDAYGSelvergqrcgvevTSMKAMedlgranrrkpkppaPEDLAVICFTSGTT 216
Cdd:cd05903 75 ---------------------KVFVVPERFRQ-------------FDPAAM---------------PDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVvecvmlcHGAKIGFFQGDIRLLMDdlkVLQP 296
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAERLGLG----PGDVFLVASPMAHQTGFV-------YGFTLPLLLGAPVVLQD---IWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 297 TVfpvVPRLLNRmfDRI-FGQANTTLKRWLLDfaskrkeAELRSGiirnnslwDRLifhkvqsslgGRVRLMVTGAAPVS 375
Cdd:cd05903 172 DK---ALALMRE--HGVtFMMGATPFLTDLLN-------AVEEAG--------EPL----------SRLRTFVCGGATVP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 376 ATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQ 453
Cdd:cd05903 222 RSLARRAAELLGAKVCSAYGSTECpgAVTSITPAPEDRRLYTDGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 454 GYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQ 530
Cdd:cd05903 301 GYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLG 378
|
490 500
....*....|....*....|....*...
gi 1832483362 531 AFLIAIVV------PDVETLCSWAQKRG 552
Cdd:cd05903 379 ERACAVVVtksgalLTFDELVAYLDRQG 406
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
109-540 |
1.47e-29 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 125.04 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 109 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDaygseLVERgqrcgveVTSMKAME 188
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLED-----LKAK-------ISKVDKLT 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 189 DLGRA--------NRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAH 260
Cdd:PRK08633 759 ALLAArllparllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFH 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 261 MFERVVECVM-LCHGAKIGFFQGDirllMDDLKVLQ-------------PTVFpvvprllnRMFDRifgqaNTTLKRwlL 326
Cdd:PRK08633 835 SFGLTVTLWLpLLEGIKVVYHPDP----TDALGIAKlvakhratillgtPTFL--------RLYLR-----NKKLHP--L 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 327 DFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT 406
Cdd:PRK08633 896 MFAS---------------------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVN 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 407 MP-----GDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL---DKDGWLH 473
Cdd:PRK08633 943 LPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYV 1022
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832483362 474 TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniymrsEPVAQVFvHGESLQafLIAIVVPD 540
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 ... |
56-564 |
2.57e-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: 2.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 56 WLSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVF 135
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 136 VDKPekakLLLEgvenklipglkiivvmdaygsELVERGQRcgvevtsmkamedlgranRRKPKPPAPE-DLAVICFTSG 214
Cdd:cd12118 107 VDRE----FEYE---------------------DLLAEGDP------------------DFEWIPPADEwDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 215 TTGNPKGAMVTHRnivsdcSAFVKATENTV----NPCPddTLISFLPLAHmfervveCVMLCHGAKIGFFQG-------- 282
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANILewemKQHP--VYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrkv 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 283 DIRLLMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIRNNSlwdrlifHKVQSSLGG 362
Cdd:cd12118 209 DAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAP-------PSDARPLPH 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 363 RVRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDWTAGHV----------GAPMPCNL-IKLV 428
Cdd:cd12118 249 RVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAWKP-EWDELPTeerarlkarqGVRYVGLEeVDVL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 429 DVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 506
Cdd:cd12118 325 DPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISS 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832483362 507 EKIENIymrsepvaqVFVHGESLQAFLIAivVPD---VETLCSW-AQKRGFEGSFEEL---CRNK 564
Cdd:cd12118 403 VEVEGV---------LYKHPAVLEAAVVA--RPDekwGEVPCAFvELKEGAKVTEEEIiafCREH 456
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
205-524 |
5.70e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 121.62 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVSD-CSAFVKATENTVNPCpddTLISFLPLAHMFERVVEC--VMLCHGAKIGFFQ 281
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMIGQV---VTLGLIPFFHIYGITGICcaTLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 282 GDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRLIFHKVqsslg 361
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 362 gRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTagcCLTMP-GDWTAGH-------VGAPMPCNLIKLVDVEE 432
Cdd:PLN02330 304 -KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 433 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 512
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 1832483362 513 YMRSEPVAQVFV 524
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
57-539 |
8.39e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 120.81 E-value: 8.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLK--KGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DkPEKAKLLLEGVENKlipglkiivVMDAYGSELVERGQrcgVEVTSMKAMEDLGRANRRKPKPPAP--EDLAVICFTSG 214
Cdd:PRK08316 115 D-PALAPTAEAALALL---------PVDTLILSLVLGGR---EAPGGWLDFADWAEAGSVAEPDVELadDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 215 TTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVecvmlchgakigffqgdirLLMDDLKVL 294
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDMS----ADDIPLHALPLYHCAQLDV-------------------FLGPYLYVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 295 QPTVFPVVPRLlNRMFDRIFGQANTTLkrwlldFASKrkeaelrsgiirnnSLWDRLIFHKV-----QSSLggrvRLMVT 369
Cdd:PRK08316 239 ATNVILDAPDP-ELILRTIEAERITSF------FAPP--------------TVWISLLRHPDfdtrdLSSL----RKGYY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 370 GAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLTMPGDwTAGHVG-APMPC-NL-IKLVDvEEMNYMAAeGE-GEV 444
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAGRPVlNVeTRVVD-DDGNDVAP-GEvGEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 445 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV 524
Cdd:PRK08316 371 VHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAV 448
|
490
....*....|....*....
gi 1832483362 525 ----HGESLQAfLIAIVVP 539
Cdd:PRK08316 449 iglpDPKWIEA-VTAVVVP 466
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
109-511 |
1.65e-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: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 109 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaYGSELVERGQRCGVEVTSMKAME 188
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG--------------------------AADRLRDALPASPDPGTVLDADG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 189 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVEC 268
Cdd:cd05922 102 IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT----ADDRALTVLPLSYDYGLSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 269 VMLCHGAKIgFFQGDIRL---LMDDLKVLQPTVFPVVPRLLNrMFDRIfgqanttlkrwlldfasKRKEAELrsgiirnN 345
Cdd:cd05922 178 THLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKL-------P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 346 SLwdRLIfhkvqSSLGGRVRlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTA---GHVGAPMPC 422
Cdd:cd05922 232 SL--RYL-----TQAGGRLP---------QETIARLRELLPGAQVYVMYGQTEATRRMT-YLPPERILekpGSIGLAIPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 423 NLIKLVDVEEMNYmaAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 501
Cdd:cd05922 295 GEFEILDDDGTPT--PPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-G 371
|
410
....*....|
gi 1832483362 502 EYIAPEKIEN 511
Cdd:cd05922 372 NRISPTEIEA 381
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
50-493 |
3.03e-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: 3.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 50 PDQPYEWLSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAQNRpEWVIIEQGC----FAYSMVIVPLYDTLGNEAITYI 125
Cdd:cd05906 33 ADGSEEFQSYQDLLEDARRLAAGLRQLGLR-PGDSVILQFDDNE-DFIPAFWACvlagFVPAPLTVPPTYDEPNARLRKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 126 VNKAELslvfVDKPekakLLLegVENKLIPGLKiivvmdaygsELVERGQRCGVEVTSMkamEDLGRANRRKPKPPA-PE 204
Cdd:cd05906 111 RHIWQL----LGSP----VVL--TDAELVAEFA----------GLETLSGLPGIRVLSI---EELLDTAADHDLPQSrPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHmferVVECVMlCHGAkigffqgDI 284
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLT----PQDVFLNWVPLDH----VGGLVE-LHLR-------AV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 285 RLLMDDLKVLQPTVFPVVPRLLnRMFDRIfgQANTTlkrWLLDFA-SKRKEAELRsgiiRNNSLWDrlifhkvQSSLggr 363
Cdd:cd05906 232 YLGCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPNFAfALLNDLLEE----IEDGTWD-------LSSL--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 364 vRLMVTGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGC--CLTMP-GDWTAGH----VGAPMPCNLIKLVDv 430
Cdd:cd05906 292 -RYLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVD- 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832483362 431 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 493
Cdd:cd05906 370 DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
63-510 |
3.85e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 118.37 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 63 AELSECIG-SALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFvdkpek 141
Cdd:PRK09088 26 AELDALVGrLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 142 aklllegvenklipglkiivvmdayGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPapEDLAVICFTSGTTGNPKG 221
Cdd:PRK09088 100 -------------------------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 222 AMVTHRNIVSDCSAFVKATENTVNPcpddtliSFLPLAHMFERV--VECV--MLCHGAKIGFFQGdirllmddlkvLQPT 297
Cdd:PRK09088 153 VMLSERNLQQTAHNFGVLGRVDAHS-------SFLCDAPMFHIIglITSVrpVLAVGGSILVSNG-----------FEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 298 vfpvvpRLLNRMFDRIFGQANTtlkrwlldFASKRKEAELRSGIIRNNSLWDRLIfhkvqsslggrvrLMVTGAAP-VSA 376
Cdd:PRK09088 215 ------RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhAAE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 377 TVLTFLraALGCQFYEGYGQTEctAGCCLTMPGDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCVKGPNV 451
Cdd:PRK09088 268 DILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPAGV-PGELLLRGPNL 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1832483362 452 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 510
Cdd:PRK09088 343 SPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
200-534 |
7.59e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.21 E-value: 7.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 200 PPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpDDTLISFLPLAHMF-ERVVECVMLCHGAKI 277
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEG--EEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 278 GFF-QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqaNTTLkrwlldfaskRKEAELRSgiirnnslwdrlifhkv 356
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 357 qsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPgdW---TAGHVGAPMPCNLIKLVDVEEM 433
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFL--WekrVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 513
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 1832483362 514 MRSEPVAQVFV-------HGESLQAFLI 534
Cdd:PRK06710 474 YEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
25-630 |
9.70e-28 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 119.57 E-value: 9.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 25 VTTLYEGFQRGIQVSNNGPCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCF 104
Cdd:PTZ00297 426 VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVR--PGDVIGVDCEASRNIVILEVACA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 105 AYSMVIVPLYDTlgNEAITYIVNKAELSLVFVDKPEKAKLL------LEGVENklipglkiivVMDAYGSELVERGQRCG 178
Cdd:PTZ00297 504 LYGFTTLPLVGK--GSTMRTLIDEHKIKVVFADRNSVAAILtcrsrkLETVVY----------THSFYDEDDHAVARDLN 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 179 VEVTSMKAMEDLGRANRRKPKPPAPED----LAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVkATENTVNPCPDDTLIS 254
Cdd:PTZ00297 572 ITLIPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVH 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 255 FLPLAHMFERVVECVMLCHGAKIGffQGDIRLLMDDLKVLQPTVFPVVPRLlnrmfdriFGQANTTLKR----------W 324
Cdd:PTZ00297 651 FTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysW 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 325 LLDfaskrKEAELRSGII---RNNSLWDRLIFHK-VQSSLGGRVRLMVTGAAPVSATvltflraalgcqfyegYGQTECT 400
Cdd:PTZ00297 721 LFE-----RAFQLRSRLInihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTS----------------FSLLEHI 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 401 AGCCltmpgdwtaghvgapMPCnliklvdVEEMNYMAAegEGEVCVKG---PNVfQGYLK---DPAKTAE----ALDKDG 470
Cdd:PTZ00297 780 SVCY---------------VPC-------LREVFFLPS--EGVFCVDGtpaPSL-QVDLEpfdEPSDGAGigqlVLAKKG 834
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 471 WL-HTGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAfLIAIVVPDVETL-CSW 547
Cdd:PTZ00297 835 EPrRTLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVeFEW 913
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 548 AQKRGFE---GSFEELCRNKDVKKA---ILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYF 621
Cdd:PTZ00297 914 RQSHCMGeggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYF 993
|
....*....
gi 1832483362 622 RSQIDDLYS 630
Cdd:PTZ00297 994 SSVIERFYS 1002
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
120-520 |
1.09e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 120 EAITYIVNKAELSLVFVDKPE-------KAKLLLEGVenkliPGLKIIVVMDayGSELVERGQRCGVEVTSMKAME---D 189
Cdd:PRK07529 119 EQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL-----PELRTVVEVD--LARYLPGPKRLAVPLIRRKAHArilD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 190 LGRANRRKP-------KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC---SAFVKATentvnpcPDDTLISFLPLA 259
Cdd:PRK07529 192 FDAELARQPgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLG-------PGDTVFCGLPLF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 260 HMFERVVEC-VMLCHGAKIGFF--QG--DIRLLMDDLKVL---QPTVFPVVPRLLNRMFDRIFGQANTtlkrwlldfask 331
Cdd:PRK07529 265 HVNALLVTGlAPLARGAHVVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDI------------ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 332 rkeaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GD 410
Cdd:PRK07529 333 --------------------------SSL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 411 WTAGHVGAPMPCNLIKLVDVEEM-NYM--AAEGE-GEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTL 486
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYF 461
|
410 420 430
....*....|....*....|....*....|....
gi 1832483362 487 KIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 520
Cdd:PRK07529 462 WLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
203-540 |
2.03e-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: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLplAHMFE-RVVECVM-LCHGAKIGff 280
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT----SESRVLQFA--SYTFDvSILEIFTtLAAGGCLC-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 qgdI---RLLMDDLkvlqptvfpvvPRLLNRMfdrifgQANTtlkrwlldfaskrkeAELRSGIIRnnslwdrLIFHKVQ 357
Cdd:cd05918 177 ---IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLDPEDV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 358 SSLggrvRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIkLVDVEEMNYM 436
Cdd:cd05918 215 PSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW-VVDPDNHDRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 437 AAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKLaQGE 502
Cdd:cd05918 288 VPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQ 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1832483362 503 YIAPEKIENIYMRSEP-----VAQVFVH-GESLQAFLIAIVVPD 540
Cdd:cd05918 367 RVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLD 410
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
43-607 |
2.28e-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: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 43 PCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCF---AYSMVIVPLYDTLGN 119
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLS--AERPLLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 120 E--AITYIVNKAELSLVFVDKPEKAKLLLEGVenkLIPGLKIIVVmdaygselveRGQRCGVEVTSMK---AMEDLGRAN 194
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVVS----------RNAVAGRGAISFAelaATPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 195 RRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchG 274
Cdd:cd05921 157 AAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCA--NQAMLEQTYPFFGEEPPVLVDWLPWNHTF-----------G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 275 AKIGF-----------------FQGDIRLLMDDLKVLQPTVFPVVPR----LLNRMfdrifgQANTTLKRWLLdfasKRK 333
Cdd:cd05921 223 GNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVPAgwemLVAAL------EKDEALRRRFF----KRL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 334 EAELRSGIIRNNSLWDRLIFHKVQSSlGGRVRlmvtgaapvsatvltflraalgcqFYEGYGQTECTAGCCLTMPGDWTA 413
Cdd:cd05921 293 KLMFYAGAGLSQDVWDRLQALAVATV-GERIP------------------------MMAGLGATETAPTATFTHWPTERS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 414 GHVGAPMPCNLIKLVdveemnymAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKII 489
Cdd:cd05921 348 GLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 490 DRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLcsWAQKRGFEGSFEELCRNKDVK 567
Cdd:cd05921 420 GRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLAC--RRLVGLQEASDAEVLRHAKVR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1832483362 568 KAILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLT 607
Cdd:cd05921 497 AAFRDRLAALNGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
204-527 |
3.76e-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: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 204 EDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATENTVNPCPDDTLISFLPLAH------MFERVVE-CVMLCHGAk 276
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH----WWSAIGSALNLGLTEDDNWLCALPLFHisglsiLMRSVIYgMTVYLVDK- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 277 igFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLkrwlldfaskrkeaelrsgiirnnslwdrlifhkv 356
Cdd:cd05912 152 --FDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL----------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 357 qsslggrvRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPMPCNLIKLVDveem 433
Cdd:cd05912 192 --------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIED---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 513
Cdd:cd05912 258 DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
330
....*....|....
gi 1832483362 514 MRSEPVAQVFVHGE 527
Cdd:cd05912 336 LSHPAIKEAGVVGI 349
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
198-512 |
4.80e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 115.71 E-value: 4.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 198 PKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVK-ATENTVNPCPDDTLISFLPLAHMFERVVECV-MLCHG 274
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfEASQYEYPGSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 275 AKI----GFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLKrwlldfaskrkeaelrsgiirnnslwdr 350
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 351 lifhkvqsSLggrvRLMVTGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTA----GCCLTMPGDWTAghVGAPMPCNLI 425
Cdd:PLN02574 320 --------SL----KQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 426 KLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 505
Cdd:PLN02574 386 KVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIA 464
|
....*..
gi 1832483362 506 PEKIENI 512
Cdd:PLN02574 465 PADLEAV 471
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
55-526 |
8.09e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.57 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 55 EWLSYKQVAELSECIGSALIQKgFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAITyivnKAELSLV 134
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYE-LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL-----NIRLT----ENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 135 FVDKpekaklllegvenklipGLKIIVVMDAYGSELVERGQRCGVE----VTSMKAMEDLGRANRrkpKPPAPEDLAVIC 210
Cdd:PRK06839 96 LKDS-----------------GTTVLFVEKTFQNMALSMQKVSYVQrvisITSLKEIEDRKIDNF---VEKNESASFIIC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 211 FTSGTTGNPKGAMVTHRNIvsdcsaFVKATEN--TVNPCPDDTLISFLPLAHMfervvecvmlchgAKIGFFQgdirllm 288
Cdd:PRK06839 156 YTSGTTGKPKGAVLTQENM------FWNALNNtfAIDLTMHDRSIVLLPLFHI-------------GGIGLFA------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 289 ddlkvlQPTVFP----VVPRLLN-----RMFDR-----IFGQAntTLKRWLLDfASKRKEAELRSgiirnnslwdrlifh 354
Cdd:PRK06839 210 ------FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS--------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 355 kvqsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLVDvEE 432
Cdd:PRK06839 266 ---------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-EN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 433 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 512
Cdd:PRK06839 335 KNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV 412
|
490
....*....|....
gi 1832483362 513 YMRSEPVAQVFVHG 526
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 ... |
57-534 |
9.38e-27 |
|
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: 113.34 E-value: 9.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKTApdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAelslvfv 136
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 dkpekaklllegvenklipGLKIIVVmdayGSELvergqrcgvevtsmkamedlgranrrkpkppapEDLAVICFTSGTT 216
Cdd:cd05935 73 -------------------GAKVAVV----GSEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHM--FERVVECVMLCHGAKIGFFQGDIRLLMDDLKVL 294
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 295 QPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPV 374
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--------ATPEFKTRDLSS---------------------------------LKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 375 SATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQG 454
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 455 YLKDPAKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV------- 524
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|
gi 1832483362 525 HGESLQAFLI 534
Cdd:cd05935 371 VGEEVKAFIV 380
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
57-560 |
1.19e-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: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVK--KGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 D----KPEKAKLLLEGVEN--KLIPGLKIIVVMDAYGSELVERGQRcgvevtsmkAMEDLgRANRRKPKPPAP---EDLA 207
Cdd:COG0365 118 AdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEGDL---------DWDEL-LAAASAEFEPEPtdaDDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 208 VICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLA----HMFervveCVM--LCHGAKIGFFQ 281
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVFWCTADIGwatgHSY-----IVYgpLLNGATVVLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 282 GDI------RL--LMDDLKVlqpTVFPVVPRLLnRMfdrifgqanttLKRWLLDFASKrkeaelrsgiirnnslWDRlif 353
Cdd:COG0365 260 GRPdfpdpgRLweLIEKYGV---TVFFTAPTAI-RA-----------LMKAGDEPLKK----------------YDL--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 354 hkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT-AGHVGAPMPCNLIKLVDvEE 432
Cdd:COG0365 306 ----SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD-ED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 433 MNYMAAEGEGEVCVKG--PNVFQGYLKDPAKTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 508
Cdd:COG0365 377 GNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAE 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1832483362 509 IENIYMRSEPVAQVFV----HGESLQAfLIAIVVPdvetlcswaqKRGFEGSfEEL 560
Cdd:COG0365 456 IESALVSHPAVAEAAVvgvpDEIRGQV-VKAFVVL----------KPGVEPS-DEL 499
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
88-551 |
2.14e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 113.72 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 88 IFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAklLLEGVENkLIPGLKIIVVMDAYG 167
Cdd:PRK07786 72 ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRD-IVPLLSTVVVAGGSS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 168 SELVergqrcgvevtsmKAMEDLGRANRrKPKPPA--PEDL-AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTV 244
Cdd:PRK07786 149 DDSV-------------LGYEDLLAEAG-PAHAPVdiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 245 NpcpDDtlISFL--PLAHM--FERVVECVMLchGAKIgffqgdirllmddlkVLQPTvfpvvprllnRMFDrifgqANTT 320
Cdd:PRK07786 215 N---SD--VGFVgvPLFHIagIGSMLPGLLL--GAPT---------------VIYPL----------GAFD-----PGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 321 LKRWlldfaskrkEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEC 399
Cdd:PRK07786 258 LDVL---------EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 400 TAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDI 477
Cdd:PRK07786 329 SPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 478 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAF---LIAIVVPD-------VETLCSW 547
Cdd:PRK07786 407 VRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEF 485
|
....
gi 1832483362 548 AQKR 551
Cdd:PRK07786 486 LTDR 489
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
48-582 |
2.24e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 114.21 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 48 RKPDQPY--------EW--LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---Y 114
Cdd:PRK08180 51 EAPDRVFlaergadgGWrrLTYAEALERVRAIAQALLDRGL--SAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 115 DTLGN--EAITYIVNKAELSLVFVDKPEKAKLLLEGVEnklIPGLKIIVVmdaygselveRGQRCGVEVTSMKAMEDLGR 192
Cdd:PRK08180 129 SLVSQdfGKLRHVLELLTPGLVFADDGAAFARALAAVV---PADVEVVAV----------RGAVPGRAATPFAALLATPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 193 ANRRKPKPPA--PEDLAVICFTSGTTGNPKGAMVTHRNIVS------DCSAFVKATEntvnpcPddTLISFLPLAHMFER 264
Cdd:PRK08180 196 TAAVDAAHAAvgPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEP------P--VLVDWLPWNHTFGG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 265 VVEC-VMLCHGAKI---------GFFQGDIRllmdDLKVLQPTVFPVVPR--------------LLNRMFDRifgqantt 320
Cdd:PRK08180 268 NHNLgIVLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemlvpalerdaaLRRRFFSR-------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 321 LKrwLLDFASkrkeAELRSgiirnnSLWDRLifHKV-QSSLGGRVRLMVtgaapvsatvltflraalgcqfyeGYGQTEc 399
Cdd:PRK08180 336 LK--LLFYAG----AALSQ------DVWDRL--DRVaEATCGERIRMMT------------------------GLGMTE- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 400 TAGCCL--TMPGDwTAGHVGAPMPCNLIKLVDVEemnymaaeGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDI 477
Cdd:PRK08180 377 TAPSATftTGPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 478 GKWL----PNGTLKIIDRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVEtLCSWAQKR 551
Cdd:PRK08180 448 VRFVdpadPERGLMFDGRIAEDFKLSSGTWVSvgPLRARAVSAGAPLVQDVVITGHD-RDEIGLLVFPNLD-ACRRLAGL 525
|
570 580 590
....*....|....*....|....*....|.
gi 1832483362 552 GFEGSFEELCRNKDVKKAILEDMVRLGKDSG 582
Cdd:PRK08180 526 LADASLAEVLAHPAVRAAFRERLARLNAQAT 556
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
57-539 |
3.97e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.84 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAElSLVFV 136
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLG--VGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 --------DKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERgqrcgveVTSMKAME---DLGR--ANRRkpkpPAP 203
Cdd:PRK13295 133 vpktfrgfDHAAMARRLRPE-----LPALRHVVVVGGDGADSFEA-------LLITPAWEqepDAPAilARLR----PGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 204 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvecvmlchgakIGFFQGD 283
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLG----ADDVILMASPMAHQ---------------TGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 284 IRLLMDDLK-VLQPTVFPVvprllnRMFDRI------FGQANTTlkrWLLDFASKRKEAElrsgiirnnslwdrlifhKV 356
Cdd:PRK13295 258 MMPVMLGATaVLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESG------------------RP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 357 QSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLTMPGD---WTAGHVGAPMPCNLIKLVDVEEM 433
Cdd:PRK13295 311 VSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDADGA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 NYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 513
Cdd:PRK13295 386 PLPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALL 461
|
490 500
....*....|....*....|....*....
gi 1832483362 514 MRSEPVAQVFVHG---ESLQAFLIAIVVP 539
Cdd:PRK13295 462 YRHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
22-544 |
1.27e-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: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 22 YDDVTTLYEGFQRgiQVSnngpclgsRKPDQP-----YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEW 96
Cdd:COG1020 472 YPADATLHELFEA--QAA--------RTPDAVavvfgDQSLTYAELNARANRLAHHLRALGVG--PGDLVGVCLERSLEM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 97 VIIEQGCF----AYsmviVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVEnklipglkiIVVMDAygselve 172
Cdd:COG1020 540 VVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVP---------VLALDA------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 173 rgqrcgvevtsmkamEDLGRANRRKPKPPA-PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDT 251
Cdd:COG1020 600 ---------------LALAAEPATNPPVPVtPDDLAYVIYTSGSTGRPKGVMVEHRALV----NLLAWMQRRYGLGPGDR 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 252 LISFLPLAH------MFervvecVMLCHGAKIGFFQGDIRLLMDDLKVL----QPTVFPVVPRLLNRMFDrifgqanttl 321
Cdd:COG1020 661 VLQFASLSFdasvweIF------GALLSGATLVLAPPEARRDPAALAELlarhRVTVLNLTPSLLRALLD---------- 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 322 krwlldfaskrkeaelrsgiirnnSLWDRLifhkvqsslgGRVRLMVTG--AAPVsATVLTFLRAALGCQFYEGYGQTEC 399
Cdd:COG1020 725 ------------------------AAPEAL----------PSLRLVLVGgeALPP-ELVRRWRARLPGARLVNLYGPTET 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 400 TAGCCL--TMPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDG 470
Cdd:COG1020 770 TVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLD-AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPG 848
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832483362 471 --WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQ--VFVHGESLQA-FLIAIVVPDVETL 544
Cdd:COG1020 849 arLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELGEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAA 926
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
55-519 |
6.13e-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: 6.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 55 EWLSYKQVAELSECIGSALIQKGfktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA---ITYIVNKAEL 131
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG---KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 132 SLVFVDKPEKAKLLLEGVENKLIPGLKIIVVmDAYGSELVERGQrcgvevtsmkamedlgranrrkPKPPAPEDLAVICF 211
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLLVV-DLLPDTSAADWP----------------------PPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 212 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH-MfervvecvmlchgakiGFFQGdirllmdd 290
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLD----PGDVVVSWLPLYHdM----------------GLIGG-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 291 lkVLQPTV--FPVV---PR-LLNRMFdrifgqanttlkRWL-----------------LDFASKRKEAELRSGIirnnsl 347
Cdd:cd05931 209 --LLTPLYsgGPSVlmsPAaFLRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL------ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 348 wdRLifhkvqsslgGRVRLMVTGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT----------AGCCLTMPGDW 411
Cdd:cd05931 269 --DL----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 412 TAGHV----------------GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE------ALDKD 469
Cdd:cd05931 337 LAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEG 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1832483362 470 GWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 519
Cdd:cd05931 417 GWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
47-540 |
6.16e-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: 6.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 47 SRKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTL 117
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVG--PDTIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 118 GNEAITYIVNKAELSLVFVDKPEKAKLLLEGvenklipglkIIVVMDAygselvergqrcgvEVTSMKAMEDLGRANRrk 197
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENLEPVSK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 198 pkppaPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGA 275
Cdd:cd17655 136 -----SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASIS--FDASVTEIFasLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 276 KIgffqgdirllmddLKVLQPTVFPVVPrllnrmFDRIFGQANTTLkrwlldfaSKRKEAELRsgiirnnslwdrlIFHK 355
Cdd:cd17655 205 TL-------------YIVRKETVLDGQA------LTQYIRQNRITI--------IDLTPAHLK-------------LLDA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 356 VQSSLGGRVRLMVTGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCC--LTMPGDWTAGHV--GAPMPCNLIKLVD 429
Cdd:cd17655 245 ADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYEPETDQQVSVpiGKPLGNTRIYILD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 503
Cdd:cd17655 325 -QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYR 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1832483362 504 IAPEKIENIYMRSEPVAQ--VFVH-GESLQAFLIAIVVPD 540
Cdd:cd17655 403 IELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE 442
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
205-542 |
6.30e-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: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFvkATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK---IGFFQ 281
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 282 GDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiIRNnslwdrlifhkvqssl 360
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 361 ggrvrlmVTGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 439
Cdd:cd17637 119 -------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 440 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYMRSE 517
Cdd:cd17637 187 ETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1832483362 518 PVAQVFVHGeslqafliaivVPDVE 542
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
57-618 |
3.34e-24 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 105.50 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAqNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLR-KGDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapEDLAVICFTSGTT 216
Cdd:cd05972 79 DA-----------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVS---DCSAFVKATENTVNPCPDDT------LISFL-PLAHMFervveCVMLCHGAKIgffqgDIRL 286
Cdd:cd05972 94 GLPKGVLHTHSYPLGhipTAAYWLGLRPDDIHWNIADPgwakgaWSSFFgPWLLGA-----TVFVYEGPRF-----DAER 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 287 LMDDLKVLQPTVFPVVPrllnrmfdrifgqanTTLKRWL-LDFASKRKeaelrsgiirnnslwdrlifhkvqsslgGRVR 365
Cdd:cd05972 164 ILELLERYGVTSFCGPP---------------TAYRMLIkQDLSSYKF----------------------------SHLR 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 366 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLTMPgdWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGE 443
Cdd:cd05972 201 LVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLtvGNFPDMP--VKPGSMGRPTPGYDVAIID-DDGRELPPGEEGD 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 444 VCVKGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQ 521
Cdd:cd05972 278 IAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAE 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 522 VFV-------HGESLQAFLIAivvpdvetlcswaqKRGFEGSfEELcrnkdvkkaiLEDMVRLGKdSGLKPFEQVKGITL 594
Cdd:cd05972 356 AAVvgspdpvRGEVVKAFVVL--------------TSGYEPS-EEL----------AEELQGHVK-KVLAPYKYPREIEF 409
|
570 580
....*....|....*....|....
gi 1832483362 595 HPELfsidngLLTPTMKAKRPELR 618
Cdd:cd05972 410 VEEL------PKTISGKIRRVELR 427
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
202-543 |
9.94e-24 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 104.64 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 APEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAHMFervveCVM-----LCHGAk 276
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFSFDL-----SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 277 igffqgdirllmddlkvlqpTVFPVvPRLLNRMFDRIF-GQANTTLKRWLldfaskrkeaelrsgiiRNNSLWDRLIFHK 355
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVWV-----------------STPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 356 --VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTmpgDWT----AGH----VGAPMPCNLI 425
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYI---EVTpevlDGYdrlpIGYAKPGAKL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 426 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 502
Cdd:cd05945 284 VILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGY 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1832483362 503 YIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDVET 543
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGA 405
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
57-618 |
1.27e-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: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DkPEKAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgqrcgvevtsmKAMEDL--GRANRRKPKPPAPEDLAVICFTSG 214
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGPEAGA------------LLLAELvaAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 215 TTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLAHMFErvvecvmLCHGAKIGFFQGDIRLLM------ 288
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 289 ----DDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWdrlifhkvQSSLGGRV 364
Cdd:cd05959 244 aavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAPNL--------PSRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 365 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 444
Cdd:cd05959 283 RLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 445 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV 524
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 525 HGESLQAFLI---AIVVPdvetlcswaqKRGFEGSfeelcrnkdvkkAILEDMVRLGKDSGLKPFEQVKGITLHPELFSi 601
Cdd:cd05959 440 VGVEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRLAPYKYPRWIVFVDELPK- 496
|
570
....*....|....*..
gi 1832483362 602 dngllTPTMKAKRPELR 618
Cdd:cd05959 497 -----TATGKIQRFKLR 508
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
47-551 |
2.53e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 104.35 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 47 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPlydtlgnea 121
Cdd:PRK06178 44 RERPQRPaIIFyghvITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVP--------- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 122 ITYIVNKAELSLVFVDKpekaklllegvenklipGLKIIVVMDAYgSELVER-GQRCGVE---VTSMKAM---------- 187
Cdd:PRK06178 113 VSPLFREHELSYELNDA-----------------GAEVLLALDQL-APVVEQvRAETSLRhviVTSLADVlpaeptlplp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 188 -------------EDLGRANRRKPKP-----PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATentVNPCPD 249
Cdd:PRK06178 175 dslraprlaaagaIDLLPALRACTAPvplppPALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVA---VVGGED 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 250 DTLISFLPlahMFervvecvmlchgakigFFQGDirllmdDLKVLQPTVF--PVVprLLNRmfdrifgqanttlkrwlld 327
Cdd:PRK06178 252 SVFLSFLP---EF----------------WIAGE------NFGLLFPLFSgaTLV--LLAR------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 328 faskrkeaelrsgiirnnslWDRLIF------HKVQSSLG---GRVRLMVTGAapVSATVLTFL---------------- 382
Cdd:PRK06178 286 --------------------WDAVAFmaaverYRVTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdy 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 383 ----RAALGCQFYEG-YGQTEcTAGCcltmpGDWTAG-------------HVGAPMPCNLIKLVDVEEMNYMAAEGEGEV 444
Cdd:PRK06178 344 rqrwRALTGSVLAEAaWGMTE-THTC-----DTFTAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEI 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 445 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV 524
Cdd:PRK06178 418 VVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQHPAVLGSAV 495
|
570 580 590
....*....|....*....|....*....|....*.
gi 1832483362 525 HG---ESLQAFLIAIVVP------DVETLCSWAQKR 551
Cdd:PRK06178 496 VGrpdPDKGQVPVAFVQLkpgadlTAAALQAWCREN 531
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
57-540 |
2.61e-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: 103.43 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWV-----IIEQGCfAYsmviVPLYDTLGNEAITYIVNKAEL 131
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGV--GPGDVVGVLAERSPELVvallaVLKAGA-AY----VPLDPELPAERLAFMLADAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 132 SLVFVDKPEKAklllegvenkLIPGLKIIVVMDAYGSELVERGQRCgvevtsmkamedlgranrrkpkPPAPEDLAVICF 211
Cdd:cd12117 96 KVLLTDRSLAG----------RAGGLEVAVVIDEALDAGPAGNPAV----------------------PVSPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 212 TSGTTGNPKGAMVTHRNIVSdcsaFVKATeNTVNPCPDDTLISFLPL---AHMFERVVEcvmLCHGAKIgffqgdirllm 288
Cdd:cd12117 144 TSGSTGRPKGVAVTHRGVVR----LVKNT-NYVTLGPDDRVLQTSPLafdASTFEIWGA---LLNGARL----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 289 ddlkVLQPtvfPVVPRLLNRMFDRIFGQANTTLkrWLldfaskrkeaelrsgiirNNSLWdRLIFHKVQSSLGGrVRLMV 368
Cdd:cd12117 205 ----VLAP---KGTLLDPDALGALIAEEGVTVL--WL------------------TAALF-NQLADEDPECFAG-LRELL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 369 TGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCCLTMPGDWTAGHV--GAPMPcNLIKLVdVEEMNYMAAEGE-G 442
Cdd:cd12117 256 TGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIA-NTRVYV-LDEDGRPVPPGVpG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 443 EVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRS 516
Cdd:cd12117 334 ELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAH 412
|
490 500
....*....|....*....|....*..
gi 1832483362 517 EPVAQVFV---HGESLQAFLIAIVVPD 540
Cdd:cd12117 413 PGVREAVVvvrEDAGGDKRLVAYVVAE 439
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
57-539 |
2.96e-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: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALiqKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfV 136
Cdd:TIGR03098 26 LTYAALSERVLALASGL--RGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRrkPKPPAPEDLAVICFTSGTT 216
Cdd:TIGR03098 103 TSSERLDLLHPA-----LPGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADP--PHPVIDSDMAAILYTSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmfervvecvmlchgakigffqgdirllmddlkvlqp 296
Cdd:TIGR03098 176 GRPKGVVLSHRNLVAGAQSVATYLENR----PDDRLLAVLPLS------------------------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 297 tvfpvvprllnrmFDRIFGQANTTL----KRWLLDFASKRK-----EAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLM 367
Cdd:TIGR03098 215 -------------FDYGFNQLTTAFyvgaTVVLHDYLLPRDvlkalEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 368 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTmPG--DWTAGHVGAPMPcNLIKLVDVEEMNYMAAEGEGEV 444
Cdd:TIGR03098 282 TNSGGAMPRATLSRLRSFLPnARLFLMYGLTEAFRSTYLP-PEevDRRPDSIGKAIP-NAEVLVLREDGSECAPGEEGEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 445 CVKGPNVFQGYLKDPAKTAEALDK----DGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 513
Cdd:TIGR03098 360 VHRGALVAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA 438
|
490 500 510
....*....|....*....|....*....|
gi 1832483362 514 MRSEPVAQVFVHG----ESLQAfLIAIVVP 539
Cdd:TIGR03098 439 YATGLVAEAVAFGvpdpTLGQA-IVLVVTP 467
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
59-551 |
3.04e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 103.50 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 59 YKQVAELSECIGSALIQKGfktapdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDk 138
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 139 pekaklllEGVENKLIPGLKIIVvmdaygSELVErgqrcgvevtsmkamedlGRANRRKPKPPAPED-LAVICFTSGTTG 217
Cdd:PRK03640 107 --------DDFEAKLIPGISVKF------AELMN------------------GPKEEAEIQEEFDLDeVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 218 NPKGAMVTHRNivsdcsAFVKATENTVNP--CPDDTLISFLPLAH------MFERVVE-CVMLCH----GAKIgffqgdI 284
Cdd:PRK03640 155 KPKGVIQTYGN------HWWSAVGSALNLglTEDDCWLAAVPIFHisglsiLMRSVIYgMRVVLVekfdAEKI------N 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 285 RLLMDDlKVlqpTVFPVVPRLLNRMFDRIfGQANTtlkrwlldfaskrkeaelrsgiirNNSLwdrlifhkvqsslggrv 364
Cdd:PRK03640 223 KLLQTG-GV---TIISVVSTMLQRLLERL-GEGTY------------------------PSSF----------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 365 RLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPM-PCNlIKLVDveEMNYMAAEG 440
Cdd:PRK03640 257 RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 441 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 520
Cdd:PRK03640 332 EGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVA 409
|
490 500 510
....*....|....*....|....*....|....*...
gi 1832483362 521 QVFVHGESLQ-------AFLIAIVVPDVETLCSWAQKR 551
Cdd:PRK03640 410 EAGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
205-551 |
3.21e-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: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATENTVNPCPDDTLISFLPLAHM--FERVVECVMLchGAKIGFFQG 282
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--AGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 283 DiRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslgg 362
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 363 rVRLMVTGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEG 442
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 443 EVCVKGPNVFQGYLKDPakTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQV 522
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350
....*....|....*....|....*....|....*.
gi 1832483362 523 FVHG---ESLQAFLIAIVV----PDVETLCSWAQKR 551
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVgrgpADPAELRAWLKDK 292
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
203-560 |
7.73e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 100.63 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVMLchgakigFFQG 282
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 283 DIRLLMDDLKVLQPTVFPVVPRLLNRMfdRIfgQANTTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLgg 362
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 363 rvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GDWTAGHVGAPMPCNLIKLVDVE-EMNYM--AA 438
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 439 EGE-GEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 517
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1832483362 518 PVaqvfvhgeslqAFLIAIVVPDV---ETLCSWAQ-KRGFEGSFEEL 560
Cdd:cd05944 280 AV-----------AFAGAVGQPDAhagELPVAYVQlKPGAVVEEEEL 315
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
48-542 |
5.36e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 100.03 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 48 RKPDQPYEW-----LSYKQVAELSECIGSAL-----IQKGfktapDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTL 117
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLqqecgVRKG-----DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 118 GNEAITYIVNKAELSLVFVdkpekAKLLLEGVEnKLI--PGLKIIVV------MDAYGSE-----LVERGQRCGVEVTSM 184
Cdd:PRK08314 96 REEELAHYVTDSGARVAIV-----GSELAPKVA-PAVgnLRLRHVIVaqysdyLPAEPEIavpawLRAEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 185 KAMEDLGRANRRkpkPPA----PEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPcpDDTLISFLPLAH 260
Cdd:PRK08314 170 VAWKEALAAGLA---PPPhtagPDDLAVLPYTSGTTGVPKGCMHTHRTVM--ANAVGSVLWSNSTP--ESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 261 mferVVECVMLCHGAkigFFQGDIRLLMddlkvlqptvfpvvPR----LLNRMFDR---IFGQANTTLkrwLLDFaskrk 333
Cdd:PRK08314 243 ----VTGMVHSMNAP---IYAGATVVLM--------------PRwdreAAARLIERyrvTHWTNIPTM---VVDF----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 334 eaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG----------- 402
Cdd:PRK08314 294 ---LASPGLAERDL----------SSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpkl 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 403 CCLTMPgdwTAGhVGApmpcnliKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA---LDKDGWLHTGDIGK 479
Cdd:PRK08314 357 QCLGIP---TFG-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGR 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 480 WLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVPDVE 542
Cdd:PRK08314 426 MDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
57-540 |
6.13e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 101.20 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGsALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKN--TPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKP--EKAKL--LLEGVENklipGLKIIVVMDaygselVERGQRCGVEVTSMKAmedlGRANRRKPKPPAPEDLAVICFT 212
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 213 SGTTGNPKGAMVTHRNIVSDC---SAFVKATentvnpcPDDTLISFLPLAHMFervvecvmlchgakiGFFQGDIRLLMD 289
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLANRaqvAARIDFS-------PEDKVFNALPVFHSF---------------GLTGGLVLPLLS 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 290 DLKVL---QPTVFPVVPRLlnrmfdrIFgQANTTL----KRWLLDFASKRKEAELRSgiirnnslwdrlifhkvqsslgg 362
Cdd:PRK06814 860 GVKVFlypSPLHYRIIPEL-------IY-DTNATIlfgtDTFLNGYARYAHPYDFRS----------------------- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 363 rVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNymaaEGeG 442
Cdd:PRK06814 909 -LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID----EG-G 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 443 EVCVKGPNVFQGYLK-DPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPvaq 521
Cdd:PRK06814 983 RLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEELAAELWP--- 1057
|
490
....*....|....*....
gi 1832483362 522 vfvhgESLQAfliAIVVPD 540
Cdd:PRK06814 1058 -----DALHA---AVSIPD 1068
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
204-535 |
1.08e-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: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 204 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISflpLAHMFErvveCVMLCHGAKIGFFQGD 283
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 284 IRLLMDD----------LKVLQPTVFPVVPRLlnrmfdrifgqanttlkrwlldFASKRKEAELRSGIIRNnslwdrlif 353
Cdd:cd05919 161 SAVLNPGwptaervlatLARFRPTVLYGVPTF----------------------YANLLDSCAGSPDALRS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 354 hkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEM 433
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 513
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*....
gi 1832483362 514 MRSEPVAQVFV------HGES-LQAFLIA 535
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
57-562 |
1.11e-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: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVF- 135
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 136 -VDKPekakllleGVENKLIPGLKIIVVMDAYGSelvergqrcGVEVTSMKAMEDlgranrrkpKPPAPEDLAVICFTSG 214
Cdd:cd05923 107 aVDAQ--------VMDAIFQSGVRVLALSDLVGL---------GEPESAGPLIED---------PPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 215 TTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMfervvecvmlchgakIGFFQgdirLLMDDLkVL 294
Cdd:cd05923 161 TTGLPKGAVIPQRAAES--RVLFMSTQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-AL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 295 QPTVFPVvprllnRMFDRIFgqanttlkrwlldfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGAAP 373
Cdd:cd05923 219 DGTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 374 VSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMPgDWTAGHVGAPMPCNLIKLVDV-EEMNYMAAEG-EGEVCVK--GP 449
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 450 NVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG--- 526
Cdd:cd05923 356 AAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvad 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 1832483362 527 ESLQAFLIAIVVPDVETLCswaqkrgfEGSFEELCR 562
Cdd:cd05923 434 ERWGQSVTACVVPREGTLS--------ADELDQFCR 461
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
202-632 |
1.25e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 99.10 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHM--FERVVECVML--CHGAKI 277
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAI----VGYGEDDVYLHTAPLCHIggLSSALAMLMVgaCHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 278 GFfqgDIRLLMDDLKVLQPTVFPVVPRLL------NRMfdRIFGQANTTLKRWLldfaskrkeaelrSGiirNNSLWDRL 351
Cdd:PLN02860 246 KF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRKIL-------------NG---GGSLSSRL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 352 IfhKVQSSLGGRVRLMVTGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCLTMPGDWTAGH-VGAPMPcnliklvDV 430
Cdd:PLN02860 305 L--PDAKKLFPNAKLFSAYGMTEACSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP-------HV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 431 EEMNYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 509
Cdd:PLN02860 374 ELKIGLdESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 510 ENIYMRSEPVAQVFVHGeSLQAFLIAIVVPDVETLCSW--------AQKRGFEGSFEEL---CRNKdvkkailedmvrlg 578
Cdd:PLN02860 453 EAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK-------------- 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1832483362 579 kdsGLKPFEQVKGITLHPELFSidnglLTPTMKAKRPELRNYFRSQIDDLYSTI 632
Cdd:PLN02860 518 ---NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
202-618 |
1.53e-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: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPlahmfervvecvmlchgAKIGFFQ 281
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLGH----LPGVQFPFNLFPRDGDLYWTP-----------------ADWAWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 282 GdirlLMDdlkVLQPTVFPVVPRLLNRM--FDRifGQANTTLKRWLLDFASKRKEAeLRsgIIRnnslwdrliFHKVQSS 359
Cdd:cd05971 145 G----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 360 LGG-RVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC---TAGCCLTMPGDwtAGHVGAPMPCNLIKLVDvEEMNY 435
Cdd:cd05971 204 HAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 436 MAAEGEGEVCVKGPN--VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 513
Cdd:cd05971 281 LPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 514 MRSEPVAQVFV-------HGESLQAFliaIVVpdvetlcswaqKRGFEGSfEELCRNkdvkkaiLEDMVRlgkdSGLKPF 586
Cdd:cd05971 359 LKHPAVLMAAVvgipdpiRGEIVKAF---VVL-----------NPGETPS-DALARE-------IQELVK----TRLAAH 412
|
410 420 430
....*....|....*....|....*....|..
gi 1832483362 587 EQVKGITLHPELfsidngLLTPTMKAKRPELR 618
Cdd:cd05971 413 EYPREIEFVNEL------PRTATGKIRRRELR 438
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
57-539 |
2.63e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.03 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGL--LPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKpekaklllEGVENKLIPGLKIIVVMDAYGSElveRGQRCG-VEVTsmkamedLGRANRRKPKPPAPEDL----AVICF 211
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGD---SGPSGGtLSVH-------LDAATEPTPATSTPEGLrpddAMIMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 212 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECV-MLCHGAKI-----GFFQGdiR 285
Cdd:PRK05852 184 TGGTTGLPKMVPWTHANIASSVRAIITGYRLS----PRDATVAVMPLYHGHGLIAALLaTLASGGAVllparGRFSA--H 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 286 LLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFA----SKRKEAELRsgIIRNNSlwdrlifhkvqsslg 361
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKPAALR--FIRSCS--------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 362 grvrlmvtgaAPVSATVLTFLRAALGCQFYEGYGQTECT----------AGCCLTmPGDWT--AGHVGAPMpcnlIKLVD 429
Cdd:PRK05852 305 ----------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQTEN-PVVSTglVGRSTGAQ----IRIVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 VEEMNYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 509
Cdd:PRK05852 370 SDGLPLPAGA-VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERV 446
|
490 500 510
....*....|....*....|....*....|...
gi 1832483362 510 ENIYMRSEPVAQVFVHGESLQAF---LIAIVVP 539
Cdd:PRK05852 447 EGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
200-540 |
2.80e-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: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 200 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 277
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 278 GFFQGDIRllMDDlkvlqptvfpvvprllnrmfdrifgqanTTLKRWLldfaskrkeAELR-SGIIRNNSLWDRLIFH-K 355
Cdd:cd17651 206 VLPPEEVR--TDP----------------------------PALAAWL---------DEQRiSRVFLPTVALRALAEHgR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 356 VQSSLGGRVRLMVTGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLTMPGD---WTA-GHVGAPMPCNLIKLVD 429
Cdd:cd17651 247 PLGVRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 503
Cdd:cd17651 327 -AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1832483362 504 IAPEKIENIYMRSEPVAQ--VFVHGE-SLQAFLIAIVVPD 540
Cdd:cd17651 405 IELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGD 444
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
204-512 |
7.07e-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: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 204 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGD 283
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVV---GDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 284 IRL--LMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfaskrkeaELRSGIIRNNSLwdRLIfhkvqsslg 361
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKLVS------------------------ELKSANATVPSL--RLI--------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 362 grvrlMVTGAAPVSATVLTFLRAALgCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAeG 440
Cdd:cd17635 123 -----GYGGSRAIAADVRFIEATGL-TNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832483362 441 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 512
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-540 |
9.63e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 97.72 E-value: 9.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 6 ARRS----ALLDSDEplvyfYDDVTTLY----EGFQRGIQVSNNGPCLGSRKPDQPY-----EWLSYKQVAELSECIGSA 72
Cdd:PRK12316 1970 AQAAlgelALLDAGE-----RQRILADWdrtpEAYPRGPGVHQRIAEQAARAPEAIAvvfgdQHLSYAELDSRANRLAHR 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 73 LIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGvenk 152
Cdd:PRK12316 2045 LRARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA---- 2118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 153 lipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVS 231
Cdd:PRK12316 2119 -------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGSTGLPKGVAVSHGALVA 2173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 232 DCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDLKVLQPtvfpvvprllNRM 309
Cdd:PRK12316 2174 HCQAAGERYELS----PADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWDP----------EQL 2228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 310 FDRIFGQANTtlkrwLLDFASkrkeaelrsgiirnnSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQ 389
Cdd:PRK12316 2229 YDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV 2288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 390 F-YEGYGQTECTA-----GCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTA 463
Cdd:PRK12316 2289 YlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLGGEGLARGYLNRPGLTA 2367
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 464 EALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV---HGESLQAfL 533
Cdd:PRK12316 2368 ERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVvaqDGASGKQ-L 2445
|
....*..
gi 1832483362 534 IAIVVPD 540
Cdd:PRK12316 2446 VAYVVPD 2452
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
195-521 |
1.56e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 96.32 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 195 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchG 274
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALPLFHSF-----------G 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 275 AKIGFFQGdirlLMDDLKVL---QPTVFPVVPRLLnrmFDR----IFGQAnTTLKRWL-----LDFAskrkeaelrsgii 342
Cdd:PRK08043 421 LTVGLFTP----LLTGAEVFlypSPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 343 rnnslwdrlifhkvqsslggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 422
Cdd:PRK08043 480 --------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 423 NLIKLVDVEEMnymaaEGEGEVCVKGPNVFQGYLK--DP-------AKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 493
Cdd:PRK08043 540 MDARLLSVPGI-----EQGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAK 614
|
330 340
....*....|....*....|....*...
gi 1832483362 494 HIFKLAqGEYIAPEKIENIYMRSEPVAQ 521
Cdd:PRK08043 615 RFAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
109-526 |
2.20e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 94.95 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 109 VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekaklllegvENKLIPGLKI-IVVMDAYGSELVERGQRCGVEVTSMKam 187
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDAGAKLLLVDE-----------EFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 188 edlgranrrkpkPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpcpDDTLISFLPLAHmferVVE 267
Cdd:PRK06145 145 ------------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTA----SERLLVVGPLYH----VGA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 268 C-----VMLCHGAKIGFFQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASKRkeaelrsgi 341
Cdd:PRK06145 205 FdlpgiAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLA--------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 342 irnnslWdrlifhkvqsSLGGrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAP 419
Cdd:PRK06145 268 ------W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 420 MPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 499
Cdd:PRK06145 325 LAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-IS 401
|
410 420
....*....|....*....|....*..
gi 1832483362 500 QGEYIAPEKIENIYMRSEPVAQVFVHG 526
Cdd:PRK06145 402 GGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
156-519 |
2.22e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.06 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 156 GLKIIVV---MDAYGSELVERGQRcGVEVTSMKAMEDLgranrrKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD 232
Cdd:PRK07768 108 GAKAVVVgepFLAAAPVLEEKGIR-VLTVADLLAADPI------DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 233 CSAFVKATENTVNpcpDDTLISFLPLAH-MfervvecvmlchgAKIGFFQGDIRLLMDDLKVlQPTVFPVVPRLLNRMFD 311
Cdd:PRK07768 181 AEAMFVAAEFDVE---TDVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELIS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 312 RIFGQ-------ANTTLKRwLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVS-ATVLTFLR 383
Cdd:PRK07768 244 KYRGTmtaapnfAYALLAR-RLRRQAKPGAFDL--------------------SSL----RFALNGAEPIDpADVEDLLD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 384 A---------ALGCqfyeGYGQTECTAGCCLTMPGD--------------------WTAGHV------GAPMPCNLIKLV 428
Cdd:PRK07768 299 AgarfglrpeAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 429 DvEEMNYMAAEGEGEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 508
Cdd:PRK07768 375 D-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTD 451
|
410
....*....|.
gi 1832483362 509 IENIYMRSEPV 519
Cdd:PRK07768 452 IERAAARVEGV 462
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
48-524 |
2.85e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 94.83 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 48 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 122
Cdd:PRK06155 33 RYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVK--RGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 123 TYIVNKAELSLVFVDkpekAKLL--LEGVENKLIPgLKIIVVMDAYGSELVERGQRcgveVTSMKAMedlgrANRRKPKP 200
Cdd:PRK06155 111 EHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAGWS----TAPLPPL-----DAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 201 PAPEDLAVICFTSGTTGNPKGAMVTH-------RNIVSDcsafvkatentVNPCPDDTLISFLPLAH-----MFERVvec 268
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAED-----------LEIGADDVLYTTLPLFHtnalnAFFQA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 269 vmLCHGAKI---------GFFqgdirllmDDLKVLQPTVF----PVVPRLLnrmfdrifgqanttlkrwlldfaSKRKEA 335
Cdd:PRK06155 243 --LLAGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL-----------------------SQPARE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 336 ELRSgiirnnslwdrlifHKVQSSLGGrvrlmvtgaaPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDwTAGH 415
Cdd:PRK06155 290 SDRA--------------HRVRVALGP----------GVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 416 VGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKG--PNVF-QGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK 492
Cdd:PRK06155 345 MGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRI 422
|
490 500 510
....*....|....*....|....*....|...
gi 1832483362 493 KHIFKlAQGEYIAPEKIENIyMRSEP-VAQVFV 524
Cdd:PRK06155 423 KDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
120-562 |
8.46e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 93.09 E-value: 8.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 120 EAITYIVNKAELSLVFVDkPEKAKLLLEGVEnkLIPGLKIIVV---MDAYGselveRGQRCG-VEVTSMKAMEDLGRAnr 195
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVIdvdDPEYP-----GGRFIGaLDYEAFLASGDPDFA-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 196 rkPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRnivsdcSAFVKATENTV--NPCPDDTLISFLPLAHmfervveCVMLC 272
Cdd:PRK08162 175 --WTLPADEwDAIALNYTSGTTGNPKGVVYHHR------GAYLNALSNILawGMPKHPVYLWTLPMFH-------CNGWC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 273 H--------GAKIGFFQGDIRLLMDDLKVLQPTVF---PVVPRLLnrmfdrifgqANTtlkrwlldfaskrkEAELRSGI 341
Cdd:PRK08162 240 FpwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEWRAGI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 342 irnnslwdrlifhkvqsslGGRVRLMVTGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLTMPGdWTA------ 413
Cdd:PRK08162 296 -------------------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAlplder 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 414 ----GHVGAPMPC-NLIKLVDVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTL 486
Cdd:PRK08162 354 aqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 487 KIIDRKKHIFkLAQGEYIAPEKIENIYMRsepvaqvfvHgeslQAFLIAIVV--PDV---ETLCSWAQ-KRGFEGSFEEL 560
Cdd:PRK08162 433 KIKDRSKDII-ISGGENISSIEVEDVLYR---------H----PAVLVAAVVakPDPkwgEVPCAFVElKDGASATEEEI 498
|
....*
gi 1832483362 561 ---CR 562
Cdd:PRK08162 499 iahCR 503
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
57-562 |
2.23e-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: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKTA-------PdqfigifaqNRPEWVIIeqgCFAYSMV-IVPLYdTL----GNEaITY 124
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGdrvvvqlP---------NVAEFVIV---FFALFRAgAIPVF-ALpahrRAE-ISH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 125 IVNKAELS-LVFVDKPEK------AKLLLEGVenkliPGLKIIVVMDAYGSELvergqrcgvevtsmkAMEDLGRANRRK 197
Cdd:COG1021 117 FAEQSEAVaYIIPDRHRGfdyralARELQAEV-----PSLRHVLVVGDAGEFT---------------SLDALLAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 198 PKP-PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPcpDDTLISFLPLAHMFervvecVMLCHGAk 276
Cdd:COG1021 177 SEPrPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL--YSVRASAEICGLDA--DTVYLAALPAAHNF------PLSSPGV- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 277 IGFFQ--GDIRL-----------LMDDLKVlqpTVFPVVPRLLNRMfdrifgqanttlkrwlLDFASKRKeAELrsgiir 343
Cdd:COG1021 246 LGVLYagGTVVLapdpspdtafpLIERERV---TVTALVPPLALLW----------------LDAAERSR-YDL------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 344 nnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGD---WTAGHVGAP 419
Cdd:COG1021 300 --------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeeVILTTQGRP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 420 M-PCNLIKLVDVEEMNymAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIF 496
Cdd:COG1021 359 IsPDDEVRIVDEDGNP--VPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQIN 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 497 KlaQGEYIAPEKIENIYMRSEPVAQVfvhgeslqafliAIV-VPDV---ETLCSWAQKRGFEGSFEELCR 562
Cdd:COG1021 437 R--GGEKIAAEEVENLLLAHPAVHDA------------AVVaMPDEylgERSCAFVVPRGEPLTLAELRR 492
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
57-541 |
7.43e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 91.76 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAITYIVNKAELS 132
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVgllaVLKAGGAY----VPLDPEYPQDRLAYMLDDSGVR 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 133 LVFVDkPEKAKLLlegvenKLIPGLKIIVvMDAYGSELVergqrcgvevtsmkamedlGRANRRKPKPPAPEDLAVICFT 212
Cdd:PRK12467 612 LLLTQ-SHLLAQL------PVPAGLRSLC-LDEPADLLC-------------------GYSGHNPEVALDPDNLAYVIYT 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 213 SGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqgdirLLMDDLK 292
Cdd:PRK12467 665 SGSTGQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDC 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 293 VLQPTVFpvvprllnrmFDRIFGQANTTLKRwlldfaskrkeaelrsgiirNNSLWDRLIFHKVQSSLGGRVRLMVTGAA 372
Cdd:PRK12467 733 ARDAEAF----------AALMADQGVTVLKI--------------------VPSHLQALLQASRVALPRPQRALVCGGEA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 373 -PVSATVLTFlRAALGCQFYEGYGQTECTAGC----CLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVK 447
Cdd:PRK12467 783 lQVDLLARVR-ALGPGARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIG 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 448 GPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVA 520
Cdd:PRK12467 861 GAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVR 939
|
490 500
....*....|....*....|...
gi 1832483362 521 QVFV--HGESLQAFLIAIVVPDV 541
Cdd:PRK12467 940 EAVVlaQPGDAGLQLVAYLVPAA 962
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
51-519 |
9.01e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 89.85 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 51 DQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPlydtlgneaityivnkae 130
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIK--PGQEVVFQITHNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 131 lslVFVDKPEKAKLLLEGVENKLI-PGLkiivvmdaygselvergqrcgveVTSMKAMEDLgranrrkpkppaPEDLAVI 209
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWNTLKnPYL-----------------------ITEEEVLCEL------------ADELAFI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 210 CFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpcpDDTLISFLPLAHMFErvvecVMLCHGAKIgfFQGDIRLLMd 289
Cdd:cd05908 112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKT----KDRILSWMPLTHDMG-----LIAFHLAPL--IAGMNQYLM- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 290 dlkvlqPT-VFPVVPRLlnrmfdrifgqanttlkrWLLDfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMV 368
Cdd:cd05908 180 ------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMIL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 369 TGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCCL----------------------------TMPGDWTAG 414
Cdd:cd05908 235 NGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKDSECLTFV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 415 HVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 493
Cdd:cd05908 315 EVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREK 391
|
490 500
....*....|....*....|....*.
gi 1832483362 494 HIFkLAQGEYIAPEKIENIYMRSEPV 519
Cdd:cd05908 392 DII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
43-607 |
9.18e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 90.11 E-value: 9.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 43 PCLGSRKPDQ-PYEWLSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---YDTLG 118
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 119 NE--AITYIVNKAELSLVFVDKPEK-----AKLLLEGVEnklipglkiIVVMDAYG--------SELVERGQRCGVEvts 183
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVT---------VVHVTGPGegiasiafADLAATPPTAAVA--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 184 mKAMEDLGranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRNIvsdCSAfVKATENTVNPCPDD---TLISFLPLAH 260
Cdd:PRK12582 212 -AAIAAIT-----------PDTVAKYLFTSGSTGMPKAVINTQRMM---CAN-IAMQEQLRPREPDPpppVSLDWMPWNH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 261 MFervvecvmlchGAKIGFfQGDIR----LLMDDLKVLqPTVFPVVPRLLNRMFDRIFGQANTTLKrwLLDFASKRKEAE 336
Cdd:PRK12582 276 TM-----------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 337 LRSgiirnnslwdrliFHKvqsslggRVRLMVTGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGccLTMPGD 410
Cdd:PRK12582 341 RRS-------------FFK-------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAP--TTTGTH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 411 WTA---GHVGAPMPCNLIKLVDVEEmNYmaaegegEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PN 483
Cdd:PRK12582 398 WDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 484 GTLKIIDRKKHIFKLAQGEYIAPEKIE-NIYMRSEPVAQ-VFVHGESlQAFLIAIVVPDVETLCSWAQKRGfeGSFEELC 561
Cdd:PRK12582 470 KGLIFDGRVAEDFKLSTGTWVSVGTLRpDAVAACSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVV 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1832483362 562 RNKDVKKAILEDMVRLGKDSGlKPFEQVKGITLHPELFSIDNGLLT 607
Cdd:PRK12582 547 KHPAVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
74-534 |
2.43e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 88.59 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 74 IQKGFKTApdqfigIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfVDKPEKAKLLLEGVENKL 153
Cdd:PRK08008 59 IRKGDKVA------LHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLL-VTSAQFYPMYRQIQQEDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 154 IPgLKIIVVMDAYGSElvERGqrcgveVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdc 233
Cdd:PRK08008 132 TP-LRHICLTRVALPA--DDG------VSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 234 SAFVKATENTVNPcpDDTLISFLPLAHM-FERVVECVMLCHGAKIGF--------FQGDIRLLmddlkvlQPTVFPVVPR 304
Cdd:PRK08008 201 AGYYSAWQCALRD--DDVYLTVMPAFHIdCQCTAAMAAFSAGATFVLlekysaraFWGQVCKY-------RATITECIPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 305 LLNRM-------FDRifgqaNTTLKRWL--LDFASKRKEA-ELRSGiirnnslwdrlifhkvqsslggrVRLMVTgaapv 374
Cdd:PRK08008 272 MIRTLmvqppsaNDR-----QHCLREVMfyLNLSDQEKDAfEERFG-----------------------VRLLTS----- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 375 satvltflraalgcqfyegYGQTECTAGCCLTMPGD---WTAghVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKG-- 448
Cdd:PRK08008 319 -------------------YGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 449 -PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHG- 526
Cdd:PRK08008 376 gKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGi 454
|
490
....*....|....
gi 1832483362 527 ------ESLQAFLI 534
Cdd:PRK08008 455 kdsirdEAIKAFVV 468
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
57-540 |
2.86e-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: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd12114 13 LTYGELAERARRVAGALKAAG--VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKPekakllleGVENKLIPGLKIIVVMDAygselvergqrcgvevtsmkamedLGRANRRKPKPPAPEDLAVICFTSGTT 216
Cdd:cd12114 91 DGP--------DAQLDVAVFDVLILDLDA------------------------LAAPAPPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH------MFErvvecvMLCHGAKIGFFQGDIR----L 286
Cdd:cd12114 139 GTPKGVMISHRAALNTILDINRRFAVG----PDDRVLALSSLSFdlsvydIFG------ALSAGATLVLPDEARRrdpaH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 287 LMDDLKVLQPTVFPVVPRLLNrMfdrifgqanttlkrwLLDfaskrkeaELRSGIIRNNSLwdRLIFHK---VQSSLGGR 363
Cdd:cd12114 209 WAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL--RLVLLSgdwIPLDLPAR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 364 VRLMVTGAAPVSatvltflraaLGcqfyegyGQTECTAGCCL----TMPGDWTAGHVGAPMPCNLIKLVDveemnymaAE 439
Cdd:cd12114 263 LRALAPDARLIS----------LG-------GATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLD--------PR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 440 GE-------GEVCVKGPNVFQGYLKDPAKTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 508
Cdd:cd12114 318 GRdcpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGE 396
|
490 500 510
....*....|....*....|....*....|....
gi 1832483362 509 IENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPD 540
Cdd:cd12114 397 IEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
203-553 |
7.40e-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: 7.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpddtlISFLPLAHMFERVVE---CVMLCHGAKIGF 279
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASFSFDVFAgdfARSLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 280 FQGDIRL----LMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKE--AELRSGIIRNNSLWDRLiF 353
Cdd:cd17650 166 CPDEVKLdpaaLYDLILKSRITLMESTP----------------ALIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD-F 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 354 HKVQSSLGGRVRLmvtgaapVSATVLTflRAALGCQFYEGYGQTECTAGcclTMPgdwtaghVGAPMPCNLIKLVDvEEM 433
Cdd:cd17650 229 KTLAARFGQGMRI-------INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 507
Cdd:cd17650 289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELG 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1832483362 508 KIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETlcSWAQKRGF 553
Cdd:cd17650 368 EIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAELRAF 414
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
57-551 |
7.87e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.11 E-value: 7.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 dKPEKAKL----LLEGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICFT 212
Cdd:PRK06164 114 -WPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 213 -SGTTGNPK------GAMVTHRNIVSDCSAFVkatentvnpcPDDTLISFLPLahmfervveCVMLCHGAKIGFFQGDIR 285
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGYD----------PGAVLLAALPF---------CGVFGFSTLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 286 LLMDDlkvlqptVF--PVVPRLL-----------NRMFDRIFGQANTTLkrwllDFASKRkeaelrsgiirnnslwdRLI 352
Cdd:PRK06164 250 LVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----------------LFG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 353 FHKVQSSLGGRVRLMVTGAAPvsatvLTFLraalgcqfyegYGQTECTA-GCCLTMPGDWTAGHV--GAPM-PCNLIKLV 428
Cdd:PRK06164 301 FASFAPALGELAALARARGVP-----LTGL-----------YGSSEVQAlVALQPATDPVSVRIEggGRPAsPEARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 429 DVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 508
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAE 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1832483362 509 IENIYMRSEPVAQVFVHGESLQ------AFLIAI--VVPDVETLCSWAQKR 551
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 ... |
104-526 |
1.01e-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: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 104 FAYSM--------VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgQ 175
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIE-KAAPECPSKPKLVWVGDPVPE--G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 176 RCGVEVTSMKAMEDLGRanRRKPKPPAPEDLAVICFTSGTTGNPKgaMVTHRNIvsdcsafvkatentvnpcpddtlisf 255
Cdd:cd05970 159 WIDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFT-------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 256 LPLAHMFErvvecVMLCHGAKigffQGDIRLLMDDLKVLQPtvfpvvprllnrMFDRIFGQANTTLKRWLLDFasKRKEA 335
Cdd:cd05970 209 YPLGHIVT-----AKYWQNVR----EGGLHLTVADTGWGKA------------VWGKIYGQWIAGAAVFVYDY--DKFDP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 336 ELRSGIIRNN---------SLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLT 406
Cdd:cd05970 266 KALLEKLSKYgvttfcappTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 407 MPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCV---KGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKW 480
Cdd:cd05970 345 FPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWM 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1832483362 481 LPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 526
Cdd:cd05970 423 DEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
83-526 |
1.65e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 85.99 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 83 DQFIGIFAQNRPEW--VIIEQGCFAysMVIVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLLLEGVENklIPGLKII 160
Cdd:PRK05620 64 DQRVGSMMYNCAEHleVLFAVACMG--AVFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 161 VVMDAYGSELVERGQRCGVEVTSMKAMEDlGRANRRkPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKA 239
Cdd:PRK05620 139 VFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLSLRTT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 240 TENTVNpcPDDTLISFLPLAHmfervvecvMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVprllnrmfdrifgqaNT 319
Cdd:PRK05620 217 DSLAVT--HGESFLCCVPIYH---------VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKII---------------AT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 320 TLKRwlldfaskrkeaeLRSGIirnNSLWDRLIFHKVQSSlGGRVRL--MVTGAAPVSATVLTFLRAALGCQFYEGYGQT 397
Cdd:PRK05620 271 AMPR-------------VAHGV---PTLWIQLMVHYLKNP-PERMSLqeIYVGGSAVPPILIKAWEERYGVDVVHVWGMT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 398 ECTAGCCLTMPGDWTAGHVGAP-------MPCNLIKLVdVEEMNYMAA--EGEGEVCVKGPNVFQGYLKDPAKT------ 462
Cdd:PRK05620 334 ETSPVGTVARPPSGVSGEARWAyrvsqgrFPASLEYRI-VNDGQVMEStdRNEGEIQVRGNWVTASYYHSPTEEgggaas 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832483362 463 ----------AEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 526
Cdd:PRK05620 413 tfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
57-543 |
1.72e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 85.89 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKTAPDQFiGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:PRK07867 29 TSWREHIRGSAARAAALRARLDPTRPPHV-GVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKPEKAklLLEGVEnkliPGLKIIVVMDAYGSELVergqrcgvevtsmkameDLGRANRRKPKPPAPEDLAVICFTSGTT 216
Cdd:PRK07867 108 ESAHAE--LLDGLD----PGVRVINVDSPAWADEL-----------------AAHRDAEPPFRVADPDDLFMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDTLISFLPLAHMFERVVE-CVMLCHGAKI---------GFfqgdirl 286
Cdd:PRK07867 165 GDPKAVRCTHRKVASAGVMLAQ----RFGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 287 lMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrWLLDFASKRKEAElrsgiirnNSLwdRLIFhkvqsslggrvrl 366
Cdd:PRK07867 234 -LPDVRRYGATYANYVGKPLS----------------YVLATPERPDDAD--------NPL--RIVY------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 367 mvtGAAPVSATVLTFlRAALGCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAPMPCnlIKLVDVE--------------E 432
Cdd:PRK07867 274 ---GNEGAPGDIARF-ARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 433 MNYMAAEGEgEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 512
Cdd:PRK07867 346 LNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERI 422
|
490 500 510
....*....|....*....|....*....|.
gi 1832483362 513 YMRSEPVAQVFVHGeslqafliaivVPDVET 543
Cdd:PRK07867 423 LLRYPDATEVAVYA-----------VPDPVV 442
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
57-540 |
2.21e-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: 85.40 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKPEKAKLllegvenklipglkiivvmdaygselvergqRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTT 216
Cdd:cd17646 102 TADLAARL-------------------------------PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVSD----CSAFVKATENTV---NPCPDDTLIS--FLPLAHMfERVVECVMLCHGaKIGFFQGdirlL 287
Cdd:cd17646 151 GRPKGVMVTHAGIVNRllwmQDEYPLGPGDRVlqkTPLSFDVSVWelFWPLVAG-ARLVVARPGGHR-DPAYLAA----L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 288 MDDLKVlqpTVFPVVPRLLnrmfdRIFGQanttlkrwlldfaskrkeaELRSGIIRNnslwdrlifhkvqsslggrVRLM 367
Cdd:cd17646 225 IREHGV---TTCHFVPSML-----RVFLA-------------------EPAAGSCAS-------------------LRRV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 368 VTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGEV 444
Cdd:cd17646 259 FCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGEL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 445 CVKGPNVFQGYLKDPAKTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEP 518
Cdd:cd17646 338 YLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPA 416
|
490 500
....*....|....*....|....*
gi 1832483362 519 VAQVFV---HGESLQAFLIAIVVPD 540
Cdd:cd17646 417 VTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
203-543 |
2.34e-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: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFErVVEcvM---LCHGAKIGF 279
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWE--IwgaLLHGGRLVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 280 FQGDIRLLMDDLkvlqptvfpvvPRLLNRMFDRIFGQANTTLKRWLldfaskrkEAELRsgiirnnslwdrliFHKVQSS 359
Cdd:cd17643 165 VPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 360 LggrvRLMVTGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCL-----TMPGDWTAGHVGAPMPCNLIKLVDvE 431
Cdd:cd17643 212 L----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaADLPAAAASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 432 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 504
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832483362 505 APEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVET 543
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
203-551 |
3.46e-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: 84.23 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVV-ECVM-LCHGAkigff 280
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG----PGSRVLQFASPS--FDASVwELLMaLLAGA----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 qgdiRLLMDDLKVLQPtvfpvvprllnrmfdrifGQAnttlkrwLLDFaskrkeaelrsgiirnnsLWDRLIFHKVQS-- 358
Cdd:cd17652 161 ----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPpa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 359 --------SLGGRVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAgcCLTMPGDWTAGHV---GAPMPCNLIKL 427
Cdd:cd17652 194 alaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTV--CATMAGPLPGGGVppiGRPVPGTRVYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 428 VDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 500
Cdd:cd17652 269 LD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-R 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 501 GEYIAPEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVV------PDVETLCSWAQKR 551
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVpapgaaPTAAELRAHLAER 406
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
86-574 |
6.32e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.30 E-value: 6.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 86 IGIFAQNRPEwviIEQGCFAYSM---VIVPLYDTLGNEAITYIVNKAELSLVFVDKP-----EKAKLLLEGVENKLIPGL 157
Cdd:PLN03102 67 VSVLAPNTPA---MYEMHFAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDRSfeplaREVLHLLSSEDSNLNLPV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 158 KIIVVMD----AYGSE-----LVERGQRCGVEVTSMKAMEDlgranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRN 228
Cdd:PLN03102 144 IFIHEIDfpkrPSSEEldyecLIQRGEPTPSLVARMFRIQD-------------EHDPISLNYTSGTTADPKGVVISHRG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 229 I-VSDCSAFVKATENTvnpCPddTLISFLPLAHmfervvecvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTVFPVVpr 304
Cdd:PLN03102 211 AyLSTLSAIIGWEMGT---CP--VYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 305 llnRMFDRIFGQANTTLKRWLLdfaskrkeaelrsgiiRNNSLwdrlifhkVQSSLGGRVRLMVTGAAPVSATVLTFLRa 384
Cdd:PLN03102 271 ---EMHNVTHMCCVPTVFNILL----------------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 385 aLGCQFYEGYGQTECTAGCCLTMPGD-WT------AGHVGAPMPCNLIKLVDVEEMNYMAAEGE-------GEVCVKGPN 450
Cdd:PLN03102 323 -LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLADVDVKNKETQESVprdgktmGEIVIKGSS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 451 VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIymrsepvaqVFVHGESLQ 530
Cdd:PLN03102 402 IMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLE 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1832483362 531 AFLIAIVVPDV-ETLCSW-AQKRGFEGSFEE----LCRNKDVKKAILEDM 574
Cdd:PLN03102 471 TAVVAMPHPTWgETPCAFvVLEKGETTKEDRvdklVTRERDLIEYCRENL 520
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
202-539 |
1.83e-16 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 82.42 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigf 279
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT----PGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 280 fqgdiRLLMDDLKVLQPtvfpvvPRLLNRMFDR----IFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhk 355
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADR------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 356 VQSSLGGRVRLMVTGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLTMPGDWTAGH---VGAPMPCNLIKLV 428
Cdd:cd17649 206 TGDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 429 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 501
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1832483362 502 EYIAPEKIENIYMRSEPVAQVFVHGES--LQAFLIAIVVP 539
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVL 400
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
205-535 |
3.33e-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: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRnivsDCSAFVKATENTVNPCPDDTLISFLPLAHMFerVVEC-----VMLChGAKIGF 279
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHN----DYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 280 FQ----GDIRLLMDDLKVlqpTVFPVVPRLLnrmfdrifgqanttlKRWLlDFASKRKEAElrsgiirnnslwdrlifhk 355
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPALV---------------SLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 356 vqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTM---PGDWTAGHVGAPM-PCNLIKLVDv 430
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE---GlLNYTRlddPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 431 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 510
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 1832483362 511 NIYMRSEPVAQVFV-------HGESLQAFLIA 535
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
57-526 |
2.61e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 79.16 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL-YDTLGNEaITYIVNKAELSLVF 135
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLG--PGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 136 VDK---PEKAKLLLEgvenklIPGLKIIVVMDAYGSELVERGqrcGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICfT 212
Cdd:PRK07798 106 YERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-T 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 213 SGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK-----IGFFQGdirll 287
Cdd:PRK07798 172 GGTTGMPKGVMWRQEDIFR--VLLGGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSG----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 288 mddlkvlQPTVFPVVPRL-------------LNRMFdrIFGQAnttLKRWLLDFASKRKEAELrsgiirnnslwdrlifh 354
Cdd:PRK07798 245 -------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL----------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 355 kvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAP--MPCNLIKLVDVE 431
Cdd:PRK07798 296 ---SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGPRTVVLDED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 432 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 508
Cdd:PRK07798 367 GNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEE 445
|
490
....*....|....*....
gi 1832483362 509 IENIyMRSEP-VAQVFVHG 526
Cdd:PRK07798 446 VEEA-LKAHPdVADALVVG 463
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
170-523 |
4.07e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.40 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 170 LVERGQRCGvevTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNP 246
Cdd:PRK09274 140 LVTVGGRLL---WGGTTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 247 CPDDTLISFLPLahmfervvecvMLCHGAKIGFfqGDIRLLMDDLKVLQptvfpVVPRllnRMFDRIFGQANTTLkrwll 326
Cdd:PRK09274 213 EPGEIDLPTFPL-----------FALFGPALGM--TSVIPDMDPTRPAT-----VDPA---KLFAAIERYGVTNL----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 327 dFASKrkeaelrsgiirnnSLWDRLIFHKVQS--SLGGrVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC--- 399
Cdd:PRK09274 267 -FGSP--------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpi 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 400 ---TAGCCLTMPGDWT---AGH-VGAPMPCNLIKLVDVEEM-------NYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAE 464
Cdd:PRK09274 331 ssiESREILFATRAATdngAGIcVGRPVDGVEVRIIAISDApipewddALRLATGEiGEIVVAGPMVTRSYYNRPEATRL 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832483362 465 A--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniymrSEPVAQVF 523
Cdd:PRK09274 411 AkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIF 462
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
203-550 |
6.75e-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: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDTLI--SFLPLAHMFErvvecvMLCH---GAKI 277
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPA---DKSLVyaSFSFDASAWE------IFPHltaGAAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 278 GFFQGDIRLLMDDLkvlqptvfpvvprllnrmfDRIFGQANTTLKRWLLDFASKRKEAElrsgiirNNSLwdrlifhkvq 357
Cdd:cd17645 174 HVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL---------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 358 sslggrvRLMVTGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMA 437
Cdd:cd17645 218 -------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 438 AEG-EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 510
Cdd:cd17645 284 PIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIE 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1832483362 511 NIYMRSEPVAQVFV-------HGESLQAFLIAIVVPDVETLCSWAQK 550
Cdd:cd17645 363 PFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
202-539 |
1.68e-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: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLAHMFER-VVECVMLCHGAKIGFF 280
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 QGDI-RLLMDDLKVLQPTVFPVVPRLLNRMfdrifgqanttlkrwlldFASKRKEAELRSGiirnnslwdrlifhkvqss 359
Cdd:cd05958 172 EEATpDLLLSAIARYKPTVLFTAPTAYRAM------------------LAHPDAAGPDLSS------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 360 lggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 439
Cdd:cd05958 215 ----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 440 GEGEVCVKGPNvfqGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 519
Cdd:cd05958 290 TIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340
....*....|....*....|...
gi 1832483362 520 AQVFVHGESLQAFLI---AIVVP 539
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVL 388
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
203-514 |
1.93e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQG 282
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 283 DIRLLMDDLkvlqPTVF---PVVPRLLNRMFDR----IFGQANTTLKrWLLDFASKRKEA--ELRSGIIRNNSLWDRLiF 353
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFD-YILKTAKKQESClpSLRFVVIGGDAFKDSL-Y 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 354 HKVQSslggrvrlmvtgaapvsatvlTFLRAALgcqfYEGYGQTECTAgcCLTMPGDWTAGH---VGAPMPCNLIKLVDv 430
Cdd:PRK06334 317 QEALK---------------------TFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGMPIRGMDVLIVS- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 431 EEMNYMAAEGE-GEVCVKGPNVFQGYL-KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 508
Cdd:PRK06334 369 EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEA 447
|
....*.
gi 1832483362 509 IENIYM 514
Cdd:PRK06334 448 LESILM 453
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
393-549 |
1.98e-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: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 393 GYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGW 471
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832483362 472 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyMRSEP-VAQVFVhgeslqafliaIVVPDVetlcSWAQ 549
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAV-----------IGVPDP----RWAQ 280
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
57-540 |
2.15e-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: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICFTSGTT 216
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVsdcsAFVKATENTvnpCPDD--------TLISF-LPLAHMFervvecVMLCHGAKIgffqgdirll 287
Cdd:cd12115 118 GRPKGVAIEHRNAA----AFLQWAAAA---FSAEelagvlasTSICFdLSVFELF------GPLATGGKV---------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 288 mddlkVLQPTVFPvvprllnrmfdrifgqanttlkrwLLDFASkRKEAELrsgIIRNNSLWDRLIFHkvqSSLGGRVRLM 367
Cdd:cd12115 175 -----VLADNVLA------------------------LPDLPA-AAEVTL---INTVPSAAAELLRH---DALPASVRVV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 368 VTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 444
Cdd:cd12115 219 NLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGEL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 445 CVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEP 518
Cdd:cd12115 298 YIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPG 376
|
490 500
....*....|....*....|....*
gi 1832483362 519 VAQ--VFVHGESL-QAFLIAIVVPD 540
Cdd:cd12115 377 VREavVVAIGDAAgERRLVAYIVAE 401
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
203-553 |
2.21e-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: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpdDTLISFLPLAhmFERVVE--CVMLCHGAKIgff 280
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS----DRVLQFASIA--FDVAAEeiYVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 qgdirllmddlkVLQPtvfpvvprllNRMFdrifgqanttlkRWLLDFASKRKEAELRSGIIrNNSLWDRLIFHKVQSSL 360
Cdd:cd17644 176 ------------VLRP----------EEMR------------SSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 361 GG--RVRLMVTGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCCLTMPGDWTAGH-----VGAPMPCNLIKLVDvE 431
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 432 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 503
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832483362 504 IAPEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETLCSWAQKRGF 553
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
120-594 |
2.63e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.90 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 120 EAITYIVNKAELSLVFVD---KPekaklLLEGVENKLiPGLKIIVVM-DAygselvergQRCGVEVTSMKAMEDL-GRAN 194
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMtDA---------AHLPAGSTPLLCYETLvGAQD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 195 RRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPCPDDTLisfLPLAHMFErvVECVMLCH 273
Cdd:PRK07008 166 GDYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 274 -----GAKIgffqgdirllmddlkvlqptVFPvvprllnrmfdrifGQAnttlkrwlLDFASKRK--EAELRSGIIRNNS 346
Cdd:PRK07008 239 sapltGAKL--------------------VLP--------------GPD--------LDGKSLYEliEAERVTFSAGVPT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 347 LWDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLT-----MPGD------W 411
Cdd:PRK07008 277 VWLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKwkhsqLPLDeqrkllE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 412 TAGHV--GAPMpcnliKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDkDGWLHTGDIGKWLPNGTLK 487
Cdd:PRK07008 357 KQGRViyGVDM-----KIVG-DDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 488 IIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAqvfvhgeslQAFLIAIVVP--DVETLCSWAQKRGFEGSFEELCRNKD 565
Cdd:PRK07008 427 ITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA---------EAACIACAHPkwDERPLLVVVKRPGAEVTREELLAFYE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1832483362 566 VKKA---ILEDMVRL--------GKDSGLKPFEQVKGITL 594
Cdd:PRK07008 497 GKVAkwwIPDDVVFVdaiphtatGKLQKLKLREQFRDYVL 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
200-544 |
3.35e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 200 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAki 277
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELT----PDDRVLQFMSFS--FDGSHEGLYhpLINGA-- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 278 gffqgdiRLLMDDLKVLQPtvfpvvprllNRMFDRIFGQANTTlkrwlLDFASkrkeaelrsgiirnnSLWDRLIFHKVQ 357
Cdd:PRK12316 4762 -------SVVIRDDSLWDP----------ERLYAEIHEHRVTV-----LVFPP---------------VYLQQLAEHAER 4804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 358 SSLGGRVRLMVTG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLTMPGDWTAG----HVGAPMPCNLIKLVDV 430
Cdd:PRK12316 4805 DGEPPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDG 4883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 431 eEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 503
Cdd:PRK12316 4884 -QLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFR 4961
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1832483362 504 IAPEKIEnIYMRSEP-------VAQVFVHGeslqAFLIAIVVPDVETL 544
Cdd:PRK12316 4962 IELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPQDPAL 5004
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
204-534 |
6.78e-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: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 204 EDLAVICFTSGTTGNPKgaMVTHrnivSDCSAFVKA----------TENTVNPCPDDTLISFLPLAHMFERVVE--CVML 271
Cdd:cd05928 174 QEPMAIYFTSGTTGSPK--MAEH----SHSSLGLGLkvngrywldlTASDIMWNTSDTGWIKSAWSSLFEPWIQgaCVFV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 272 CHGAKIgffqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLL--DFASkrkeaelrsgiirnnslwd 349
Cdd:cd05928 248 HHLPRF-----DPLVILKTLSSYPITTFCGAP----------------TVYRMLVqqDLSS------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 350 rlifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG-DWTAGHVGAPMPCNLIKLV 428
Cdd:cd05928 288 ----YKFPS-----LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGmKIKPGSMGKASPPYDVQII 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 429 DvEEMNYMAAEGEGEVCVK-GPN----VFQGYLKDPAKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 503
Cdd:cd05928 358 D-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYR 434
|
330 340 350
....*....|....*....|....*....|....*...
gi 1832483362 504 IAPEKIENIYMRSEPVAQVFV-------HGESLQAFLI 534
Cdd:cd05928 435 IGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
200-542 |
1.60e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.98 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 200 PPAPEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFvkatenTVNpcpDDTLISfLPLAHmfervvecV---- 269
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQAHlasaegVLSLMPF------TAQ---DSWLLS-LPLFH--------Vsgqg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 270 ----MLCHGAKIGFfqGDIRLLMDDLkvLQPTVFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnn 345
Cdd:PRK09029 193 ivwrWLYAGATLVV--RDKQPLEQAL--AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 346 slwdrlifhkvqsslGGrvrlmvtGAAPVSatvLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTAGhVGAPMPCNLI 425
Cdd:PRK09029 248 ---------------GG-------AAIPVE---LTEQAEQQGIRCWCGYGLTEMASTVC-AKRADGLAG-VGSPLPGREV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 426 KLVDveemnymaaegeGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIA 505
Cdd:PRK09029 301 KLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQ 365
|
330 340 350
....*....|....*....|....*....|....*..
gi 1832483362 506 PEKIENIYMRSEPVAQVFVhgeslqafliaIVVPDVE 542
Cdd:PRK09029 366 PEEIERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
188-540 |
2.84e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.77 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 188 EDLGRANRRKPKPPAPEDLAVIC---FTSGTTGNPKGAMVTHRNIvsdcsAFVkATENTVNPCPD----DTLISFLPLAH 260
Cdd:PRK07470 144 EALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQM-----AFV-ITNHLADLMPGtteqDASLVVAPLSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 261 MfERVVECVMLCHGAKigffqgDIRLLMDDLKVlqPTVFPVVPRL-LNRMFdrifgQANTTLKRWLLDFASKRKEaelrs 339
Cdd:PRK07470 218 G-AGIHQLCQVARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD----- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 340 giirnnslwdrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGC------CLTMPGDWTA 413
Cdd:PRK07470 279 -----------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNitvlppALHDAEDGPD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 414 GHVGapmPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLK 487
Cdd:PRK07470 337 ARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLY 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832483362 488 IIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPD 540
Cdd:PRK07470 412 ITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD 452
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
201-575 |
5.13e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.89 E-value: 5.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 201 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKIG 278
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 279 FFQGDIRL----LMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFAskrkEAELRSGIIRnnslwdRLIFh 354
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ----------------LLQMD----EQVEHPLSLR------RVVC- 1841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 355 kvqsslGGRvrlmvtgAAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CCLTMPGDWTAGHVGAPMPcNLIKLV 428
Cdd:PRK12467 1842 ------GGE-------ALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIA-NLSTYI 1905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 429 DVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQG 501
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RG 1984
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832483362 502 EYIAPEKIENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPDVETLCSWAQKRGfeGSFEELcrnKDVKKAILED-MV 575
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 ... |
201-523 |
5.44e-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: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 201 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchGAKIGff 280
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFA----AQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 qgdirllmddLKVLQPTVFPVVPrllnrmfdrifGQANttlKRWLLDFASKRKEaelrSGIIRNNSLWDRLIFHKVQSSL 360
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 361 G-GRVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LTMPGDWTAGH----VGAPMPCNLIKL 427
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 428 VDVEEMNYMAAEGE--------GEVCVKGPNVFQGYLKDPAKTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 495
Cdd:cd05910 277 IEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*...
gi 1832483362 496 FKLAQGEYIapekieniymrSEPVAQVF 523
Cdd:cd05910 357 VITTGGTLY-----------TEPVERVF 373
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
346-524 |
9.38e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 70.67 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 346 SLWdRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLI 425
Cdd:cd05974 185 TVW-RMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRV 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 426 KLVDVEEmnymAAEGEGEVCV-----KGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 500
Cdd:cd05974 264 ALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SS 337
|
170 180
....*....|....*....|....
gi 1832483362 501 GEYIAPEKIENIYMRSEPVAQVFV 524
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAEAAV 361
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
186-539 |
1.49e-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: 70.10 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 186 AMEDLGRANRRKPKPPAPEDLA--VICFTSGTTGNPKGAMVTHrnivsDCsafvkatentvNPCPDDTLISF-LPLAHMF 262
Cdd:cd05929 105 GLEDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGL-----PG-----------GPPDNDTLMAAaLGFGPGA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 263 ERVVECVM-LCHGAKIGFFQGDIRL-----LM---DDLKVLQP------TVFPVVPRLLNRMfdrifgqanttLK----- 322
Cdd:cd05929 169 DSVYLSPApLYHAAPFRWSMTALFMggtlvLMekfDPEEFLRLieryrvTFAQFVPTMFVRL-----------LKlpeav 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 323 RWLLDFASkrkeaeLRSgiirnnslwdrlIFHkvqsslggrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG 402
Cdd:cd05929 238 RNAYDLSS------LKR------------VIH---------------AAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 403 CCLTmPGDWTA--GHVGAPMPCNLiKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDGWLHTGDIGKW 480
Cdd:cd05929 285 TIIN-GEEWLThpGSVGRAVLGKV-HILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYL 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832483362 481 LPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVP 539
Cdd:cd05929 361 DEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
197-522 |
1.49e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 197 KPKPPAPEDLAVIcFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHM--FERVVECVMlcHG 274
Cdd:PRK05857 163 NADQGSEDPLAMI-FTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIggLWWILTCLM--HG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 275 AKI---GFFQGDIRLLMDDLKVLQPTVfpvVPRLLNRMFdrifgqanttlkrwlldfaskrkeAELRSGIIRNNSLwdrl 351
Cdd:PRK05857 240 GLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPSL---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 352 ifhkvqsslggrvRLMVTGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 426
Cdd:PRK05857 289 -------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 427 LVDVEEMNYMAAEGE-----GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 501
Cdd:PRK05857 355 LAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGG 432
|
330 340
....*....|....*....|.
gi 1832483362 502 EYIAPEKIENIymrSEPVAQV 522
Cdd:PRK05857 433 VNIAPDEVDRI---AEGVSGV 450
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
57-534 |
1.76e-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: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAQNrPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd05973 1 LTFGELRALSARFANALQELGVG-PGDVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 DKPEKAKLllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICFTSGTT 216
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 217 GNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDtliSFLPLAH------MFERVVECVMLCHGAKI---GFFQGDIRLL 287
Cdd:cd05973 101 GLPKGVPVPLRALA----AFGAYLRDAVDLRPED---SFWNAADpgwaygLYYAITGPLALGHPTILlegGFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 288 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkeaeLRSGIirnnslwdrlifhKVQSSLGGRVRLM 367
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLL------------------------------MAAGA-------------EVPARPKGRLRRV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 368 VTGAAPVSATVLTFLRAALGCQFYEGYGQTEctagccLTMP--GDWTAGHV------GAPMP---CNLIKLVDVEemnym 436
Cdd:cd05973 211 SSAGEPLTPEVIRWFDAALGVPIHDHYGQTE------LGMVlaNHHALEHPvhagsaGRAMPgwrVAVLDDDGDE----- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 437 AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 511
Cdd:cd05973 280 LGPGEpGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
490 500 510
....*....|....*....|....*....|
gi 1832483362 512 IYMRSEPVAQVFV-------HGESLQAFLI 534
Cdd:cd05973 355 ALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
57-521 |
3.45e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.20 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNrPEWVIIEQGCFaYSMVI-VPLYDTLGN-----EAITYIVNKAE 130
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQARA--SFGDRAVLLFPSG-PDYVAAFFGCL-YAGVIaVPAYPPESArrhhqERLLSIIADAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 131 LSLVFVDkpekAKLL--LEGVENKLIPGLKIIVVMDAYGSELVERGQrcgvevtsmkamedlgranrrKPKPPaPEDLAV 208
Cdd:PRK05691 117 PRLLLTV----ADLRdsLLQMEELAAANAPELLCVDTLDPALAEAWQ---------------------EPALQ-PDDIAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 209 ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcPDDTLISFLPLAHmfervvecvmlchgaKIGFFQGdirllm 288
Cdd:PRK05691 171 LQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLN--PDDVIVSWLPLYH---------------DMGLIGG------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 289 ddlkVLQPtVFPVVPRLLnrMFDRIFGQANTtlkRWLldfaskrkEA--ELRSGIIRNNSLWDRLIFHKV-QSSLGG--- 362
Cdd:PRK05691 228 ----LLQP-IFSGVPCVL--MSPAYFLERPL---RWL--------EAisEYGGTISGGPDFAYRLCSERVsESALERldl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 363 -RVRLMVTGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECT---AGC-------CLTMPGDWTAGHV--------- 416
Cdd:PRK05691 290 sRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgipALELDAEALARNRaepgtgsvl 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 417 ---GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-LDKDG--WLHTGDIGkWLPNGTLKIID 490
Cdd:PRK05691 370 mscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTG 448
|
490 500 510
....*....|....*....|....*....|.
gi 1832483362 491 RKKHIFkLAQGEYIAPEKIENIYMRSEPVAQ 521
Cdd:PRK05691 449 RLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
364-533 |
4.31e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 69.10 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 364 VRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDW------TAGHVGAPMPCNLIKL-----VD 429
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstVCAWKP-EWdslppeEQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 VEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 507
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190
....*....|....*....|....*....|...
gi 1832483362 508 KIENIYMRSEPVAQVFV-------HGESLQAFL 533
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
48-526 |
5.12e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.56 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 48 RKPDQPY-------EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNE 120
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLK--RGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 121 AITYIVNKAELSLVF--VDKPEKAKLLLegvenKLIPGLKIIVVMDAYGSelvergqrcgvevtsMKAMEDLGRANRRKP 198
Cdd:PRK13391 87 EAAYIVDDSGARALItsAAKLDVARALL-----KQCPGVRHRLVLDGDGE---------------LEGFVGYAEAVAGLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 199 KPPAPEDL--AVICFTSGTTGNPKGamvthrnivsdcsafVKAtentvnPCPDDTLISFLPLAHMFERVV----ECVMLC 272
Cdd:PRK13391 147 ATPIADESlgTDMLYSSGTTGRPKG---------------IKR------PLPEQPPDTPLPLTAFLQRLWgfrsDMVYLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 273 -----HGAKIGFFQGDIRL-----LMDD------LKVLQP---TVFPVVPRllnrMFDRIFGQANTTLKRWLLdfaskrk 333
Cdd:PRK13391 206 paplyHSAPQRAVMLVIRLggtviVMEHfdaeqyLALIEEygvTHTQLVPT----MFSRMLKLPEEVRDKYDL------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 334 eaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDWTA 413
Cdd:PRK13391 275 ------------------------SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 414 --GHVGAPMpCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDG-WLHTGDIGKWLPNGTLKIID 490
Cdd:PRK13391 326 hpGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTD 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 1832483362 491 RKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 526
Cdd:PRK13391 403 RAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
37-544 |
1.84e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 66.97 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 37 QVSNNGPCLGSRkpDQPYEWlsyKQVAELSECIGSALIQKGFKTAPDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDT 116
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTW---REVLAEAAARAAALIALADPDRPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLNTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 117 LGNEAITYIVNKAELSLVFVDKPEKAklLLEGVEnklIPGLKIIVVMDAYGSELVERGQRCgvevtsmkamedlgranrr 196
Cdd:PRK13388 86 RRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTPAYAELVAAAGAL------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 197 KP-KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvECVM----- 270
Cdd:PRK13388 142 TPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT----RDDVCYVSMPLFHS-----NAVMagwap 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 271 -LCHGAKI---------GFfqgdirllMDDLKVLQPTVFPVVPRLL-------NRMFDrifgqANTTLKRWLLDFASKRK 333
Cdd:PRK13388 213 aVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPRD 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 334 EAElrsgiirnnslwdrlifhkvqsslggrvrlmvtgaapvsatvltFLRAaLGCQFYEGYGQTEctAGCCLTMPGDWTA 413
Cdd:PRK13388 280 IAE--------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPP 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 414 GHVGAPMPCnlIKLVDVEEM---------------NymAAEGEGE-VCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDI 477
Cdd:PRK13388 313 GSIGRGAPG--VAIYNPETLtecavarfdahgallN--ADEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDL 387
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832483362 478 GKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG----ESLQAFLIAIVVPDVETL 544
Cdd:PRK13388 388 AYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATF 457
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
120-526 |
1.87e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 66.70 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 120 EAITYIVNKAELSLVFVDK---PekaklLLEGVENKLiPGLKIIVVMdaygselverGQRCGVEVTSMK---AMED-LGR 192
Cdd:PRK06018 101 EQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVVL----------TDAAHMPQTTLKnavAYEEwIAE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 193 ANRRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPCPDDTLISFLPLAH-------MFER 264
Cdd:PRK06018 165 ADGDFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHRSNV--LHALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 265 VVECVMLCHGAKIGffQGDIRLLMDDLKVlqpTVFPVVPrllnrmfdrifgqantTLKRWLLDF--ASKRKEAELRSGII 342
Cdd:PRK06018 243 SMGTKLVMPGAKLD--GASVYELLDTEKV---TFTAGVP----------------TVWLMLLQYmeKEGLKLPHLKMVVC 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 343 rnnslwdrlifhkvqsslGGrvrlmvtgaapvSATVLTFLRA--ALGCQFYEGYGQTECT---AGCCLTMPGDWTAGHV- 416
Cdd:PRK06018 302 ------------------GG------------SAMPRSMIKAfeDMGVEVRHAWGMTEMSplgTLAALKPPFSKLPGDAr 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 417 -------GAPMPCNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDKDGWLHTGDIGKWLPNGTLK 487
Cdd:PRK06018 352 ldvlqkqGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMR 427
|
410 420 430
....*....|....*....|....*....|....*....
gi 1832483362 488 IIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 526
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 ... |
203-544 |
3.18e-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: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpCPDDTLISFLPlAHMFERVVE--CVMLCHGAKIGFF 280
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGR---DNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 QGDIRL-------LMDDLKVlqpTVFPVVPRLLNRM-FDRIfgqanTTLKRWLL---DFASKRkeaelrsgiirnnslwd 349
Cdd:cd17648 169 PDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV----------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 350 rliFHKVQSSLGGRVrlmVTGAAPVSATVLTFLRaalgcqFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIklvd 429
Cdd:cd17648 224 ---FEKLRSRFAGLI---INAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 veemnymaaegeGEVCVKGPNVFQGYLKDPAKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHI 495
Cdd:cd17648 288 ------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQ 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832483362 496 FKLaQGEYIAPEKIENIYMRSEPVAQVFV--------HGESLQAFLIAIVVPDVETL 544
Cdd:cd17648 356 VKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
365-540 |
5.91e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.40 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 365 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGDwTAGHV----GAPM-PCNLIKLVDvEEMNYMAa 438
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GlVNYTRLDD-SDERIfttqGRPMsPDDEVWVAD-ADGNPLP- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 439 EGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIY 513
Cdd:PRK10946 377 QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLL 451
|
170 180
....*....|....*....|....*..
gi 1832483362 514 MRsepvaqvfvHGESLQAFLIAIvvPD 540
Cdd:PRK10946 452 LR---------HPAVIHAALVSM--ED 467
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
205-526 |
8.09e-11 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 64.68 E-value: 8.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 205 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVE-CVMLCHGAKIGF---F 280
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL----PSDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 QGdiRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfASKRKEAELRsgiirnnslwdrlifHKVQSSL 360
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 361 GGRVRLMVTGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGCCLTMPGDWTAGHVGA----PMPCNLIKlVDVEEMN- 434
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSGFINFFGKPGAIGRNPSllrkVAPLALVK-YDLESGEp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 435 ------YMAAEGEGEV--CV-----KGPnvFQGYLkDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHI 495
Cdd:cd05940 272 irdaegRCIKVPRGEPglLIsrinpLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDT 348
|
330 340 350
....*....|....*....|....*....|.
gi 1832483362 496 FKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 526
Cdd:cd05940 349 FRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
358-542 |
1.49e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 63.77 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 358 SSLggrvRLMVTGAAPVSATVLtflRAAL---GCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNlIKLVDvEE 432
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-ED 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 433 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 511
Cdd:PRK08276 332 GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
170 180 190
....*....|....*....|....*....|.
gi 1832483362 512 IYMRSEPVAQVFVHGeslqafliaivVPDVE 542
Cdd:PRK08276 410 LLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
203-550 |
1.70e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.80 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpdDTLISFLPLAhmFERVVECVM--LCHGAKIGFF 280
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN----DRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 QGDIRllmDDLKVLQptvfpvvprLLNRmfDRIfgqanTTlkrwlLDFASkrkeaelrsgiirnNSLWDRLIFHKVQSsl 360
Cdd:PRK12467 3310 DNDLW---DPEELWQ---------AIHA--HRI-----SI-----ACFPP--------------AYLQQFAEDAGGAD-- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 361 GGRVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKL---VDVEEMNY 435
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLDGQLNP 3429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 436 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 508
Cdd:PRK12467 3430 VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGE 3508
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1832483362 509 IENIYMRSEPVAQVFVHGESLQA--FLIAIVVPDVETlCSWAQK 550
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQ-GDWRET 3551
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
120-540 |
1.77e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.56 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 120 EAITYIVN--KAELSLVFVDkpekaklLLEGVENKLIPGLKIIVV------MDAYGSELVERGQRCGvevtsMKAMEDLG 191
Cdd:PRK12406 73 EEIAYILEdsGARVLIAHAD-------LLHGLASALPAGVTVLSVptppeiAAAYRISPALLTPPAG-----AIDWEGWL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 192 RANRRKPKPPAPEDLAVIcFTSGTTGNPKGamvthrnivsdcsafVKATentvNPCPDDTL--ISFLPLAHMFERVVECV 269
Cdd:PRK12406 141 AQQEPYDGPPVPQPQSMI-YTSGTTGHPKG---------------VRRA----APTPEQAAaaEQMRALIYGLKPGIRAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 270 M---LCHGAKIGFFQGDIRLlmDDLKVLQP-----------------TVFpVVPRllnrMFDRifgqanttlkrwLLDFA 329
Cdd:PRK12406 201 LtgpLYHSAPNAYGLRAGRL--GGVLVLQPrfdpeellqlierhritHMH-MVPT----MFIR------------LLKLP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 330 SKRKEAelrsgiirnnslWDrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG 409
Cdd:PRK12406 262 EEVRAK------------YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 410 DWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNV--FQgYLKDPAKTAEaLDKDGWLHTGDIGKWLPNGT 485
Cdd:PRK12406 318 DALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832483362 486 LKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 540
Cdd:PRK12406 395 LFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
48-542 |
2.20e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 64.21 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 48 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 122
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 123 TYIVNKAELsLVFVDKPEKAKLLLEGVENKLipglkiivvmdaygselVERGQrcgvevtsmkamEDLGRANrrKPKPPA 202
Cdd:PRK12316 3147 AYMLEDSGA-QLLLSQSHLRLPLAQGVQVLD-----------------LDRGD------------ENYAEAN--PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHrnivSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqg 282
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRH----SALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV----- 3265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 283 dirllmddlkVLQPTVFPVVPRLLNRMFDRifGQANTTLKRWlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGG 362
Cdd:PRK12316 3266 ----------VLAGPEDWRDPALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTS 3312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 363 RVRLMVTGAAPVSATVltfLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGH--VGAPMPCNLIKLVDVeEMNYMAAEG 440
Cdd:PRK12316 3313 LKRIVCGGEALPADLQ---QQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGA 3388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 441 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYM 514
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLL 3467
|
490 500
....*....|....*....|....*...
gi 1832483362 515 RSEPVAQVFVHGESLQAfLIAIVVPDVE 542
Cdd:PRK12316 3468 EHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
165-522 |
2.78e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.25 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 165 AYGSELvergQRCGVEVTSMkAMEDL---GRANRRKPKPPAP-EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAT 240
Cdd:PRK05851 114 SHGSHL----ERLRAVDSSV-TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 241 ENTVnpcPDDTLISFLPLAH-MFERVVECVMLChGAKIGffqgdirllmddlkvLQPT-VFPVVP-RLLNrmfdrifgqa 317
Cdd:PRK05851 189 GLDA---ATDVGCSWLPLYHdMGLAFLLTAALA-GAPLW---------------LAPTtAFSASPfRWLS---------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 318 nttlkrWLLDF-ASKRKEAELRSGIIRNNSlwdrlifHKVQSSLGGRVRLMVTGAAPVSATVLT-FLRAALGCQFYEG-- 393
Cdd:PRK05851 240 ------WLSDSrATLTAAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaa 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 394 ---YGQTECTagCCLTMP---------------GDWTAGH--VGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQ 453
Cdd:PRK05851 307 apsYGLAEST--CAVTVPvpgiglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMS 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832483362 454 GYLKDPAktaeaLDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIymrsepVAQV 522
Cdd:PRK05851 385 GYLGQAP-----IDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
57-543 |
7.97e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 61.87 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRpEWVIIEQGCFAYSMVIVPLYDT-LGNEAITYIVNKAELSLVF 135
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVR--AGDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 136 VDKpEKAKLLlEGVENKLIPGLKIIVVMDAygselvERGQRCGVEVtsmkaMEDLGRANRRKPKPPAPEDLAVICFTSGT 215
Cdd:PRK07788 152 YDD-EFTDLL-SALPPDLGRLRAWGGNPDD------DEPSGSTDET-----LDDLIAGSSTAPLPKPPKPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 216 TGNPKGAMVTHRNIVSDCSAFV-----KATENTVNPCPddtlisflplahMFervvecvmlcHG-----AKIGFFQG--- 282
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLLsrvpfRAGETTLLPAP------------MF----------HAtgwahLTLAMALGstv 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 283 ------DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwLLDFASKRKEAelrsgiirnnslwdrlifhkv 356
Cdd:PRK07788 277 vlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPEVLAKYDT--------------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 357 qSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECtAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMN 434
Cdd:PRK07788 323 -SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-ENGN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 435 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 514
Cdd:PRK07788 396 EVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLA 470
|
490 500
....*....|....*....|....*....
gi 1832483362 515 RSEPVAQVFVHGeslqafliaivVPDVET 543
Cdd:PRK07788 471 GHPDVVEAAVIG-----------VDDEEF 488
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
49-574 |
1.24e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 61.06 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 49 KPDQP-YEWL----SYKQVAELSECIGSALIQKGF-KTAPdqfIGIFAQNRPEWVI-----IEQGCfAYsmviVPLYDTL 117
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSLKLpDKSP---IIVFGHMSPEMLAtflgaVKAGH-AY----IPVDVSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 118 GNEAITYIVNKAELSLVFvdkpEKAKLLLEGVENKLIpglkiivvmdayGSELVERGQRCGVEVTSMKAMEDlgranrrk 197
Cdd:PRK04813 87 PAERIEMIIEVAKPSLII----ATEELPLEILGIPVI------------TLDELKDIFATGNPYDFDHAVKG-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 198 pkppapEDLAVICFTSGTTGNPKGAMVTHRNIVS----DCSAFVKATENTV-NPCPddtlISFlplahmfervvecvmlc 272
Cdd:PRK04813 143 ------DDNYYIIFTSGTTGKPKGVQISHDNLVSftnwMLEDFALPEGPQFlNQAP----YSF----------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 273 hgakigffqgdirllmdDLKV--LQP------TVFPVVPRLLNRmfdriFGQANTTLKR-----W----------LLD-- 327
Cdd:PRK04813 196 -----------------DLSVmdLYPtlasggTLVALPKDMTAN-----FKQLFETLPQlpinvWvstpsfadmcLLDps 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 328 FASKrKEAELRsgiirnnslwdRLIF------HKVQSSLGGRVrlmvtgaaPvSATVltflraalgcqfYEGYGQTECTA 401
Cdd:PRK04813 254 FNEE-HLPNLT-----------HFLFcgeelpHKTAKKLLERF--------P-SATI------------YNTYGPTEATV 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 402 GC------------CLTMPgdwtaghVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DK 468
Cdd:PRK04813 301 AVtsieitdemldqYKRLP-------IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTF 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 469 DGW--LHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDve 542
Cdd:PRK04813 373 DGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GYRIELEEIEQNLRQSSYVESAVVvpynKDHKVQY-LIAYVVPK-- 447
|
570 580 590
....*....|....*....|....*....|..
gi 1832483362 543 tlcswaqkrgfEGSFEelcRNKDVKKAILEDM 574
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 ... |
204-542 |
2.63e-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: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 204 EDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAH--MFERVVECvmLCHGAKIGFFQ 281
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVN----LLHFEREKTNINFSDKVLQFATCSFdvCYQEIFST--LLSGGTLYIIR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 282 GDIRLLMDDLKVL------QPTVFPVVprLLNRMFDrifgqanttLKRWLLDFASKRKEAeLRSG--IIRNNSLWDRLIF 353
Cdd:cd17656 202 EETKRDVEQLFDLvkrhniEVVFLPVA--FLKFIFS---------EREFINRFPTCVKHI-ITAGeqLVITNEFKEMLHE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 354 HkvqsslggrvrlmvtgaapvsatvltflraalGCQFYEGYGQTEC-TAGCCLTMPGDWTAGH--VGAPMPCNLIKLVDv 430
Cdd:cd17656 270 H--------------------------------NVHLHNHYGPSEThVVTTYTINPEAEIPELppIGKPISNTWIYILD- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 431 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 504
Cdd:cd17656 317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI-RGYRI 395
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1832483362 505 APEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVVPDVE 542
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
200-510 |
4.93e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.25 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 200 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkaTENTVNPCPDDTLISFLPLAH-MfervvecvmlchgAKIG 278
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI---SHDGLKVRPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 279 FFQGDI--RLLMDDLKVLQptvFPVVPRLLNRMFDR---------IFG------------QANTTLKRW----------- 324
Cdd:PRK09192 236 FLLTPVatQLSVDYLPTRD---FARRPLQWLDLISRnrgtisyspPFGyelcarrvnskdLAELDLSCWrvagigadmir 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 325 ---LLDFASKRKEA-----------------------ELRSGIIRNNSLWDRLIFHKVQSSLGGRVRlmvtgaaPVSATV 378
Cdd:PRK09192 313 pdvLHQFAEAFAPAgfddkafmpsyglaeatlavsfsPLGSGIVVEEVDRDRLEYQGKAVAPGAETR-------RVRTFV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 379 LtflraalgcqfyegygqtectagcCltmpgdwtaghvGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKD 458
Cdd:PRK09192 386 N------------------------C------------GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRD 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1832483362 459 PAkTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 510
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 ... |
201-544 |
5.45e-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: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 201 PAPEDLAVICFTSGTTGNPKGAMVTHR----NIVSDCSAFvkatentvNPCPDDTLIsFLPLAHMFERVVECVM-LCHGA 275
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKcilpNIQHFRSLF--------NITSEDILF-LTSPLTFDPSVVEIFLsLSSGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 276 KIgffqgdirllmddlkVLQPTVFPVVPRLLNRMFDRIFG----QANTTLKRwllDFASKRKEAELRSGIirnnslwdrl 351
Cdd:cd17654 186 TL---------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT---------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 352 ifhkvqSSLggRVrLMVTGAAPVSATVLTFLRAA-LGCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVD 429
Cdd:cd17654 238 ------SSL--RV-LALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAyKVPEEDSPVQLGSPLLGTVIEVRD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 VEemnymAAEGEGEVCVKGPNVfQGYLKDPAKTAEALdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 509
Cdd:cd17654 309 QN-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLI 376
|
330 340 350
....*....|....*....|....*....|....*
gi 1832483362 510 ENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETL 544
Cdd:cd17654 377 QQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSR 411
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
209-540 |
4.95e-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: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 209 ICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAH-MFERVVECVMLCHGAKIGFFQGDIRLL 287
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 288 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkEAELRSGIIRnnslwdrlifHKVQSSLGGrvrlm 367
Cdd:cd17633 81 IRKINQYNATVIYLVPTML---------------------------QALARTLEPE----------SKIKSIFSS----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 368 vtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCnliklVDVEEMNymAAEGE-GEVCV 446
Cdd:cd17633 119 --GQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRN--ADGGEiGKIFV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 447 KGPNVFQGYLKdpaktAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 526
Cdd:cd17633 190 KSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
330
....*....|....*..
gi 1832483362 527 ESLQAF---LIAIVVPD 540
Cdd:cd17633 264 IPDARFgeiAVALYSGD 280
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
204-535 |
5.06e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 204 EDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFF- 280
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 281 ---QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlLDFASKRKEAELRsgiirnnslwDRLIFHKVQ 357
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELR----------NRVLQRLPQ 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 358 SSLGGRvrlmvtgaapvsatvltflraalgcqfyegYGQTE----CTAGCCLTMPGDWTAghVGAPMPCNLIKLVDvEEM 433
Cdd:PRK05691 1415 VQLHNR------------------------------YGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD-AEL 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 434 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 506
Cdd:PRK05691 1462 NLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEP 1540
|
330 340 350
....*....|....*....|....*....|.
gi 1832483362 507 EKIENIYMRSEPVAQ--VFVHGESLQAFLIA 535
Cdd:PRK05691 1541 EEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
179-260 |
7.18e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.33 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 179 VEVTSMkameDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC----SAFVKATENTvnPCPDDTLIS 254
Cdd:PRK05850 139 IEVDLL----DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVS 212
|
....*.
gi 1832483362 255 FLPLAH 260
Cdd:PRK05850 213 WLPFYH 218
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
197-590 |
1.15e-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: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 197 KPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPddTLISFLPLAHmfervveCVMLCHGA 275
Cdd:cd05915 145 ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH-------VNAWCLPY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 276 KIGFFQGDIRLLMDdlkVLQPTVfpvvprllnrMFDRIFGQANTTL--KRWLLDFASKRKEAelrsgiirnnslwdrlif 353
Cdd:cd05915 216 AATLVGAKQVLPGP---RLDPAS----------LVELFDGEGVTFTagVPTVWLALADYLES------------------ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 354 hkVQSSLGGRVRLMVTGAAPvsATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPgDWT------AGHVGAPMPCN-L 424
Cdd:cd05915 265 --TGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspVVVQNFVKS-HLEslseeeKLTLKAKTGLPiP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 425 IKLVDVEEMNYMAAEGEGE----VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 500
Cdd:cd05915 340 LVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG- 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 501 GEYIAPEKIENIYMRSEPVAQVFVHGEslqafliaivvPDV---ETLCSWAQKRGFEGSFEEL---CRNKDVKKAILEDM 574
Cdd:cd05915 419 GEWISSVDLENALMGHPKVKEAAVVAI-----------PHPkwqERPLAVVVPRGEKPTPEELnehLLKAGFAKWQLPDA 487
|
410
....*....|....*.
gi 1832483362 575 VRLGKDSGLKPFEQVK 590
Cdd:cd05915 488 YVFAEEIPRTSAGKFL 503
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
50-542 |
2.03e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 53.86 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 50 PDQPY-------EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPE-----WVIIEQGcfaysmvivpLYDTl 117
Cdd:PRK13390 11 PDRPAvivaetgEQVSYRQLDDDSAALARVLYDAGLR--TGDVVALLSDNSPEalvvlWAALRSG----------LYIT- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 118 gneAITYIVNKAELSLVFVDKPEK---AKLLLEGVENKLIPGLKIIVvmdAYGSELVERGQrcgVEVTsmkamedLGRAN 194
Cdd:PRK13390 78 ---AINHHLTAPEADYIVGDSGARvlvASAALDGLAAKVGADLPLRL---SFGGEIDGFGS---FEAA-------LAGAG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 195 RRKPKPPAPedlAVICFTSGTTGNPKGAM--VTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFE-RVVECVML 271
Cdd:PRK13390 142 PRLTEQPCG---AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 272 CHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskRKEAELRSGiirnnslwdrl 351
Cdd:PRK13390 219 LGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRTR----------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 352 ifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNLiKLVD 429
Cdd:PRK13390 267 --YDVSS-----LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDL-HICD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 430 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 507
Cdd:PRK13390 338 -DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQ 415
|
490 500 510
....*....|....*....|....*....|....*
gi 1832483362 508 KIENIYMRSEPVAQVFVHGeslqafliaivVPDVE 542
Cdd:PRK13390 416 ETENALTMHPAVHDVAVIG-----------VPDPE 439
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
201-526 |
4.46e-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: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 201 PAPEDLAVICfTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDD---------TLISFLPLAHmfervvecvmL 271
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFR--MLMGGADFGTGEFTPSEdahkaaaaaAGTVMFPAPP----------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 272 CHGAK-----IGFFQGDiRLLMDDLKVLQPTVFPVVPR-LLNRMFdrIFGQAnttLKRWLLDfaskrkeaELRSGiiRNN 345
Cdd:cd05924 68 MHGTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 346 SLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLT-FLRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMPcn 423
Cdd:cd05924 132 DL----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 424 LIKLVDvEEMNYM--AAEGEGEVCVKGpNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKL 498
Cdd:cd05924 196 DTVVLD-DDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINT 273
|
330 340
....*....|....*....|....*....
gi 1832483362 499 AqGEYIAPEKIENIyMRSEP-VAQVFVHG 526
Cdd:cd05924 274 G-GEKVFPEEVEEA-LKSHPaVYDVLVVG 300
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
49-226 |
5.51e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.59 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 49 KPDQPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIgiFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNK 128
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 129 AElSLVFVDKPEkaklLLEGVENKLIPGLKIIVVMDAYGSELvergqrcGVEVTSMKAMEDlgrANRRKPKPP-APEDLA 207
Cdd:PRK04319 144 SE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDVEEG-------PGTLDFNALMEQ---ASDEFDIEWtDREDGA 208
|
170 180
....*....|....*....|....*
gi 1832483362 208 VICFTSGTTGNPKG------AMVTH 226
Cdd:PRK04319 209 ILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
190-525 |
6.24e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 52.74 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 190 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIV------------SDCSAFVKATentvnPCPDDtlIS--- 254
Cdd:PRK10252 584 LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllwmqnhyplTADDVVLQKT-----PCSFD--VSvwe 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 255 -FLPlahmfervvecvMLChGAKIGFFQGD-------IRLLMDDLKVlqpTVFPVVPRLL----NRMFDRIFGQANTTLK 322
Cdd:PRK10252 657 fFWP------------FIA-GAKLVMAEPEahrdplaMQQFFAEYGV---TTTHFVPSMLaafvASLTPEGARQSCASLR 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 323 RWlldFASKRK-EAELRsgiirnnSLWDRLIfhkvqsslggrvrlmvtgAAPVsatvltflraalgcqfYEGYGQTECT- 400
Cdd:PRK10252 721 QV---FCSGEAlPADLC-------REWQQLT------------------GAPL----------------HNLYGPTEAAv 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 401 ------AGccltmpGDWTAGHVGAPMPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDK 468
Cdd:PRK10252 757 dvswypAF------GEELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIA 829
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832483362 469 DGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVH 525
Cdd:PRK10252 830 DPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
57-226 |
9.57e-07 |
|
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: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKTApDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 136
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKG-DR-VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 137 -------DKP-------EKAKLLLEGVEnklipglKIIVVmdaygselvergQRCGVEVTSMKAmEDLGRANRRKPKPPA 202
Cdd:cd05968 170 adgftrrGREvnlkeeaDKACAQCPTVE-------KVVVV------------RHLGNDFTPAKG-RDLSYDEEKETAGDG 229
|
170 180
....*....|....*....|....*....
gi 1832483362 203 -----PEDLAVICFTSGTTGNPKGAMVTH 226
Cdd:cd05968 230 aerteSEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
57-260 |
1.07e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.80 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGcFAYSMVIVPLYDT-LGNEAITYIVNKAELSLVF 135
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVG--KGDVVALLMENRPEYLAAWLG-LAKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 136 VDkPEKAKLLlEGVENKLIPGLKIIVVMDAYGSELVergqrcgvevtsmkAMEDLGRANRRKPKPPAP-------EDLAV 208
Cdd:PRK08279 140 VG-EELVEAF-EEARADLARPPRLWVAGGDTLDDPE--------------GYEDLAAAAAGAPTTNPAsrsgvtaKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1832483362 209 ICFTSGTTGNPKGAMVTHRNIVSDCSAFVkateNTVNPCPDDTLISFLPLAH 260
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFG----GLLRLTPDDVLYCCLPLYH 251
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
182-537 |
2.10e-06 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 50.80 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 182 TSMKAMEDLGRANRRKP---KPPAPEDLAVICFTSGTTGNPKGAMvtHRNivSDCSAFVKAT-ENTVNPCPDDtlisflp 257
Cdd:PRK06060 120 RVAEAAELMSEAARVAPggyEPMGGDALAYATYTSGTTGPPKAAI--HRH--ADPLTFVDAMcRKALRLTPED------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 258 lahmfervvecVMLChGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPrllnrmfdrIFGQANTTLkrwlldfaSKRKEAEL 337
Cdd:PRK06060 189 -----------TGLC-SARMYFAYGLGNSVWFPLATGGSAVINSAP---------VTPEAAAIL--------SARFGPSV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 338 RSGIirnNSLWDRLIFHKVQSSLGGrVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHV 416
Cdd:PRK06060 240 LYGV---PNFFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWRLGTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 417 GAPMPCNLIKLVdVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTaeaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIf 496
Cdd:PRK06060 316 GRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDT- 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1832483362 497 KLAQGEYIAPEKIENIYMRSEPVAQVFVHG-------ESLQAFLIAIV 537
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
202-535 |
2.40e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 202 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV--------KATENTVNPCPDDTLISFLPlAHMFERVVECV--ML 271
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVpylalseaDVIAQTASQSFDISVWQFLA-APLFGARVEIVpnAI 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 272 CHgakigffqgDIRLLMDDLKVLQPTVFPVVPRLLNRMF--DRifgQANTTLkRWLLDfaskrkeaelrsgiirnnslwd 349
Cdd:PRK05691 3946 AH---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLP---------------------- 3990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 350 rlifhkvqsslggrvrlmvTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGH---VGAPMPCNLI 425
Cdd:PRK05691 3991 -------------------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfRVDLASTRGSylpIGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 426 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHIFKL 498
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1832483362 499 aQGEYIAPEKIENIYMRSEPV------AQVFVHGESLQAFLIA 535
Cdd:PRK05691 4131 -RGYRIELGEIEARLHEQAEVreaavaVQEGVNGKHLVGYLVP 4172
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
57-551 |
3.22e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 57 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAITYIVNKAELS 132
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERG--VGPDVLVGVAMERSIEMVVallaILKAGGAY----VPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 133 LVFVDKPEKAKL-LLEGVENklipglkiiVVMDAYGSELveRGQRCGVEVTSMkamedlgranrrkpkppAPEDLAVICF 211
Cdd:PRK12316 611 LLLSQSHLGRKLpLAAGVQV---------LDLDRPAAWL--EGYSEENPGTEL-----------------NPENLAYVIY 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 212 TSGTTGNPKGAMVTHRNIVSDCSAFVKATEntvnpcpddtlisfLPLAhmfERVVECVMLCHGAKIGFFQGDirlLMDDL 291
Cdd:PRK12316 663 TSGSTGKPKGAGNRHRALSNRLCWMQQAYG--------------LGVG---DTVLQKTPFSFDVSVWEFFWP---LMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 292 KVLqptvfpVVPRLLNRMFDRIFGQANTTLKRwLLDFASKRKEAELRSGiirnnslwdrlifhKVQSSLGgrVRLMVTGA 371
Cdd:PRK12316 723 RLV------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE--------------DVASCTS--LRRIVCSG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 372 APVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCltmpgDWTAGH-------VGAPMPCNLIKLVDVeEMNYMAAEGEGE 443
Cdd:PRK12316 780 EALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVT-----HWTCVEeggdsvpIGRPIANLACYILDA-NLEPVPVGVLGE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 444 VCVKGPNVFQGYLKDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSE 517
Cdd:PRK12316 854 LYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHP 932
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1832483362 518 PVAQVFVHGESLQAfLIAIVVPD------VETLCSWAQKR 551
Cdd:PRK12316 933 WVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
169-261 |
6.86e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.21 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 169 ELVERGQRCGV--EVTSMKAMEDLGRANRRKPKPPAPEDL---------AVICFTSGTTGNPKGAMVTHRNIVSdCSAFV 237
Cdd:cd05938 98 ALRADGVSVWYlsHTSNTEGVISLLDKVDAASDEPVPASLrahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGFL 176
|
90 100
....*....|....*....|....
gi 1832483362 238 KATentvNPCPDDTLISFLPLAHM 261
Cdd:cd05938 177 SLC----GVTADDVIYITLPLYHS 196
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
203-530 |
5.96e-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: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkatENTVNPCPDDTLISFLPLAH---MFERVVECVMlcHGAKIGF 279
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLL----SHDLNLKNGDRTYTCMPLYHgtaAFLGACNCLM--SGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 280 ---FQgdIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfaskrkeaelrSGIIrnnSLWDRLifHKV 356
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLL------------STPP---SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 357 QSSLGGRVRLMVTGAapvsatvltfLRAALGC-QFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVE---- 431
Cdd:cd05937 205 RVAWGNGLRPDIWER----------FRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 432 -----EMNYM---------AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEALDK------DGWLHTGDIGKWLPNGTL 486
Cdd:cd05937 275 mdpetDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1832483362 487 KIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHGESLQ 530
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
441-526 |
7.48e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 441 EGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 520
Cdd:PRK07638 333 IGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVD 410
|
....*.
gi 1832483362 521 QVFVHG 526
Cdd:PRK07638 411 EIVVIG 416
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
197-540 |
8.67e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 197 KPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATENTVNPcPDDTLISfLPLAHmfervvecvmlchgak 276
Cdd:PRK07824 28 RVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTA--SA--DATHDRLGG-PGQWLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 277 IGFFQGDIRLLM---DDLKVLQPTVF--PVVPRLLNRM-FDRIF-GQANTTLKRWLLDFASKRKEAELRSGIIrnnslwd 349
Cdd:PRK07824 86 IAGLQVLVRSVIagsEPVELDVSAGFdpTALPRAVAELgGGRRYtSLVPMQLAKALDDPAATAALAELDAVLV------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 350 rlifhkvqsslggrvrlmvtGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLtmpgdwtagHVGAPMPCNLIKLV 428
Cdd:PRK07824 159 --------------------GGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 429 DveemnymaaegeGEVCVKGPNVFQGY--LKDPAKTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAP 506
Cdd:PRK07824 207 D------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLP 268
|
330 340 350
....*....|....*....|....*....|....*..
gi 1832483362 507 EKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 540
Cdd:PRK07824 269 QVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGD 305
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
203-498 |
8.25e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 203 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDtlisflplahmfervveCVMlcHGAKIGFFQG 282
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE----RFGMRADD-----------------CEL--HFYSINFDAA 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 283 DIRLLmddlkvlqptvfpvVPRLLN-RMFDRIFGQanttlkrWlldfaskrkEAELRSGIIRNNSLwDRLIFHKVQSS-- 359
Cdd:PRK05691 2389 SERLL--------------VPLLCGaRVVLRAQGQ-------W---------GAEEICQLIREQQV-SILGFTPSYGSql 2437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 360 ---LGGR-----VRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTE-------CTAGccLTMPGDWTAGHVGAPMPCN 423
Cdd:PRK05691 2438 aqwLAGQgeqlpVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGAR 2515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832483362 424 LIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIF 496
Cdd:PRK05691 2516 VAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQV 2594
|
..
gi 1832483362 497 KL 498
Cdd:PRK05691 2595 KI 2596
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
195-226 |
1.54e-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: 1.54e-03
10 20 30
....*....|....*....|....*....|..
gi 1832483362 195 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTH 226
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT 254
|
|
| |
