|
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 ... |
117-695 |
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: 965.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 117 QPYEWLSYKQVEDMSECVGSALIHKGFKAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGEL 196
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 197 SLVFVDKpekanlllegvenklipglktiilmdsygidllergkkcGVEIMSMKALEDLGRANRRKPKPPAPEDLAVICF 276
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 277 TSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFSPSSDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 356
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 357 KALQPTIFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDKLIFHKIQSSLGGKVRLMVT 434
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 435 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAA--KGEGEVCVK 512
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 513 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGE 592
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 593 SLQAFLIAIVVPDVETLGHWA-QKRGFVGSFEELCRNKDVKKAILEDMLRLGRDAGLKSFEQVRGISLHPELFSIDNGLL 671
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 309243088 672 TPTMKAKRPELRNYFRSQIDELYS 695
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
87-695 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 710.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 87 YDDVRTLYEGFQRGIRVSNNGPCLGSR-KPDQ---PYEWLSYKQVEDMSECVGSALIHKGFKagPENFVGIFAQNRPEWV 162
Cdd:PLN02736 40 HPEIGTLHDNFVYAVETFRDYKYLGTRiRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 163 IIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVdKPEKANLLLEGVENklIPGLKTIILMDSYGIDLLERGKKC 242
Cdd:PLN02736 118 IVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 243 GVEIMSMKALEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDktFSPSsdDTLISFLP 322
Cdd:PLN02736 195 GVEIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTK--FYPS--DVHISYLP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 323 LAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKALQPTIFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEA 400
Cdd:PLN02736 271 LAHIYERVNQIVMLHYGVAVGFYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 401 ELRSGiiRNNS-LWDKLIFHKIQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAG 479
Cdd:PLN02736 351 ALENG--KNPSpMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSG 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 480 HVGAPMPCSLIKLVDVEEMNYLAAKG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 556
Cdd:PLN02736 429 HVGSPNPACEVKLVDVPEMNYTSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 557 KKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPDVETLGHWAQKRGF-VGSFEELCRNKDVKKAI 635
Cdd:PLN02736 509 KKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIkYEDLKQLCNDPRVRAAV 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 636 LEDMLRLGRDAGLKSFEQVRGISLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYS 695
Cdd:PLN02736 589 LADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYA 648
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
87-695 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 546.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 87 YDDVRTLYEGFQRGIRVSNNGPCLgSRKPDQPYEWLSYKQVEDMSECVGSALIHKGFKAGpENfVGIFAQNRPEWVIIEQ 166
Cdd:COG1022 7 VPPADTLPDLLRRRAARFPDRVAL-REKEDGIWQSLTWAEFAERVRALAAGLLALGVKPG-DR-VAILSDNRPEWVIADL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 167 GCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVDKPEKANLLLEGVENklIPGLKTIILMDsygidllERGKKCGVEI 246
Cdd:COG1022 84 AILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 247 MSMKALEDLGRANR------RKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVtdktFSPSSDDTLISF 320
Cdd:COG1022 155 LSLDELLALGREVAdpaeleARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 321 LPLAHMFERVVECVMLCHGAKIGFfQGDIRLLMDDLKALQPTIFPVVPRLLNRMFDRIFGQAN--TTLKRWLLDFA---S 395
Cdd:COG1022 231 LPLAHVFERTVSYYALAAGATVAF-AESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 396 KRKEAELRSGiiRNNSLW--------DKLIFHKIQSSLGGKVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAG 467
Cdd:COG1022 310 RRYARARLAG--KSPSLLlrlkhalaDKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 468 CSLTVPGDWTAGHVGAPMPCSLIKLVDveemnylaakgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 547
Cdd:COG1022 387 ITVNRPGDNRIGTVGPPLPGVEVKIAE-----------DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDE 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 548 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESlQAFLIAIVVPDVETLGHWAQKRG-FVGSFEELC 626
Cdd:COG1022 456 DGFLRITGRKKDLIVTSGGKNVAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGlPYTSYAELA 534
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309243088 627 RNKDVKKAILEDMLRLgrDAGLKSFEQVRGISLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYS 695
Cdd:COG1022 535 QDPEVRALIQEEVDRA--NAGLSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
117-682 |
1.59e-170 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 495.96 E-value: 1.59e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 117 QPYEWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGEL 196
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPG--DRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 197 SLVFVDKPEkanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppapeDLAVICF 276
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 277 TSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMFERV-VECVMLCHGAKIGFFQgDIRLLMDD 355
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAERLPAT----EGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 356 LKALQPTIFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdklifhkiqsslGGKVRLMVTG 435
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 436 AAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDveemnylaakgEGEVCVKGPN 515
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 516 VFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESlQ 595
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 596 AFLIAIVVPDVETLGHWAQKRG-FVGSFEELCRNKDVKKAILEDMLRLGrdAGLKSFEQVRGISLHPELFSIDNGLLTPT 674
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAAN--ARLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 309243088 675 MKAKRPEL 682
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
118-679 |
6.37e-162 |
|
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: 475.94 E-value: 6.37e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 118 PYEWLSYKQVEDMSECVGSALIHKGFKagPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELS 197
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 198 LVFVDkpekanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkpPAPEDLAVICFT 277
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 278 SGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfsPSSDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD--- 354
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPEL--LGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 355 -----DLKALQPTIFPVVPRLLNRMFDRIFGQANT--TLKRWLLDFASKRKEAELRSGIirNNSLWDKLIFHKIQSSLGG 427
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 428 KVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGE- 506
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYSTDKPPp 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 507 -GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVA 585
Cdd:cd17639 330 rGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 586 QVFVHGESLQAFLIAIVVPDVETLGHWAQKRGFVGS-FEELCRNKDVKKAILEDMLRLGRDAGLKSFEQVRGISLHPELF 664
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVINSeWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 309243088 665 SIDNGLLTPTMKAKR 679
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
78-699 |
5.10e-160 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 476.64 E-value: 5.10e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 78 DSDEPLAYFYDDVRTLYEGFQRGIRVSNNGPClgsrkpdQPYEWLSYKQVEDMSECVGSALIHKGFKagPENFVGIFAQN 157
Cdd:PLN02861 41 DIDSPWQFFSDAVKKYPNNQMLGRRQVTDSKV-------GPYVWLTYKEVYDAAIRIGSAIRSRGVN--PGDRCGIYGSN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 158 RPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVDKPEKANLLleGVENKLIPGLKTIILMDSYGIDLLE 237
Cdd:PLN02861 112 CPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 238 RGKKCGVEIMSMKALEDLGRANRRKPkPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSA---FVKVTDKtfSPSSD 314
Cdd:PLN02861 190 EAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYTSGTTGEPKGVILTNRAIIAEVLStdhLLKVTDR--VATEE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 315 DTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKALQPTIFPVVPRLlnrmFDRIFG------QANTTLKR 388
Cdd:PLN02861 267 DSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDVQALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 389 WLLDFASKRKEAELRSGIIRNNS--LWDKLIFHKIQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTA 466
Cdd:PLN02861 343 KLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 467 GCSLTVPGDWT-AGHVGAPMPCSLIKLVDVEEMNY--LAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIG 543
Cdd:PLN02861 423 GCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYdaLSDVPRGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 544 KWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPDVETLGHWAQKRGFVGSFE 623
Cdd:PLN02861 502 EWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFK 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309243088 624 ELCRNKDVKKAILEDMLRLGRDAGLKSFEQVRGISLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYSTVKV 699
Cdd:PLN02861 582 SLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
88-698 |
8.94e-157 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 468.73 E-value: 8.94e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 88 DDVRTLYEGFQRGIRVSNNGPCLGSR-----KPDQpYEWLSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWV 162
Cdd:PLN02614 42 EGMDSCWDVFRMSVEKYPNNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKDEAK--CGIYGANSPEWI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 163 IIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVDKPEKANLLlegvenKLIPG----LKTIILMDSYGIDLLER 238
Cdd:PLN02614 119 ISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELF------KTCPNsteyMKTVVSFGGVSREQKEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 239 GKKCGVEIMSMKALEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVK-VTDKTFSPSSDDTL 317
Cdd:PLN02614 193 AETFGLVIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRlLKSANAALTVKDVY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 318 ISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKALQPTIFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFAS 395
Cdd:PLN02614 273 LSYLPLAHIFDRVIEECFIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAF 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 396 KRKEAELRSGI--IRNNSLWDKLIFHKIQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVP 473
Cdd:PLN02614 353 SYKFGNMKKGQshVEASPLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 474 GDW-TAGHVGAPMPCSLIKLVDVEEMNY--LAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGT 550
Cdd:PLN02614 433 DELdMLGTVGPPVPNVDIRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGS 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 551 LKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPDVETLGHWAQKRGFVGSFEELCRNKD 630
Cdd:PLN02614 512 MKIIDRKKNIFKLSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEK 591
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309243088 631 VKKAILEDMLRLGRDAGLKSFEQVRGISLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYSTVK 698
Cdd:PLN02614 592 AKEFILGELVKMAKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
118-697 |
8.39e-154 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 460.82 E-value: 8.39e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 118 PYEWLSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELS 197
Cdd:PLN02430 73 PYMWKTYKEVYEEVLQIGSALRASG--AEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEID 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 198 LVFV-DKpeKANLLLEGvENKLIPGLKTIILMDSYGIDLLERGKKCGVEIMSMKALEDLGRANRRKPKPPAPEDLAVICF 276
Cdd:PLN02430 151 FVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 277 TSGTTGNPKGAMITHRNVvsdcSAFVKVTD---KTFSP--SSDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRL 351
Cdd:PLN02430 228 TSGTSGDPKGVVLTHEAV----ATFVRGVDlfmEQFEDkmTHDDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 352 LMDDLKALQPTIFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNS--LWDKLIFHKIQSSLGG 427
Cdd:PLN02430 304 LRDDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 428 KVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTA-GHVGAPMPCSLIKLVDVEEMNY--LAAK 504
Cdd:PLN02430 384 RLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEP 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 505 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPV 584
Cdd:PLN02430 464 PRGEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIV 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 585 AQVFVHGESLQAFLIAIVVPDVETLGHWAQKRGFVGSFEELCRNKDVKKAILEDMLRLGRDAGLKSFEQVRGISLHPELF 664
Cdd:PLN02430 543 EDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPF 622
|
570 580 590
....*....|....*....|....*....|...
gi 309243088 665 SIDNGLLTPTMKAKRPELRNYFRSQIDELYSTV 697
Cdd:PLN02430 623 DVERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
63-695 |
8.03e-137 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 417.98 E-value: 8.03e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 63 VEVAGSDG-ARRSAilDSDEPLAYFYDDVRTLYEGFQRGIRVSNNGPCLGSRK---------PDQ---------PYEWLS 123
Cdd:PLN02387 31 VDVGGEPGyAIRNA--RFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTRKlisrefetsSDGrkfeklhlgEYEWIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 124 YKQVEDMSECVGSALIHKGFKAgpENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVDK 203
Cdd:PLN02387 109 YGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 204 PEKANLLleGVENKLiPGLKTIILMDSYGIDLLERGKK-CGVEIMSMKALEDLGRANRRKPKPPAPEDLAVICFTSGTTG 282
Cdd:PLN02387 187 KQLKKLI--DISSQL-ETVKRVIYMDDEGVDSDSSLSGsSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 283 NPKGAMITHRNVVSDCSAFVKVTDKTfspSSDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD-------- 354
Cdd:PLN02387 264 LPKGVMMTHGNIVATVAGVMTVVPKL---GKNDVYLAYLPLAHILELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkg 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 355 ---DLKALQPTIFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKEAELR------SGIIRnnSLWDKLIFHKIQS 423
Cdd:PLN02387 339 tkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDIAYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRA 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 424 SLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAA 503
Cdd:PLN02387 417 VLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLIS 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 504 KG---EGEVCVKGPNVFQGYLKDPAKTAEA--LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIEN 576
Cdd:PLN02387 497 DKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTGDIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEA 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 577 IYLRSEPVAQVFVHGESLQAFLIAIVVPDVETLGHWAQKRGF-VGSFEELCRNKDVKKAILEDMLRLGRDAGLKSFEQVR 655
Cdd:PLN02387 577 ALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIdYSNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPA 656
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 309243088 656 GISLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELYS 695
Cdd:PLN02387 657 KIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
113-564 |
2.39e-129 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 388.98 E-value: 2.39e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 113 RKPDQP------YEWLSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEA 186
Cdd:pfam00501 7 RTPDKTalevgeGRRLTYRELDERANRLAAGLRALG--VGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 187 ITYIINKGELSLVFVDKPEKANLLLEGVENKLIPGLKTIILMDSygidllergkkcGVEIMSMKALEDLGRANRRKPKPP 266
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDP------------VLKEEPLPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFSPSSDDTLISFLPLAHMFERVVEC-VMLCHGAKIGFF 345
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 QGDIRL----LMDDLKALQPTIFPVVPRLLNRMFDrifgqanttlkrwlldfaSKRKEAELRSGiirnnslwdklifhki 421
Cdd:pfam00501 233 PGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------------------AGAPKRALLSS---------------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 422 qsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDW---TAGHVGAPMPCSLIKLVDVEEM 498
Cdd:pfam00501 279 -------LRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETG 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309243088 499 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
61-694 |
9.60e-104 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 331.94 E-value: 9.60e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 61 QSVEVAGSDGARRSAIldsdeplayfYDDVRTLYEGFQRGIRVSNNGPCLGSR-------KPDQP---Y----------- 119
Cdd:PTZ00216 32 QNVPVPGTETENASAI----------YRIAGVTDEEHERLRNEWYYGPNFLQRlerickeRGDRRalaYrpvervekevv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 120 --------EW----------LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDT 181
Cdd:PTZ00216 102 kdadgkerTMevthfnetryITYAELWERIVNFGRGLAELGLTKG--SNVAIYEETRWEWLASIYGIWSQSMVAATVYAN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 182 LGTEAITYIINKGELSLVfVDKPEKANLLLEGVENKLIPGLkTIILMDSYGIDLlergKKCGVEIMSMKALEDLGRANRR 261
Cdd:PTZ00216 180 LGEDALAYALRETECKAI-VCNGKNVPNLLRLMKSGGMPNT-TIIYLDSLPASV----DTEGCRLVAWTDVVAKGHSAGS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 262 KPKPPAPE---DLAVICFTSGTTGNPKGAMITHRNVVSDCSAFV-KVTDKTFSPSSDDTLISFLPLAHMFERVVECVMLC 337
Cdd:PTZ00216 254 HHPLNIPEnndDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEdRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 338 HGAKIGFfqGDIRLLMD-------DLKALQPTIFPVVPRLlnrmFDRI----------FGqantTLKRWLLDFASKRKEA 400
Cdd:PTZ00216 334 RGALIGF--GSPRTLTDtfarphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 401 ELRSGiiRNNSLWDKLIFHKIQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCqFYEGYGQTEcTAGC-SLTVPGDWTAG 479
Cdd:PTZ00216 404 ALKEG--KDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTE-TVCCgGIQRTGDLEPN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 480 HVGAPMPCSLIKLVDVEEMNYlAAKGE--GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 557
Cdd:PTZ00216 480 AVGQLLKGVEMKLLDTEEYKH-TDTPEprGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 558 KHIFKLAQGEYIAPEKIENIYLRSEPVAQ----VFVHgeSLQAFLIAIVVPDVETLGHWAQKRGFVGSFEELCRNKDVKK 633
Cdd:PTZ00216 559 KALAKNCLGEYIALEALEALYGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQK 636
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 309243088 634 AILEDMLRLGRDAGLKSFEQVRGISLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELY 694
Cdd:PTZ00216 637 KATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
117-680 |
8.94e-95 |
|
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: 301.20 E-value: 8.94e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 117 QPYEWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGEL 196
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVKAG--EKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 197 SLVFVdkpekanlllegvENklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppAPEDLAVICF 276
Cdd:cd17640 79 VALVV-------------EN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 277 TSGTTGNPKGAMITHRNVVSDCSAFVKVtdktFSPSSDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMDDL 356
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSDI----VPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 357 KALQPTIFPVVPRLlnrmfdrifgqanttlkrWlldfaskrkEAeLRSGI---IRNNSLWDKLIFHKIQSslGGKVRLMV 433
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 434 TGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKG 513
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 514 PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGES 593
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 594 lQAFLIAIVVPDVETLGHWAQKRG--FVGSFEELCRNKDVKKAI-LEDMLRLGRDAGLKSFEQVRGISLHPELFsIDNGL 670
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGE 456
|
570
....*....|
gi 309243088 671 LTPTMKAKRP 680
Cdd:cd17640 457 MTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
119-679 |
2.05e-81 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 267.41 E-value: 2.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 119 YEWLSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSL 198
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSK--IALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 199 VFVDK----PEKANLLLEGVENKLIPGLKTiiLMDSYGIDllergkkcgvEIMSMKALEDlgranrRKPkPPAPEDLAVI 274
Cdd:cd05932 82 LFVGKlddwKAMAPGVPEGLISISLPPPSA--ANCQYQWD----------DLIAQHPPLE------ERP-TRFPEQLATL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 275 CFTSGTTGNPKGAMITHRNVVSDCSAFVKvtdkTFSPSSDDTLISFLPLAHMFERV-VECVMLCHGAKIgFFQGDIRLLM 353
Cdd:cd05932 143 IYTSGTTGQPKGVMLTFGSFAWAAQAGIE----HIGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 354 DDLKALQPTIFPVVPRLLNRMFDRIFgqanttlkrwlldfaSKRKEAELRsgIIRNNSLWDKLIFHKIQSSLG-GKVRLM 432
Cdd:cd05932 218 EDVQRARPTLFFSVPRLWTKFQQGVQ---------------DKIPQQKLN--LLLKIPVVNSLVKRKVLKGLGlDQCRLA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 433 VTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDveemnylaakgEGEVCVK 512
Cdd:cd05932 281 GCGSAPVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 513 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGE 592
Cdd:cd05932 349 SPALMMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGS 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 593 SLQAfLIAIVVPDVEtlGHWAQKRGFVGSFEELCRnkdvkkAILEDMlrlgrDAGLKSFEQVRGISLHPELFSIDNGLLT 672
Cdd:cd05932 429 GLPA-PLALVVLSEE--ARLRADAFARAELEASLR------AHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILT 494
|
....*..
gi 309243088 673 PTMKAKR 679
Cdd:cd05932 495 PTLKIKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
113-616 |
2.97e-75 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 249.34 E-value: 2.97e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 113 RKPDQP-----YEWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAI 187
Cdd:COG0318 11 RHPDRPalvfgGRRLTYAELDARARRLAAALRALGVGPG--DRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 188 TYIINKGELSLVFVdkpekanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppa 267
Cdd:COG0318 89 AYILEDSGARALVT------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 pedlAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKvtdkTFSPSSDDTLISFLPLAHMFERVVECVM-LCHGAKI---- 342
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAA----ALGLTPGDVVLVALPLFHVFGLTVGLLApLLAGATLvllp 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 GFfqgDIRLLMDDLKALQPTIFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELRSgiirnnslwdklifhkiq 422
Cdd:COG0318 175 RF---DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------ 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 423 sslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTA--GHVGAPMPCSLIKLVDvEEMNY 500
Cdd:COG0318 217 ------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 501 LAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLR 580
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAA 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 309243088 581 SEPVAQVFV-------HGESLQAFLI--AIVVPDVETLGHWAQKR 616
Cdd:COG0318 368 HPGVAEAAVvgvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
114-694 |
5.72e-74 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 249.97 E-value: 5.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 114 KPDQPYEWLSYKQVEDMSECVGSALIhkgfKAGPENF--VGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYII 191
Cdd:cd05933 1 KRGDKWHTLTYKEYYEACRQAAKAFL----KLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 192 NKGELSLVFVDKPEKANLLLEgVENKLiPGLKTIIlmdSYGIDLLErgKKCGVeiMSMKALEDLGR-----ANRRKPKPP 266
Cdd:cd05933 77 ETSEANILVVENQKQLQKILQ-IQDKL-PHLKAII---QYKEPLKE--KEPNL--YSWDEFMELGRsipdeQLDAIISSQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFSPSSDDTLISFLPLAHMFERVVEcVMLC--HGAKIGF 344
Cdd:cd05933 148 KPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPikVGGQVYF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 345 FQGDIR--LLMDDLKALQPTIFPVVPRLLNRMFDRI--FGQANTTLKRWLLDFAsKRKEAE-------LRSGIIRNNSLW 413
Cdd:cd05933 227 AQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSPLFYRLA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 414 DKLIFHKIQSSLG-GKVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKL 492
Cdd:cd05933 306 KKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKI 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 493 VDVEemnylaAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 572
Cdd:cd05933 385 HNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPPV 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 573 KIENIYLRSEP-VAQVFVHGESLQaFLIAIVV----PDVET------LGHWAQkrgfvgsfeELCRNKDVKKAILEDMLR 641
Cdd:cd05933 459 PIEDAVKKELPiISNAMLIGDKRK-FLSMLLTlkceVNPETgepldeLTEEAI---------EFCRKLGSQATRVSEIAG 528
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 642 LGRDAGLKSFEQvrGIS-----------------LHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDELY 694
Cdd:cd05933 529 GKDPKVYEAIEE--GIKrvnkkaisnaqkiqkwvILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
123-679 |
6.02e-74 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 249.26 E-value: 6.02e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 123 SYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIE---QGCFAYSMvvvPLYDTLGTEAITYIINKGELSLV 199
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRG--DVVAILGDNRPEWVWAElaaQAIGALSL---GIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 200 FVDKPEKANLLLEGVENklIPGLKTIILMDSYGIDLLERGKkcgveIMSMKALEDLGRA-NRRKPK-------PPAPEDL 271
Cdd:cd17641 88 IAEDEEQVDKLLEIADR--IPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 272 AVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKtfspSSDDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQgDIR 350
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPL----GPGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 351 LLMDDLKALQPTIFPVVPRLLNRM--FDRIFGQANTTLKRWLLDF--------ASKRKEAELRSGIIRNNS-LWDKLIFH 419
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 420 KIQSSLG-GKVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVeem 498
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 499 nylaakgeGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENiY 578
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIEN-K 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 579 LRSEPV---AQVFVHGeslQAFLIAIVVPDVETLGHWAQKRGFV-GSFEELCRNKDVKKAILEDMLRLGRDagLKSFEQV 654
Cdd:cd17641 463 LKFSPYiaeAVVLGAG---RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRI 537
|
570 580
....*....|....*....|....*
gi 309243088 655 RGISLHPELFSIDNGLLTPTMKAKR 679
Cdd:cd17641 538 RRFLLLYKELDADDGELTRTRKVRR 562
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
119-672 |
5.74e-68 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 233.89 E-value: 5.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 119 YEWLSYKQVEDMSECVGSALiHKGFKAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSL 198
Cdd:cd17632 65 FETITYAELWERVGAVAAAH-DPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 199 VFVDK---PEKANLLLEGvenkliPGLKTIILMDSYGIDLLER-----------GKKCGVEIMSMKALEDLG-RANRRKP 263
Cdd:cd17632 144 LAVSAehlDLAVEAVLEG------GTPPRLVVFDHRPEVDAHRaalesarerlaAVGIPVTTLTLIAVRGRDlPPAPLFR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 264 KPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFSPSSddtLISFLPLAHMFERVVECVMLCHGAkIG 343
Cdd:cd17632 218 PEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASI---TLNFMPMSHIAGRISLYGTLARGG-TA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 344 FFQG--DIRLLMDDLKALQPTIFPVVPRLLNRMFDRIfgQAntTLKRWLLDFA-----SKRKEAELRsgiirnnslwdkl 416
Cdd:cd17632 294 YFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRY--QA--ELDRRSVAGAdaetlAERVKAELR------------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 417 ifhkiQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCSLTvpgdwtAGHVGAPmPCSLIKLVDVE 496
Cdd:cd17632 357 -----ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVIL------DGVIVRP-PVLDYKLVDVP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 497 EMNYLAAKG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEK 573
Cdd:cd17632 423 ELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELGPDRLVYVDRRNNVLKLSQGEFVTVAR 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 574 IENIYLRSEPVAQVFVHGESLQAFLIAIVVPDVETLGHWAQKRgfvgsfeelcrnkdVKKAILEDMLRLGRDAGLKSFEQ 653
Cdd:cd17632 503 LEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTAR--------------LRAALAESLQRIAREAGLQSYEI 568
|
570
....*....|....*....
gi 309243088 654 VRGISLHPELFSIDNGLLT 672
Cdd:cd17632 569 PRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
122-679 |
1.61e-66 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 226.55 E-value: 1.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTG--DRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKPEkanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppapeDLAVICFTSGTT 281
Cdd:cd05914 86 SDED----------------------------------------------------------------DVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVSDCsAFVKVTDKTfspSSDDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQGDIRLLMDDLKALQ 360
Cdd:cd05914 102 GNSKGVMLTYRNIVSNV-DGVKEVVLL---GKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALAFAQ 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 361 PTIFPVVPRLLNRMFDRIFGQANTTLKRWLLdfaskrkeaeLRSGIIRNNSLWDKLIFHKIQSSLGGKVRLMVTGAAPVS 440
Cdd:cd05914 178 VTPTLGVPVPLVIEKIFKMDIIPKLTLKKFK----------FKLAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKIN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 441 ATVLTFLRAaLGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPmpcslIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGY 520
Cdd:cd05914 248 PDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNVMKGY 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 521 LKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVA--QVFVHGESLQAfl 598
Cdd:cd05914 322 YKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKLVA-- 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 599 IAIVVPDVEtlghwaqkrgfvgsFEELCRNKDVKKAILEDmLRLGRDAGLKSFEQVRGISLHPELFSidnglLTPTMKAK 678
Cdd:cd05914 400 LAYIDPDFL--------------DVKALKQRNIIDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFE-----KTPKGKIK 459
|
.
gi 309243088 679 R 679
Cdd:cd05914 460 R 460
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
111-616 |
1.02e-65 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 225.55 E-value: 1.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 111 GSRKPDQPY-----EWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIieqGCFAYSM---VVVPLYDTL 182
Cdd:PRK07656 15 ARRFGDKEAyvfgdQRLTYAELNARVRRAAAALAALGIGKG--DRVAIWAPNSPHWVI---AALGALKagaVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 183 GTEAITYIINKGELSLVFVdkpekANLLLeGVENKL---IPGLKTIILMDSygidllERGKKCGVEIMSMKALedLGRAN 259
Cdd:PRK07656 90 TADEAAYILARGDAKALFV-----LGLFL-GVDYSAttrLPALEHVVICET------EEDDPHTEKMKTFTDF--LAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 260 RRKPKPP-APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMF---ERVVECVM 335
Cdd:PRK07656 156 PAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLT----EGDRYLAANPFFHVFgykAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 336 lcHGAKI----GFfqgDIRLLMDDLKALQPTIFPVVPrllnrmfdrifgqantTLKRWLLDFAsKRKEAELRSgiirnns 411
Cdd:PRK07656 232 --RGATIlplpVF---DPDEVFRLIETERITVLPGPP----------------TMYNSLLQHP-DRSAEDLSS------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 412 lwdklifhkiqsslggkVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCSLTVPGD---WTAGHVGAPMPC 487
Cdd:PRK07656 283 -----------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAIAG 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 488 SLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 567
Cdd:PRK07656 346 VENKIVN-ELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IVGGF 423
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309243088 568 YIAPEKIENIYLRSEPVAQVFV-------HGESLQAFliaiVVP------DVETLGHWAQKR 616
Cdd:PRK07656 424 NVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
270-616 |
1.41e-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: 219.85 E-value: 1.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 270 DLAVICFTSGTTGNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQG-D 348
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKfD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 349 IRLLMDDLKALQPTIFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiirnnslwdklifhkiqsslggk 428
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAP-----------------ESAGYDLSS------------------------ 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 429 VRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWT--AGHVGAPMPCSLIKLVDVEEmNYLAAKGE 506
Cdd:cd04433 116 LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPPGEI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 507 GEVCVKGPNVFQGYLKDPAKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQ 586
Cdd:cd04433 195 GELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPGVAE 272
|
330 340 350
....*....|....*....|....*....|....*....
gi 309243088 587 VFVHG---ESLQAFLIAIVVP------DVETLGHWAQKR 616
Cdd:cd04433 273 AAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
122-591 |
1.46e-63 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 219.01 E-value: 1.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKG--DVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKPEKANLLlEGVenKLIPGLKTIILMDSygidlleRGKKCGVEIMSMKALEDLGRANRRKPKPPAPEDLAVICFTSGTT 281
Cdd:cd05911 89 DPDGLEKVK-EAA--KELGPKDKIIVLDD-------KPDGVLSIEDLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVSDCS---AFVKVTDktfspSSDDTLISFLPLAHMFervveCVMLCHGAKIgffQGDIRLLMDD--- 355
Cdd:cd05911 159 GLPKGVCLSHRNLIANLSqvqTFLYGND-----GSNDVILGFLPLYHIY-----GLFTTLASLL---NGATVIIMPKfds 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 356 ---LKALQP---TIFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDKlifHKIQSslggkV 429
Cdd:cd05911 226 elfLDLIEKykiTFLYLVPPIAAALA---------------------------------KSPLLDK---YDLSS-----L 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 430 RLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGE 508
Cdd:cd05911 265 RVILSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 509 VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVF 588
Cdd:cd05911 345 ICVRGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAA 423
|
...
gi 309243088 589 VHG 591
Cdd:cd05911 424 VIG 426
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
113-610 |
3.61e-60 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 209.34 E-value: 3.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 113 RKPDQPY-----EWLSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAI 187
Cdd:cd05936 11 RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQPGDR--VALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 188 TYIINKGelslvfvdkpekanlllegvenklipGLKTIILMDSygidllergkkcgveimsmkaLEDLGRANRRKPKPPA 267
Cdd:cd05936 89 EHILNDS--------------------------GAKALIVAVS---------------------FTDLLAAGAPLGERVA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 --PEDLAVICFTSGTTGNPKGAMITHRNVVSD---CSAFVKVTDktfspSSDDTLISFLPLAHMFERVVECV-MLCHGAK 341
Cdd:cd05936 122 ltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANalqIKAWLEDLL-----EGDDVVLAALPLFHVFGLTVALLlPLALGAT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 IGFFQG-DIRLLMDDLKALQPTIFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiirnnslwdklifhk 420
Cdd:cd05936 197 IVLIPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS---------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 iqsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC---TAGCSLTvpGDWTAGHVGAPMPCSLIKLVDvEE 497
Cdd:cd05936 244 --------LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETspvVAVNPLD--GPRKPGSIGIPLPGTEVKIVD-DD 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 498 MNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 577
Cdd:cd05936 313 GEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEV 390
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 309243088 578 YLRSEPVAQVFV-------HGESLQAFliaIVVPDVETLG 610
Cdd:cd05936 391 LYEHPAVAEAAVvgvpdpySGEAVKAF---VVLKEGASLT 427
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
123-592 |
2.11e-56 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 200.41 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 123 SYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIieqgC-FAYSM---VVVPLYDTLGTEAITYIINKGELSL 198
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKKG--DRVAVFDWNSHEYLE----AyFAVPKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 199 VFVDkPEKANLLlEGVENKLiPGLKTIILMDSYgiDLLERGKKCGveimsmkALEDLgRANRRkPKPPAPE----DLAVI 274
Cdd:PRK06187 107 VLVD-SEFVPLL-AAILPQL-PTVRTVIVEGDG--PAAPLAPEVG-------EYEEL-LAAAS-DTFDFPDidenDAAAM 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 275 CFTSGTTGNPKGAMITHRNVVSD---CSAFVKVTDktfspssDDTLISFLPLAHMFERVVECVMLCHGAKI---GFFqgD 348
Cdd:PRK06187 173 LYTSGTTGHPKGVVLSHRNLFLHslaVCAWLKLSR-------DDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--D 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 349 IRLLMDDLKALQPTIFPVVPRLLNRMFdrifgQANTTLKRWLldfaskrkeaelrsgiirnnslwdklifhkiqSSLggk 428
Cdd:PRK06187 244 PENLLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF--------------------------------SSL--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 429 vRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCSLT----VPGDWT-AGHVGAPMPCSLIKLVDvEEMNYLA 502
Cdd:PRK06187 284 -RLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqLPGQWTkRRSAGRPLPGVEARIVD-DDGDELP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 503 AKGE--GEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLR 580
Cdd:PRK06187 362 PDGGevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYG 439
|
490
....*....|..
gi 309243088 581 SEPVAQVFVHGE 592
Cdd:PRK06187 440 HPAVAEVAVIGV 451
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
122-583 |
2.83e-45 |
|
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: 168.95 E-value: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIeqgCFAYSM--VVVPLYDTLGTEA-ITYIINKGELSL 198
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKG--DVVLLLSPNSIEFPVA---FLAVLSlgAVVTTANPLSTPAeIAKQVKDSGAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 199 VFVDkpekanllLEGVEnKLIPGLKTIILMDSYGIDLLErgkkcgveimSMKALEDLGRANRRKPKPPaPEDLAVICFTS 278
Cdd:cd05904 108 AFTT--------AELAE-KLASLALPVVLLDSAEFDSLS----------FSDLLFEADEAEPPVVVIK-QDDVAALLYSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 279 GTTGNPKGAMITHRNVVSDCSAFVKVTDKTFSPssDDTLISFLPLAHMFERVVECV-MLCHGAKI----GFfqgDIRLLM 353
Cdd:cd05904 168 GTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDS--EDVFLCVLPMFHIYGLSSFALgLLRLGATVvvmpRF---DLEELL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 354 DDLKALQPTIFPVVPRLLNRMfdrifgqanttlkrwlldfaskrkeaeLRSGIIRNNSLwdklifhkiqSSLggkvRLMV 433
Cdd:cd05904 243 AAIERYKVTHLPVVPPIVLAL---------------------------VKSPIVDKYDL----------SSL----RQIM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 434 TGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAP---MPCSLIKLVDVEEMNYLAAKGEGEV 509
Cdd:cd05904 282 SGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTGVVAMCFAPEKDRAKYGSVgrlVPNVEAKIVDPETGESLPPNQTGEL 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309243088 510 CVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIyLRSEP 583
Cdd:cd05904 362 WIRGPSIMKGYLNNPEATAATIDKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL-LLSHP 433
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
112-605 |
4.75e-45 |
|
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: 167.02 E-value: 4.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 112 SRKPDQP-YEW----LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEA 186
Cdd:cd17631 6 RRHPDRTaLVFggrsLTYAELDERVNRLAHALRALGVAKG--DRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 187 ITYIINKGELSLVFvdkpekanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkpp 266
Cdd:cd17631 84 VAYILADSGAKVLF------------------------------------------------------------------ 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 apEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKvtdkTFSPSSDDTLISFLPLAHMFERVVECVM-LCHGAKI--- 342
Cdd:cd17631 98 --DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNALA----ALDLGPDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVvil 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 -GFfqgDIRLLMDDLKALQPTIFPVVPRLLNRMFDRifGQANTTlkrwllDFASkrkeaelrsgiirnnslwdklifhki 421
Cdd:cd17631 172 rKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS-------------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 422 qsslggkVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCSLTVPGDW--TAGHVGAPMPCSLIKLVDvEEMN 499
Cdd:cd17631 215 -------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIVD-PDGR 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 500 YLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYL 579
Cdd:cd17631 286 EVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAEVEDVLY 363
|
490 500 510
....*....|....*....|....*....|...
gi 309243088 580 RSEPVAQVFV-------HGESlqafLIAIVVPD 605
Cdd:cd17631 364 EHPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
270-616 |
4.01e-44 |
|
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: 164.39 E-value: 4.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 270 DLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMFERVV----------ECVMLchg 339
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGLVNallcplfagaSVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 340 akiGFFQGDIRLLMDDLKALqpTIFPVVPRllnrMFDRIFGQANTTLKrwllDFASKRKEAElrsgiirnnslwdklifh 419
Cdd:cd05941 163 ---PKFDPKEVAISRLMPSI--TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA------------------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 420 kiqsslgGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCSLTVP--GDWTAGHVGAPMPCSLIKLVDVEE 497
Cdd:cd05941 212 -------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVDEET 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 498 MNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEKIEN 576
Cdd:cd05941 283 GEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALEIER 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 309243088 577 IYLRSEPVAQVFVHGESLQAF---LIAIVVP-------DVETLGHWAQKR 616
Cdd:cd05941 362 VLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
234-695 |
8.80e-42 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 162.58 E-value: 8.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 234 DLLERGKKCGVEIMSmkaLEDLGRANRR--KPKPPAPEDLAVICFTSGTTGNPKGAMITHRNV------VSDCSAFvkvt 305
Cdd:PTZ00342 270 DLKEKAKKLGISIIL---FDDMTKNKTTnyKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIF---- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 306 dKTFSPssdDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDLKALQPTIFPVVPRLLNRMFDRIFGQAN-- 383
Cdd:PTZ00342 343 -KKYNP---KTHLSYLPISHIYERVIAYLSFMLGGTINIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnl 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 384 TTLKRWLLdfaskRKEAELRSGiiRNNSLWDKL---IFH---KIQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYE 457
Cdd:PTZ00342 419 PPLKRFLV-----KKILSLRKS--NNNGGFSKFlegITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQ 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 458 GYGQTECTAGCSLTVPGDWTAGHVGAPM-PCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW 536
Cdd:PTZ00342 492 GYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKVRTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGY 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 537 LHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAFLIAIVVPD----------- 605
Cdd:PTZ00342 572 FKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETDMLNNLYSQISFINFCVVYGDDSMDGPLAIISVDkyllfkclkdd 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 606 --VETLGhwAQKRGFVGSFEELCRNKDV-KKAILEDMLRLGRDAGLKSFEQVRGISLHPELFSIDNgLLTPTMKAKRPEL 682
Cdd:PTZ00342 652 nmLESTG--INEKNYLEKLTDETINNNIyVDYVKGKMLEVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYV 728
|
490
....*....|....*.
gi 309243088 683 ---RNYFRSQIDELYS 695
Cdd:PTZ00342 729 fkdYAFFIDQVKKIYK 744
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
116-599 |
1.64e-39 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 152.47 E-value: 1.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 116 DQPYEWLSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVI-----IEQGCfaysmVVVPLYDTLGTEAITYI 190
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIKKGDR--VAIALPNGLEFVVaflaaARAGA-----VVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 191 INKGELSLVFVDKPEkanlLLEGVENKLipglktiilmdSYGIDLLERGKKCGVEIMSMKAlEDLG-----RANRRKPKP 265
Cdd:cd05926 82 LADLGSKLVLTPKGE----LGPASRAAS-----------KLGLAILELALDVGVLIRAPSA-ESLSnlladKKNAKSEGV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 266 PAPEDLAVICFTSGTTGNPKGAMITHRNVVSDcsafVKVTDKTFSPSSDDTLISFLPLAHMFERVVECV-MLCHGAKI-- 342
Cdd:cd05926 146 PLPDDLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLsTLAAGGSVvl 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 --GFfqgDIRLLMDDLKALQPTIFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEAELrsgiirnnslwdklifhk 420
Cdd:cd05926 222 ppRF---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEPNPESPP------------------ 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 iqsslgGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT--VPGDWTAGHVGAPmpcSLIKLVDV-EE 497
Cdd:cd05926 265 ------PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKP---VGVEVRILdED 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 498 MNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:cd05926 336 GEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGV 414
|
490 500
....*....|....*....|....*....
gi 309243088 578 YLRSEPVAQ--VF-----VHGESLQAFLI 599
Cdd:cd05926 415 LLSHPAVLEavAFgvpdeKYGEEVAAAVV 443
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
122-617 |
8.11e-39 |
|
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: 150.17 E-value: 8.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSeCVGSALIHKGFKagPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd05909 8 LTYRKLLTGA-IALARKLAKMTK--EGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKP--EKANLLLEGVenklIPGLKTIILMDsygiDLLER---GKKCGVEIMSMKALEDLGRANRRKPKppAPEDLAVICF 276
Cdd:cd05909 85 SKQfiEKLKLHHLFD----VEYDARIVYLE----DLRAKiskADKCKAFLAGKFPPKWLLRIFGVAPV--QPDDPAVILF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 277 TSGTTGNPKGAMITHRNVVSDCSAFVKVtdktFSPSSDDTLISFLPLAHMFERVVeCVM--LCHGAKIGFfqgdirllmd 354
Cdd:cd05909 155 TSGSEGLPKGVVLSHKNLLANVEQITAI----FDPNPEDVVFGALPFFHSFGLTG-CLWlpLLSGIKVVF---------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 355 dlkALQPTIFPVVPRLLNRMFDRIFGQANTTLKRWLldfasKRKEAELRSGIirnnslwdklifhkiqsslggkvRLMVT 434
Cdd:cd05909 220 ---HPNPLDYKKIPELIYDKKATILLGTPTFLRGYA-----RAAHPEDFSSL-----------------------RLVVA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 435 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPG-DWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKG 513
Cdd:cd05909 269 GAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGGLLLVRG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 514 PNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEP----VAQVFV 589
Cdd:cd05909 349 PNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEILPedneVAVVSV 426
|
490 500 510
....*....|....*....|....*....|..
gi 309243088 590 ----HGESLQAFLIAIvVPDVETLGHWAQKRG 617
Cdd:cd05909 427 pdgrKGEKIVLLTTTT-DTDPSSLNDILKNAG 457
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
112-600 |
8.15e-39 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 151.74 E-value: 8.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 112 SRKPDQPY-----EWLSYKQVEDMSECVgSALIHKGFKAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVV---PLY---- 179
Cdd:PRK08974 34 ARYADQPAfinmgEVMTFRKLEERSRAF-AAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVnvnPLYtpre 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 180 ------DTlGTEAITYIINkgelslvFvdkpekANLLLEGVENKLIpglKTIILMdSYGiDLLERGKKCGVEI------- 246
Cdd:PRK08974 113 lehqlnDS-GAKAIVIVSN-------F------AHTLEKVVFKTPV---KHVILT-RMG-DQLSTAKGTLVNFvvkyikr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 247 ----------MSMKALEDLGRaNRRKPKPP-APEDLAVICFTSGTTGNPKGAMITHRNVVSDcsafVKVTDKTFSP---S 312
Cdd:PRK08974 174 lvpkyhlpdaISFRSALHKGR-RMQYVKPElVPEDLAFLQYTGGTTGVAKGAMLTHRNMLAN----LEQAKAAYGPllhP 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 313 SDDTLISFLPLAHMFERVVECVMLCHgakigffQGDIRLLMD---DLKALqptifpvVPRLLNRMFDRIFGqANTTLKRW 389
Cdd:PRK08974 249 GKELVVTALPLYHIFALTVNCLLFIE-------LGGQNLLITnprDIPGF-------VKELKKYPFTAITG-VNTLFNAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 390 LldfaskrkeaelrsgiirNNSLWDKLIFhkiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---A 466
Cdd:PRK08974 314 L------------------NNEEFQELDF----SSL----KLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 467 GCSLTVPGdwTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWL 546
Cdd:PRK08974 368 VNPYDLDY--YSGSIGLPVPSTEIKLVD-DDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMD 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 309243088 547 PNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVF-------VHGESLQAFLIA 600
Cdd:PRK08974 444 EEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVMLHPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
270-628 |
1.97e-37 |
|
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: 142.64 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 270 DLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMFERVVECVM-LCHGAKI---GFF 345
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLT----EDDRYLIINPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 qgDIRLLMDDLKALQPTIFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELrsgiirnnslwdklifhkiqSSL 425
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 426 ggkvRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGcSLTVPGD---WTAGHVGAPMPCSLIKLVDveemnyl 501
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAGVA-TMCRPGDdaeTVATTCGRACPGFEVRIAD------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 502 aakgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 581
Cdd:cd17638 186 ----DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALAEH 260
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 309243088 582 EPVAQVFV-------HGESLQAFLIA--IVVPDVETLGHWAQKR-------GFVGSFEELCRN 628
Cdd:cd17638 261 PGVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRERlanykvpRFVRFLDELPRN 323
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
123-579 |
1.98e-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: 146.90 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 123 SYKQVEDMSECVGSALIHKGFKAgpENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVD 202
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 203 KPEKANLLleGVENKLiPGLKTIILMDSYgIDLleRGKKCgveIMSMKALEDLGRANRRKPKPPA---PEDLAVICFTSG 279
Cdd:cd17642 124 KKGLQKVL--NVQKKL-KIIKTIIILDSK-EDY--KGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 280 TTGNPKGAMITHRNVvsdCSAFVKVTDKTF--SPSSDDTLISFLPLAHMFERVVECVMLCHGAKIGF-FQGDIRLLMDDL 356
Cdd:cd17642 195 STGLPKGVQLTHKNI---VARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 357 KALQPTIFPVVPRLLnrmfdrIFGQANTTLKRWllDFASkrkeaelrsgiirnnslwdkliFHKIQSslggkvrlmvtGA 436
Cdd:cd17642 272 QDYKVQSALLVPTLF------AFFAKSTLVDKY--DLSN----------------------LHEIAS-----------GG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 437 APVSATVLTFLRAALGCQFY-EGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPN 515
Cdd:cd17642 311 APLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGELCVKGPM 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309243088 516 VFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYL 579
Cdd:cd17642 391 IMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESILL 453
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
255-609 |
3.64e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 146.83 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 255 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSD---CSAFVKVTDKtfspSSDDTLISFLPLAHMFERVV 331
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGSNLN----EGCEILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 332 EC-VMLCHGAKigffqgdirllmddlkalqpTIFPVVPRLLNRMFdrifgqanTTLKRWLLdfaskrkeaelrSGIIRNN 410
Cdd:PRK05677 269 HCmAMMLIGNH--------------------NILISNPRDLPAMV--------KELGKWKF------------SGFVGLN 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 411 SLWDKLI----FHKIQSSlggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMP 486
Cdd:PRK05677 309 TLFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVP 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 487 CSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 566
Cdd:PRK05677 386 STLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSG 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 309243088 567 EYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFliaIVVPDVETL 609
Cdd:PRK05677 464 FNVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-616 |
3.94e-37 |
|
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: 142.42 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDcSAFVKVTDKTfspSSDDTLISFLPLAHMFERVVEcVMLC--HGAKIGFf 345
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIGERLGL---TEQDRLCIPVPLFHCFGSVLG-VLACltHGATMVF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 qgdIRLLMDDLKALQ-------------PTIFPvvpRLLNRMFDRIFgqanttlkrwllDFASkrkeaeLRSGIIrnnsl 412
Cdd:cd05917 75 ---PSPSFDPLAVLEaiekekctalhgvPTMFI---AELEHPDFDKF------------DLSS------LRTGIM----- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 413 wdklifhkiqsslggkvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCSLTVPGD---WTAGHVGAPMPCS 488
Cdd:cd05917 126 ----------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDsieKRVNTVGRIMPHT 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 489 LIKLVDvEEMNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 567
Cdd:cd05917 184 EAKIVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGE 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 309243088 568 YIAPEKIENIYLRSEPVAQVFV-------HGESLQAFLI--AIVVPDVETLGHWAQKR 616
Cdd:cd05917 262 NIYPREIEEFLHTHPKVSDVQVvgvpderYGEEVCAWIRlkEGAELTEEDIKAYCKGK 319
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
151-616 |
3.92e-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: 141.43 E-value: 3.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 151 VGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVDKPekanLLLEGVenklipglktiilmDS 230
Cdd:TIGR01923 27 VALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL----LEEKDF--------------QA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 231 YGIDLLERGKKCGVEIMSMKALEDLgranrrkpkppapedlAVICFTSGTTGNPKGAMITHRNVvsdcSAFVKVTDKTFS 310
Cdd:TIGR01923 89 DSLDRIEAAGRYETSLSASFNMDQI----------------ATLMFTSGTTGKPKAVPHTFRNH----YASAVGSKENLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 311 PSSDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLmDDLKALQPTIFPVVPRLLNRMFDRifGQANTTLKRWL 390
Cdd:TIGR01923 149 FTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERVTHISLVPTQLNRLLDE--GGHNENLRKIL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 391 LdfaskrkeaelrsgiirnnslwdklifhkiqsslggkvrlmvtGAAPVSATVLTFLRAaLGCQFYEGYGQTE-CTAGCS 469
Cdd:TIGR01923 226 L-------------------------------------------GGSAIPAPLIEEAQQ-YGLPIYLSYGMTEtCSQVTT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 470 LTVPGDWTAGHVGAPMPCSLIKL-VDVEEmnylaakGEGEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPN 548
Cdd:TIGR01923 262 ATPEMLHARPDVGRPLAGREIKIkVDNKE-------GHGEIMVKGANLMKGYL-YQGELTPAFEQQGWFNTGDIGELDGE 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 309243088 549 GTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFLIAIVVPDVETLGHWAQKR 616
Cdd:TIGR01923 334 GFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQVPVAYIVSESDISQAKLIAYLTEK 407
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
255-560 |
4.46e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 143.60 E-value: 4.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 255 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCS---AFVKVTdktfsPSSDDTLISFLPLAHMF--ER 329
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGL-----GDGPERVLAALPMFHAYglTL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 330 VVECVMLCHGAKIGFFQGDIRLLMDDLKALQPTIFPVVPRLlnrmFDRIfgqanttlkrwlldfaskRKEAELRsGIirn 409
Cdd:PRK05605 280 CLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 410 nslwdklifhkiqsSLGGkVRLMVTGAA--PVSaTVLTFlRAALGCQFYEGYGQTECT---AGCSLTvpGDWTAGHVGAP 484
Cdd:PRK05605 334 --------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSpiiVGNPMS--DDRRPGYVGVP 394
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 309243088 485 MPCSLIKLVDVEEMNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PRK05605 395 FPDTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
247-600 |
5.02e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 140.34 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 247 MSMKALEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSD------CSAFVKVTDKTFSPSSDDTLISF 320
Cdd:PRK12492 185 VPFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAP 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 321 LPLAHMFERVVECVMLchgakigFFQGDIRLLMDDlkalqptifpvvPRLLNRMFDRifgqanttLKRWLLdfaskrkea 400
Cdd:PRK12492 265 LPLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF--------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 401 elrSGIIRNNSLWDKLIFHKIQSSLGGKvRLMVT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCSLTVPGDWT 477
Cdd:PRK12492 309 ---SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 478 A-GHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR 556
Cdd:PRK12492 384 RlGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDR 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 309243088 557 KKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFLIA 600
Cdd:PRK12492 463 KKDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
267-608 |
1.17e-34 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 137.27 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSdcsaFVKVTDKTFSPSSDDTLISFLPLAH-MFerVVE-CVMLCHGAKI-- 342
Cdd:cd05930 91 DPDDLAYVIYTSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEiFGALLAGATLvv 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 --GFFQGDIRLLMDDLKALQPTIFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwdklifhk 420
Cdd:cd05930 165 lpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL-------------------------------- 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 iqsslggkvrLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTV--PGDWTAGHV--GAPMPCSLIKLVDvE 496
Cdd:cd05930 213 ----------VLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRvpPDDEEDGRVpiGRPIPNTRVYVLD-E 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 497 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIA 570
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIE 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 309243088 571 PEKIENIYLRSEPVAQVFV---HGESLQAFLIAIVVPDVET 608
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVvarEDGDGEKRLVAYVVPDEGG 401
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
255-684 |
4.03e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 137.70 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 255 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSD---CSAFVKVTDKTfsPSSDDTLISFLPLAHMFERVV 331
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKL--EEGCEVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 332 ECVMLchgAKIGFFQG------DIRLLMDDLKALQPTIFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsg 405
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 406 iirNNSLWDKLIFHKIQSSLGGkvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTECT-AGCSLTVPGDWTAGHVGAP 484
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 485 MPCSLIKLVDveEMNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 563
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 564 AQGEYIAPEKIENIYLRSEPVAQVfvhgeslqaflIAIVVPDvetlghwaQKRGfvgsfeELCRNKDVKK--AILEDMLR 641
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 309243088 642 LGRDAGLKSFEQVRGISLHPELFSIDNGlltptmKAKRPELRN 684
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
123-609 |
4.67e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 135.11 E-value: 4.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 123 SYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVD 202
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDR--VALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 203 kpekanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppapedLAVICFTSGTTG 282
Cdd:cd05934 83 --------------------------------------------------------------------PASILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 283 NPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMFERVVEC-VMLCHGAKI--------GFFQGDIRllm 353
Cdd:cd05934 95 PPKGVVITHANLTFAGYYSARRFGLG----EDDVYLTVLPLFHINAQAVSVlAALSVGATLvllprfsaSRFWSDVR--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 354 ddlkALQPTIF---PVVPRLLNRMFDRIFGQANttlkrwlldfaskrkeaelrsgiirnnslwdklifhkiqsslggkvR 430
Cdd:cd05934 168 ----RYGATVTnylGAMLSYLLAQPPSPDDRAH----------------------------------------------R 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 431 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVC 510
Cdd:cd05934 198 LRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGELV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 511 VK---GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQV 587
Cdd:cd05934 277 IRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREA 354
|
490 500
....*....|....*....|....*.
gi 309243088 588 FVHG----ESLQAFLIAIVVPDVETL 609
Cdd:cd05934 355 AVVAvpdeVGEDEVKAVVVLRPGETL 380
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
112-591 |
9.68e-34 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 135.84 E-value: 9.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 112 SRKPDQPYEWLSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYII 191
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDR--VATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 192 NKGELSLVFVDkpekANL--LLEGVENKLiPGLKTIILMDSygidlleRGKKCGVEIMSMKALEDL-GRANRRKPKPPAP 268
Cdd:cd12119 94 NHAEDRVVFVD----RDFlpLLEAIAPRL-PTVEHVVVMTD-------DAAMPEPAGVGVLAYEELlAAESPEYDWPDFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 269 E-DLAVICFTSGTTGNPKGAMITHRNVVSdcSAFVKVTDKTFSPSSDDTlisFLPLAHMFErvVE-------CVMLchGA 340
Cdd:cd12119 162 EnTAAAICYTSGTTGNPKGVVYSHRSLVL--HAMAALLTDGLGLSESDV---VLPVVPMFH--VNawglpyaAAMV--GA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 341 KI----GFFQGDirLLMDDLKALQPTIFPVVPRLLNRMFDRifgqanttLKRWLLDFASKRkeaelrsgiirnnslwdkl 416
Cdd:cd12119 233 KLvlpgPYLDPA--SLAELIEREGVTFAAGVPTVWQGLLDH--------LEANGRDLSSLR------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 417 ifhkiqsslggkvRLMVTGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCSLTVPGDWTAGHV----------GAPM 485
Cdd:cd12119 284 -------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 486 PCSLIKLVDvEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd12119 349 PGVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKS 426
|
490 500
....*....|....*....|....*...
gi 309243088 564 AqGEYIAPEKIENIYLRSEPVAQVFVHG 591
Cdd:cd12119 427 G-GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
256-638 |
1.57e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 134.35 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 256 GRANRRKPKPPaPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMfervvecvm 335
Cdd:PRK07787 116 ARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHV--------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 336 lcHGakigffqgdirLLMDDLKALqptifpvvprllnrmfdRIFGQANTTLKrwlldFASKRKEAELRSGiirnNSLWDK 415
Cdd:PRK07787 182 --HG-----------LVLGVLGPL-----------------RIGNRFVHTGR-----PTPEAYAQALSEG----GTLYFG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 416 L--IFHKIQSSLG-----GKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCS 488
Cdd:PRK07787 223 VptVWSRIAADPEaaralRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 489 LIKLVDvEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHI 560
Cdd:PRK07787 303 ETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 561 FKLAQGEyiapekIENIYLRSEPVAQVFVHGE---SLQAFLIAIVVP-----DVETLGHWAQ-----KRGFVGSF-EELC 626
Cdd:PRK07787 382 YRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGaddvaADELIDFVAQqlsvhKRPREVRFvDALP 455
|
410
....*....|....*
gi 309243088 627 RN---KDVKKAILED 638
Cdd:PRK07787 456 RNamgKVLKKQLLSE 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
78-591 |
2.37e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 135.29 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 78 DSDEPLAyfyddVRTLYEGFQRGIRVSNNGPCLGSRKPDQPYewlSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQN 157
Cdd:PRK12583 10 GGDKPLL-----TQTIGDAFDATVARFPDREALVVRHQALRY---TWRQLADAVDRLARGLLALGVQPGDR--VGIWAPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 158 RPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVDK---------------PEKANLLLEGVENKLIPGL 222
Cdd:PRK12583 80 CAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafktsdyhamlqellPGLAEGQPGALACERLPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 223 KTIILMD---SYGI----DLLERGkkcgvEIMSMKALEDLGRANRRkpkppapEDLAVICFTSGTTGNPKGAMITHRNVV 295
Cdd:PRK12583 160 RGVVSLApapPPGFlawhELQARG-----ETVSREALAERQASLDR-------DDPINIQYTSGTTGFPKGATLSHHNIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 296 SDcSAFVKvtdKTFSPSSDDTLISFLPLAHMFERVVeCVMLC--HGAKIGF----FQGDIRLLM---DDLKALQ--PTIF 364
Cdd:PRK12583 228 NN-GYFVA---ESLGLTEHDRLCVPVPLYHCFGMVL-ANLGCmtVGACLVYpneaFDPLATLQAveeERCTALYgvPTMF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 365 pvVPRLLNRMFDRifgqanttlkrwlLDFASkrkeaeLRSGIIrnnslwdklifhkiqsslggkvrlmvtGAAPVSATVL 444
Cdd:PRK12583 303 --IAELDHPQRGN-------------FDLSS------LRTGIM---------------------------AGAPCPIEVM 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 445 TFLRAALGC-QFYEGYGQTECTAGCSLTVPGD---WTAGHVGAPMPCSLIKLVDVEemNYLAAKGE-GEVCVKGPNVFQG 519
Cdd:PRK12583 335 RRVMDEMHMaEVQIAYGMTETSPVSLQTTAADdleRRVETVGRTQPHLEVKVVDPD--GATVPRGEiGELCTRGYSVMKG 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309243088 520 YLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG 591
Cdd:PRK12583 413 YWNNPEATAESIDEDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG 483
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
267-575 |
4.50e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 134.34 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFSPSSDDTLISFLPLAHMFErvVECVMLCH---GAKIG 343
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 344 FFQG-DIRLLMDDLKALQPTIFPVVPRLLnrmfdrifgqanttlkrwlLDFAskrkeaelRSGIIRNNSLwdklifhkiq 422
Cdd:PLN02246 255 IMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL---------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 423 SSlggkVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCSLTV-------PGDWTAGHVGAPMPCSLIKLVD 494
Cdd:PLN02246 298 SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 495 VEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 574
Cdd:PLN02246 372 PETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAEL 450
|
.
gi 309243088 575 E 575
Cdd:PLN02246 451 E 451
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
256-599 |
7.39e-33 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 133.99 E-value: 7.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 256 GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDC--------SAFVKvtdktfsPSSDDTLISF--LPLAH 325
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYH 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 326 MFERVVECVMlchGAKIGffqG---------DIRLLMDDLKALQPTIFPVVPRLLNRMFdrifgqanttlkrwlldfask 396
Cdd:PRK07059 264 IFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL--------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 397 rkeaelrsgiirNNSLWDKLIFHKIQSSLGGkvrlmvtGAApVSATVLTFLRAALGCQFYEGYG--QTECTAGCSLTVPG 474
Cdd:PRK07059 317 ------------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVDAT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 475 DWTaGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKII 554
Cdd:PRK07059 377 EFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIV 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 309243088 555 DRKKHIFkLAQGEYIAPEKIENIyLRSEP----VAQVFVH----GESLQAFLI 599
Cdd:PRK07059 455 DRKKDMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
114-579 |
7.60e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 133.72 E-value: 7.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 114 KPDQPYEWlSYKQVEDMSECVGSALIHKGFKAGpenfvGIFAQNRPEW---VIIEQGCFAYSMVVVPLYDTLGTEAITYI 190
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPG-----DRVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 191 INKGELSLVFVDKPEKAN----LLLEGVENklIPGLKTIILMDsygidlleRGKKCGVEIMSMKALEDLGRANrrKPKPP 266
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKQTrpvdLILPLQNQ--LPQLQQIVGVD--------KLAPATSSLSLSQIIADYEPLT--TAITT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHmfervveCVMLCHGAKIGFFQ 346
Cdd:PRK06087 185 HGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH-------ATGFLHGVTAPFLI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 347 GDIRLLMDDLKALQPTifpvvpRLLNRmfDRIFGQANTTlkRWLLDFASKRKEAELRSgiirnnslwdklifhkiqSSLg 426
Cdd:PRK06087 254 GARSVLLDIFTPDACL------ALLEQ--QRCTCMLGAT--PFIYDLLNLLEKQPADL------------------SAL- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 427 gkvRLMVTGAAPVSATVLtflRAAL--GCQFYEGYGQTECT--AGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLA 502
Cdd:PRK06087 305 ---RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-EARKTLP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 309243088 503 AKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYL 579
Cdd:PRK06087 378 PGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILL 453
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
115-599 |
4.91e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 131.47 E-value: 4.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 115 PDQPYEWlSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEqgcFAYS-----MVVV-PLYDTlgtEAIT 188
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIEKGDR--VGIWAPNVPEWVLTQ---FATAkigaiLVTInPAYRL---SELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 189 YIINKGELS-LVFVDK--------------PEKANLLLEGVENKLIPGLKTIILMDSygidllerGKKCGV----EIMSM 249
Cdd:PRK08315 109 YALNQSGCKaLIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGD--------EKHPGMlnfdELLAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 250 KALEDLGRANRRKPKPpAPEDLAVICFTSGTTGNPKGAMITHRNV------VSDCSAFvkvtdktfspSSDDTLISFLPL 323
Cdd:PRK08315 181 GRAVDDAELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNIlnngyfIGEAMKL----------TEEDRLCIPVPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 324 AHMFErvveCVM-----LCHGAKI-----GFfqgdirllmDDLKALQ-------------PTIFpvVPRLLNRMFDRifg 380
Cdd:PRK08315 250 YHCFG----MVLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 381 qanttlkrwlLDFASkrkeaeLRSGIirnnslwdklifhkiqssLGGK---VRLM-----------VTGAapvsatvltf 446
Cdd:PRK08315 312 ----------FDLSS------LRTGI------------------MAGSpcpIEVMkrvidkmhmseVTIA---------- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 447 lraalgcqfyegYGQTECTAGCSLTVPGD------WTaghVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGY 520
Cdd:PRK08315 348 ------------YGMTETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVDPETGETVPRGEQGELCTRGYSVMKGY 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 521 LKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPV--AQVF-V----HGES 593
Cdd:PRK08315 413 WNDPEKTAEAIDADGWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIqdVQVVgVpdekYGEE 491
|
....*.
gi 309243088 594 LQAFLI 599
Cdd:PRK08315 492 VCAWII 497
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
122-558 |
4.95e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 130.77 E-value: 4.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLyDTLGTEA-ITYIINKGELSLVF 200
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDR--VAVQVEKSPEALALYLATLRAGAVFLPL-NTAYTLAeLDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 201 VDkPEKANLLLEGVENKLIPGLKTiiLMDSYGIDLLERGKkcgveimsmkaledlGRANRRKPKPPAPEDLAVICFTSGT 280
Cdd:PRK07514 106 CD-PANFAWLSKIAAAAGAPHVET--LDADGTGSLLEAAA---------------AAPDDFETVPRGADDLAAILYTSGT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 281 TGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAH---MFerVVECVMLCHGAKIGFFQgdiRLLMDDLK 357
Cdd:PRK07514 168 TGRSKGAMLSHGNLLSNALTLVDYWRFT----PDDVLIHALPIFHthgLF--VATNVALLAGASMIFLP---KFDPDAVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 358 ALQP--TIFPVVP----RLL-NRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdklifhkiqsSLGGKVR 430
Cdd:PRK07514 239 ALMPraTVMMGVPtfytRLLqEPRLTR----------------------------------------------EAAAHMR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 431 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVC 510
Cdd:PRK07514 273 LFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPETGAELPPGEIGMIE 352
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 309243088 511 VKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 558
Cdd:PRK07514 353 VKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
112-604 |
2.06e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 128.95 E-value: 2.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 112 SRKPDQP-YEW----LSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPE-WVIIEQGCFAySMVVVPLYdTLGTE 185
Cdd:PRK06188 23 KRYPDRPaLVLgdtrLTYGQLADRISRYIQAFEALG--LGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALH-PLGSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 186 AI-TYIINKGELSLVFVDK---PEKANLLLEGVenkliPGLKTIILMDS--YGIDLLERGKKCGVeimsmKALEDlgran 259
Cdd:PRK06188 99 DDhAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDLLAAAAKFGP-----APLVA----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 260 rrkpkPPAPEDLAVICFTSGTTGNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDTLISFLPLAHMFERVVECVMLCHG 339
Cdd:PRK06188 164 -----AALPPDIAGLAYTGGTTGKPKGVMGTHRSIA----TMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLPTLLRGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 340 AKI---GFfqgDIRLLMDDLKALQPTIFPVVPRLLNRmfdrifgqanttlkrwLLDFASKRKeAELrsgiirnnslwdkl 416
Cdd:PRK06188 235 TVIvlaKF---DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPDLRT-RDL-------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 417 ifhkiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHV------GAPMPCSLI 490
Cdd:PRK06188 281 ------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 491 KLVDvEEMNYLAAkGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 569
Cdd:PRK06188 351 ALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDEDGFYYIVDRKKDMI-VTGGFNV 426
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 309243088 570 APEKIENIYLRSEPVAQVFV-------HGESLQafliAIVVP 604
Cdd:PRK06188 427 FPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
122-604 |
7.34e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 127.36 E-value: 7.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLKKGDR--VAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DkPEKANLLLEGVENKlipGLKTIILMDSYGIDLLERGkkcgveimsMKALEDLGRANRRKPKPPAP--EDLAVICFTSG 279
Cdd:PRK08316 115 D-PALAPTAEAALALL---PVDTLILSLVLGGREAPGG---------WLDFADWAEAGSVAEPDVELadDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 280 TTGNPKGAMITHRNVVSD-CSAFVkvtdkTFSPSSDDTLISFLPLAHMFERVV---ECVMLchGAKIGFFQG-DIRLLMD 354
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEyVSCIV-----AGDMSADDIPLHALPLYHCAQLDVflgPYLYV--GATNVILDApDPELILR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 355 DLKALQPTIF---PVV-PRLLNR-MFDRIfgqanttlkrwllDFASKRKeaelrsgiirnnslwdklIFHkiqsslggkv 429
Cdd:PRK08316 255 TIEAERITSFfapPTVwISLLRHpDFDTR-------------DLSSLRK------------------GYY---------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 430 rlmvtGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSLTVPGDwTAGHVG-APMPCSLI--KLVDvEEMNYLAAKG 505
Cdd:PRK08316 294 -----GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAGRPVLNVetRVVD-DDGNDVAPGE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 506 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPVA 585
Cdd:PRK08316 367 VGEIVHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVA 444
|
490 500
....*....|....*....|...
gi 309243088 586 QVFV----HGESLQAfLIAIVVP 604
Cdd:PRK08316 445 EVAViglpDPKWIEA-VTAVVVP 466
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
234-589 |
7.63e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 127.79 E-value: 7.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 234 DLLERGKKCGVEIMSMKALEdlgranrrkpkppapEDLAVICFTSGTTGNPKGAMITHRNVVSD-CSAFVKVTDKTFSPS 312
Cdd:PLN02330 164 ELLEAADRAGDTSDNEEILQ---------------TDLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMIGQV 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 313 sddTLISFLPLAHMFERVVEC--VMLCHGAKIGFFQGDIRLLMDDLKALQPTIFPVVPRLLNRMFdrifgqanttlkrwl 390
Cdd:PLN02330 229 ---VTLGLIPFFHIYGITGICcaTLRNKGKVVVMSRFELRTFLNALITQEVSFAPIVPPIILNLV--------------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 391 ldfaskrkeaelrsgiirNNSLWDKLIFHKIqsslggKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTagCS 469
Cdd:PLN02330 291 ------------------KNPIVEEFDLSKL------KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS--CI 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 470 LTVPGDWTAGH-------VGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDI 542
Cdd:PLN02330 345 TLTHGDPEKGHgiakknsVGFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDI 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 309243088 543 GKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFV 589
Cdd:PLN02330 425 GYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAILLTHPSVEDAAV 470
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
265-589 |
1.15e-30 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 125.07 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 265 PPAPEDLAVICFTSGTTGNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDTLISFLPLAHMFervveCVM-----LCHG 339
Cdd:TIGR01733 116 PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLV----NLLAWLARRYGLDPDDRVLQFASLSFDA-----SVEeifgaLLAG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 340 AK--------IGFFQGDIRLLMDDLKAlqpTIFPVVPRLLNRMfdrifgqanttlkrwlldfaskrkeaeLRSGIIRNNS 411
Cdd:TIGR01733 187 ATlvvppedeERDDAALLAALIAEHPV---TVLNLTPSLLALL---------------------------AAALPPALAS 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 412 LwdklifhkiqsslggkvRLMVTGA-APVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT-VPGDWTAGHV----GAPM 485
Cdd:TIGR01733 237 L-----------------RLVILGGeALTPALVDRWRARGPGARLINLYGPTETTVWSTATlVDPDDAPRESpvpiGRPL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 486 PCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRK 557
Cdd:TIGR01733 300 ANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYLNRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRI 378
|
330 340 350
....*....|....*....|....*....|..
gi 309243088 558 KHIFKLaQGEYIAPEKIENIYLRSEPVAQVFV 589
Cdd:TIGR01733 379 DDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
120-605 |
1.55e-30 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 125.48 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 120 EWLSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLV 199
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 200 FVDKpekanlllegvenklipglktiilmdsygiDLLERGKKCGVEIMsmKALEDLGRANRRKPKPPAPEDLAVICFTSG 279
Cdd:cd12116 89 LTDD------------------------------ALPDRLPAGLPVLL--LALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 280 TTGNPKGAMITHRNVVSdcsaFVKVTDKTFSPSSDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFFQGDI----RLLM 353
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 354 DDLKALQPTIFpvvprllnrmfdrifgQANTTLKRWLLDfaskrkeaelrSGiirnnslWDKLifhkiqsslgGKVRLMV 433
Cdd:cd12116 211 RLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR----------AGLTALC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 434 TGAA--PVSATVLTflraALGCQFYEGYGQTECT--AGCSLTVPGDwTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEV 509
Cdd:cd12116 247 GGEAlpPDLAARLL----SRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGEL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 510 CVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSE 582
Cdd:cd12116 321 YIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHP 399
|
490 500
....*....|....*....|....*
gi 309243088 583 PVAQ--VFVHGESLQAFLIAIVVPD 605
Cdd:cd12116 400 GVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
174-605 |
3.46e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 127.73 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 174 VVVPLYDTLGTEAITYIINKGELSLV-----FVDKPEKANLLLEgvenklIPGLKTIILMDsygiDLLERGKKcgVEIMS 248
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVitsrkFLEKLKNKGFDLE------LPENVKVIYLE----DLKAKISK--VDKLT 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 249 MKALEDLGRA---NRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDcsafVKVTDKTFSPSSDDTLISFLPLAH 325
Cdd:PRK08633 759 ALLAARLLPArllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFH 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 326 MFERVVECVM-LCHGAKIGFFQgdirllmDDLKALqpTIFPVVPRllNR---MFdrifgqANTTLkrwlldfaskrkeae 401
Cdd:PRK08633 835 SFGLTVTLWLpLLEGIKVVYHP-------DPTDAL--GIAKLVAK--HRatiLL------GTPTF--------------- 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 402 LRSgIIRNNSLwDKLIFhkiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVP-----GDW 476
Cdd:PRK08633 883 LRL-YLRNKKL-HPLMF----ASL----RLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVNLPdvlaaDFK 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 477 T-----AGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEAL---DKDGWLHTGDIGKWLPN 548
Cdd:PRK08633 953 RqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYVTGDKGHLDED 1032
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 309243088 549 GTLKIIDRKKHIFKLAqGEYIAPEKIEniylrsEPVAQVFvHGESLQafLIAIVVPD 605
Cdd:PRK08633 1033 GFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD 1079
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
268-688 |
1.76e-29 |
|
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: 122.65 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDK------------TFSPSSDDTlisFLPLAHMFervveCVm 335
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLtsesrvlqfasyTFDVSILEI---FTTLAAGG-----CL- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 336 lCHGAKigffqgdiRLLMDDLkalqptifpvvPRLLNRMfdrifgQANTtlkrwlldfaskrkeAELRSGIIRnnslwdk 415
Cdd:cd05918 176 -CIPSE--------EDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 416 LIFHKIQSSLggkvRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCSLT-VPGDWTAGHVGAPMPCSLIkLVD 494
Cdd:cd05918 208 LLDPEDVPSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSpVVPSTDPRNIGRPLGATCW-VVD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 495 VEEMNYLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHI 560
Cdd:cd05918 281 PDNHDRLVPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 561 FKLaQGEYIAPEKIENIYLRSEP-----VAQVFVH-GESLQAFLIAIVVPDVETLGHWAQKRGFVGSFEELCRNkdvkKA 634
Cdd:cd05918 361 VKI-RGQRVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRAL----VA 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 309243088 635 ILEDMLRlgrdAGLKSFeqvrgisLHPELF-SIDNGLLTPTMKAKRPELRNYFRS 688
Cdd:cd05918 436 ELRSKLR----QRLPSY-------MVPSVFlPLSHLPLTASGKIDRRALRELAES 479
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
265-609 |
3.12e-29 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 121.26 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 265 PPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSA-----FVKVTDKT---FSPSSDDTLisflplAHMFervvecVML 336
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQpparlDVGPGSRVaqvLSIAFDACI------GEIF------STL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 337 CHGAKIgFFQGDIRLLMDDLKALqpTIFPVVPRLLnrmfdrifgqanTTLKRwlLDFASkrkeaelrsgiirnnslwdkl 416
Cdd:cd17653 169 CNGGTL-VLADPSDPFAHVARTV--DALMSTPSIL------------STLSP--QDFPN--------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 417 ifhkiqsslggkVRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCSLT--VPGDWTagHVGAPMPCSLIKLVD 494
Cdd:cd17653 211 ------------LKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 495 VEEMNYLAAKgEGEVCVKGPNVFQGYLKDPAKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 568
Cdd:cd17653 275 ADLQPVPEGV-VGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFR 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 309243088 569 IAPEKIENIYLRSEPVAQ---VFVHGEslqaFLIAIVVP---DVETL 609
Cdd:cd17653 353 INLEEIEEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGL 395
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
145-585 |
6.68e-29 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 122.37 E-value: 6.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 145 AGPENFVGIFAQNRPEWVIIEQGCFAYSmVVVPLYDTLGTEAITYIINKGELSLVFVDKPE-------KANLLLEGVenk 217
Cdd:PRK07529 80 VGPGDVVAFLLPNLPETHFALWGGEAAG-IANPINPLLEPEQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 218 liPGLKTIILMDsyGIDLLERGKKCGVEIMSMKA---LEDLGRANRRKP-------KPPAPEDLAVICFTSGTTGNPKGA 287
Cdd:PRK07529 156 --PELRTVVEVD--LARYLPGPKRLAVPLIRRKAharILDFDAELARQPgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 288 MITHRNVVSDC---SAFVKVTDktfspssDDTLISFLPLAHMFERVVEC-VMLCHGAKIGF-----FQGDirLLMDDLKA 358
Cdd:PRK07529 232 QHTHGNEVANAwlgALLLGLGP-------GDTVFCGLPLFHVNALLVTGlAPLARGAHVVLatpqgYRGP--GVIANFWK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 359 L----QPTIFPVVPRLLNRMFDRIFGQANTtlkrwlldfaskrkeaelrsgiirnnslwdklifhkiqSSLggkvRLMVT 434
Cdd:PRK07529 303 IveryRINFLSGVPTVYAALLQVPVDGHDI--------------------------------------SSL----RYALC 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 435 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVP-GDWTAGHVGAPMPCSLIKLVDVEEM-NYL--AAKGE-GEV 509
Cdd:PRK07529 341 GAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVL 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309243088 510 CVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVA 585
Cdd:PRK07529 421 CIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYFWLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
251-558 |
1.68e-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: 120.46 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 251 ALEDLGRANRRKPKPPA-PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAfvKVTDKTFSPssDDTLISFLPLAHmfer 329
Cdd:cd05906 148 SIEELLDTAADHDLPQSrPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG--KIQHNGLTP--QDVFLNWVPLDH---- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 330 VVECVMlCHGAkigffqgDIRLLMDDLKALQPTIFPVVPRLLnRMFDRIfgQANTTlkrWLLDFA-SKRKEAELRsgiiR 408
Cdd:cd05906 220 VGGLVE-LHLR-------AVYLGCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPNFAfALLNDLLEE----I 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 409 NNSLWDklifhkiQSSLggkvRLMVTGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGCSLTVP---GDWTAG 479
Cdd:cd05906 282 EDGTWD-------LSSL----RYLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGVIYSRSfptYDHSQA 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 480 H----VGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIID 555
Cdd:cd05906 351 LefvsLGRPIPGVSMRIVD-DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITG 428
|
...
gi 309243088 556 RKK 558
Cdd:cd05906 429 RTK 431
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
174-576 |
2.57e-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: 118.70 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 174 VVVPLYDTLGTEAITYIINKGELSLVFVDkpekanlllEGVENKLipglkTIILMDSYgidllergkkcgveIMSMKALE 253
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLAD---------AGAADRL-----RDALPASP--------------DPGTVLDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 254 DLGRANRR--KPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMFERVV 331
Cdd:cd05922 100 DGIRAARAsaPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT----ADDRALTVLPLSYDYGLSV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 332 ECVMLCHGAKIgFFQGDIRL---LMDDLKALQPTIFPVVPRLLNrMFDRIfgqanttlkrwlldfasKRKEAELRSgiir 408
Cdd:cd05922 176 LNTHLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKLPS---- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 409 nnslwdklifhkiqsslggkVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSlTVPGDWTA---GHVGAP 484
Cdd:cd05922 233 --------------------LRYLTQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMT-YLPPERILekpGSIGLA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 485 MPCSLIKLVDVEEMnyLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd05922 292 IPGGEFEILDDDGT--PTPPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKL 369
|
410
....*....|...
gi 309243088 564 AqGEYIAPEKIEN 576
Cdd:cd05922 370 F-GNRISPTEIEA 381
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
263-583 |
3.02e-28 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 119.95 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 263 PKPP-APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFS-PSSDDTLISFLPLAHMFERVVECV-MLCHG 339
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQYEyPGSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 340 AKI----GFFQGDIRLLMDDLKAlqpTIFPVVPRLLNRMFDRIFGQANTTLKrwlldfaskrkeaelrsgiirnnslwdk 415
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 416 lifhkiqsslggKVRLMVTGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTA----GCSLTVPGDWTAghVGAPMPCSLI 490
Cdd:PLN02574 320 ------------SLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 491 KLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 570
Cdd:PLN02574 386 KVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIA 464
|
330
....*....|...
gi 309243088 571 PEKIENIyLRSEP 583
Cdd:PLN02574 465 PADLEAV-LISHP 476
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
269-592 |
4.94e-28 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 117.06 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 269 EDLAVICFTSGTTGNPKGAMITHRNVvsdcSAFVKVTDKTFSPSSDDTLISFLPLAH------MFERVVE-CVMLCHGAk 341
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH----WWSAIGSALNLGLTEDDNWLCALPLFHisglsiLMRSVIYgMTVYLVDK- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 igfFqgDIRLLMDDLKALQPTIFPVVPRLLNRMFDRIFGQANTTLkrwlldfaskrkeaelrsgiirnnslwdklifhki 421
Cdd:cd05912 152 ---F--DAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNL----------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 422 qsslggkvRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTEcTAGCSLTVPGDWTA---GHVGAPMPCSLIKLVDVEEm 498
Cdd:cd05912 192 --------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIEDDGQ- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 499 nylAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:cd05912 261 ---PPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
330
....*....|....
gi 309243088 579 LRSEPVAQVFVHGE 592
Cdd:cd05912 336 LSHPAIKEAGVVGI 349
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
265-599 |
8.06e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.60 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 265 PPAPE-DLAVICFTSGTTGNPKGAMITHRNVVSDcsAFVKVTDKTFSPSSDDTLISFLPLAHMF-ERVVECVMLCHGAKI 342
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSN--TLMGVQWLYNCKEGEEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 GFF-QGDIRLLMDDLKALQPTIFPVVPRLLNRMFdrifgqaNTTLkrwlldfaskRKEAELRSgiirnnslwdklifhki 421
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 422 qsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT------VPGDwtaghVGAPMPCSLIKLVDV 495
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNflwekrVPGS-----IGVPWPDTEAMIMSL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 496 EEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 575
Cdd:PRK06710 393 ETGEALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVE 470
|
330 340 350
....*....|....*....|....*....|.
gi 309243088 576 NIYLRSEPVAQVFV-------HGESLQAFLI 599
Cdd:PRK06710 471 EVLYEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
122-627 |
1.38e-27 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 116.33 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELslvfv 201
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALG--VGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 dkpekanlllegvenklipglKTIILMDSYGidllergkkcgveimsmkaledlgranRRKPKPpAPEDLAVICFTSGTT 281
Cdd:cd05903 75 ---------------------KVFVVPERFR---------------------------QFDPAA-MPDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVSDCSAFVKvtDKTFSPSsdDTLISFLPLAHMFERVvecvmlcHGAKIGFFQGDIRLLMDDLKALQp 361
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAE--RLGLGPG--DVFLVASPMAHQTGFV-------YGFTLPLLLGAPVVLQDIWDPDK- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 362 tifpvVPRLLNRmfDRI-FGQANTTLKRWLLDfASKRKEAELRSgiirnnslwdklifhkiqsslggkVRLMVTGAAPVS 440
Cdd:cd05903 174 -----ALALMRE--HGVtFMMGATPFLTDLLN-AVEEAGEPLSR------------------------LRTFVCGGATVP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 441 ATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGD-WTAGHV-GAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQ 518
Cdd:cd05903 222 RSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPeDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 519 GYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG---ESLQ 595
Cdd:cd05903 301 GYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLG 378
|
490 500 510
....*....|....*....|....*....|..
gi 309243088 596 AFLIAIVVPdvetlghwaqKRGFVGSFEELCR 627
Cdd:cd05903 379 ERACAVVVT----------KSGALLTFDELVA 400
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
81-695 |
2.79e-27 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 118.80 E-value: 2.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 81 EPLAYfyddVRTLYEGFQRGIRVSNNGPCLGSRKPDQPYEWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPE 160
Cdd:PTZ00297 421 NPLAG----VRSLGEMWERSVTRHSTFRCLGQTSESGESEWLTYGTVDARARELGSGLLALGVRPG--DVIGVDCEASRN 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 161 WVIIEQGCFAYSMVVVPLYDTLGTeaITYIINKGELSLVFVDKPEKANLLLEGVENklipgLKTIILMDS-YGIDLLERG 239
Cdd:PTZ00297 495 IVILEVACALYGFTTLPLVGKGST--MRTLIDEHKIKVVFADRNSVAAILTCRSRK-----LETVVYTHSfYDEDDHAVA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 240 KKCGVEIMSMKALEDLGRANRRKPKPPAPED----LAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVtdkTFSPSS-- 313
Cdd:PTZ00297 568 RDLNITLIPYEFVEQKGRLCPVPLKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLVMT---GVLPSSfk 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 314 DDTLISFLPLAHMFERVVECVMLCHGAKIGffQGDIRLLMDDLKALQPTIFPVVPRLlnrmfdriFGQANTTLKR----- 388
Cdd:PTZ00297 645 KHLMVHFTPFAMLFNRVFVLGLFAHGSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanery 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 389 -----WLLDfaskrKEAELRSGII----RNNSLWDKLIFHKIQSSLGGKVRLMVTGAAPVSATvltflraalgcqfyegY 459
Cdd:PTZ00297 715 savysWLFE-----RAFQLRSRLInihrRDSSLLRFIFFRATQELLGGCVEKIVLCVSEESTS----------------F 773
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 460 GQTECTAGCSltvpgdwtaghvgapMPCsliklvdVEEMNYLAAkgEGEVCVKG---PNVfQGYLK---DPAKTAE---- 529
Cdd:PTZ00297 774 SLLEHISVCY---------------VPC-------LREVFFLPS--EGVFCVDGtpaPSL-QVDLEpfdEPSDGAGigql 828
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 530 ALDKDGWL-HTGDI-GKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEPVAQVFVHGESLQAfLIAIVVPDVE 607
Cdd:PTZ00297 829 VLAKKGEPrRTLPIaAQWKRDRTLRLLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRD 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 608 TLG-HWAQKRGFV---GSFEELCRNKDVKKA---ILEDMLRLGRDAGLKSFEQVRGISLHPELFSIDNGLLTPTMKAKRP 680
Cdd:PTZ00297 908 TVEfEWRQSHCMGeggGPARQLGWTELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRD 987
|
650
....*....|....*
gi 309243088 681 ELRNYFRSQIDELYS 695
Cdd:PTZ00297 988 AVHSYFSSVIERFYS 1002
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
121-629 |
3.18e-27 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 115.86 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 121 WLSYKQVEDMSECVGSALIHKGFkaGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVF 200
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 201 VDKPekanlllegvenklipglktiilmdSYGIDLLERGKKcgveimsmkaledlgranRRKPKPPAPE-DLAVICFTSG 279
Cdd:cd12118 107 VDRE-------------------------FEYEDLLAEGDP------------------DFEWIPPADEwDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 280 TTGNPKGAMITHRnvvsdcSAFVkvtdktfspSSDDTLISF-----------LPLAHmfervveCVMLCHGAKIGFFQG- 347
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYL---------NALANILEWemkqhpvylwtLPMFH-------CNGWCFPWTVAAVGGt 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 -------DIRLLMDDLKALQPTIFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIRNNSlwdklifHK 420
Cdd:cd12118 202 nvclrkvDAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAP-------PS 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 IQSSLGGKVRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG----CSL-----TVPGDWTAG---HVGAPMPCS 488
Cdd:cd12118 242 DARPLPHRVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatvCAWkpewdELPTEERARlkaRQGVRYVGL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 489 L-IKLVDVEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQ 565
Cdd:cd12118 319 EeVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISG 396
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309243088 566 GEYIAPEKIENIylrsepvaqVFVHGESLQAFLIAivVPDvETLGHW-----AQKRGFVGSFEEL---CRNK 629
Cdd:cd12118 397 GENISSVEVEGV---------LYKHPAVLEAAVVA--RPD-EKWGEVpcafvELKEGAKVTEEEIiafCREH 456
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
120-591 |
3.97e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 115.73 E-value: 3.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 120 EWLSYKQVEDMSECVGSALIHK-GFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLydtlgteaiTYIINKGELSL 198
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYElNVKKGER--IAILSQNSLEYIVLLFAIAKVECIAVPL---------NIRLTENELIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 199 VFVDKpekanlllegvenklipGLKTIILMDSYGIDLLERGKKCGVE-IMSMKALEDLGRANRRKPKPPAPEDLAVICFT 277
Cdd:PRK06839 95 QLKDS-----------------GTTVLFVEKTFQNMALSMQKVSYVQrVISITSLKEIEDRKIDNFVEKNESASFIICYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 278 SGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMfervvecvmlchgAKIGFFqgdirllmddlk 357
Cdd:PRK06839 158 SGTTGKPKGAVLTQENMFWNALNNTFAIDLT----MHDRSIVLLPLFHI-------------GGIGLF------------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 358 ALqPTIFP----VVPRLLN-----RMFDR-----IFGQAntTLKRWLLDfASKRKEAELRSgiirnnslwdklifhkiqs 423
Cdd:PRK06839 209 AF-PTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 424 slggkVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCSLTVPGDW--TAGHVGAPMPCSLIKLVDvEEMNYL 501
Cdd:PRK06839 266 -----VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-ENKNKV 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 502 AAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRS 581
Cdd:PRK06839 339 EVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQVINKL 416
|
490
....*....|
gi 309243088 582 EPVAQVFVHG 591
Cdd:PRK06839 417 SDVYEVAVVG 426
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
120-609 |
4.09e-27 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 118.04 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 120 EWLSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCF----AYsmvvVPLYDTLGTEAITYIINKGE 195
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALG--VGPGDLVGVCLERSLEMVVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 196 LSLVFVDKPEKANLLLEGVEnklipglktIILMDSygidllergkkcgveimsmkalEDLGRANRRKPKPPA-PEDLAVI 274
Cdd:COG1020 574 ARLVLTQSALAARLPELGVP---------VLALDA----------------------LALAAEPATNPPVPVtPDDLAYV 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 275 CFTSGTTGNPKGAMITHRNVVSdcsaFVKVTDKTFSPSSDDTLISFLPLAH------MFervvecVMLCHGAKIGFFQGD 348
Cdd:COG1020 623 IYTSGSTGRPKGVMVEHRALVN----LLAWMQRRYGLGPGDRVLQFASLSFdasvweIF------GALLSGATLVLAPPE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 349 IRLLMDDLKAL----QPTIFPVVPRLLNRMFDRIFGQAnttlkrwlldfaskrkeAELRsgiirnnslwdklifhkiqss 424
Cdd:COG1020 693 ARRDPAALAELlarhRVTVLNLTPSLLRALLDAAPEAL-----------------PSLR--------------------- 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 425 lggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTV--PGDWTAGHV--GAPMPCSLIKLVDvEEMNy 500
Cdd:COG1020 735 -----LVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEvtPPDADGGSVpiGRPIANTRVYVLD-AHLQ- 807
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 501 LAAKG-EGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 572
Cdd:COG1020 808 PVPVGvPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIELG 886
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 309243088 573 KIENIyLRSEP-VAQ--VFVHGESLQA-FLIAIVVPDVETL 609
Cdd:COG1020 887 EIEAA-LLQHPgVREavVVAREDAPGDkRLVAYVVPEAGAA 926
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
122-577 |
6.85e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 115.59 E-value: 6.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKG--DRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 D----KPEKANLLLEGVEN--KLIPGLKTIILMDSYGIDLLERGkkcgveimsMKALEDLgRANRRKPKPPAP---EDLA 272
Cdd:COG0365 118 AdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEG---------DLDWDEL-LAAASAEFEPEPtdaDDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 273 VICFTSGTTGNPKGAMITHRNVVSDCSAFVKvtdKTFSPSSDDTLISFLPLA----HMFervveCVM--LCHGAKIGFFQ 346
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVFWCTADIGwatgHSY-----IVYgpLLNGATVVLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 347 G-----DIRLLMDDLKALQPTIFPVVPRLLnRMfdrifgqanttLKRWLLDFASKRkeaelrsgiirnnSLwdklifhki 421
Cdd:COG0365 260 GrpdfpDPGRLWELIEKYGVTVFFTAPTAI-RA-----------LMKAGDEPLKKY-------------DL--------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 422 qSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWT-AGHVGAPMPCSLIKLVDvEEMNY 500
Cdd:COG0365 306 -SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD-EDGNP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 501 LAAKGEGEVCVKG--PNVFQGYLKDPAKTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 576
Cdd:COG0365 380 VPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAEIES 458
|
.
gi 309243088 577 I 577
Cdd:COG0365 459 A 459
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
112-605 |
9.02e-27 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 114.73 E-value: 9.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 112 SRKPDQPY-----EWLSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVI----IEQGCFAYsmvvVPLYDTL 182
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKG--VGPDTIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 183 GTEAITYIINKGELSLVFVDKPEKANLLLEGvenklipglkTIILMDSygidllergkkcgvEIMSMKALEDLGRANRrk 262
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENLEPVSK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 263 pkppaPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFvkvtDKTFSPSSDDTLISFLPLAhmFERVVEcvmlchgaki 342
Cdd:cd17655 136 -----SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWA----NKVIYQGEHLRVALFASIS--FDASVT---------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 gffqgdirllmddlkalqpTIFPvvPRLL-NRMFdrIFGQANTTLKRWLLDFASKRkeaelRSGIIRNNSLWDKLIFHkI 421
Cdd:cd17655 195 -------------------EIFA--SLLSgNTLY--IVRKETVLDGQALTQYIRQN-----RITIIDLTPAHLKLLDA-A 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 422 QSSLGGKVRLMVTGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCS--LTVPGDWTAGHV--GAPMPCSLIKLVDv 495
Cdd:cd17655 246 DDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYEPETDQQVSVpiGKPLGNTRIYILD- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 496 EEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 569
Cdd:cd17655 325 QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYRI 403
|
490 500 510
....*....|....*....|....*....|....*....
gi 309243088 570 APEKIENIYLRSEPVAQ--VFVH-GESLQAFLIAIVVPD 605
Cdd:cd17655 404 ELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
122-599 |
1.24e-26 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 113.34 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 dkpekanlllegvenklipglktiilmdsygidllergkkcGVEImsmkaledlgranrrkpkppapEDLAVICFTSGTT 281
Cdd:cd05935 80 -----------------------------------------GSEL----------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVSDCSAFVKVTDKTFSpssdDTLISFLPLAHM--FERVVECVMLCHGAKIGFFQGDIRLLMDDLKAL 359
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLTPS----DVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 360 QPTIFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnslwDKLIFHKIQSSLGGKVRLMVTGAAPV 439
Cdd:cd05935 173 KVTFWTNIPTMLV-----------------------------------------DLLATPEFKTRDLSSLKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 440 SATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQG 519
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 520 YLKDPAKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPVAQVFV------- 589
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|
gi 309243088 590 HGESLQAFLI 599
Cdd:cd05935 371 VGEEVKAFIV 380
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
122-604 |
1.35e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 114.77 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGElSLVFV 201
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLG--VGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 --------DKPEKANLLLEGvenklIPGLKTIILMDSYGIDLLERgkkcgveIMSMKALE---DLGR--ANRRkpkpPAP 268
Cdd:PRK13295 133 vpktfrgfDHAAMARRLRPE-----LPALRHVVVVGGDGADSFEA-------LLITPAWEqepDAPAilARLR----PGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 269 EDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMfervvecvmlchgakIGFFQGD 348
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLG----ADDVILMASPMAHQ---------------TGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 349 IRLLMddLKA---LQPTIFPVvprllnRMFDRI------FGQANTTlkrWLLDFASKRKEAELRSgiirnnslwdklifh 419
Cdd:PRK13295 258 MMPVM--LGAtavLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESGRPV--------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 420 kiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCSLTVPGD---WTAGHVGAPMPCSLIKLVDvE 496
Cdd:PRK13295 312 ---SSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVD-A 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 497 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 576
Cdd:PRK13295 383 DGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEA 459
|
490 500 510
....*....|....*....|....*....|.
gi 309243088 577 IYLRSEPVAQVFVHG---ESLQAFLIAIVVP 604
Cdd:PRK13295 460 LLYRHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
267-608 |
3.60e-26 |
|
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: 112.34 E-value: 3.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSdcsaFVKVTDKTFSPSSDDTLISFLPLAHMFervveCVM-----LCHGAk 341
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFSFDL-----SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 igffqgdirllmddlkalqpTIFPVvPRLLNRMFDRIF-GQANTTLKRWLldfaskrkeaelrsgiiRNNSLWDKLIFHK 420
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVWV-----------------STPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 --IQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLT-VPGDWTAGH----VGAPMPCSLIKLV 493
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIeVTPEVLDGYdrlpIGYAKPGAKLVIL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 494 DvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 570
Cdd:cd05945 287 D-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGYRIE 364
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 309243088 571 PEKIENIYLRSEPVAQVFV----HGESLQAfLIAIVVPDVET 608
Cdd:cd05945 365 LEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGA 405
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
114-616 |
4.89e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 112.95 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 114 KPDQPY-----EWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAIT 188
Cdd:PRK07786 30 QPDAPAlrflgNTTTWRELDDRVAALAGALSRRGVGFG--DRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 189 YIINKGELSLVFVDkPEKANLLlEGVENkLIPGLKTIILMDSYGIDllergkkcgveimSMKALEDLGRANRrKPKPPA- 267
Cdd:PRK07786 108 FLVSDCGAHVVVTE-AALAPVA-TAVRD-IVPLLSTVVVAGGSSDD-------------SVLGYEDLLAEAG-PAHAPVd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 -PEDL-AVICFTSGTTGNPKGAMITHRNVVSDCSAFVKvTDKTFSPSSddtlISFL--PLAHM--FERVVECVMLchGAK 341
Cdd:PRK07786 171 iPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLR-TNGADINSD----VGFVgvPLFHIagIGSMLPGLLL--GAP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 IgffqgdirlLMDDLKALQPTifpvvprllnrmfdrifgqanttlkrWLLDFAskrkEAELRSGIIRNNSLWDKLIFHKI 421
Cdd:PRK07786 244 T---------VIYPLGAFDPG--------------------------QLLDVL----EAEKVTGIFLVPAQWQAVCAEQQ 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 422 QSSLGGKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT-AGCSLTvpGD---WTAGHVGAPMPCSLIKLVDvE 496
Cdd:PRK07786 285 ARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEMSpVTCMLL--GEdaiRKLGSVGKVIPTVAARVVD-E 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 497 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 576
Cdd:PRK07786 362 NMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDLVRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVEN 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 309243088 577 IYLRSEPVAQVFVHGESLQAF---LIAIVVPD-------VETLGHWAQKR 616
Cdd:PRK07786 440 VLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEFLTDR 489
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
122-599 |
3.09e-25 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 108.96 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKG--DRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKpekanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppapEDLAVICFTSGTT 281
Cdd:cd05972 79 DA-----------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVSDCSAFVKVTDKtfspSSDD-------------TLISFL-PLAHMFervveCVMLCHGAKIgffqg 347
Cdd:cd05972 94 GLPKGVLHTHSYPLGHIPTAAYWLGL----RPDDihwniadpgwakgAWSSFFgPWLLGA-----TVFVYEGPRF----- 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 DIRLLMDDLKALQPTIFPVVPrllnrmfdrifgqanTTLKRWL-LDFASKRKEAelrsgiirnnslwdklifhkiqsslg 426
Cdd:cd05972 160 DAERILELLERYGVTSFCGPP---------------TAYRMLIkQDLSSYKFSH-------------------------- 198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 427 gkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGE 506
Cdd:cd05972 199 --LRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIID-DDGRELPPGEE 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 507 GEVCVKGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPV 584
Cdd:cd05972 276 GDIAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAV 353
|
490 500
....*....|....*....|..
gi 309243088 585 AQVFV-------HGESLQAFLI 599
Cdd:cd05972 354 AEAAVvgspdpvRGEVVKAFVV 375
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
122-591 |
5.25e-25 |
|
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: 109.14 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKagPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVF- 200
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 201 -VDKPekanlllegvenklipGLKTIILMdsygidllergkkcGVEIMSMKALEDLGRANRR----KPKPPAPEDLAVIC 275
Cdd:cd05923 107 aVDAQ----------------VMDAIFQS--------------GVRVLALSDLVGLGEPESAgpliEDPPREPEQPAFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 276 FTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFspSSDDTLISFLPLAHMfervvecvmlchgakIGFFQgdirLLMDD 355
Cdd:cd05923 157 YTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRH--GRHNVVLGLMPLYHV---------------IGFFA----VLVAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 356 LkALQPTIFPVvprllnRMFDRIfgqanttlkrwlldFASKRKEAELRSGIIRNNSLWDKLIFHKIQSSLGGK-VRLMVT 434
Cdd:cd05923 216 L-ALDGTYVVV------EEFDPA--------------DALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSsLRHVTF 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 435 GAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCSLTVPgDWTAGHVGAPMPCSLIKLVDV-EEMNYLAAKG-EGEVCVK 512
Cdd:cd05923 275 AGATMPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 513 --GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVH 590
Cdd:cd05923 352 aaADAAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVI 429
|
.
gi 309243088 591 G 591
Cdd:cd05923 430 G 430
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
263-575 |
5.92e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 109.13 E-value: 5.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 263 PKPPAPED-LAVICFTSGTTGNPKGAMITHRNVVSDCSAFvKVTDKTFSPSSddtlisFLPLAHMFERV--VECV--MLC 337
Cdd:PRK09088 128 DTPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQTAHNF-GVLGRVDAHSS------FLCDAPMFHIIglITSVrpVLA 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 338 HGAKI----GFFQGDIRLLMDDLkALQPTIFPVVPRllnrMFDRIFGQAnttlkrwllDFASkrkeAELRSgiirnnslw 413
Cdd:PRK09088 201 VGGSIlvsnGFEPKRTLGRLGDP-ALGITHYFCVPQ----MAQAFRAQP---------GFDA----AALRH--------- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 414 dklifhkiqsslggkVRLMVTGAAP-VSATVLTFLraALGCQFYEGYGQTEctAGCSLTVPGDWT-----AGHVGAPMPC 487
Cdd:PRK09088 254 ---------------LTALFTGGAPhAAEDILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 488 SLIKLVDVEEmNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 567
Cdd:PRK09088 315 VQTRVVDDQG-NDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGE 392
|
....*...
gi 309243088 568 YIAPEKIE 575
Cdd:PRK09088 393 NVYPAEIE 400
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
108-672 |
1.24e-24 |
|
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: 108.67 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 108 PCLGSRKPDQPYEWLSYKQVEDMSECVGSALIHKGFKAG-PenfVGIFAQNRPEWVIIEQGCF---AYSMVVVPLYDTLG 183
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLSAErP---LLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 184 TE--AITYIINKGELSLVFVDKPEKANLLLEGVenkLIPGLKTIIlmdSYGiDLLERGKKCGVEIMSMKALEDLGRANRR 261
Cdd:cd05921 89 QDlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVV---SRN-AVAGRGAISFAELAATPPTAAVDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 262 KpkppAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVtdKTFSPSSDDTLISFLPLAHMFervvecvmlchGAK 341
Cdd:cd05921 162 V----GPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQT--YPFFGEEPPVLVDWLPWNHTF-----------GGN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 IGF-----------------FQGDIRLLMDDLKALQPTIFPVVPrllnrmfdrifgqanttlKRWLLDFASKRKEAELRS 404
Cdd:cd05921 225 HNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVP------------------AGWEMLVAALEKDEALRR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 405 GIIRNnslwdklifhkiqsslggkVRLMVTGAAPVSATVLTFLRAaLGCQ-------FYEGYGQTECTAGCSLTVPGDWT 477
Cdd:cd05921 287 RFFKR-------------------LKLMFYAGAGLSQDVWDRLQA-LAVAtvgeripMMAGLGATETAPTATFTHWPTER 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 478 AGHVGAPMPCSLIKLVDVEemnylaakGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKI 553
Cdd:cd05921 347 SGLIGLPAPGTELKLVPSG--------GKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 554 IDRKKHIFKLAQGEYIA--PEKIENIYLRSEPVAQVFVHGESlQAFLIAIVVPDVETLghwaqkRGFVG----SFEELCR 627
Cdd:cd05921 419 DGRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLAC------RRLVGlqeaSDAEVLR 491
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 309243088 628 NKDVKKAILEDMLRLGRDAGLKSFEQVRgISLHPELFSIDNGLLT 672
Cdd:cd05921 492 HAKVRAAFRDRLAALNGEATGSSSRIAR-ALLLDEPPSIDKGEIT 535
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
48-647 |
1.28e-24 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 108.81 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 48 RPRALKPPcdlamqSVEV-AGSDGARrsaILDSDEPLAyfyDDVRTLYEGFQRGIRVSNNGPCLGSRKPDQPYEWLSYKQ 126
Cdd:PRK08180 7 RPVAFAPP------AVEVeRRADGTI---YLRSAEPLG---DYPRRLTDRLVHWAQEAPDRVFLAERGADGGWRRLTYAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 127 VEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPL---YDTLGT--EAITYIINKGELSLVFV 201
Cdd:PRK08180 75 ALERVRAIAQALLDRG--LSAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaYSLVSQdfGKLRHVLELLTPGLVFA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKPEKANLLLEGVEnklIPGLKTIILmdsygidlleRGKKCGVEIMSMKALEDLGRANRRKPKPPA--PEDLAVICFTSG 279
Cdd:PRK08180 153 DDGAAFARALAAVV---PADVEVVAV----------RGAVPGRAATPFAALLATPPTAAVDAAHAAvgPDTIAKFLFTSG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 280 TTGNPKGAMITHRNVVS------DCSAFVKvtdktfspSSDDTLISFLPLAHMFERVVEC-VMLCHGAKI---------G 343
Cdd:PRK08180 220 STGLPKAVINTHRMLCAnqqmlaQTFPFLA--------EEPPVLVDWLPWNHTFGGNHNLgIVLYNGGTLyiddgkptpG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 344 FFQGDIRllmdDLKALQPTIFPVVPR----LLNRMfdrifgqanttlkrwlldfaskRKEAELRSgiirnnslwdklifh 419
Cdd:PRK08180 292 GFDETLR----NLREISPTVYFNVPKgwemLVPAL----------------------ERDAALRR--------------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 420 kiqsSLGGKVRLMVTGAAPVSATVLTFL----RAALGCQ--FYEGYGQTEcTAGCSL--TVPGDwTAGHVGAPMPCSLIK 491
Cdd:PRK08180 331 ----RFFSRLKLLFYAGAALSQDVWDRLdrvaEATCGERirMMTGLGMTE-TAPSATftTGPLS-RAGNIGLPAPGCEVK 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 492 LVDVEemnylaakGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKIIDRKKHIFKLAQGE 567
Cdd:PRK08180 405 LVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDAVRFVdpadPERGLMFDGRIAEDFKLSSGT 476
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 568 YIA--PekieniyLRSE------PVAQ-VFVHGESlQAFLIAIVVPDVetlghwAQKRGFVG-----SFEELCRNKDVKK 633
Cdd:PRK08180 477 WVSvgP-------LRARavsagaPLVQdVVITGHD-RDEIGLLVFPNL------DACRRLAGlladaSLAEVLAHPAVRA 542
|
650
....*....|....
gi 309243088 634 AILEDMLRLGRDAG 647
Cdd:PRK08180 543 AFRERLARLNAQAT 556
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
270-607 |
1.01e-23 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 102.73 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 270 DLAVICFTSGTTGNPKGAMITHRNVVsdCSAFVkvTDKTFSPSSDDTLISFLPLAHMFERVVECVMLCHGAKigffqgdi 349
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANLQ--LIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 350 RLLM---DDLKALQ------PTIFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiIRNnslwdklifhk 420
Cdd:cd17637 69 NVVMekfDPAEALElieeekVTLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH----------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 iqsslggkvrlmVTGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMN 499
Cdd:cd17637 119 ------------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 500 YLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENI 577
Cdd:cd17637 182 PVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKV 259
|
330 340 350
....*....|....*....|....*....|
gi 309243088 578 YLRSEPVAQVFVHGeslqafliaivVPDVE 607
Cdd:cd17637 260 ILEHPAIAEVCVIG-----------VPDPK 278
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
113-611 |
2.27e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 104.66 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 113 RKPDQPYEW-----LSYKQVEDMSECVGSALIHK-GFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEA 186
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLQQEcGVRKG--DRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 187 ITYIINKGELSLVFVdkpekANLLLEGVEnKLI--PGLKTII-------LMDSYGID----LLERGKKCGVEIMSMKALE 253
Cdd:PRK08314 100 LAHYVTDSGARVAIV-----GSELAPKVA-PAVgnLRLRHVIvaqysdyLPAEPEIAvpawLRAEPPLQALAPGGVVAWK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 254 DLGRANRRkpkPPA----PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHmfer 329
Cdd:PRK08314 174 EALAAGLA---PPPhtagPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST----PESVVLAVLPLFH---- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 330 VVECVMLCHGAkigFFQGDIRLLMddlkalqptifpvvPR----LLNRMFDR---IFGQANTTLkrwLLDFaskrkeaeL 402
Cdd:PRK08314 243 VTGMVHSMNAP---IYAGATVVLM--------------PRwdreAAARLIERyrvTHWTNIPTM---VVDF--------L 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 403 RSGIIRNNSLwdklifhkiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCSLTVPGDwtaghvg 482
Cdd:PRK08314 295 ASPGLAERDL----------SSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-TMAQTHSNPPD------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 483 APMPCSL--------IKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEA---LDKDGWLHTGDIGKWLPNGTL 551
Cdd:PRK08314 353 RPKLQCLgiptfgvdARVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGRMDEEGYF 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 309243088 552 KIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQVFV-------HGESLQAFliaiVVPDVETLGH 611
Cdd:PRK08314 433 FITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPEARGK 494
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
69-605 |
5.06e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.42 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 69 DGARRS----AILDSDEPLAYFYDDVRTLyEGFQRGIRVSNNGPCLGSRKPDQPY-----EWLSYKQVEDMSECVGSALI 139
Cdd:PRK12316 1968 EDAQAAlgelALLDAGERQRILADWDRTP-EAYPRGPGVHQRIAEQAARAPEAIAvvfgdQHLSYAELDSRANRLAHRLR 2046
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 140 HKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVDKPEKANLLLEGvenkli 219
Cdd:PRK12316 2047 ARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPA------ 2118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 220 pglktiilmdsygidllergkkcGVEIMSMKALEDLGRANRRKPKPP-APEDLAVICFTSGTTGNPKGAMITHRNVVSDC 298
Cdd:PRK12316 2119 -----------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGSTGLPKGVAVSHGALVAHC 2175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 299 SAfvkvTDKTFSPSSDDTLISFLPLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDLKALQPtifpvvprllNRMFD 376
Cdd:PRK12316 2176 QA----AGERYELSPADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDELWDP----------EQLYD 2230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 377 RIFGQANTtlkrwLLDFASkrkeaelrsgiirnnSLWDKLIFHKIQSSLGGKVRLMVTGAAPVSATVLTFLRAALGCQF- 455
Cdd:PRK12316 2231 EMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYl 2290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 456 YEGYGQTECTagcslTVPGDWTAGHV------GAPMPCSLIKL---VDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAK 526
Cdd:PRK12316 2291 FNGYGPTEAV-----VTPLLWKCRPQdpcgaaYVPIGRALGNRrayILDADLNLLAPGMAGELYLGGEGLARGYLNRPGL 2365
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 527 TAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFV---HGESLQA 596
Cdd:PRK12316 2366 TAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVREAVVvaqDGASGKQ 2444
|
....*....
gi 309243088 597 fLIAIVVPD 605
Cdd:PRK12316 2445 -LVAYVVPD 2452
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
268-592 |
6.10e-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: 101.02 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMFERVVECVMLchgakigFFQG 347
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 DIRLLMDDLKALQPTIFPVVPRLLNRMfdRIfgQANTTLKRWLLDFASKRKEAELrsgiirnnslwdklifhkiqSSLgg 427
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 428 kvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVP-GDWTAGHVGAPMPCSLIKLVDVE-EMNYL--AA 503
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 504 KGE-GEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSE 582
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330
....*....|
gi 309243088 583 PVAQVFVHGE 592
Cdd:cd05944 280 AVAFAGAVGQ 289
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
122-616 |
1.45e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 101.58 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKG--DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DkpekanlllEGVENKLIPGLKTIIlmdsygidllergkkcgveimsmkalEDLGRANRRKPKPPAPEDL---AVICFTS 278
Cdd:PRK03640 106 D---------DDFEAKLIPGISVKF--------------------------AELMNGPKEEAEIQEEFDLdevATIMYTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 279 GTTGNPKGAMITHRN----VVSdcSAF-VKVTDktfspssDDTLISFLPLAH------MFERVVecvmlcHGAKIGFFQG 347
Cdd:PRK03640 151 GTTGKPKGVIQTYGNhwwsAVG--SALnLGLTE-------DDCWLAAVPIFHisglsiLMRSVI------YGMRVVLVEK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 -DIRLLMDDLKALQPTIFPVVPRLLNRMFDRIfGQANTtlkrwlldfaskrkeaelrsgiirNNSLwdklifhkiqsslg 426
Cdd:PRK03640 216 fDAEKINKLLQTGGVTIISVVSTMLQRLLERL-GEGTY------------------------PSSF-------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 427 gkvRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCSLTVPGDWTA---GHVGAPM-PCSlIKLVDveEMNYLA 502
Cdd:PRK03640 257 ---RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 503 AKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSE 582
Cdd:PRK03640 329 PFEEGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHP 406
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 309243088 583 PVAQVFVHGESLQ-------AFLIAIVVPDVETLGHWAQKR 616
Cdd:PRK03640 407 GVAEAGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
122-611 |
1.64e-22 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 101.78 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVfV 201
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGER--VAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKPEKANLLLEGVENklIPGLKTIILMDSYGIDlleRGKKCGVEIMSMKALEDLGRANRrkPKPPAPEDLAVICFTSGTT 281
Cdd:TIGR03098 103 TSSERLDLLHPALPG--CHDLRTLIIVGDPAHA---SEGHPGEEPASWPKLLALGDADP--PHPVIDSDMAAILYTSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDTLISFLPLAhmfervvecvmlchgakigffqgdirllmddlkalqp 361
Cdd:TIGR03098 176 GRPKGVVLSHRNLV----AGAQSVATYLENRPDDRLLAVLPLS------------------------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 362 tifpvvprllnrmFDRIFGQANTTL----KRWLLDFASKRK-----EAELRSGIIRNNSLWDKLIFHKIQSSLGGKVRLM 432
Cdd:TIGR03098 215 -------------FDYGFNQLTTAFyvgaTVVLHDYLLPRDvlkalEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 433 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTEctAGCSLTVPG---DWTAGHVGAPMPCSLIkLVDVEEMNYLAAKGEGE 508
Cdd:TIGR03098 282 TNSGGAMPRATLSRLRSFLPnARLFLMYGLTE--AFRSTYLPPeevDRRPDSIGKAIPNAEV-LVLREDGSECAPGEEGE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 509 VCVKGPNVFQGYLKDPAKTAEALDK----DGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:TIGR03098 359 LVHRGALVAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEV 437
|
490 500 510
....*....|....*....|....*....|....
gi 309243088 578 YLRSEPVAQVFVHGeslqafliaivVPDVeTLGH 611
Cdd:TIGR03098 438 AYATGLVAEAVAFG-----------VPDP-TLGQ 459
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
120-584 |
2.95e-22 |
|
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: 101.16 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 120 EWLSYKQVEDMSECVGSALIHKGfKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEA---ITYIINKGEL 196
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG-KPGDR--VLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 197 SLVFVDKPEKANLLLEGVENKLIPGLKTIilmdsyGIDLLErgkkcgveimsmkaledLGRANRRKPKPPAPEDLAVICF 276
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLL------VVDLLP-----------------DTSAADWPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 277 TSGTTGNPKGAMITHRNVVSDCSAfvkvTDKTFSPSSDDTLISFLPLAH-MfervvecvmlchgakiGFFQGdirllmdd 355
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQ----IRRAYGLDPGDVVVSWLPLYHdM----------------GLIGG-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 356 lkALQPtifpvvprllnrmfdrIFGQANTTL----------KRWL-----------------LDFASKRKEAELRSGIir 408
Cdd:cd05931 209 --LLTP----------------LYSGGPSVLmspaaflrrpLRWLrlisryratisaapnfaYDLCVRRVRDEDLEGL-- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 409 nnslwDkLifhkiqsslgGKVRLMVTGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECTAGCSLTVPG-------- 474
Cdd:cd05931 269 -----D-L----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATLFVSGGPPGtgpvvlrv 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 475 --DWTAGHV----------------GAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE------A 530
Cdd:cd05931 333 drDALAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaA 412
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 309243088 531 LDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPV 584
Cdd:cd05931 413 TDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
265-605 |
3.78e-22 |
|
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: 100.50 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 265 PPAPEDLAVICFTSGTTGNPKGAMITHRNVVSdcsaFVKVTDKTFSPSSDDTLISFLPLAhmFERVVECVM--LCHGAKI 342
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 GFFQGDIRLLMDDLKALqptifpvvprLLNRMFDRIFgqANTTLKRWLLdfaskrkEAELRSGiirnnslwdklifhkiq 422
Cdd:cd17651 206 VLPPEEVRTDPPALAAW----------LDEQRISRVF--LPTVALRALA-------EHGRPLG----------------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 423 sSLGGKVRLMVTGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCSLTVPGD---WTA-GHVGAPMPCSLIKLVDvE 496
Cdd:cd17651 250 -VRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD-A 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 497 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 570
Cdd:cd17651 328 ALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFRIE 406
|
330 340 350
....*....|....*....|....*....|....*...
gi 309243088 571 PEKIENIYLRSEPVAQ--VFVHGE-SLQAFLIAIVVPD 605
Cdd:cd17651 407 LGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGD 444
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
112-580 |
4.03e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 100.89 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 112 SRKPDQP-YEW----LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVP--------- 177
Cdd:PRK06178 44 RERPQRPaIIFyghvITYAELDELSDRFAALLRQRGVGAG--DRVAVFLPNCPQFHIVFFGILKLGAVHVPvsplfrehe 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 178 ----LYDTLGTEAITYIinkgelSLVFVDKPEKANLLLEGV----ENKLIPGLKTIILMDSYGIDLLErgkkCGVEIMSM 249
Cdd:PRK06178 122 lsyeLNDAGAEVLLALD------QLAPVVEQVRAETSLRHVivtsLADVLPAEPTLPLPDSLRAPRLA----AAGAIDLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 250 KALEDLGRANRRKPkpPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTdktFSPSSDDTLISFLPlahMFer 329
Cdd:PRK06178 192 PALRACTAPVPLPP--PALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVA---VVGGEDSVFLSFLP---EF-- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 330 vvecvmlchgakigFFQGDirllmdDLKALQPTIF--PVVprLLNRmfdrifgqanttlkrwlldfaskrkeaelrsgii 407
Cdd:PRK06178 262 --------------WIAGE------NFGLLFPLFSgaTLV--LLAR---------------------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 408 rnnslWDKLIF------HKIQSSLG---GKVRLMVTGAapVSATVLTFL--------------------RAALGCQFYEG 458
Cdd:PRK06178 286 -----WDAVAFmaaverYRVTRTVMlvdNAVELMDHPR--FAEYDLSSLrqvrvvsfvkklnpdyrqrwRALTGSVLAEA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 459 -YGQTEcTAGCSltvpgDWTAG-------------HVGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDP 524
Cdd:PRK06178 359 aWGMTE-THTCD-----TFTAGfqdddfdllsqpvFVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKP 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 309243088 525 AKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLR 580
Cdd:PRK06178 433 EATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV-NGMSVFPSEVEALLGQ 486
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
269-600 |
5.64e-22 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 99.46 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 269 EDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKvtdKTFSPSSDDTLISflpLAHMFErvveCVMLCHGAKIGFFQGD 348
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 349 IRLLMDD----------LKALQPTIFPVVPRLlnrmfdrifgqanttlkrwlldFASKRKEAELRSGIIRNnslwdklif 418
Cdd:cd05919 161 SAVLNPGwptaervlatLARFRPTVLYGVPTF----------------------YANLLDSCAGSPDALRS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 419 hkiqsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEM 498
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 499 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 578
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*....
gi 309243088 579 LRSEPVAQVFV------HGES-LQAFLIA 600
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
48-672 |
6.12e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 100.51 E-value: 6.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 48 RPRALKPPcDLamqSVEVAGsDGarrSAILDSDEPLAyfyDDVRTLYEGFQRGIRVSNNGPCLGSRKPDQ-PYEWLSYKQ 126
Cdd:PRK12582 17 RPLNWKPP-DI---SVERRA-DG---SIVIKSRHPLG---PYPRSIPHLLAKWAAEAPDRPWLAQREPGHgQWRKVTYGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 127 VEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPL---YDTLGTE--AITYIINKGELSLVFV 201
Cdd:PRK12582 86 AKRAVDALAQALLDLG--LDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMSHDhaKLKHLFDLVKPRVVFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKPEK-----ANLLLEGVE----NKLIPGLKTIILMDsygidLLERGKKCGVEimsmKALEDLGranrrkpkppaPEDLA 272
Cdd:PRK12582 164 QSGAPfaralAALDLLDVTvvhvTGPGEGIASIAFAD-----LAATPPTAAVA----AAIAAIT-----------PDTVA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 273 VICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDktFSPSSD-DTLISFLPLAHMFervvecvmlchGAKIGFfQGDIR- 350
Cdd:PRK12582 224 KYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRP--REPDPPpPVSLDWMPWNHTM-----------GGNANF-NGLLWg 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 351 ---LLMDDLKALqPTIFPVVPRLLNRMFDRIFGQANTTLKrwLLDFASKRKEAELRSgiirnnslwdkliFHKiqsslgg 427
Cdd:PRK12582 290 ggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDALRRS-------------FFK------- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 428 KVRLMVTGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGCSLTVpgDWTA---GHVGAPMPCSLIKLVDVEEm 498
Cdd:PRK12582 347 NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAPTTTGT--HWDTervGLIGLPLPGVELKLAPVGD- 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 499 NYlaakgegEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKIIDRKKHIFKLAQGEYIAPEKi 574
Cdd:PRK12582 423 KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPEKGLIFDGRVAEDFKLSTGTWVSVGT- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 575 eniyLR------SEPVAQ-VFVHGESlQAFLIAIVVPDVETLghwaqkRGFVG----SFEELCRNKDVkKAILEDMLRLG 643
Cdd:PRK12582 495 ----LRpdavaaCSPVIHdAVVAGQD-RAFIGLLAWPNPAAC------RQLAGdpdaAPEDVVKHPAV-LAILREGLSAH 562
|
650 660
....*....|....*....|....*....
gi 309243088 644 RDAGLKSFEQVRGISLHPELFSIDNGLLT 672
Cdd:PRK12582 563 NAEAGGSSSRIARALLMTEPPSIDAGEIT 591
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
122-619 |
6.40e-22 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 99.58 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWV-----IIEQGCfAYsmvvVPLYDTLGTEAITYIINKGEL 196
Cdd:cd12117 23 LTYAELNERANRLARRLRAAG--VGPGDVVGVLAERSPELVvallaVLKAGA-AY----VPLDPELPAERLAFMLADAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 197 SLVFVDKPEKANLllegvenkliPGLKTIILMDsygidllergkkcgveimsmkalEDLGRANRRKPKPPA-PEDLAVIC 275
Cdd:cd12117 96 KVLLTDRSLAGRA----------GGLEVAVVID-----------------------EALDAGPAGNPAVPVsPDDLAYVM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 276 FTSGTTGNPKGAMITHRNVVSdcsaFVKVTD-KTFSPssDDTLISFLPL---AHMFERVVEcvmLCHGAkigffqgdiRL 351
Cdd:cd12117 143 YTSGSTGRPKGVAVTHRGVVR----LVKNTNyVTLGP--DDRVLQTSPLafdASTFEIWGA---LLNGA---------RL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 352 LMDDlkalqptifPVVPRLLNRMFDRIFGQANTTLkrWLldfaskrkEAELrsgiirnnslwdkliFHKI----QSSLGG 427
Cdd:cd12117 205 VLAP---------KGTLLDPDALGALIAEEGVTVL--WL--------TAAL---------------FNQLadedPECFAG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 428 kVRLMVTGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCSLTVPGDWTAGHV--GAPMPCSLIKLVDveEMNYLA 502
Cdd:cd12117 251 -LRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIANTRVYVLD--EDGRPV 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 503 AKGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 575
Cdd:cd12117 328 PPGVpGELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIE 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 309243088 576 NIYLRSEPVAQVFV---HGESLQAFLIAIVVPDvETLGHwAQKRGFV 619
Cdd:cd12117 407 AALRAHPGVREAVVvvrEDAGGDKRLVAYVVAE-GALDA-AELRAFL 451
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
113-589 |
1.28e-21 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 99.06 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 113 RKPDQPY-----EWLSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAI 187
Cdd:PRK06155 33 RYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVKRGDR--VALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 188 TYIINKGELSLVFVDkpekANLL--LEGVENKLIPgLKTIILMDSYGIDLLERGkkcgVEIMSMKALedlgrANRRKPKP 265
Cdd:PRK06155 111 EHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAG----WSTAPLPPL-----DAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 266 PAPEDLAVICFTSGTTGNPKGAMITH-------RNVVSDcsafVKVTDktfspssDDTLISFLPLAH-----MFERVvec 333
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAED----LEIGA-------DDVLYTTLPLFHtnalnAFFQA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 334 vmLCHGAKI---------GFFqgdirllmDDLKALQPTIF----PVVPRLLnrmfdrifgqanttlkrwlldfaSKRKEA 400
Cdd:PRK06155 243 --LLAGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL-----------------------SQPARE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 401 ELRSgiirnnslwdklifHKIQSSLGGKVrlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDwTAGH 480
Cdd:PRK06155 290 SDRA--------------HRVRVALGPGV----------PAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 481 VGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKG--PNVF-QGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK 557
Cdd:PRK06155 345 MGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRI 422
|
490 500 510
....*....|....*....|....*....|...
gi 309243088 558 KHIFKlAQGEYIAPEKIENIyLRSEP-VAQVFV 589
Cdd:PRK06155 423 KDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
54-606 |
1.39e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 101.01 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 54 PPCDLAmqsvEVAGSDGARRSAILDSDEPLAYFYDDvRTLYEGFQRGIRVSNNGPCLGSRKpdqpyEWLSYKQVEDMSEC 133
Cdd:PRK12467 480 PRRRLG----ELPLLDAEERARELVRWNAPATEYAP-DCVHQLIEAQARQHPERPALVFGE-----QVLSYAELNRQANR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 134 VGSALIHKGfkAGPENFVGIFAQNRPEWVI----IEQGCFAYsmvvVPLYDTLGTEAITYIINKGELSLVfvdkpekanl 209
Cdd:PRK12467 550 LAHVLIAAG--VGPDVLVGIAVERSIEMVVgllaVLKAGGAY----VPLDPEYPQDRLAYMLDDSGVRLL---------- 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 210 llegvenklipglktiiLMDSYGIDLLERgkKCGVEIMSMKALEDL--GRANRRKPKPPAPEDLAVICFTSGTTGNPKGA 287
Cdd:PRK12467 614 -----------------LTQSHLLAQLPV--PAGLRSLCLDEPADLlcGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGV 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 288 MITHRNVVSdcsaFVKVTDKTFSPSSDDTLISFLPLAHMFERVVECVMLCHGAKIgffqgdirLLMDDLKALQPTIFpvv 367
Cdd:PRK12467 675 AISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDCARDAEAF--- 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 368 prllnrmFDRIFGQANTTLKRwlldfaskrkeaelrsgiirNNSLWDKLIFHKIQSSLGGKVRLMVTGAA-PVSATVLTF 446
Cdd:PRK12467 740 -------AALMADQGVTVLKI--------------------VPSHLQALLQASRVALPRPQRALVCGGEAlQVDLLARVR 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 447 lRAALGCQFYEGYGQTECTAGCSL----TVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLK 522
Cdd:PRK12467 793 -ALGPGARLINHYGPTETTVGVSTyelsDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIGGAGLARGYHR 870
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 523 DPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFV--HGES 593
Cdd:PRK12467 871 RPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVREAVVlaQPGD 949
|
570
....*....|...
gi 309243088 594 LQAFLIAIVVPDV 606
Cdd:PRK12467 950 AGLQLVAYLVPAA 962
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
270-611 |
1.46e-21 |
|
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: 96.25 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 270 DLAVICFTSGTTGNPKGAMITHRNVVSdcSAfvKVTDKTFSPSSDDTLISFLPLAHM--FERVVECVMLchGAKIGFFQG 347
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--AGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 DiRLLMDDLKALQPTIFPVVPRLLNRMFDRifGQANTTLKRwlldfaskrkeaelrsgiirnnslwdklifhkiqsslgg 427
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 428 kVRLMVTGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDveemnylaakgEG 507
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 508 EVCVKGPNVFQGYLKDPakTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQV 587
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340
....*....|....*....|....
gi 309243088 588 FVHGeslqafliaivVPDvETLGH 611
Cdd:cd17630 257 FVVG-----------VPD-EELGQ 268
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
260-586 |
1.77e-21 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 99.40 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 260 RRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDktFSPssDDTLISFLPLAHMFERVVECVM-LCH 338
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIAD--FTP--NDRFMSALPLFHSFGLTVGLFTpLLT 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 339 GAKIGFFQgdirllmddlkalQPTIFPVVPRLLnrmFDR----IFGQAnTTLKRWL-----LDFAskrkeaelrsgiirn 409
Cdd:PRK08043 432 GAEVFLYP-------------SPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA--------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 410 nslwdklifhkiqsslggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSL 489
Cdd:PRK08043 480 ------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMD 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 490 IKLVDVEEMnylaAKGeGEVCVKGPNVFQGYLK--DP-------AKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:PRK08043 542 ARLLSVPGI----EQG-GRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRF 616
|
330 340
....*....|....*....|....*.
gi 309243088 561 FKLAqGEYIAPEKIENIYLRSEPVAQ 586
Cdd:PRK08043 617 AKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
122-683 |
1.83e-21 |
|
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: 98.60 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKagPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DkPEKANLLLEGVEnKLIPGLKTIILMDSYGIDLLErgkkcgveimsmKALEDL--GRANRRKPKPPAPEDLAVICFTSG 279
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGPEAGA------------LLLAELvaAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 280 TTGNPKGAMITHRNVVSDCSAFVKVTDKTfspSSDDTLISFLPLAHMFErvvecvmLCHGAKIGFFQGDIRLLM------ 353
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYARNVLGI---REDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 354 ----DDLKALQPTIFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWdklifhkiQSSLGGKV 429
Cdd:cd05959 244 aavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAPNL--------PSRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 430 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEV 509
Cdd:cd05959 283 RLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 510 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQVFV 589
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 590 HGESLQAFLI---AIVVPdvetlghwaqKRGFVGSfeelcrnkdvkkAILEDMLRLGRDAGLKSFEQVRGISLHPELFSi 666
Cdd:cd05959 440 VGVEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRLAPYKYPRWIVFVDELPK- 496
|
570
....*....|....*..
gi 309243088 667 dngllTPTMKAKRPELR 683
Cdd:cd05959 497 -----TATGKIQRFKLR 508
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
123-599 |
2.04e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 97.50 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 123 SYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVD 202
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKG--DRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 203 kpekanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppAPEDLAVICFTSGTTG 282
Cdd:cd05971 86 ----------------------------------------------------------------GSDDPALIIYTSGTTG 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 283 NPKGAMITHRnVVSDCSAFVKVTDKTFSPSSDdtlISFLPlahmfervvecvmlchgAKIGFFQGdirlLMDdlkALQPT 362
Cdd:cd05971 102 PPKGALHAHR-VLLGHLPGVQFPFNLFPRDGD---LYWTP-----------------ADWAWIGG----LLD---VLLPS 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 363 IFPVVPRLLNRM--FDRifGQANTTLKRWLLDFASKRKEAeLRsgIIRnnslwdkliFHKIQSSLGG-KVRLMVTGAAPV 439
Cdd:cd05971 154 LYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLKHAQvKLRAIATGGESL 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 440 SATVLTFLRAALGCQFYEGYGQTEC---TAGCSLTVPGDwtAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPN- 515
Cdd:cd05971 220 GEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTPLPPGEVGEIAVELPDp 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 516 -VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPVAQVFV----- 589
Cdd:cd05971 297 vAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECLLKHPAVLMAAVvgipd 374
|
490
....*....|..
gi 309243088 590 --HGESLQAFLI 599
Cdd:cd05971 375 piRGEIVKAFVV 386
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
256-577 |
2.42e-21 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 99.65 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 256 GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDktFSPSsdDTLISFLPLAHMFERVVECVM 335
Cdd:PRK06814 780 GRFPLVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID--FSPE--DKVFNALPVFHSFGLTGGLVL 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 336 -LCHGAKIGFFQgdirllmddlkalQPTIFPVVPRLlnrmfdrIFgQANTTL----KRWLLDFASKRKEAELRSgiirnn 410
Cdd:PRK06814 856 pLLSGVKVFLYP-------------SPLHYRIIPEL-------IY-DTNATIlfgtDTFLNGYARYAHPYDFRS------ 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 411 slwdklifhkiqsslggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLI 490
Cdd:PRK06814 909 ------------------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEY 970
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 491 KLVDVEEMNylaaKGeGEVCVKGPNVFQGYLK-DPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYI 569
Cdd:PRK06814 971 RLEPVPGID----EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMI 1043
|
....*...
gi 309243088 570 APEKIENI 577
Cdd:PRK06814 1044 SLAAVEEL 1051
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
267-695 |
4.76e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 97.56 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKtfspSSDDTLISFLPLAHM--FERVVECVML--CHGAKI 342
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAIVGY----GEDDVYLHTAPLCHIggLSSALAMLMVgaCHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 GFfqgDIRLLMDDLKALQPTIFPVVPRLL------NRMfdRIFGQANTTLKRWLLDFASkrkeaeLRSGIIRNNslwdKL 416
Cdd:PLN02860 246 KF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRKILNGGGS------LSSRLLPDA----KK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 417 IF--HKIQSSLGgkvrlmVTGAApvsaTVLTFLRaalgcqFYEGYGQTECTAGCSLTVPGDWTAGH-----VGAPMPCSL 489
Cdd:PLN02860 311 LFpnAKLFSAYG------MTEAC----SSLTFMT------LHDPTLESPKQTLQTVNQTKSSSVHQpqgvcVGKPAPHVE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 490 IKLVDVEEMNylaakgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYI 569
Cdd:PLN02860 375 LKIGLDESSR------VGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENV 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 570 APEKIENIYLRSEPVAQVFVHGeSLQAFLIAIVVPDVETLGHW--------AQKRGFVGSFEEL---CRNKdvkkailed 638
Cdd:PLN02860 448 YPEEVEAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK--------- 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 309243088 639 mlrlgrdaGLKSFEQVRGISLHPELFSidnglLTPTMKAKRPELRNYFRSQIDELYS 695
Cdd:PLN02860 518 --------NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPS 561
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
113-591 |
1.93e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 95.34 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 113 RKPDQPY-----EWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAI 187
Cdd:PRK06145 14 RTPDRAAlvyrdQEISYAEFHQRILQAAGMLHARGIGQG--DVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 188 TYIINKGELSLVFVDKpekanlllegvENKLIPGLKT-IILMDSYGIDLLERGKKCGVEIMSMKaledlgranrrkpkPP 266
Cdd:PRK06145 92 AYILGDAGAKLLLVDE-----------EFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA--------------AV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVvsdcsaFVKVTDKTFS--PSSDDTLISFLPLAHmferVVEC-----VMLCHG 339
Cdd:PRK06145 147 APTDLVRLMYTSGTTDRPKGVMHSYGNL------HWKSIDHVIAlgLTASERLLVVGPLYH----VGAFdlpgiAVLWVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 340 akigffqGDIRLLMD-DLKALQPTIFP-------VVPRLLNRMFdrifgqanTTLKRWLLDFASKRkeaelrsgiirnns 411
Cdd:PRK06145 217 -------GTLRIHREfDPEAVLAAIERhrltcawMAPVMLSRVL--------TVPDRDRFDLDSLA-------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 412 lWdklifhkiqsSLGGkvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDW--TAGHVGAPMPCSL 489
Cdd:PRK06145 268 -W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREieKIGSTGRALAHVE 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 490 IKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYI 569
Cdd:PRK06145 330 IRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENI 406
|
490 500
....*....|....*....|..
gi 309243088 570 APEKIENIYLRSEPVAQVFVHG 591
Cdd:PRK06145 407 ASSEVERVIYELPEVAEAAVIG 428
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
122-610 |
2.54e-20 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 95.21 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAG-------PenfvgifaqNRPEWVIIeqgCFAYSMV-VVPLYdTL----GTEaITY 189
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGdrvvvqlP---------NVAEFVIV---FFALFRAgAIPVF-ALpahrRAE-ISH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 190 IINKGELS-LVFVDKPEKANL--LLEGVeNKLIPGLKTIILMDSYGidllergkkcgveimSMKALEDLGRANRRKPKP- 265
Cdd:COG1021 117 FAEQSEAVaYIIPDRHRGFDYraLAREL-QAEVPSLRHVLVVGDAG---------------EFTSLDALLAAPADLSEPr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 266 PAPEDLAVICFTSGTTGNPKgaMI--THR----NVV--SDCSAFvkvtdktfspSSDDTLISFLPLAHMFervvecVMLC 337
Cdd:COG1021 181 PDPDDVAFFQLSGGTTGLPK--LIprTHDdylySVRasAEICGL----------DADTVYLAALPAAHNF------PLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 338 HGAkIGFFQGDIRLLM------DDLKAL----QPTIFPVVPRLLNRMfdrifgqanttlkrwlLDFASKRKeAELrsgii 407
Cdd:COG1021 243 PGV-LGVLYAGGTVVLapdpspDTAFPLiereRVTVTALVPPLALLW----------------LDAAERSR-YDL----- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 408 rnnslwdklifhkiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE----CTagcSLTVPGDWTAGHVGA 483
Cdd:COG1021 300 ---------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEglvnYT---RLDDPEEVILTTQGR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 484 PMpCSL--IKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HI 560
Cdd:COG1021 358 PI-SPDdeVRIVD-EDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQI 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 309243088 561 FKlaQGEYIAPEKIENIYLRSEPVAQVfvhgeslqafliAIV-VPDvETLG 610
Cdd:COG1021 436 NR--GGEKIAAEEVENLLLAHPAVHDA------------AVVaMPD-EYLG 471
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
268-608 |
4.68e-20 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 93.53 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDTLISFLPLAHMFErVVEcvM---LCHGAKIgf 344
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWE--IwgaLLHGGRL-- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 345 fqgdirLLMDDLKALQPTIFPvvpRLLNRMFDRIFGQANTTLKRWLldfaskrkEAELRsgiirnnslwdkliFHKIQSS 424
Cdd:cd17643 163 ------VVVPYEVARSPEDFA---RLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 425 LggkvRLMVTGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCSLTV--PGDW---TAGHVGAPMPCSLIKLVDvE 496
Cdd:cd17643 212 L----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRPldAADLpaaAASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 497 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 569
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 309243088 570 APEKIENIYLRSEPVAQVFV---HGESLQAFLIAIVVPDVET 608
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
254-604 |
6.25e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 93.80 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 254 DLGRANRRKPKPPAPEDL----AVICFTSGTTGNPKGAMITHRNVVSDCSAFvkVTDKTFSPSsdDTLISFLPLAHMFER 329
Cdd:PRK05852 157 HLDAATEPTPATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAI--ITGYRLSPR--DATVAVMPLYHGHGL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 330 VVECV-MLCHGAKI-----GFFQGdiRLLMDDLKALQPTIFPVVPrllnrmfdrifgqantTLKRWLLDFA----SKRKE 399
Cdd:PRK05852 233 IAALLaTLASGGAVllparGRFSA--HTFWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 400 AELRsgIIRNNSlwdklifhkiqsslggkvrlmvtgaAPVSATVLTFLRAALGCQFYEGYGQTECT----------AGCS 469
Cdd:PRK05852 295 AALR--FIRSCS-------------------------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 470 LTvPGDWT--AGHVGAPMpcslIKLVDVEEMNyLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLP 547
Cdd:PRK05852 348 EN-PVVSTglVGRSTGAQ----IRIVGSDGLP-LPAGAVGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSA 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 548 NGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPVAQVFVHGESLQAF---LIAIVVP 604
Cdd:PRK05852 421 AGDLSIRGRIKELINRG-GEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
122-605 |
7.02e-20 |
|
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: 93.49 E-value: 7.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKpekanlllegvenklipglktiilmdsygiDLLERGKKCGVEIMSMKALEDLGRANRRKPkPPAPEDLAVICFTSGTT 281
Cdd:cd17646 102 TA------------------------------DLAARLPAGGDVALLGDEALAAPPATPPLV-PPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVS---------DCSAFVKVTDKTfsPSSDDTLIS--FLPLAHMfERVVECVMLCHGakigffqgDIR 350
Cdd:cd17646 151 GRPKGVMVTHAGIVNrllwmqdeyPLGPGDRVLQKT--PLSFDVSVWelFWPLVAG-ARLVVARPGGHR--------DPA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 351 LLMDDLKALQPTIFPVVPRLLnrmfdRIFGQanttlkrwlldfaskrkeaELRSGIIRNnslwdklifhkiqsslggkVR 430
Cdd:cd17646 220 YLAALIREHGVTTCHFVPSML-----RVFLA-------------------EPAAGSCAS-------------------LR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 431 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSL-TVPGDWTAGHV--GAPMPCSLIKLVDvEEMNYLAAKGEG 507
Cdd:cd17646 257 RVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 508 EVCVKGPNVFQGYLKDPAKTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIyLRS 581
Cdd:cd17646 336 ELYLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAA-LAA 413
|
490 500
....*....|....*....|....*...
gi 309243088 582 EP-VAQVFV---HGESLQAFLIAIVVPD 605
Cdd:cd17646 414 HPaVTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
269-577 |
1.57e-19 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 90.40 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 269 EDLAVICFTSGTTGNPKGAMITHRNVVSdcsAFVKVTDKTFSPSSDDTLISFLPLAHMFERVVECVMLCHGAKIGFFqGD 348
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFA---VPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG-GE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 349 IRLLMDDLKALQ---PTIFPVVPRLLNRMfdrifgqanttlkrwLLDFASKRKEAElrsgiirnnslwdklifhkiqssl 425
Cdd:cd17635 77 NTTYKSLFKILTtnaVTTTCLVPTLLSKL---------------VSELKSANATVP------------------------ 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 426 ggKVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWT-AGHVGAPMPCSLIKLVDVEEMNYLAAk 504
Cdd:cd17635 118 --SLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSIeINAVGRPYPGVDVYLAATDGIAGPSA- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 309243088 505 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:cd17635 195 SFGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
251-575 |
3.09e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 91.60 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 251 ALEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDktFSPSSDdTLISFLPLAH-Mfer 329
Cdd:PRK07768 134 TVADLLAADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAE--FDVETD-VMVSWLPLFHdM--- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 330 vvecvmlchgAKIGFFQGDIRLLMDDLKaLQPTIFPVVPRLLNRMFDRIFGQ-------ANTTLKRwLLDFASKRKEAEL 402
Cdd:PRK07768 208 ----------GMVGFLTVPMYFGAELVK-VTPMDFLRDPLLWAELISKYRGTmtaapnfAYALLAR-RLRRQAKPGAFDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 403 rsgiirnnslwdklifhkiqSSLggkvRLMVTGAAPVS-ATVLTFLRA---------ALGCqfyeGYGQTECTAGCSLTV 472
Cdd:PRK07768 276 --------------------SSL----RFALNGAEPIDpADVEDLLDAgarfglrpeAILP----AYGMAEATLAVSFSP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 473 PGD--------------------WTAGHV------GAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLkDPAK 526
Cdd:PRK07768 328 CGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYL-TMDG 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 309243088 527 TAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 575
Cdd:PRK07768 406 FIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTDIE 453
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
268-618 |
3.16e-19 |
|
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: 90.99 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKV------TDKTFSPSSddtlISFLPLAHMFERVvecvmLCHGak 341
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREyeldsfPVRLLQMAS----FSFDVFAGDFARS-----LLNG-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 igffqGDIRLLMDDLKALQPTIFpvvpRLLNRMFDRIFgQANTTLKRWLLDFASKRKE--AELRSGIIRNNSLWDKLiFH 419
Cdd:cd17650 161 -----GTLVICPDEVKLDPAALY----DLILKSRITLM-ESTPALIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD-FK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 420 KIQSSLGGKVRLmvtgaapVSATVLTflRAALGCQFYEGYGQTECTAGcslTVPgdwtaghVGAPMPCSLIKLVDvEEMN 499
Cdd:cd17650 230 TLAARFGQGMRI-------INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERLQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 500 YLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 573
Cdd:cd17650 290 PQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELGE 368
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 309243088 574 IENIYLRSEPVAQVFV---HGESLQAFLIAIVVPDVETlgHWAQKRGF 618
Cdd:cd17650 369 IESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAELRAF 414
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
122-605 |
9.43e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 90.19 E-value: 9.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRG--DRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 -------DKPEkanlLLEGVENKLIPGLKTIILMDSYGIDLLERGKKCGVEIMSMKALEDLGRAnrrkPKPPAPEDLAVI 274
Cdd:PRK06164 114 wpgfkgiDFAA----ILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 275 CFT-SGTTGNPKGAMITHRNVVSDCSAFVKVtdktFSPSSDDTLISFLPLahmfervveCVMLCHGAKIGFFQGDIRLLM 353
Cdd:PRK06164 186 LFTtSGTTSGPKLVLHRQATLLRHARAIARA----YGYDPGAVLLAALPF---------CGVFGFSTLLGALAGGAPLVC 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 354 DDLKALQPTIfpvvpRLL-----------NRMFDRIFGQANTTLkrwllDFASKRkeaelrsgiirnnslwdklifhkiq 422
Cdd:PRK06164 253 EPVFDAARTA-----RALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR------------------------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 423 sslggkvRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCSL-TVPGDWTAGHV--GAPM-PCSLIKLVDVEEM 498
Cdd:PRK06164 298 -------LFGFASFAPALGELAALARAR-GVPLTGLYGSSEVQALVALqPATDPVSVRIEggGRPAsPEARVRARDPQDG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 499 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 578
Cdd:PRK06164 370 ALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAEIEHAL 448
|
490 500
....*....|....*....|....*....
gi 309243088 579 LRSEPVAQVFVHGESL--QAFLIAIVVPD 605
Cdd:PRK06164 449 EALPGVAAAQVVGATRdgKTVPVAFVIPT 477
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
174-591 |
1.40e-18 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 89.84 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 174 VVVPLYDTLGTEAITYIINKGELSLVFVDkPEKANLLLEGVENklIPGLKTIILMDSYGIDLLERGKKCGVEIMSMKALE 253
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAVVFIGPSDADSAAAHMPEGIKVYSYEALL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 254 DlGRANRRkPKPPAPEDLAV-ICFTSGTTGNPKGAMITHRNVVSDCSAfVKVTDkTFSPSSDDTLISFLPLAHmfervve 332
Cdd:PRK05620 167 D-GRSTVY-DWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLS-LRTTD-SLAVTHGESFLCCVPIYH------- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 333 cvMLCHGAKIGFFQGDIRLLMDDLKALQPTIFPVVprllnrmfdrifgqaNTTLKRwlldfaskrkeaeLRSGIirnNSL 412
Cdd:PRK05620 236 --VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKII---------------ATAMPR-------------VAHGV---PTL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 413 WDKLIFHKIQS-----SLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAP--- 484
Cdd:PRK05620 283 WIQLMVHYLKNppermSL----QEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPPSGVSGEARWAyrv 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 485 ----MPCSL-IKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKT----------------AEALDKDGWLHTGDIG 543
Cdd:PRK05620 359 sqgrFPASLeYRIVNDGQVMESTDRNEGEIQVRGNWVTASYYHSPTEEgggaastfrgedvedaNDRFTADGWLRTGDVG 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 309243088 544 KWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPVAQVFVHG 591
Cdd:PRK05620 439 SVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
174-599 |
1.83e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 89.36 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 174 VVVPLYDTLGTEAITYIINKGELSLVfVDKPEKANLLLEGVENKLIPgLKTIILMDSYGidllerGKKCGVeiMSMKALE 253
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLL-VTSAQFYPMYRQIQQEDATP-LRHICLTRVAL------PADDGV--SSFTQLK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 254 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVsdcsaFVKV-TDKTFSPSSDDTLISFLPLAHM-FERVV 331
Cdd:PRK08008 158 AQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLR-----FAGYySAWQCALRDDDVYLTVMPAFHIdCQCTA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 332 ECVMLCHGAKIGF--------FQGDIRllmdDLKAlqpTIFPVVPRLLNRM-------FDRifgqaNTTLKRWL--LDFA 394
Cdd:PRK08008 233 AMAAFSAGATFVLlekysaraFWGQVC----KYRA---TITECIPMMIRTLmvqppsaNDR-----QHCLREVMfyLNLS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 395 SKRKEA-ELRSGiirnnslwdklifhkiqsslggkVRLMVTgaapvsatvltflraalgcqfyegYGQTECTAGCSLTVP 473
Cdd:PRK08008 301 DQEKDAfEERFG-----------------------VRLLTS------------------------YGMTETIVGIIGDRP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 474 GD---WTAghVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKG---PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 547
Cdd:PRK08008 334 GDkrrWPS--IGRPGFCYEAEIRD-DHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDE 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 548 NGTLKIIDRKKHIFKLAqGEYIAPEKIENIyLRSEP-VAQVFVHG-------ESLQAFLI 599
Cdd:PRK08008 411 EGFFYFVDRRCNMIKRG-GENVSCVELENI-IATHPkIQDIVVVGikdsirdEAIKAFVV 468
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
116-584 |
2.09e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 88.70 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 116 DQPYEWLSYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPlydtlgteaityiinkge 195
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIKPGQE--VVFQITHNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 196 lslVFVDKPEKANLLLEGVENKLI-PGLktiilmdsygidllergkkcgveIMSMKALEDLgranrrkpkppaPEDLAVI 274
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWNTLKnPYL-----------------------ITEEEVLCEL------------ADELAFI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 275 CFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspsSDDTLISFLPLAHMFErvvecVMLCHGAKIgfFQGDIRLLMd 354
Cdd:cd05908 112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWK----TKDRILSWMPLTHDMG-----LIAFHLAPL--IAGMNQYLM- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 355 dlkalqPT-IFPVVPRLlnrmfdrifgqanttlkrWLLDfASKRKEAELRSGIIRNNSLWDKLIFHKIQSSLGGKVRLMV 433
Cdd:cd05908 180 ------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMIL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 434 TGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCSL----------------------------TVPGDWTAG 479
Cdd:cd05908 235 NGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKDSECLTFV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 480 HVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKH 559
Cdd:cd05908 315 EVGKPIDETDIRICD-EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREKD 392
|
490 500
....*....|....*....|....*
gi 309243088 560 IFkLAQGEYIAPEKIENIYLRSEPV 584
Cdd:cd05908 393 II-FVNGQNVYPHDIERIAEELEGV 416
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
122-605 |
2.54e-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: 88.48 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd12114 13 LTYGELAERARRVAGALKAAG--VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKPekanlllegVENKLIPGLKTIILmdsygidllergkkcgveimsmkALEDLGRANRRKPKPPAPEDLAVICFTSGTT 281
Cdd:cd12114 91 DGP---------DAQLDVAVFDVLIL-----------------------DLDALAAPAPPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHR---NVVSDcsafvkvTDKTFSPSSDDTLISFLPLAH------MFErvvecvMLCHGAKIGFFQGDIR-- 350
Cdd:cd12114 139 GTPKGVMISHRaalNTILD-------INRRFAVGPDDRVLALSSLSFdlsvydIFG------ALSAGATLVLPDEARRrd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 351 --LLMDDLKALQPTIFPVVPRLLNrMfdrifgqanttlkrwLLDfaskrkeaELRSGIIRNNSLwdKLIFHK---IQSSL 425
Cdd:cd12114 206 paHWAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL--RLVLLSgdwIPLDL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 426 GGKVRLMVTGAAPVSatvltflraaLGcqfyegyGQTEcTAGCSL-----TVPGDWTAGHVGAPMPCSLIKLVDveemny 500
Cdd:cd12114 260 PARLRALAPDARLIS----------LG-------GATE-ASIWSIyhpidEVPPDWRSIPYGRPLANQRYRVLD------ 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 501 laAKGE-------GEVCVKGPNVFQGYLKDPAKTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 569
Cdd:cd12114 316 --PRGRdcpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRI 392
|
490 500 510
....*....|....*....|....*....|....*...
gi 309243088 570 APEKIENIYLRSEPVAQ--VFVHGESLQAFLIAIVVPD 605
Cdd:cd12114 393 ELGEIEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
123-591 |
3.13e-18 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 88.71 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 123 SYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVD 202
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKG--DTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 203 KpekANLLLEGVEnKLIPGLKTIILMDSYGIDLLErgKKCGVEIMSMKALEDLGRanRRKPKPPAPEDLAVICFTSGTTG 282
Cdd:cd05970 127 A---EDNIPEEIE-KAAPECPSKPKLVWVGDPVPE--GWIDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 283 NPKgaMITHrnvvsdcsafvkvtDKTFspssddtlisflPLAHMFErvvecVMLCHGAKigffQGDIRLLMDDL---KAl 359
Cdd:cd05970 199 MPK--MVEH--------------DFTY------------PLGHIVT-----AKYWQNVR----EGGLHLTVADTgwgKA- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 360 qptifpvvprllnrMFDRIFGQANTTLKRWLLDFasKRKEAELRSGIIRNN---------SLWDKLIFHKIQSSLGGKVR 430
Cdd:cd05970 241 --------------VWGKIYGQWIAGAAVFVYDY--DKFDPKALLEKLSKYgvttfcappTIYRFLIREDLSRYDLSSLR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 431 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCSLTVPG-DWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEV 509
Cdd:cd05970 305 YCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIATFPWmEPKPGSMGKPAPGYEIDLID-REGRSCEAGEEGEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 510 CV---KGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYLRSEPV 584
Cdd:cd05970 383 VIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWMDEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAV 460
|
....*..
gi 309243088 585 AQVFVHG 591
Cdd:cd05970 461 LECAVTG 467
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
122-605 |
3.86e-18 |
|
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: 87.76 E-value: 3.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFkaGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGV--GPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DkpekanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppaPEDLAVICFTSGTT 281
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVsdcsAFVKVTDKTFSPssDD-------TLISF-LPLAHMFervvecVMLCHGAKIGFFQGDIRLLm 353
Cdd:cd12115 118 GRPKGVAIEHRNAA----AFLQWAAAAFSA--EElagvlasTSICFdLSVFELF------GPLATGGKVVLADNVLALP- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 354 dDLKALQP-TIFPVVPrllnrmfdrifgqantTLKRWLLDfaskrkeaelrsgiirnnslwdklifhkiQSSLGGKVRLM 432
Cdd:cd12115 185 -DLPAAAEvTLINTVP----------------SAAAELLR-----------------------------HDALPASVRVV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 433 VTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEV 509
Cdd:cd12115 219 NLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGEL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 510 CVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEP 583
Cdd:cd12115 298 YIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPG 376
|
490 500
....*....|....*....|....*
gi 309243088 584 VAQ--VFVHGESL-QAFLIAIVVPD 605
Cdd:cd12115 377 VREavVVAIGDAAgERRLVAYIVAE 401
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
225-608 |
1.39e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 86.66 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 225 IILMDSYGIDLLErGKKCGVEIMSMKALE--DLGRANRRKPKPPA---PEDLAVICFTSGTTGNPKGAMITHRNVVSdcs 299
Cdd:PRK07867 104 LVLTESAHAELLD-GLDPGVRVINVDSPAwaDELAAHRDAEPPFRvadPDDLFMLIFTSGTSGDPKAVRCTHRKVAS--- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 300 AFVKVTDKtFSPSSDDTLISFLPLAHMFERVVE-CVMLCHGAKI---------GFfqgdirllMDDLKALQPTIFPVVPR 369
Cdd:PRK07867 180 AGVMLAQR-FGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF--------LPDVRRYGATYANYVGK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 370 LLNrmfdrifgqanttlkrWLLDFASKRKEAElrsgiirnNSLwdklifhkiqsslggkvRLMV-TGAAPVSatVLTFlR 448
Cdd:PRK07867 251 PLS----------------YVLATPERPDDAD--------NPL-----------------RIVYgNEGAPGD--IARF-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 449 AALGCQFYEGYGQTEctAGCSLTVPGDWTAGHVGAPMPCslIKLVDVE--------------EMNYLAAKGEgEVCVKGP 514
Cdd:PRK07867 287 RRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrLLNADEAIGE-LVNTAGP 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 515 NVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHGesl 594
Cdd:PRK07867 362 GGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERILLRYPDATEVAVYA--- 436
|
410
....*....|....
gi 309243088 595 qafliaivVPDVET 608
Cdd:PRK07867 437 --------VPDPVV 442
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
267-614 |
7.28e-17 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 83.57 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAfvkvTDKTFSPSSDDTLISFLPLAhmFERVVECVM--LCHGAkigf 344
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQA----TAERYGLTPGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 345 fqgdiRLLMDDLKALQPtifpvvPRLLNRMFDR----IFGQANTTLKRWLLDFASKrkeaelrsgiirnnslwdklifhk 420
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADRT------------------------ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 iQSSLGGKVRLMVTGAAPVSAtvlTFLRAALGC--QFYEGYGQTECTAGCSLTV--PGDWTAGH---VGAPMPCSLIKLV 493
Cdd:cd17649 207 -GDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEATVTPLVWKceAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 494 DvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 566
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 309243088 567 EYIAPEKIENIYLRSEPVAQVFVHGES--LQAFLIAIVVP-DVETLGHWAQ 614
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVLrAAAAQPELRA 411
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
146-604 |
9.97e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 83.92 E-value: 9.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 146 GPENFVGIFAQNRPEwviIEQGCFAYSM---VVVPLYDTLGTEAITYIINKGELSLVFVDKpEKANLLLEGVenKLIPGL 222
Cdd:PLN03102 62 TKNDVVSVLAPNTPA---MYEMHFAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDR-SFEPLAREVL--HLLSSE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 223 KT-----IILMDSygIDLLERgkkcgveiMSMKALEDLGRANRRKPKPPA---------PEDLAVICFTSGTTGNPKGAM 288
Cdd:PLN03102 136 DSnlnlpVIFIHE--IDFPKR--------PSSEELDYECLIQRGEPTPSLvarmfriqdEHDPISLNYTSGTTADPKGVV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 289 ITHRNV-VSDCSAFVKVTDKTFSpssddTLISFLPLAHmfervvecvmlCHGAKIGF---FQGDIRLLMDDLKAlqPTIF 364
Cdd:PLN03102 206 ISHRGAyLSTLSAIIGWEMGTCP-----VYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMRHVTA--PEIY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 365 PVVprllnRMFDRIFGQANTTLKRWLLdfaskrkeaelrsgiiRNNSLwdklifhkIQSSLGGKVRLMVTGAAPVSATVL 444
Cdd:PLN03102 268 KNI-----EMHNVTHMCCVPTVFNILL----------------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 445 TFLRaaLGCQFYEGYGQTECTAGCSLTVPGD-WT------AGHVGAPMPCSLIKLVDVEEMNYLA-------AKGEGEVC 510
Cdd:PLN03102 319 KVQR--LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLADVDVKNKETqesvprdGKTMGEIV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 511 VKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIylrsepvaqVFVH 590
Cdd:PLN03102 397 IKGSSIMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKY 465
|
490
....*....|....
gi 309243088 591 GESLQAFLIAIVVP 604
Cdd:PLN03102 466 PKVLETAVVAMPHP 479
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
268-618 |
2.02e-16 |
|
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: 82.48 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspSSDDTLIsFLPLAhmFERVVE--CVMLCHGAKIgff 345
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGIT---SSDRVLQ-FASIA--FDVAAEeiYVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 qgdirllmddlkALQPtifpvvprllNRMFdrifgqanttlkRWLLDFASKRKEAELRSGIIrNNSLWDKLIFHKIQSSL 425
Cdd:cd17644 176 ------------VLRP----------EEMR------------SSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 426 GG--KVRLMVTGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCSLTVPGDWTAGH-----VGAPMPCSLIKLVDvE 496
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 497 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 568
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 309243088 569 IAPEKIENIYLRSEPVAQVFV---HGESLQAFLIAIVVPDVETLGHWAQKRGF 618
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
122-611 |
2.88e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 82.24 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPL---YdtlgTEA-ITYIINKGELS 197
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQG--LGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyrY----VEDeLRYLLDDSDAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 198 LVFVDK---PEKANLLLEgvenklIPGLKTIILMDSYGIDLLERGkkcGVEIMSMKALEDLGRAnrrkPKPPAPEDLAVI 274
Cdd:PRK07798 103 ALVYERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 275 CfTSGTTGNPKGAMITHRNVVSdcSAFVKVTDKTFSPSSDDTLISFLPLAHMFERVVECVMLCHGAK-----IGFFQGdi 349
Cdd:PRK07798 170 Y-TGGTTGMPKGVMWRQEDIFR--VLLGGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSG-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 350 rllmddlkalQPTIFPVVPRL-------------LNRMFdrIFGQAnttLKRWLLDFASKRKEAELrsgiirnnslwdkl 416
Cdd:PRK07798 245 ----------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL-------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 417 ifhkiqSSLggkvRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSLTVPGDwtAGHVGAP--MPCSLIKLV 493
Cdd:PRK07798 296 ------SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSETGFGGSGTVAKG--AVHTGGPrfTIGPRTVVL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 494 DvEEMNYLAAkGEGEVCV--KGPNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEY 568
Cdd:PRK07798 364 D-EDGNPVEP-GSGEIGWiaRRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEK 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 309243088 569 IAPEKIENIyLRSEP-VAQVFVHGeslqafliaivVPDvETLGH 611
Cdd:PRK07798 441 VFPEEVEEA-LKAHPdVADALVVG-----------VPD-ERWGQ 471
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
123-589 |
5.39e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 81.53 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 123 SYKQVEDMSECVGSALIHKGFkaGPENFVGIFAQNRPEWViieQGCFAYSM---VVVPLYDTLGTEAITYIINKGELSLV 199
Cdd:PRK08162 45 TWAETYARCRRLASALARRGI--GRGDTVAVLLPNIPAMV---EAHFGVPMagaVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 200 FVDkPEKANLLLEGVEnkLIPGLKtIILMDsygIDLLERGKKCGVEIMSMKALEDLGRANRrKPKPPAPE-DLAVICFTS 278
Cdd:PRK08162 120 IVD-TEFAEVAREALA--LLPGPK-PLVID---VDDPEYPGGRFIGALDYEAFLASGDPDF-AWTLPADEwDAIALNYTS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 279 GTTGNPKGAMITHR----NVVSDCSAFvkvtdkTFSPSSddTLISFLPLAHmfervveCVMLCH--------GAKIGFFQ 346
Cdd:PRK08162 192 GTTGNPKGVVYHHRgaylNALSNILAW------GMPKHP--VYLWTLPMFH-------CNGWCFpwtvaaraGTNVCLRK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 347 GDIRLLMDDLKALQPTIF---PVVPRLLnrmfdrifgqANTtlkrwlldfaskrkEAELRSGIirnnslwdklifhkiqs 423
Cdd:PRK08162 257 VDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEWRAGI----------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 424 slGGKVRLMVTGAAPVSAtVLTFLRAAlGCQFYEGYGQTEcTAGCSlTV---PGDWTA----------GHVGAPMPC-SL 489
Cdd:PRK08162 296 --DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTE-TYGPA-TVcawQPEWDAlplderaqlkARQGVRYPLqEG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 490 IKLVDVEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 567
Cdd:PRK08162 370 VTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYIKIKDRSKDII-ISGGE 447
|
490 500
....*....|....*....|..
gi 309243088 568 YIAPEKIENIYLRSEPVAQVFV 589
Cdd:PRK08162 448 NISSIEVEDVLYRHPAVLVAAV 469
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
268-616 |
7.14e-16 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 80.37 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKT--------FSPSSDdtlISFLPLahmfervveCVMLCHG 339
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGpgsrvlqfASPSFD---ASVWEL---------LMALLAG 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 340 AkigffqgdiRLLMDDLKALQPTifPVVPRLLNRmfDRIfgqANTTLKRWLLDFASKRKEAELRSgiirnnslwdklifh 419
Cdd:cd17652 160 A---------TLVLAPAEELLPG--EPLADLLRE--HRI---THVTLPPAALAALPPDDLPDLRT--------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 420 kiqsslggkvrLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAGCSLTVP-GDWTAGHVGAPMPCSLIKLVDvEEM 498
Cdd:cd17652 209 -----------LVVAGEACPAELVD---RWAPGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLD-ARL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 499 NYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 571
Cdd:cd17652 274 RPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-RGFRIEL 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 309243088 572 EKIENIYLRSEPVAQ--VFVHGESL-QAFLIAIVV------PDVETLGHWAQKR 616
Cdd:cd17652 353 GEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVpapgaaPTAAELRAHLAER 406
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
268-577 |
1.17e-15 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 80.63 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVtdktFSPSSDDTLISFLPLAHMFervvecvmlchgakiGFFQG 347
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 DIRLLMDDLkalqPTIF---PVVPRLLNRMFDR----IFGQANTTLKrWLLDFASKRKEA--ELRSGIIRNNSLWDKLif 418
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFD-YILKTAKKQESClpSLRFVVIGGDAFKDSL-- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 419 hkiqsslggkvrlmvtgaapVSATVLTFLRAALgcqfYEGYGQTECTAGCSL-TVPGDWTAGHVGAPMPCSLIKLVDvEE 497
Cdd:PRK06334 316 --------------------YQEALKTFPHIQL----RQGYGTTECSPVITInTVNSPKHESCVGMPIRGMDVLIVS-EE 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 498 MNYLAAKGE-GEVCVKGPNVFQGYL-KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 575
Cdd:PRK06334 371 TKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEALE 449
|
..
gi 309243088 576 NI 577
Cdd:PRK06334 450 SI 451
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
120-609 |
1.41e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 81.54 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 120 EWLSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIInkgelslv 199
Cdd:PRK12316 4575 EKLTYAELNRRANRLAHALIARG--VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMM-------- 4644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 200 fvdKPEKANLLLegVENKLIPGLKTIILMDSYGIDllergkkcgveimsmKALEDLGRANRRKPKPPAPEDLAVICFTSG 279
Cdd:PRK12316 4645 ---EDSGAALLL--TQSHLLQRLPIPDGLASLALD---------------RDEDWEGFPAHDPAVRLHPDNLAYVIYTSG 4704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 280 TTGNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDTLISFLPLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDLK 357
Cdd:PRK12316 4705 STGRPKGVAVSHGSLV----NHLHATGERYELTPDDRVLQFMSFS--FDGSHEGLYhpLINGA---------SVVIRDDS 4769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 358 ALQPtifpvvprllNRMFDRIFGQANTTLkrwllDFASkrkeaelrsgiirnnSLWDKLIFHKIQSSLGGKVRLMVTG-- 435
Cdd:PRK12316 4770 LWDP----------ERLYAEIHEHRVTVL-----VFPP---------------VYLQQLAEHAERDGEPPSLRVYCFGge 4819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 436 AAPVSATVLTFlRAALGCQFYEGYGQTECTAGCSL-TVPGDWTAG----HVGAPMPCSLIKLVDVEeMNYLAAKGEGEVC 510
Cdd:PRK12316 4820 AVAQASYDLAW-RALKPVYLFNGYGPTETTVTVLLwKARDGDACGaaymPIGTPLGNRSGYVLDGQ-LNPLPVGVAGELY 4897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 511 VKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIEnIYLRSEP 583
Cdd:PRK12316 4898 LGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFRIELGEIE-ARLREHP 4975
|
490 500 510
....*....|....*....|....*....|...
gi 309243088 584 -------VAQVFVHGeslqAFLIAIVVPDVETL 609
Cdd:PRK12316 4976 avreavvIAQEGAVG----KQLVGYVVPQDPAL 5004
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
270-600 |
2.27e-15 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 79.29 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 270 DLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTdktfSPSSDDTLISFLPLAHMFervvecVMLCHGAkIGFFQGDI 349
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVC----GLDQDTVYLAVLPAAHNF------PLACPGV-LGTLLAGG 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 350 RLLM------DDLKAL----QPTIFPVVPRLLnrmfdrifgqanttlKRWLlDFASKRKEAElrsgiirnnslwdklifh 419
Cdd:cd05920 209 RVVLapdpspDAAFPLiereGVTVTALVPALV---------------SLWL-DAAASRRADL------------------ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 420 kiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTE----CTAgcsLTVPGDWTAGHVGAPM-PCSLIKLVD 494
Cdd:cd05920 255 ---SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEgllnYTR---LDDPDEVIIHTQGRPMsPDDEIRVVD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 495 vEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 574
Cdd:cd05920 325 -EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEV 402
|
330 340 350
....*....|....*....|....*....|...
gi 309243088 575 ENIYLRSEPVAQVFV-------HGESLQAFLIA 600
Cdd:cd05920 403 ENLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
458-614 |
2.99e-15 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 77.34 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 458 GYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAkGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGW 536
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 309243088 537 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyLRSEP-VAQVFVhgeslqafliaIVVPDVEtlghWAQ 614
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAV-----------IGVPDPR----WAQ 280
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
246-588 |
3.53e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.79 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 246 IMSMKALEDLGRANRRKPKPPA---PEDLAVICFTSGTTGNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDTLISFLP 322
Cdd:PRK09274 148 LWGGTTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGIEPGEIDLPTFP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 323 LahmfervvecvMLCHGAKIGffqgdirllmddLKALQPTIFPVVPRLLN--RMFDRIFGQANTTLkrwlldFASKrkea 400
Cdd:PRK09274 224 L-----------FALFGPALG------------MTSVIPDMDPTRPATVDpaKLFAAIERYGVTNL------FGSP---- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 401 elrsgiirnnSLWDKLIFHKIQS--SLGGkVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCS------L 470
Cdd:PRK09274 271 ----------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEALPISSiesreiL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 471 TVPGDWT---AGH-VGAPMPCSLIKLVDV--------EEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEA--LDKDG- 535
Cdd:PRK09274 340 FATRAATdngAGIcVGRPVDGVEVRIIAIsdapipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAkiPDGQGd 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 309243088 536 -WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniylrSEPVAQVF 588
Cdd:PRK09274 420 vWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIF 462
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
265-611 |
1.18e-14 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 76.83 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 265 PPAPEDLAVICFTSGTTGNPKGAMITHR----NVVSDCSAFvkvtdkTFSPSsDDTLISfLPLAHmfervvecV------ 334
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQahlaSAEGVLSLM------PFTAQ-DSWLLS-LPLFH--------Vsgqgiv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 335 --MLCHGAKIGFfqGDIRLLMDDLkaLQPTIFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnsl 412
Cdd:PRK09029 195 wrWLYAGATLVV--RDKQPLEQAL--AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL--------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 413 wdklifhkiqsslGGkvrlmvtGAAPVSatvLTFLRAALGCQFYEGYGQTECTAgcslTV---PGDWTAGhVGAPMPCSL 489
Cdd:PRK09029 248 -------------GG-------AAIPVE---LTEQAEQQGIRCWCGYGLTEMAS----TVcakRADGLAG-VGSPLPGRE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 490 IKLVDveemnylaakgeGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYI 569
Cdd:PRK09029 300 VKLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGI 364
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 309243088 570 APEKIENIYLRSEPVAQVFVhgeslqafliaIVVPDVEtLGH 611
Cdd:PRK09029 365 QPEEIERVINQHPLVQQVFV-----------VPVADAE-FGQ 394
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
108-604 |
2.03e-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: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 108 PCLgsRKPDQpyEWlSYKQVEDMSECVGSALIHKGFKAgPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAI 187
Cdd:cd05958 2 TCL--RSPER--EW-TYRDLLALANRIANVLVGELGIV-PGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 188 TYIINKGELSLVFVDKPEKANlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgranrrkpkppa 267
Cdd:cd05958 76 AYILDKARITVALCAHALTAS----------------------------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 pEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKvtdKTFSPSSDDTLISFLPLAHMFER-VVECVMLCHGAKIGFFQ 346
Cdd:cd05958 97 -DDICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLE 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 347 GDI-RLLMDDLKALQPTIFPVVPRLLNRMFdrifgqanttlkrwlldfASKRKEAELRSGiirnnslwdklifhkiqssl 425
Cdd:cd05958 173 EATpDLLLSAIARYKPTVLFTAPTAYRAML------------------AHPDAAGPDLSS-------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 426 ggkVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKG 505
Cdd:cd05958 215 ---LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDGT 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 506 EGEVCVKGPNvfqGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPVA 585
Cdd:cd05958 291 IGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAVA 366
|
490 500
....*....|....*....|..
gi 309243088 586 QVFVHGESLQAFLI---AIVVP 604
Cdd:cd05958 367 ECAVVGHPDESRGVvvkAFVVL 388
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
253-605 |
3.07e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 75.85 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 253 EDLGRANRRKPKPPAPEDLAVIC---FTSGTTGNPKGAMITHRNVvsdcsAFVkVT----DKTFSPSSDDTLISFLPLAH 325
Cdd:PRK07470 144 EALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQM-----AFV-ITnhlaDLMPGTTEQDASLVVAPLSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 326 MfERVVECVMLCHGAKigffqgDIRLLMDDLKAlqPTIFPVVPRL-LNRMFdrifgQANTTLKRWLLDFASKRKEaelrs 404
Cdd:PRK07470 218 G-AGIHQLCQVARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD----- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 405 giirnnslwdklifhkiQSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGCsLTV-------PGDWT 477
Cdd:PRK07470 279 -----------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GN-ITVlppalhdAEDGP 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 478 AGHVGapmPCSL------IKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTL 551
Cdd:PRK07470 336 DARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFL 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 309243088 552 KIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHGeslqafliaivVPD 605
Cdd:PRK07470 411 YITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD 452
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
69-609 |
3.21e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 77.12 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 69 DGARRSAILDSDEPLAYFYDDVRTLYEGFQRGIRVSNNGPCL--GSRKpdqpyewLSYKQVEDMSECVGSALIHKGfkAG 146
Cdd:PRK12467 1552 DEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALvfGEQE-------LTYGELNRRANRLAHRLIALG--VG 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 147 PENFVGIFAQNRPEWVI----IEQGCFAYsmvvVPLYDTLGTEAITYIINKGELSLVFVDKPEKANL-LLEGVEnklipg 221
Cdd:PRK12467 1623 PEVLVGIAVERSLEMVVgllaILKAGGAY----VPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLpLPDGLR------ 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 222 lktIILMDSygidllergkkcgveimsmkalEDLGRANRRKPKP---PAPEDLAVICFTSGTTGNPKGAMITHRNVVsdc 298
Cdd:PRK12467 1693 ---SLVLDQ----------------------EDDWLEGYSDSNPavnLAPQNLAYVIYTSGSTGRPKGAGNRHGALV--- 1744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 299 sAFVKVTDKTFSPSSDDTLISFLPLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDlkalqptifPVVPRLLNRMFD 376
Cdd:PRK12467 1745 -NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGA---------RLVIAP---------PGAHRDPEQLIQ 1803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 377 RIFGQANTTlkrwlLDFASkrkeaelrsgiirnnSLWDKLIFHKIQSSLGGKVRLMVTG--AAPVSATVLTFlrAALG-C 453
Cdd:PRK12467 1804 LIERQQVTT-----LHFVP---------------SMLQQLLQMDEQVEHPLSLRRVVCGgeALEVEALRPWL--ERLPdT 1861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 454 QFYEGYGQTECTAG-----CSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTA 528
Cdd:PRK12467 1862 GLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIANLSTYILD-ASLNPVPIGVAGELYLGGVGLARGYLNRPALTA 1940
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 529 EAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENiYLRSEPV---AQVFVHGESLQAFL 598
Cdd:PRK12467 1941 ERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEA-RLREQGGvreAVVIAQDGANGKQL 2018
|
570
....*....|.
gi 309243088 599 IAIVVPDVETL 609
Cdd:PRK12467 2019 VAYVVPTDPGL 2029
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
268-615 |
5.32e-14 |
|
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: 74.90 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDC----SAF-VKVTDKTFSPSSddtlISFLPLA-HMFERvvecvmLCHGAK 341
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCewhrPYFgVTPADKSLVYAS----FSFDASAwEIFPH------LTAGAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 IGFFQGDIRLlmdDLKALqptifpvvprllnrmfDRIFGQANTTLKRWLLDFASKRKEAElrsgiirNNSLwdklifhki 421
Cdd:cd17645 173 LHVVPSERRL---DLDAL----------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL--------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 422 qsslggkvRLMVTGAAPVSATVLTflraalGCQFYEGYGQTECTAgCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEMNYL 501
Cdd:cd17645 218 --------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 502 AAKG-EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 574
Cdd:cd17645 283 QPIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEI 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 309243088 575 ENIYLRSEPVAQVFV-------HGESLQAFLIAIVVPDVETLGHWAQK 615
Cdd:cd17645 362 EPFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
421-589 |
9.37e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 73.76 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 IQSSLGG---KVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEE 497
Cdd:cd05974 191 IQQDLASfdvKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 498 mnylAAKGEGEVCV-----KGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPE 572
Cdd:cd05974 271 ----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SSDYRISPF 344
|
170
....*....|....*..
gi 309243088 573 KIENIYLRSEPVAQVFV 589
Cdd:cd05974 345 ELESVLIEHPAVAEAAV 361
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
433-599 |
2.55e-13 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 72.88 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 433 VTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVK 512
Cdd:cd05928 297 VTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIID-DNGNVLPPGTEGDIGIR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 513 -GPN----VFQGYLKDPAKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQV 587
Cdd:cd05928 376 vKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYRIGPFEVESALIEHPAVVES 453
|
170
....*....|....*....
gi 309243088 588 FV-------HGESLQAFLI 599
Cdd:cd05928 454 AVvsspdpiRGEVVKAFVV 472
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
123-577 |
2.57e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 73.20 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 123 SYKQVEDMSECVGSALIHKGFKAGPEnfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFVD 202
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDR--VGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 203 ---KPekanlLLEGVENKLiPGLKTIILM-DSygiDLLERGKkcgveiMSMKALEDL-GRANRRKPKPPAPEDLAV-ICF 276
Cdd:PRK07008 119 ltfLP-----LVDALAPQC-PNVKGWVAMtDA---AHLPAGS------TPLLCYETLvGAQDGDYDWPRFDENQASsLCY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 277 TSGTTGNPKGAMITHRNVVsdCSAFVKVTDKTFSPSSDDTLisfLPLAHMFErvVECVMLCH-----GAKIgffqgdirl 351
Cdd:PRK07008 184 TSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPYsapltGAKL--------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 352 lmddlkalqptIFPvvprllnrmfdrifGQAnttlkrwlLDFASKRK--EAELRSGIIRNNSLWDKLIFHKIQSSLG-GK 428
Cdd:PRK07008 248 -----------VLP--------------GPD--------LDGKSLYEliEAERVTFSAGVPTVWLGLLNHMREAGLRfST 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 429 VRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCSLT-----VPGD------WTAGHV--GAPMpcsliKL 492
Cdd:PRK07008 295 LRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKwkhsqLPLDeqrkllEKQGRViyGVDM-----KI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 493 VDVE--EMNYlAAKGEGEVCVKGPNVFQGYLKdpaKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIA 570
Cdd:PRK07008 370 VGDDgrELPW-DGKAFGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWIS 443
|
....*..
gi 309243088 571 PEKIENI 577
Cdd:PRK07008 444 SIDIENV 450
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-588 |
2.60e-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: 72.49 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 266 PAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFvkvtDKTFSPSSDDTLISFLPLAHMFervvecvmlchGAKIGff 345
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL----RQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 qgdirllmddLKALQPTIFPVVPrllnrmfdrifGQANttlKRWLLDFASKRKEaelrSGIIRNNSLWDKLIFHKIQSSL 425
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 426 G-GKVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCS------LTVPGDWTAGH----VGAPMPCSLIKL 492
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 493 VDVEEMNY--------LAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 560
Cdd:cd05910 277 IEIDDEPIaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*...
gi 309243088 561 FKLAQGEYIapekieniylrSEPVAQVF 588
Cdd:cd05910 357 VITTGGTLY-----------TEPVERVF 373
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
233-683 |
4.95e-13 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 72.02 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 233 IDLLERGKKCGVEIM--SMKALEDLGRANRRKPKPPAPEDLA--VICFTSGTTGNPKGAMITHrnvvsdcsafvkvtdkT 308
Cdd:cd05929 85 IEIKAAALVCGLFTGggALDGLEDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGL----------------P 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 309 FSPSSDDTLISF-LPLAHMFERVVECVM-LCHGAKIGFFQGDIRL-----LM---DDLKALQP------TIFPVVPRLLN 372
Cdd:cd05929 149 GGPPDNDTLMAAaLGFGPGADSVYLSPApLYHAAPFRWSMTALFMggtlvLMekfDPEEFLRLieryrvTFAQFVPTMFV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 373 RMfdrifgqanttLK-----RWLLDFASkrkeaeLRSgiirnnslwdklIFHkiqsslggkvrlmvtGAAPVSATVLTFL 447
Cdd:cd05929 229 RL-----------LKlpeavRNAYDLSS------LKR------------VIH---------------AAAPCPPWVKEQW 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 448 RAALGCQFYEGYGQTECTAGCSLTvPGDWTA--GHVGAPMPcSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQgYLKDPA 525
Cdd:cd05929 265 IDWGGPIIWEYYGGTEGQGLTIIN-GEEWLThpGSVGRAVL-GKVHILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 526 KTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG---ESLQAFLIAIV 602
Cdd:cd05929 341 KTAAARNEGGWSTLGDVGYLDEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 603 VPDVETlghwaqkrgfvgsfeelcrnkDVKKAILEDMLRLGRDAgLKSFEQVRGISLHPELFSIDNGlltptmKAKRPEL 682
Cdd:cd05929 420 QPAPGA---------------------DAGTALAEELIAFLRDR-LSRYKCPRSIEFVAELPRDDTG------KLYRRLL 471
|
.
gi 309243088 683 R 683
Cdd:cd05929 472 R 472
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
112-591 |
2.04e-12 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 70.17 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 112 SRKPDQPYEWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYII 191
Cdd:PRK06018 30 TRSVEGPIVRTTYAQIHDRALKVSQALDRDGIKLG--DRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWII 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 192 NKGELSLVFVDK---PekanlLLEGVENKLiPGLKTIILmdsygidLLERGKKCGVEIMSMKALED-LGRANRRKPKPPA 267
Cdd:PRK06018 108 NHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVV-------LTDAAHMPQTTLKNAVAYEEwIAEADGDFAWKTF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAV-ICFTSGTTGNPKGAMITHR-NVVSdcsAFVKVTDKTFSPSSDDTLISFLPLAH-------MFERVVECVMLCH 338
Cdd:PRK06018 175 DENTAAgMCYTSGTTGDPKGVLYSHRsNVLH---ALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAPSMGTKLVMP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 339 GAKIGffQGDIRLLMDDLKAlqpTIFPVVPRLlnrmfdrifgqanttlkrWLLDFASKRKEaelrsgiirnnslwDKLIF 418
Cdd:PRK06018 252 GAKLD--GASVYELLDTEKV---TFTAGVPTV------------------WLMLLQYMEKE--------------GLKLP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 419 HKIQSSLGGkvrlmvtgaapvSATVLTFLRA--ALGCQFYEGYGQTECTAGCSL--------TVPGDWTAGHV---GAPM 485
Cdd:PRK06018 295 HLKMVVCGG------------SAMPRSMIKAfeDMGVEVRHAWGMTEMSPLGTLaalkppfsKLPGDARLDVLqkqGYPP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 486 PCSLIKLVDvEEMNYLAAKGE--GEVCVKGPNVFQGYLKdpaKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKl 563
Cdd:PRK06018 363 FGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMRITDRSKDVIK- 437
|
490 500
....*....|....*....|....*...
gi 309243088 564 AQGEYIAPEKIENIYLRSEPVAQVFVHG 591
Cdd:PRK06018 438 SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
268-609 |
4.47e-12 |
|
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: 68.58 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKvtdKTFSPSSDDTLISFLPlAHMFERVVE--CVMLCHGAKIGFF 345
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSE---RYFGRDNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 QGDIRLLMDDLKAL----QPTIFPVVPRLLNRM-FDRIfgqanTTLKRWLL---DFASKRkeaelrsgiirnnslwdkli 417
Cdd:cd17648 169 PDEMRFDPDRFYAYinreKVTYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV-------------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 418 FHKIQSSLGGkvrLMVTGAAPVSATVLTFLRaalgcqFYEGYGQTECTagcsltvpgdwtaghVGAPMPCSLIKLVDvEE 497
Cdd:cd17648 224 FEKLRSRFAG---LIINAYGPTETTVTNHKR------FFPGDQRFDKS---------------LGRPVRNTKCYVLN-DA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 498 MNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:cd17648 279 MKRVPVGAVGELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQVKI 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 309243088 564 aQGEYIAPEKIENIYLRSEPVAQVFV--------HGESLQAFLIAIVVPDVETL 609
Cdd:cd17648 359 -RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
270-591 |
4.88e-12 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 68.53 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 270 DLAVICFTSGTTGNPKGAMITHRNVVSdCSAFVKVTDKTFSpssDDTLISFLPLAHMFERVVE-CVMLCHGAKIGF---F 345
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWR-GGAFFAGSGGALP---SDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 QGdiRLLMDDLKALQPTIFPVVPRLLnrmfdrifgqanttlkRWLLdfASKRKEAELRsgiirnnslwdklifHKIQSSL 425
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 426 GGKVRLMVTGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGcSLTVPG-DWTAGHVGA----PMPCSLIKlVDVEEMN 499
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSG-FINFFGkPGAIGRNPSllrkVAPLALVK-YDLESGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 500 YL---------AAKGE-----GEVCVKGPnvFQGYLkDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKH 559
Cdd:cd05940 271 PIrdaegrcikVPRGEpglliSRINPLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
330 340 350
....*....|....*....|....*....|..
gi 309243088 560 IFKLaQGEYIAPEKIENIYLRSEPVAQVFVHG 591
Cdd:cd05940 348 TFRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
115-607 |
6.57e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 68.50 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 115 PDQPY-------EWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAI 187
Cdd:PRK13390 11 PDRPAvivaetgEQVSYRQLDDDSAALARVLYDAGLRTG--DVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 188 TYII-NKGELSLVfvdkpekANLLLEGVENKLipglktiilmdsyGIDLLERgKKCGVEIMSMKALED-LGRANRRKPKP 265
Cdd:PRK13390 89 DYIVgDSGARVLV-------ASAALDGLAAKV-------------GADLPLR-LSFGGEIDGFGSFEAaLAGAGPRLTEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 266 PAPedlAVICFTSGTTGNPKGAM--ITHRNVVSDCSAFVKVTDKTFSPSSDDTLISFLPLAHMFE-RVVECVMLCHGAKI 342
Cdd:PRK13390 148 PCG---AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYHAAPlRWCSMVHALGGTVV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 GFFQGDIRLLMDDLKALQPTIFPVVPRLLNRMFdrifgqanttlkrwlldfaskRKEAELRSgiirnnsLWDklifhkiQ 422
Cdd:PRK13390 225 LAKRFDAQATLGHVERYRITVTQMVPTMFVRLL---------------------KLDADVRT-------RYD-------V 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 423 SSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCSLTVPGDWTA--GHVGAPMPCSLiKLVDvEEMNY 500
Cdd:PRK13390 270 SSL----RAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDWLAhpGSVGRSVLGDL-HICD-DDGNE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 501 LAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 578
Cdd:PRK13390 343 LPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLYLADRKSFMI-ISGGVNIYPQETENAL 421
|
490 500
....*....|....*....|....*....
gi 309243088 579 LRSEPVAQVFVHGeslqafliaivVPDVE 607
Cdd:PRK13390 422 TMHPAVHDVAVIG-----------VPDPE 439
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
430-610 |
8.90e-12 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 68.09 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 430 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGHV-GAPM-PCSLIKLVDvEEMNYLAAKGEG 507
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGLVNYTRLDDSDERIFTTqGRPMsPDDEVWVAD-ADGNPLPQGEVG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 508 EVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIYLRsep 583
Cdd:PRK10946 382 RLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLLLR--- 453
|
170 180
....*....|....*....|....*..
gi 309243088 584 vaqvfvHGESLQAFLIAIvvPDvETLG 610
Cdd:PRK10946 454 ------HPAVIHAALVSM--ED-ELMG 471
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
429-598 |
1.24e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.56 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 429 VRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAGCSlTVPG---DW------TAGHVGAPMPCSLIKL-----VD 494
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGPS-TVCAwkpEWdslppeEQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 495 VEEMNYLAAKGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 572
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190
....*....|....*....|....*....|...
gi 309243088 573 KIENIYLRSEPVAQVFV-------HGESLQAFL 598
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
102-609 |
1.41e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 67.36 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 102 RVSNNGPCLGSRkpDQPYEWlsyKQVEDMSECVGSALIHKGFKAGPENfVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDT 181
Cdd:PRK13388 12 RAGDDTIAVRYG--DRTWTW---REVLAEAAARAAALIALADPDRPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLNTT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 182 LGTEAITYIINKGELSLVFVDKPEKAnlLLEGVEnklIPGLkTIILMDS--YgidllergkkcgveimsmkaLEDLGRAN 259
Cdd:PRK13388 86 RRGAALAADIRRADCQLLVTDAEHRP--LLDGLD---LPGV-RVLDVDTpaY--------------------AELVAAAG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 260 RRKP-KPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAfvkVTDKtFSPSSDDTLISFLPLAHMfervvECVM--- 335
Cdd:PRK13388 140 ALTPhREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRA---LTER-FGLTRDDVCYVSMPLFHS-----NAVMagw 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 336 ---LCHGAKI---------GFfqgdirllMDDLKALQPTIFPVVPRLL-------NRMFDrifgqANTTLKRWLLDFASK 396
Cdd:PRK13388 211 apaVASGAAValpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 397 RKEAElrsgiirnnslwdklifhkiqsslggkvrlmvtgaapvsatvltFLRAaLGCQFYEGYGQTEctAGCSLTVPGDW 476
Cdd:PRK13388 278 RDIAE--------------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 477 TAGHVGAPMPCslIKLVDVEEM---------------NYLAAKGEgEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGD 541
Cdd:PRK13388 311 PPGSIGRGAPG--VAIYNPETLtecavarfdahgallNADEAIGE-LVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGD 386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309243088 542 IGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHG----ESLQAFLIAIVVPDVETL 609
Cdd:PRK13388 387 LAYRDADGWIYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATF 457
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
122-608 |
2.52e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 66.87 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRpEWVIIEQGCFAYSMVVVPLYDT-LGTEAITYIINKGELSLVF 200
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAG--DGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 201 VDkpEKANLLLEGVENKLiPGLKTIIlmdSYGIDLLERGKKCGVeimsmkaLEDLGRANRRKPKPPAPEDLAVICFTSGT 280
Cdd:PRK07788 152 YD--DEFTDLLSALPPDL-GRLRAWG---GNPDDDEPSGSTDET-------LDDLIAGSSTAPLPKPPKPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 281 TGNPKGAMITHrnvvsdcsafvkvtdktfsPSsddtliSFLPLAHMFERV---VECVMLC-----HG-----AKIGFFQG 347
Cdd:PRK07788 219 TGTPKGAPRPE-------------------PS------PLAPLAGLLSRVpfrAGETTLLpapmfHAtgwahLTLAMALG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 ---------DIRLLMDDLKALQPTIFPVVPRLLNRMFDrifgqanttlkrwLLDFASKRKEAelrsgiirnnslwdklif 418
Cdd:PRK07788 274 stvvlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPEVLAKYDT------------------ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 419 hkiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECtAGCSLTVPGDWTA--GHVGAPMPCSLIKLVDvE 496
Cdd:PRK07788 323 ----SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-E 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 497 EMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 576
Cdd:PRK07788 393 NGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVED 467
|
490 500 510
....*....|....*....|....*....|..
gi 309243088 577 IYLRSEPVAQVFVHGeslqafliaivVPDVET 608
Cdd:PRK07788 468 LLAGHPDVVEAAVIG-----------VDDEEF 488
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
262-587 |
4.13e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 66.19 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 262 KPKPPAPEDLAVIcFTSGTTGNPKGAMITHRNvvsdcsaFVKVTD-------KTFSPSSDDTLISFLPLAHM--FERVVE 332
Cdd:PRK05857 163 NADQGSEDPLAMI-FTSGTTGEPKAVLLANRT-------FFAVPDilqkeglNWVTWVVGETTYSPLPATHIggLWWILT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 333 CVMlcHGAKIGFFQGDIRLLMDDLKALQPTIFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeAELRSGIIRNNSL 412
Cdd:PRK05857 235 CLM--HGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLV------------------------SELKSANATVPSL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 413 wdklifhkiqsslggkvRLMVTGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCSLTVPGDWT---AGHVGAPMPC 487
Cdd:PRK05857 289 -----------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 488 SLIKLVDVEEMNYLAAKGE-----GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFk 562
Cdd:PRK05857 351 VDVYLAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI- 428
|
330 340
....*....|....*....|....*
gi 309243088 563 LAQGEYIAPEKIENIylrSEPVAQV 587
Cdd:PRK05857 429 ICGGVNIAPDEVDRI---AEGVSGV 450
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
423-607 |
4.89e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 65.70 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 423 SSLggkvRLMVTGAAPVSATVLtflRAAL---GCQFYEGYGQTEctaGCSLTV--PGDWTA--GHVGAPMpCSLIKLVDv 495
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE---GGGVTVitSEDWLAhpGSVGKAV-LGEVRILD- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 496 EEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKI 574
Cdd:PRK08276 330 EDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEI 407
|
170 180 190
....*....|....*....|....*....|...
gi 309243088 575 ENIYLRSEPVAQVFVHGeslqafliaivVPDVE 607
Cdd:PRK08276 408 ENLLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
113-607 |
7.30e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.13 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 113 RKPDQPY-----EWLSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAI 187
Cdd:PRK12316 3069 RTPDAVAlafgeQRLSYAELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 188 TYIINKGELsLVFVDKPEKANLLLEGVENKLipglktiilmdsygidlLERGKkcgveimsmkalEDLGRANrrKPKPPA 267
Cdd:PRK12316 3147 AYMLEDSGA-QLLLSQSHLRLPLAQGVQVLD-----------------LDRGD------------ENYAEAN--PAIRTM 3194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHrnvvSDCSAFVKVTDKTFSPSSDDTLISFLPLAHMFERVVECVMLCHGAKIgfFQG 347
Cdd:PRK12316 3195 PENLAYVIYTSGSTGKPKGVGIRH----SALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV--VLA 3268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 DIRLLMDdlkalqptifpvvPRLLNRMFDRifGQANTTLKRWlldfaskrkeaelrsgiirnnSLWDKLIFHKIQSSLGG 427
Cdd:PRK12316 3269 GPEDWRD-------------PALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTS 3312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 428 KVRLMVTGAAPVSATVltfLRAALGCQFYEGYGQTECTAGCSLTVPGDWTAGH--VGAPMPCSLIKLVDVeEMNYLAAKG 505
Cdd:PRK12316 3313 LKRIVCGGEALPADLQ---QQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGA 3388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 506 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYL 579
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLL 3467
|
490 500
....*....|....*....|....*...
gi 309243088 580 RSEPVAQVFVHGESLQAfLIAIVVPDVE 607
Cdd:PRK12316 3468 EHPWVREAVVLAVDGRQ-LVAYVVPEDE 3494
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
113-591 |
7.46e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 65.10 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 113 RKPDQPY-------EWLSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTE 185
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLKRG--DHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 186 AITYIINKGELSLVF--VDKPEKANLLLegvenKLIPGLKTIILMDSYGidllergkkcgveimSMKALEDLGRANRRKP 263
Cdd:PRK13391 87 EAAYIVDDSGARALItsAAKLDVARALL-----KQCPGVRHRLVLDGDG---------------ELEGFVGYAEAVAGLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 264 KPPAPEDL--AVICFTSGTTGNPKGamithrnVVSDCSafvkvtdktfSPSSDDTLisflPLAHMFERVV----ECVMLC 337
Cdd:PRK13391 147 ATPIADESlgTDMLYSSGTTGRPKG-------IKRPLP----------EQPPDTPL----PLTAFLQRLWgfrsDMVYLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 338 -----HGAKIGFFQGDIRL-----LMDDLKALQP---------TIFPVVPRllnrMFDRIFGQANTTLKRWLLdfaskrk 398
Cdd:PRK13391 206 paplyHSAPQRAVMLVIRLggtviVMEHFDAEQYlalieeygvTHTQLVPT----MFSRMLKLPEEVRDKYDL------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 399 eaelrsgiirnnslwdklifhkiqSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCSLTVPGDWTA 478
Cdd:PRK13391 275 ------------------------SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 479 --GHVGAPMpCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQgYLKDPAKTAEALDKDG-WLHTGDIGKWLPNGTLKIID 555
Cdd:PRK13391 326 hpGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTD 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 309243088 556 RKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG 591
Cdd:PRK13391 403 RAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
64-615 |
1.12e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 65.57 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 64 EVAGSDGARRSAILDSDEPLAYFYDDVRTLYEGFQRGIrvsnngpclgSRKPDQPY-----EWLSYKQVEDMSECVGSAL 138
Cdd:PRK12467 3068 ELPTLAAHERRQVLHAWNATAAAYPSERLVHQLIEAQV----------ARTPEAPAlvfgdQQLSYAELNRRANRLAHRL 3137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 139 IHKGfkAGPENFVGIfAQNRPewviIEqgcfaysmVVVPLYDTLGTEAityiinkgelSLVFVDKPEKANLLLEGVENKl 218
Cdd:PRK12467 3138 IAIG--VGPDVLVGV-AVERS----VE--------MIVALLAVLKAGG----------AYVPLDPEYPRERLAYMIEDS- 3191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 219 ipGLKTIILMDSygidLLER-GKKCGVEIMSMKALeDLGRANRRKPKPPA-PEDLAVICFTSGTTGNPKGAMITHRNVVS 296
Cdd:PRK12467 3192 --GVKLLLTQAH----LLEQlPAPAGDTALTLDRL-DLNGYSENNPSTRVmGENLAYVIYTSGSTGKPKGVGVRHGALAN 3264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 297 DCSAFvkvtDKTFSPSSDDTLISFLPLAhmFERVVECVM--LCHGAKIGFFQGDIR---LLMDDLKALQPTIFPVVPRLL 371
Cdd:PRK12467 3265 HLCWI----AEAYELDANDRVLLFMSFS--FDGAQERFLwtLICGGCLVVRDNDLWdpeELWQAIHAHRISIACFPPAYL 3338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 372 NrmfdrifgqanttlkrwllDFASkrkeaelrsgiirnnslwdkliFHKIQSslGGKVRLMVTGAAPVSATVLTFLRAAL 451
Cdd:PRK12467 3339 Q-------------------QFAE----------------------DAGGAD--CASLDIYVFGGEAVPPAAFEQVKRKL 3375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 452 G-CQFYEGYGQTECTAGCSL-TVPGDWTAGHVGAPMPCSLIKL---VDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAK 526
Cdd:PRK12467 3376 KpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSL 3455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 527 TAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHGESLQA--F 597
Cdd:PRK12467 3456 TAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGEIEARLLQHPSVREAVVLARDGAGgkQ 3534
|
570
....*....|....*...
gi 309243088 598 LIAIVVPDVETlGHWAQK 615
Cdd:PRK12467 3535 LVAYVVPADPQ-GDWRET 3551
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
251-587 |
1.77e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.02 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 251 ALEDL---GRANRRKPKPPAP-EDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTfspSSDDTLISFLPLAH- 325
Cdd:PRK05851 130 TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLD---AATDVGCSWLPLYHd 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 326 MfervvecvmlchgakigffqGDIRLLMDDLKA----LQPT-IFPVVP-RLLNrmfdrifgqanttlkrWLLDF-ASKRK 398
Cdd:PRK05851 207 M--------------------GLAFLLTAALAGaplwLAPTtAFSASPfRWLS----------------WLSDSrATLTA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 399 EAELRSGIIRNNSlwdklifHKIQSSLGGKVRLMVTGAAPVSATVLT-FLRAALGCQFYEG-----YGQTECTagCSLTV 472
Cdd:PRK05851 251 APNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaaapsYGLAEST--CAVTV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 473 P---------------GDWTAGH--VGAPMPCSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAktaeaLDKDG 535
Cdd:PRK05851 322 PvpgiglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGYLGQAP-----IDPDD 396
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 309243088 536 WLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIylrsepVAQV 587
Cdd:PRK05851 397 WFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
269-607 |
2.23e-10 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 63.65 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 269 EDLAVICFTSGTTGNPKGAMITHRNVVSdcsaFVKVT-DKTFSPSSDDTL----ISFLPLAHmfervvECV-MLCHGAKI 342
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVN----LLHFErEKTNINFSDKVLqfatCSFDVCYQ------EIFsTLLSGGTL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 343 GFFQGDIRLLMDDLKAL------QPTIFPVVprLLNRMFDrifgqanttLKRWLLDFASKRKEAeLRSG--IIRNNSLWD 414
Cdd:cd17656 198 YIIREETKRDVEQLFDLvkrhniEVVFLPVA--FLKFIFS---------EREFINRFPTCVKHI-ITAGeqLVITNEFKE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 415 KLIFHkiqsslggkvrlmvtgaapvsatvltflraalGCQFYEGYGQTECTAGCSLTV-PGDWTAGH--VGAPMPCSLIK 491
Cdd:cd17656 266 MLHEH--------------------------------NVHLHNHYGPSETHVVTTYTInPEAEIPELppIGKPISNTWIY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 492 LVDVEEMnyLAAKGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLa 564
Cdd:cd17656 314 ILDQEQQ--LQPQGIvGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI- 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 309243088 565 QGEYIAPEKIENIYLRSEPVAQ--VFVHGESL-QAFLIAIVVPDVE 607
Cdd:cd17656 391 RGYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
245-586 |
2.87e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.03 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 245 EIMSMKALEDLGRANRRKPKPPaPEDLAVICFTSGTTGNPKGAMITHRNVVSD-----CSAFVKVTDktfspssDDTLIS 319
Cdd:PRK05691 143 ELLCVDTLDPALAEAWQEPALQ-PDDIAFLQYTSGSTALPKGVQVSHGNLVANeqlirHGFGIDLNP-------DDVIVS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 320 FLPLAHmfervvecvmlchgaKIGFFQGdirllmddlkALQPtIFPVVPRLLnrMFDRIFGQANTtlkRWLL-------- 391
Cdd:PRK05691 215 WLPLYH---------------DMGLIGG----------LLQP-IFSGVPCVL--MSPAYFLERPL---RWLEaiseyggt 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 392 -----DFA----SKR-KEAELRSgiiRNNSLWdklifhkiqsslggkvRLMVTGAAPVSATVL-TFLRAALGC-----QF 455
Cdd:PRK05691 264 isggpDFAyrlcSERvSESALER---LDLSRW----------------RVAYSGSEPIRQDSLeRFAEKFAACgfdpdSF 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 456 YEGYGQTECT---AGC-------SLTVPGDWTAGHVGAP------MPCSL------IKLVDVEEMNYLAAKGEGEVCVKG 513
Cdd:PRK05691 325 FASYGLAEATlfvSGGrrgqgipALELDAEALARNRAEPgtgsvlMSCGRsqpghaVLIVDPQSLEVLGDNRVGEIWASG 404
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 309243088 514 PNVFQGYLKDPAKTAEA-LDKDG--WLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQ 586
Cdd:PRK05691 405 PSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTGRLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
274-605 |
4.58e-10 |
|
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: 61.65 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 274 ICFTSGTTGNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDTLISFLPLAH-MFERVVECVMLCHGAKIGFFQGDIRLL 352
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 353 MDDLKALQPTIFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkEAELRSGIIRNnslwdklifhkiqsslggKVRLM 432
Cdd:cd17633 81 IRKINQYNATVIYLVPTML---------------------------QALARTLEPES------------------KIKSI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 433 VTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVDVEEmnylaaKGEGEVCV 511
Cdd:cd17633 116 FSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG------GEIGKIFV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 512 KGPNVFQGYLKdpaktAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQVFVHG 591
Cdd:cd17633 190 KSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
330
....*....|....*..
gi 309243088 592 ESLQAF---LIAIVVPD 605
Cdd:cd17633 264 IPDARFgeiAVALYSGD 280
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
254-558 |
7.77e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 61.88 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 254 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDC----SAFVKVTDKTfsPSSDDTLISFLPLAH-MFE 328
Cdd:PRK05850 145 DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVSWLPFYHdMGL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 329 RVVECV-MLC-HGAK----IGFFQGDIRLLmdDLKALQPTIFPVVPrllNRMFdrifgqanttlkrwllDFASKRKEAEL 402
Cdd:PRK05850 223 VLGVCApILGgCPAVltspVAFLQRPARWM--QLLASNPHAFSAAP---NFAF----------------ELAVRKTSDDD 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 403 RSGIirnnslwdklifhkiqsSLGGkVRLMVTGAAPV-SATVLTFLR--AALGcqFYE-----GYGQTECTAGCSLTVPG 474
Cdd:PRK05850 282 MAGL-----------------DLGG-VLGIISGSERVhPATLKRFADrfAPFN--LREtairpSYGLAEATVYVATREPG 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 475 D-----------WTAGHV--------------GAPMPcSLIKLVDVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKT-- 527
Cdd:PRK05850 342 QppesvrfdyekLSAGHAkrcetgggtplvsyGSPRS-PTVRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETer 420
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 309243088 528 ---AEALDK-----DG-WLHTGDIGkWLPNGTLKIIDRKK 558
Cdd:PRK05850 421 tfgATLVDPspgtpEGpWLRTGDLG-FISEGELFIVGRIK 459
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
114-604 |
1.10e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 61.45 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 114 KPDQP-YEWL----SYKQVEDMSECVGSALIHKGFKAG-PenfVGIFAQNRPEWVI-----IEQGCfAYsmvvVPLYDTL 182
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSLKLPDKsP---IIVFGHMSPEMLAtflgaVKAGH-AY----IPVDVSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 183 GTEAITYIINKGELSLVFvdkpEKANLLLEGVENKLIpglktiilmdsyGIDLLERGKKCGVEIMSMKALEDlgranrrk 262
Cdd:PRK04813 87 PAERIEMIIEVAKPSLII----ATEELPLEILGIPVI------------TLDELKDIFATGNPYDFDHAVKG-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 263 pkppapEDLAVICFTSGTTGNPKGAMITHRNVVS----DCSAFVKVTDKTF---SPSSDDtlISflplahmfervvecVM 335
Cdd:PRK04813 143 ------DDNYYIIFTSGTTGKPKGVQISHDNLVSftnwMLEDFALPEGPQFlnqAPYSFD--LS--------------VM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 336 -----LCHGAKIGFFQGDI----RLLMDDLKALQPTIFPVVPR-----LLNRMFDrifGQANTTLKRWLLDfaskrkeae 401
Cdd:PRK04813 201 dlyptLASGGTLVALPKDMtanfKQLFETLPQLPINVWVSTPSfadmcLLDPSFN---EEHLPNLTHFLFC--------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 402 lrsGIIRNNSLWDKLifhkiqsslggKVRLmvtgaaPvSATVltflraalgcqfYEGYGQTECT-AGCSLTVPGDWTAGH 480
Cdd:PRK04813 269 ---GEELPHKTAKKL-----------LERF------P-SATI------------YNTYGPTEATvAVTSIEITDEMLDQY 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 481 ----VGAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEAL-DKDGW--LHTGDIGKwLPNGTLKI 553
Cdd:PRK04813 316 krlpIGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTFDGQpaYHTGDAGY-LEDGLLFY 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 309243088 554 IDRKKHIFKLAqGEYIAPEKIENIYLRSEPVAQVFV----HGESLQAfLIAIVVP 604
Cdd:PRK04813 394 QGRIDFQIKLN-GYRIELEEIEQNLRQSSYVESAVVvpynKDHKVQY-LIAYVVP 446
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
265-605 |
1.27e-09 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 61.25 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 265 PPAPEDLAVIcFTSGTTGNPKGamithrnvvsdcsafvkVTDKTFSPSSDDTLISFLPLAHMFERVVECVM---LCHGAK 341
Cdd:PRK12406 149 PPVPQPQSMI-YTSGTTGHPKG-----------------VRRAAPTPEQAAAAEQMRALIYGLKPGIRALLtgpLYHSAP 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 IGFFQGDIRLlmDDLKALQPTIFP----------------VVPRllnrMFDRifgqanttlkrwLLDFASKRKEAelrsg 405
Cdd:PRK12406 211 NAYGLRAGRL--GGVLVLQPRFDPeellqlierhrithmhMVPT----MFIR------------LLKLPEEVRAK----- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 406 iirnnslWDklifhkiQSSLggkvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCSLTVPGDWTA--GHVGA 483
Cdd:PRK12406 268 -------YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSEDALShpGTVGK 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 484 PMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNV--FQgYLKDPAKTAEaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:PRK12406 329 AAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGYLFLCDRKRDMV 405
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 309243088 562 kLAQGEYIAPEKIENIYLRSEPVAQVFVHG---ESLQAFLIAIVVPD 605
Cdd:PRK12406 406 -ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
269-600 |
1.87e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 269 EDLAVICFTSGTTGNPKGAMITHRNVVSDcsafVKVTDKTFSPSSDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFF- 345
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 ---QGDIRLLMDDLKALQPTIFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaeLRSGiirnnslwdklifhkiQ 422
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR-------------LFSG----------------G 1397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 423 SSLGGKVRLMVTGAAPvsatvltflraalGCQFYEGYGQTE---------CTAGCSLTVPgdwtaghVGAPMPCSLIKLV 493
Cdd:PRK05691 1398 EALPAELRNRVLQRLP-------------QVQLHNRYGPTEtainvthwqCQAEDGERSP-------IGRPLGNVLCRVL 1457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 494 DvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 566
Cdd:PRK05691 1458 D-AELNLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RG 1535
|
330 340 350
....*....|....*....|....*....|....*.
gi 309243088 567 EYIAPEKIENIYLRSEPVAQ--VFVHGESLQAFLIA 600
Cdd:PRK05691 1536 FRVEPEEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
266-611 |
1.91e-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: 60.56 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 266 PAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFvkvtDKTFSPSSDDTLIsFLPLAHMFERVVECVM-LCHGAKigf 344
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHF----RSLFNITSEDILF-LTSPLTFDPSVVEIFLsLSSGAT--- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 345 fqgdirLLmddlkaLQPTIFPVVPRLLNRMFDRIFG----QANTTLKRwllDFASKRKEAELRSGIirnnslwdklifhk 420
Cdd:cd17654 187 ------LL------IVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT-------------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 421 iqSSLggkvRLMVTGAAP-VSATVLTFLRAA-LGCQFYEGYGQTECTAGCSL-TVPGDWTAGHVGAPMPCSLIKLVDVEe 497
Cdd:cd17654 238 --SSL----RVLALGGEPfPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAyKVPEEDSPVQLGSPLLGTVIEVRDQN- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 498 mnylAAKGEGEVCVKGPNVfQGYLKDPAKTAEALdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 577
Cdd:cd17654 311 ----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLIQQV 379
|
330 340 350
....*....|....*....|....*....|....
gi 309243088 578 YLRSEPVAQVFVHGESLQAFLIAIVVPDVETLGH 611
Cdd:cd17654 380 IESCLGVESCAVTLSDQQRLIAFIVGESSSSRIH 413
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
482-575 |
2.39e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 60.40 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 482 GAPMPCSLIKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIF 561
Cdd:PRK09192 388 GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI 464
|
90
....*....|....
gi 309243088 562 kLAQGEYIAPEKIE 575
Cdd:PRK09192 465 -IINGRNIWPQDIE 477
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
122-599 |
3.36e-09 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 59.45 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINKGELSLVFV 201
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPG--DVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 202 DKpekanlllegvenklipglktiilmdsygidllergkkcgveimsmkaledlgrANRRKpkppAPEDLAVICFTSGTT 281
Cdd:cd05973 79 DA------------------------------------------------------ANRHK----LDSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 282 GNPKGAMITHRNVVsdcsAFVKVTDKTFSPSSDDtliSFLPLAhmfervvecvmlchgaKIGFFQGDIRLLMDDLKALQP 361
Cdd:cd05973 101 GLPKGVPVPLRALA----AFGAYLRDAVDLRPED---SFWNAA----------------DPGWAYGLYYAITGPLALGHP 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 362 TIF---PVVPRLLNRMFDRiFG----QANTTLKRWLLdfaSKRKEAELRsgiirnnslwdklifhkiqssLGGKVRLMVT 434
Cdd:cd05973 158 TILlegGFSVESTWRVIER-LGvtnlAGSPTAYRLLM---AAGAEVPAR---------------------PKGRLRRVSS 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 435 GAAPVSATVLTFLRAALGCQFYEGYGQTEctagCSLTVPGDWTAGHV------GAPMPCSLIKLVDvEEMNYLAAKGEGE 508
Cdd:cd05973 213 AGEPLTPEVIRWFDAALGVPIHDHYGQTE----LGMVLANHHALEHPvhagsaGRAMPGWRVAVLD-DDGDELGPGEPGR 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 509 VCVKGPNV----FQGYLKDPAKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYLRSEPV 584
Cdd:cd05973 288 LAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVESALIEHPAV 362
|
490 500
....*....|....*....|..
gi 309243088 585 AQVFV-------HGESLQAFLI 599
Cdd:cd05973 363 AEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
114-291 |
7.39e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 58.75 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 114 KPDQPYEWLSYKQVEDMSECVGSALIHKGFKAGPENFvgIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAITYIINK 193
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVF--IFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 194 GELSlVFVDKPEkanlLLEGVENKLIPGLKTIILMDSYG------IDLLERgkkcgveimsMKALEDlgranRRKPKPPA 267
Cdd:PRK04319 144 SEAK-VLITTPA----LLERKPADDLPSLKHVLLVGEDVeegpgtLDFNAL----------MEQASD-----EFDIEWTD 203
|
170 180 190
....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKG------AMITH 291
Cdd:PRK04319 204 REDGAILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
276-591 |
3.47e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 56.71 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 276 FTSGTTGNPKGAMITHRNVVS--DCSAfvkvtdKTFSPSSDD------TLISFLPLahmfervvecvmlcHGAKIGFFQG 347
Cdd:PRK07638 150 FTSGSTGKPKAFLRAQQSWLHsfDCNV------HDFHMKREDsvliagTLVHSLFL--------------YGAISTLYVG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 348 DIRLLMddlkalqPTIFPvvprllNRMFDRIFGQANTTLKRwlldfASKRKEAELRSGIIRNNSLwdklifhKIQSSlGG 427
Cdd:PRK07638 210 QTVHLM-------RKFIP------NQVLDKLETENISVMYT-----VPTMLESLYKENRVIENKM-------KIISS-GA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 428 KvrlmvTGAAPVSATVLTFLRAalgcQFYEGYGQTECTAGCSLtVPGDWTAGHVGAPMPCSLIKLVDVEEMNYLAAKGE- 506
Cdd:PRK07638 264 K-----WEAEAKEKIKNIFPYA----KLYEFYGASELSFVTAL-VDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEi 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 507 GEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYLRSEPVAQ 586
Cdd:PRK07638 334 GTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVDE 411
|
....*
gi 309243088 587 VFVHG 591
Cdd:PRK07638 412 IVVIG 416
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
267-600 |
1.42e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 55.17 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 267 APEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFV--------KVTDKTFSPSSDDTLISFLPlAHMFERVVECV--ML 336
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVpylalseaDVIAQTASQSFDISVWQFLA-APLFGARVEIVpnAI 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 337 CHgakigffqgDIRLLMDDLKALQPTIFPVVPRLLNRMF--DRifgQANTTLkRWLLDfaskrkeaelrsgiirnnslwd 414
Cdd:PRK05691 3946 AH---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLP---------------------- 3990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 415 klifhkiqsslggkvrlmvTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCSL-TVPGDWTAGH---VGAPMPCSLI 490
Cdd:PRK05691 3991 -------------------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfRVDLASTRGSylpIGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 491 KLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHIFKL 563
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 309243088 564 aQGEYIAPEKIENIYLRSEPV------AQVFVHGESLQAFLIA 600
Cdd:PRK05691 4131 -RGYRIELGEIEARLHEQAEVreaavaVQEGVNGKHLVGYLVP 4172
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
82-325 |
1.61e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 54.50 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 82 PLAYFYDDVRTLYEGFQRGIRVSNNGPCL--------GSRKPDQP---YE--WLSYKQVEDMSECVGSALIHKGFKAGpe 148
Cdd:PRK08279 10 RLPRRLPDLPGILRGLKRTALITPDSKRSlgdvfeeaAARHPDRPallFEdqSISYAELNARANRYAHWAAARGVGKG-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 149 NFVGIFAQNRPEWVIIEQGcFAYSMVVVPLYDT-LGTEAITYIINKGELSLVFVDkPEKANLLlEGVENKLIPGLKTIIL 227
Cdd:PRK08279 88 DVVALLMENRPEYLAAWLG-LAKLGAVVALLNTqQRGAVLAHSLNLVDAKHLIVG-EELVEAF-EEARADLARPPRLWVA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 228 MDSYGIDLLergkkcgveimsmkALEDLGRANRRKPKPPAP-------EDLAVICFTSGTTGNPKGAMITHRNVVSDCSA 300
Cdd:PRK08279 165 GGDTLDDPE--------------GYEDLAAAAAGAPTTNPAsrsgvtaKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG 230
|
250 260
....*....|....*....|....*
gi 309243088 301 FVKVTDKTfspsSDDTLISFLPLAH 325
Cdd:PRK08279 231 FGGLLRLT----PDDVLYCCLPLYH 251
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
122-616 |
2.30e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.58 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGfkAGPENFVGIFAQNRPEWVI----IEQGCFAYsmvvVPLYDTLGTEAITYIINKGELS 197
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERG--VGPDVLVGVAMERSIEMVVallaILKAGGAY----VPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 198 LvfvdkpekanLLLEGVENKLIPGLKTIILMDsygidlLERGkkcgveimsmkALEDLGRANRRKPKPPAPEDLAVICFT 277
Cdd:PRK12316 611 L----------LLSQSHLGRKLPLAAGVQVLD------LDRP-----------AAWLEGYSEENPGTELNPENLAYVIYT 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 278 SGTTGNPKGAMITHRNVVS---------DCSAFVKVTDKTfsPSSDDTLIS--FLPLAhmfervvecvmlcHGAkigffq 346
Cdd:PRK12316 664 SGSTGKPKGAGNRHRALSNrlcwmqqayGLGVGDTVLQKT--PFSFDVSVWefFWPLM-------------SGA------ 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 347 gdiRLLmddlkalqptifpVVPRLLNRMFDRIFGQANTTLKRwLLDFASKRKEAELRSGiirnnslwdklifhKIQSSLg 426
Cdd:PRK12316 723 ---RLV-------------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE--------------DVASCT- 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 427 gKVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAG--CSLTVPGDWTAGHVGAPMPCSLIKLVDVeEMNYLAA 503
Cdd:PRK12316 771 -SLRRIVCSGEALPADAQEQVFAKLpQAGLYNLYGPTEAAIDvtHWTCVEEGGDSVPIGRPIANLACYILDA-NLEPVPV 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 504 KGEGEVCVKGPNVFQGYLKDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 577
Cdd:PRK12316 849 GVLGELYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEAR 927
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 309243088 578 YLRSEPVAQVFVHGESLQAfLIAIVVPD------VETLGHWAQKR 616
Cdd:PRK12316 928 LLEHPWVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
266-649 |
5.34e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 52.38 E-value: 5.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 266 PAPEDLAVICfTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFSPSSD-------DTLISFLPLAHmfervvecvmLCH 338
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFRMLMGGADFGTGEFTPSEDahkaaaaAAGTVMFPAPP----------LMH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 339 GAK-----IGFFQGDiRLLMDDLKALQPTIFPVVPR-LLNRMFdrIFGQAnttLKRWLLDfaskrkeaELRSGiiRNNSL 412
Cdd:cd05924 70 GTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPYDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 413 wdklifhkiqSSLggkvRLMVTGAAPVSATVLT-FLRAALGCQFYEGYGQTECTAGCSLTVPGdwtAGHVGAP--MPCSL 489
Cdd:cd05924 134 ----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFTGSGHSAG---SGPETGPftRANPD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 490 IKLVDvEEMNYLAAK--GEGEVCVKGpNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLA 564
Cdd:cd05924 197 TVVLD-DDGRVVPPGsgGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 565 qGEYIAPEKIENIyLRSEP-VAQVFVHGeslqafliaivVPDvETlghWAQKRGFVGSFEELCrnkDVKKAILEDMLRlG 643
Cdd:cd05924 275 -GEKVFPEEVEEA-LKSHPaVYDVLVVG-----------RPD-ER---WGQEVVAVVQLREGA---GVDLEELREHCR-T 333
|
....*.
gi 309243088 644 RDAGLK 649
Cdd:cd05924 334 RIARYK 339
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
265-326 |
1.10e-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: 51.91 E-value: 1.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309243088 265 PPAPEDLAVICFTSGTTGNPKGAMITHRNVVSdCSAFVKVTDKTfspsSDDTLISFLPLAHM 326
Cdd:cd05938 140 HVTIKSPALYIYTSGTTGLPKAARISHLRVLQ-CSGFLSLCGVT----ADDVIYITLPLYHS 196
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
59-291 |
1.92e-06 |
|
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: 51.04 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 59 AMQSVEVAGSDGARRSAILDSDEPLAYFYDDVR--TLYEGFQRGIRvsNNGPCLG----SRKPDQPYEWlSYKQVEDMSE 132
Cdd:cd17634 19 AGKILDWITPYQKVKNTSFAPGAPSIKWFEDATlnLAANALDRHLR--ENGDRTAiiyeGDDTSQSRTI-SYRELHREVC 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 133 CVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAI-TYIINKGELSLVFVD---KPEKAN 208
Cdd:cd17634 96 RFAGTLLDLGVKKG--DRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVaGRIIDSSSRLLITADggvRAGRSV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 209 LLLEGVENKL---IPGLKTIILMDSYGIDLlerGKKCGVEIMSMKALEDlgRANRRKPKPPAPEDLAVICFTSGTTGNPK 285
Cdd:cd17634 174 PLKKNVDDALnpnVTSVEHVIVLKRTGSDI---DWQEGRDLWWRDLIAK--ASPEHQPEAMNAEDPLFILYTSGTTGKPK 248
|
....*.
gi 309243088 286 GAMITH 291
Cdd:cd17634 249 GVLHTT 254
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
255-590 |
2.16e-06 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 51.20 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 255 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVS---------DCSAFVKVTDKTfsPSSDDtlIS----FL 321
Cdd:PRK10252 584 LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNrllwmqnhyPLTADDVVLQKT--PCSFD--VSvwefFW 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 322 PlahmfervvecvMLChGAKigffqgdirLLMDDLKALQPtifpvvPRLLNRMFDRifgQANTTLkrwlldfaskrkeae 401
Cdd:PRK10252 660 P------------FIA-GAK---------LVMAEPEAHRD------PLAMQQFFAE---YGVTTT--------------- 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 402 lrsgiirnnslwdklifHKIQSSLGGKVRLMVTGAAPVSATVLT--F-----LRAALgCQFYEG---------YGQTECT 465
Cdd:PRK10252 694 -----------------HFVPSMLAAFVASLTPEGARQSCASLRqvFcsgeaLPADL-CREWQQltgaplhnlYGPTEAA 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 466 AGCS-LTVPGDWTAGHVGAPMPCSL------IKLVDvEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL- 537
Cdd:PRK10252 756 VDVSwYPAFGEELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAp 834
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 309243088 538 -----HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVH 590
Cdd:PRK10252 835 germyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
452-602 |
8.28e-06 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 49.26 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 452 GCQFYEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKLVdVEEMNYLAAKGEGEVCVKGPNVFQGYLKDPAKTaeaL 531
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---V 361
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 309243088 532 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIfKLAQGEYIAPEKIENIYLRSEPVAQVFVHG-------ESLQAFLIAIV 602
Cdd:PRK06060 362 ANEGWLDTRDRVCIDSDGWVTYRCRADDT-EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
268-595 |
1.90e-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: 47.81 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 268 PEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKV-----TDKTFSPssddtlisfLPLAH---MFERVVECVMlcHG 339
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDlnlknGDRTYTC---------MPLYHgtaAFLGACNCLM--SG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 340 AKIGF---FQgdIRLLMDDLKALQPTIFPVVPRLLnrmfdrifgqanttlkRWLLDFASKRKEAELRSGIIRNNSL---- 412
Cdd:cd05937 155 GTLALsrkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLLSTPPSPYDRDHKVRVAWGNGLrpdi 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 413 WDKLifhkiqsslggKVRLMVtgaaPVSAtvltflraalgcqfyEGYGQTECTAGCSLTVPGDWTAGHVGAPMPCSLIKL 492
Cdd:cd05937 217 WERF-----------RERFNV----PEIG---------------EFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 493 VDVE---------EMNYL---------AAKGE-GEVCVKGPNV----FQGYLKDPAKTAEALDK------DGWLHTGDIG 543
Cdd:cd05937 267 ENQVvlvkmdpetDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLL 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 309243088 544 KWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHGESLQ 595
Cdd:cd05937 347 RQDADGRWYFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
122-608 |
8.03e-05 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 45.88 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 122 LSYKQVEDMSECVGSALIHKGFKAGpeNFVGIFAQNRPEWVIIEQGcFAYSMVVVPLYDT-LGTEAITYIINKGELSLVF 200
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSG--DVVALFMENRLEFVALWLG-LAKIGVETALINSnLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 201 VDkpekanlllegvenklipgLKTIILMDSYgidllergkkcgveimsmkaledlgranRRKPKPPAPEDLAVICF--TS 278
Cdd:cd05939 81 FN-------------------LLDPLLTQSS----------------------------TEPPSQDDVNFRDKLFYiyTS 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 279 GTTGNPKGAMITHRNVVSdCSAFVKvtdKTFSPSSDDTLISFLPLAHMFERVVeCV--MLCHGAKIgffqgDIRL----- 351
Cdd:cd05939 114 GTTGLPKAAVIVHSRYYR-IAAGAY---YAFGMRPEDVVYDCLPLYHSAGGIM-GVgqALLHGSTV-----VIRKkfsas 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 352 -LMDDLKALQPTIfpvvprllnrmfdrifGQANTTLKRWLLdfASKRKEAELRsgiirnnslwdklifHkiqsslggKVR 430
Cdd:cd05939 184 nFWDDCVKYNCTI----------------VQYIGEICRYLL--AQPPSEEEQK---------------H--------NVR 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 431 LMVTGAapvsatvltfLRAALGCQFY---------EGYGQTECTagCSLtvpGDWTaGHVGAP--MPCSL-----IKLVD 494
Cdd:cd05939 223 LAVGNG----------LRPQIWEQFVrrfgipqigEFYGATEGN--SSL---VNID-NHVGACgfNSRILpsvypIRLIK 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 495 VEEMNYLAAKGEGEVCVK-GPN----------------VFQGYLKDPAkTAEALDKDGWLH------TGDIGKWLPNGTL 551
Cdd:cd05939 287 VDEDTGELIRDSDGLCIPcQPGepgllvgkiiqndplrRFDGYVNEGA-TNKKIARDVFKKgdsaflSGDVLVMDELGYL 365
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 309243088 552 KIIDRKKHIFKLaQGEYIAPEKIENIYLRSEPVAQVFVHGESL-----QAFLIAIVVPDVET 608
Cdd:cd05939 366 YFKDRTGDTFRW-KGENVSTTEVEGILSNVLGLEDVVVYGVEVpgvegRAGMAAIVDPERKV 426
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
262-613 |
9.76e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 262 KPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAfvkVTDKTFSPSSddTLISfLPLAHmfervvecvmlchgak 341
Cdd:PRK07824 28 RVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADA---THDRLGGPGQ--WLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 342 IGFFQGDIRLLmddLKALQPTIFPV--------VPRLLNRM-FDRIF-GQANTTLKRWLLDFASKRKEAELRSGIIrnns 411
Cdd:PRK07824 86 IAGLQVLVRSV---IAGSEPVELDVsagfdptaLPRAVAELgGGRRYtSLVPMQLAKALDDPAATAALAELDAVLV---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 412 lwdklifhkiqsslggkvrlmvtGAAPVSATVLTflRA-ALGCQFYEGYGQTECTAGCSltvpgdwtagHVGAPMPCSLI 490
Cdd:PRK07824 159 -----------------------GGGPAPAPVLD--AAaAAGINVVRTYGMSETSGGCV----------YDGVPLDGVRV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 491 KLVDveemnylaakgeGEVCVKGPNVFQGY--LKDPAKTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEY 568
Cdd:PRK07824 204 RVED------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLT 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 309243088 569 IAPEKIENIYLRSEPVAQVFVHG---ESLQAFLIAIVVPDvetlGHWA 613
Cdd:PRK07824 266 VLPQVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGD----GGPA 309
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
110-583 |
1.28e-04 |
|
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: 45.11 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 110 LGSRK-PDQPYEWlsyKQVEDMSECVGSALIHKGFKAgpENFVGIFAQNRPEWVIIEQGCFAYSMVVVPLYDTLGTEAIT 188
Cdd:cd05915 15 SRLHTgEVHRTTY---AEVYQRARRLMGGLRALGVGV--GDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 189 YIINKGELSLVFVDKPekanlLLEGVENKLipglktiilmdsygiDLLERGKKCGVEIMSMKALEDL---GRANRRKPKP 265
Cdd:cd05915 90 YILNHAEDKVLLFDPN-----LLPLVEAIR---------------GELKTVQHFVVMDEKAPEGYLAyeeALGEEADPVR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 266 PAPEDLAVICFTSGTTGNPKGAMITHRNVVSDCSAFVKVTDKTFSPSSddTLISFLPLAHmfervveCVMLCHGAKIGFF 345
Cdd:cd05915 150 VPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH-------VNAWCLPYAATLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 346 QGDI---------RLLMDDLKALQPTIFPVVPRLLNrmfdrIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwdkl 416
Cdd:cd05915 221 GAKQvlpgprldpASLVELFDGEGVTFTAGVPTVWL-----ALADYLESTGH---------------------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 417 ifhkiqsSLGGKVRLMVTGAAPvsATVLTFLRAALGCQFYEGYGqteCTAGCSLTVPGDWTAGHVGAPMPCSL------- 489
Cdd:cd05915 268 -------RLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYG---LTETSPVVVQNFVKSHLESLSEEEKLtlkaktg 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 309243088 490 ----IKLVDVEEMNYLAAKGEGE----VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIF 561
Cdd:cd05915 336 lpipLVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLI 415
|
490 500
....*....|....*....|..
gi 309243088 562 KLAqGEYIAPEKIENIyLRSEP 583
Cdd:cd05915 416 KSG-GEWISSVDLENA-LMGHP 435
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
262-325 |
1.06e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 42.41 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 309243088 262 KPKPPAPEDLAVICFTSGTTGNPKGAMITHRNVvsdCSAFVKVTDkTFSPSSDDTLISFLPLAH 325
Cdd:PRK07769 173 VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNL---PTNVLQVID-ALEGQEGDRGVSWLPFFH 232
|
|
| |
