|
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 ... |
67-645 |
0e+00 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 980.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 67 QPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 146
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKPAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 147 SLVFVDKpekaklllegvenklipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICF 226
Cdd:cd05927 81 SIVFCDA---------------------------------------GVKVYSLEEFEKLGKKNKVPPPPPKPEDLATICY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 306
Cdd:cd05927 122 TSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSGDIRLLLDDI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 307 KVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVT 384
Cdd:cd05927 202 KALKPTVFPGVPRVLNRIYDKIFNkvQAKGPLKRKLFNFALNYKLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 385 GAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAA--EGEGEVCVK 462
Cdd:cd05927 282 GSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKdpNPRGEVCIR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 463 GPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGE 542
Cdd:cd05927 362 GPNVFSGYYKDPEKTAEALDEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENIYARSPFVAQIFVYGD 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 543 SLQAFLIAIVVPDVETLCSWA-QKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLL 621
Cdd:cd05927 442 SLKSFLVAIVVPDPDVLKEWAaSKGGGTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKAIHLEPEPFSVENGLL 521
|
570 580
....*....|....*....|....
gi 1832481686 622 TPTMKAKRPELRNYFRSQIDDLYS 645
Cdd:cd05927 522 TPTFKLKRPQLKKYYKKQIDEMYK 545
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
58-647 |
0e+00 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 706.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 58 PCLGSR-KPDQ---PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLG 133
Cdd:PLN02736 61 KYLGTRiRVDGtvgEYKWMTYGEAGTARTAIGSGLVQHGIP--KGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 134 NEAITYIVNKAELSLVFVdKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKP 213
Cdd:PLN02736 139 PDAVKFIVNHAEVAAIFC-VPQTLNTLLSCLSE--IPSVRLIVVVGGADEPLPSLPSGTGVEIVTYSKLLAQGRSSPQPF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 214 KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENtvnpCPDDTLISFLPLAHMFERVVECVMLCHGAKIG 293
Cdd:PLN02736 216 RPPKPEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKF----YPSDVHISYLPLAHIYERVNQIVMLHYGVAVG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 294 FFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGiiRNNS-LWDRLIFHK 370
Cdd:PLN02736 292 FYQGDNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNavKESGGLKERLFNAAYNAKKQALENG--KNPSpMWDRLVFNK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 371 VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNY 450
Cdd:PLN02736 370 IKAKLGGRVRFMSSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNY 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 451 MAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENI 527
Cdd:PLN02736 450 TSEDQpypRGEICVRGPIIFKGYYKDEVQTREVIDEDGWLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENV 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 528 YMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKG 606
Cdd:PLN02736 530 YAKCKFVAQCFVYGDSLNSSLVAVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKA 609
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1832481686 607 ITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 647
Cdd:PLN02736 610 VTLVPEPFTVENGLLTPTFKVKRPQAKAYFAKAISDMYAEL 650
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
63-645 |
0e+00 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 538.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 63 RKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVN 142
Cdd:COG1022 32 EKEDGIWQSLTWAEFAERVRALAAGLLALGVK--PGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 143 KAELSLVFVDKPEKAKLLLEGVENklIPGLKIIVVMDaygselvERGQRCGVEVTSMKAMEDLGRANR------RKPKPP 216
Cdd:COG1022 110 DSGAKVLFVEDQEQLDKLLEVRDE--LPSLRHIVVLD-------PRGLRDDPRLLSLDELLALGREVAdpaeleARRAAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfQ 296
Cdd:COG1022 181 KPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER----LPLGPGDRTLSFLPLAHVFERTVSYYALAAGATVAF-A 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 297 GDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLDFA---SKRKEAELRSGiiRNNSLW-------- 363
Cdd:COG1022 256 ESPDTLAEDLREVKPTFMLAVPRVWEKVYAGIQAKAEeaGGLKRKLFRWAlavGRRYARARLAG--KSPSLLlrlkhala 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 364 DRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLv 443
Cdd:COG1022 334 DKLVFSKLREALGGRLRFAVSGGAALGPELARFFRA-LGIPVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 dveemnymaAEgEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEK 523
Cdd:COG1022 412 ---------AE-DGEILVRGPNVMKGYYKNPEATAEAFDADGWLHTGDIGELDEDGFLRITGRKKDLIVTSGGKNVAPQP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 524 IENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRG-FEGSFEELCRNKDVKKAILEDMVRLGKdsGLKPFE 602
Cdd:COG1022 482 IENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGlPYTSYAELAQDPEVRALIQEEVDRANA--GLSRAE 558
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1832481686 603 QVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 645
Cdd:COG1022 559 QIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYA 601
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
67-632 |
8.58e-176 |
|
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: 507.52 E-value: 8.58e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 67 QPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 146
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVE--PGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 147 SLVFVDKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDLAVICF 226
Cdd:cd05907 79 KALFVEDPD----------------------------------------------------------------DLATIIY 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIGFFQgDIRLLMDD 305
Cdd:cd05907 95 TSGTTGRPKGVMLSHRNILSNALALAER----LPATEGDRHLSFLPLAHVFERRaGLYVPLLAGARIYFAS-SAETLLDD 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 306 LKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslGGRVRLMVTG 385
Cdd:cd05907 170 LSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFDLAV------------------------------GGRLRFAASG 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 386 AAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPN 465
Cdd:cd05907 220 GAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD-----------DGEILVRGPN 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 466 VFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESlQ 545
Cdd:cd05907 288 VMLGYYKNPEATAEALDADGWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLISQAVVIGDG-R 366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 546 AFLIAIVVPDVETLCSWAQKRG-FEGSFEELCRNKDVKKAILEDMVRLGKdsGLKPFEQVKGITLHPELFSIDNGLLTPT 624
Cdd:cd05907 367 PFLVALIVPDPEALEAWAEEHGiAYTDVAELAANPAVRAEIEAAVEAANA--RLSRYEQIKKFLLLPEPFTIENGELTPT 444
|
....*...
gi 1832481686 625 MKAKRPEL 632
Cdd:cd05907 445 LKLKRPVI 452
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
68-629 |
7.72e-159 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 466.31 E-value: 7.72e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 68 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 147
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLK--PGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 148 LVFVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpPAPEDLAVICFT 227
Cdd:cd17639 80 AIFTD---------------------------------------------------------------GKPDDLACIMYT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 228 SGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD--- 304
Cdd:cd17639 97 SGSTGNPKGVMLTHGNLVAGIAGLGDRVPELL--GPDDRYLAYLPLAHIFELAAENVCLYRGGTIGY--GSPRTLTDksk 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 305 -----DLKVLQPTVFPVVPRLLNRMFDRIFGQANT--TLKRWLLDFASKRKEAELRSGIirNNSLWDRLIFHKVQSSLGG 377
Cdd:cd17639 173 rgckgDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPmgGLKRTLFWTAYQSKLKALKEGP--GTPLLDELVFKKVRAALGG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 378 RVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYM--AAEG 455
Cdd:cd17639 251 RLRYMLSGGAPLSADTQEFL-NIVLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYStdKPPP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 456 EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA 535
Cdd:cd17639 330 RGEILIRGPNVFKGYYKNPEKTKEAFDGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 536 QVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-EGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELF 614
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGViNSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*
gi 1832481686 615 SIDNGLLTPTMKAKR 629
Cdd:cd17639 490 TPENGLVTAAQKLKR 504
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
68-649 |
1.93e-158 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 470.86 E-value: 1.93e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 68 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 147
Cdd:PLN02861 74 PYVWLTYKEVYDAAIRIGSAIRSRGVN--PGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 148 LVFVDKPEKAKLLleGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPkPPAPEDLAVICFT 227
Cdd:PLN02861 152 IAFVQESKISSIL--SCLPKCSSNLKTIVSFGDVSSEQKEEAEELGVSCFSWEEFSLMGSLDCELP-PKQKTDICTIMYT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 228 SGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCP-DDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLMDDL 306
Cdd:PLN02861 229 SGTTGEPKGVILTNRAIIAEVLSTDHLLKVTDRVATeEDSYFSYLPLAHVYDQVIETYCISKGASIGFWQGDIRYLMEDV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 307 KVLQPTVFPVVPRLlnrmFDRIFG------QANTTLKRWLLDFASKRKEAELRSGIIRNNS--LWDRLIFHKVQSSLGGR 378
Cdd:PLN02861 309 QALKPTIFCGVPRV----YDRIYTgimqkiSSGGMLRKKLFDFAYNYKLGNLRKGLKQEEAspRLDRLVFDKIKEGLGGR 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 379 VRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT-AGHVGAPMPCNLIKLVDVEEMNYMAAEG-- 455
Cdd:PLN02861 385 VRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSmVGTVGVPMTTIEARLESVPEMGYDALSDvp 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 456 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA 535
Cdd:PLN02861 465 RGEICLRGNTLFSGYHKRQDLTEEVL-IDGWFHTGDIGEWQPNGAMKIIDRKKNIFKLSQGEYVAVENLENTYSRCPLIA 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 536 QVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFS 615
Cdd:PLN02861 544 SIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGKKLQLRGFEMLKAIHLEPNPFD 623
|
570 580 590
....*....|....*....|....*....|....
gi 1832481686 616 IDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIKV 649
Cdd:PLN02861 624 IERDLITPTFKLKRPQLLKYYKDCIDQLYSEAKG 657
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
68-647 |
3.75e-158 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 470.07 E-value: 3.75e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 68 PYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELS 147
Cdd:PLN02430 73 PYMWKTYKEVYEEVLQIGSALRASGAE--PGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHAEID 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 148 LVFV-DKpeKAKLLLEGvENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICF 226
Cdd:PLN02430 151 FVFVqDK--KIKELLEP-DCKSAKRLKAIVSFTSVTEEESDKASQIGVKTYSWIDFLHMGKENPSETNPPKPLDICTIMY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRN---IVSDCSAFVKATENTVNPcpDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLM 303
Cdd:PLN02430 228 TSGTSGDPKGVVLTHEAvatFVRGVDLFMEQFEDKMTH--DDVYLSFLPLAHILDRMIEEYFFRKGASVGYYHGDLNALR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 304 DDLKVLQPTVFPVVPRLLNRMFDRIFG--QANTTLKRWLLDFASKRKEAELRSGIIRNNS--LWDRLIFHKVQSSLGGRV 379
Cdd:PLN02430 306 DDLMELKPTLLAGVPRVFERIHEGIQKalQELNPRRRLIFNALYKYKLAWMNRGYSHKKAspMADFLAFRKVKAKLGGRL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 380 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTA-GHVGAPMPCNLIKLVDVEEMNY--MAAEGE 456
Cdd:PLN02430 386 RLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAVYNELRLEEVPEMGYdpLGEPPR 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 457 GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQ 536
Cdd:PLN02430 466 GEICVRGKCLFSGYYKNPELTEEVM-KDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEYLENVYGQNPIVED 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 537 VFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSI 616
Cdd:PLN02430 545 IWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSELKSTAEKNKLRGFEYIKGVILETKPFDV 624
|
570 580 590
....*....|....*....|....*....|.
gi 1832481686 617 DNGLLTPTMKAKRPELRNYFRSQIDDLYSTI 647
Cdd:PLN02430 625 ERDLVTATLKKRRNNLLKYYQVEIDEMYRKL 655
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
56-648 |
2.98e-154 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 460.26 E-value: 2.98e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 56 NGPCLGSR-----KPDQpYEWLSYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYD 130
Cdd:PLN02614 60 NNPMLGRReivdgKPGK-YVWQTYQEVYDIVIKLGNSLRSVGVKD--EAKCGIYGANSPEWIISMEACNAHGLYCVPLYD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 131 TLGNEAITYIVNKAELSLVFVDKPEKAKLLlegvenKLIPG----LKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLG 206
Cdd:PLN02614 137 TLGAGAVEFIISHSEVSIVFVEEKKISELF------KTCPNsteyMKTVVSFGGVSREQKEEAETFGLVIYAWDEFLKLG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 207 RANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENtVNPC--PDDTLISFLPLAHMFERVVECV 284
Cdd:PLN02614 211 EGKQYDLPIKKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKS-ANAAltVKDVYLSYLPLAHIFDRVIEEC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 285 MLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDFASKRKEAELRSGI--IRNN 360
Cdd:PLN02614 290 FIQHGAAIGFWRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKKLSDGgfLKKFVFDSAFSYKFGNMKKGQshVEAS 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 361 SLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW-TAGHVGAPMPCNL 439
Cdd:PLN02614 370 PLCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELdMLGTVGPPVPNVD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 440 IKLVDVEEMNY--MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGE 517
Cdd:PLN02614 450 IRLESVPEMEYdaLASTPRGEICIRGKTLFSGYYKREDLTKEVL-IDGWLHTGDVGEWQPNGSMKIIDRKKNIFKLSQGE 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 518 YIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSG 597
Cdd:PLN02614 529 YVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKMAKEKK 608
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1832481686 598 LKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYSTIK 648
Cdd:PLN02614 609 MKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMYKTTN 659
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
58-645 |
5.70e-135 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 411.43 E-value: 5.70e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 58 PCLGSRK---------PDQ---------PYEWLSYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCF 119
Cdd:PLN02387 75 RLLGTRKlisrefetsSDGrkfeklhlgEYEWITYGQVFERVCNFASGLVALGHNK--EERVAIFADTRAEWLIALQGCF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 120 AYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLleGVENKLiPGLKIIVVMDAYGSELVERG-QRCGVEVTS 198
Cdd:PLN02387 153 RQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLI--DISSQL-ETVKRVIYMDDEGVDSDSSLsGSSNWTVSS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 199 MKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVkatenTVNP--CPDDTLISFLPLAHM 276
Cdd:PLN02387 230 FSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVM-----TVVPklGKNDVYLAYLPLAHI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 277 FERVVECVMLCHGAKIGFfqGDIRLLMD-----------DLKVLQPTVFPVVPRLLNRMFDRIFGQANTT--LKRWLLDF 343
Cdd:PLN02387 305 LELAAESVMAAVGAAIGY--GSPLTLTDtsnkikkgtkgDASALKPTLMTAVPAILDRVRDGVRKKVDAKggLAKKLFDI 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 344 ASKRKEAELR------SGIIRnnSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG 417
Cdd:PLN02387 383 AYKRRLAAIEgswfgaWGLEK--LLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 418 CCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEA--LDKDG--WLHTG 490
Cdd:PLN02387 461 ATFSEWDDTSVGRVGPPLPCCYVKLVSWEEGGYLISDKpmpRGEIVIGGPSVTLGYFKNQEKTDEVykVDERGmrWFYTG 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 491 DIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGFE- 569
Cdd:PLN02387 541 DIGQFHPDGCLEIIDRKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDy 620
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481686 570 GSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 645
Cdd:PLN02387 621 SNFAELCEKEEAVKEVQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLYE 696
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
63-514 |
7.87e-131 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 391.29 E-value: 7.87e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 63 RKPDQP------YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 136
Cdd:pfam00501 7 RTPDKTalevgeGRRLTYRELDERANRLAAGLRALGVG--KGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 137 ITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDAYGSELVergqrcgvevtsMKAMEDLGRANRRKPKPP 216
Cdd:pfam00501 85 LAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEP------------LPEEAKPADVPPPPPPPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVEC-VMLCHGAKIGFF 295
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLlGPLLAGATVVLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 QGDIRL----LMDDLKVLQPTVFPVVPRLLNRMFDrifgqaNTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkv 371
Cdd:pfam00501 233 PGFPALdpaaLLELIERYKVTVLYGVPTLLNMLLE------AGAPKRALL------------------------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 372 qsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDW---TAGHVGAPMPCNLIKLVDVEEM 448
Cdd:pfam00501 277 -----SSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETG 351
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481686 449 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 514
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
72-644 |
7.40e-104 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 330.79 E-value: 7.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfV 151
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLT--KGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAI-V 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPEKAKLLLEGVENKLIPGLKIIvvmdaYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPE---DLAVICFTS 228
Cdd:PTZ00216 199 CNGKNVPNLLRLMKSGGMPNTTII-----YLDSLPASVDTEGCRLVAWTDVVAKGHSAGSHHPLNIPEnndDLALIMYTS 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 229 GTTGNPKGAMVTHRNIVSDCSAFV-KATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMD--- 304
Cdd:PTZ00216 274 GTTGDPKGVMHTHGSLTAGILALEdRLNDLIGPPEEDETYCSYLPLAHIMEFGVTNIFLARGALIGF--GSPRTLTDtfa 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 305 ----DLKVLQPTVFPVVPRLlnrmFDRI----------FGqantTLKRWLLDFASKRKEAELRSGiiRNNSLWDRLIFHK 370
Cdd:PTZ00216 352 rphgDLTEFRPVFLIGVPRI----FDTIkkaveaklppVG----SLKRRVFDHAYQSRLRALKEG--KDTPYWNEKVFSA 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 371 VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCqFYEGYGQTECTagCC--LTMPGDWTAGHVGAPMPCNLIKLVDVEEM 448
Cdd:PTZ00216 422 PRAVLGGRVRAMLSGGGPLSAATQEFVNVVFGM-VIQGWGLTETV--CCggIQRTGDLEPNAVGQLLKGVEMKLLDTEEY 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENI 527
Cdd:PTZ00216 499 KHTdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGWFHTGDVGSIAANGTLRIIGRVKALAKNCLGEYIALEALEAL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 528 YMRSEPVAQ----VFVHgeSLQAFLIAIVVPDVETLCSWAQKRGFEGSFEELCRNKDVKKAILEDMVRLGKDSGLKPFEQ 603
Cdd:PTZ00216 579 YGQNELVVPngvcVLVH--PARSYICALVLTDEAKAMAFAKEHGIEGEYPAILKDPEFQKKATESLQETARAAGRKSFEI 656
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1832481686 604 VKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 644
Cdd:PTZ00216 657 VRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
67-630 |
1.83e-96 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 304.28 E-value: 1.83e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 67 QPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAEL 146
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGLRSLGVK--AGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 147 SLVFVdkpekaklllegvENklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppAPEDLAVICF 226
Cdd:cd17640 79 VALVV-------------EN--------------------------------------------------DSDDLATIIY 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFfqGDIRLLMDDL 306
Cdd:cd17640 96 TSGTTGNPKGVMLTHANLLHQIRSLSD----IVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAY--TSIRTLKDDL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 307 KVLQPTVFPVVPRLlnrmfdrifgqanttlkrWlldfaskrkEAeLRSGI---IRNNSLWDRLIFHKVQSslGGRVRLMV 383
Cdd:cd17640 170 KRVKPHYIVSVPRL------------------W---------ES-LYSGIqkqVSKSSPIKQFLFLFFLS--GGIFKFGI 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 384 TGAAPVSATVLTFLRaALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKG 463
Cdd:cd17640 220 SGGGALPPHVDTFFE-AIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRG 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 464 PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGES 543
Cdd:cd17640 299 PQVMKGYYKNPEATSKVLDSDGWFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQD 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 544 lQAFLIAIVVPDVETLCSWAQKRG--FEGSFEELCRNKDVKKAI-LEDMVRLGKDSGLKPFEQVKGITLHPELFsIDNGL 620
Cdd:cd17640 379 -QKRLGALIVPNFEELEKWAKESGvkLANDRSQLLASKKVLKLYkNEIKDEISNRPGFKSFEQIAPFALLEEPF-IENGE 456
|
570
....*....|
gi 1832481686 621 LTPTMKAKRP 630
Cdd:cd17640 457 MTQTMKIKRN 466
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
69-629 |
1.23e-81 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 266.64 E-value: 1.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 69 YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSL 148
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLE--PGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 149 VFVDKPEKAKLLLEGVenkliPGlKIIVVMDAYGSELvergqRCGVEVTSMKAMedlGRANRRKPkPPAPEDLAVICFTS 228
Cdd:cd05932 82 LFVGKLDDWKAMAPGV-----PE-GLISISLPPPSAA-----NCQYQWDDLIAQ---HPPLEERP-TRFPEQLATLIYTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 229 GTTGNPKGAMVTHRNIVSDCSAFVkateNTVNPCPDDTLISFLPLAHMFERV-VECVMLCHGAKIgFFQGDIRLLMDDLK 307
Cdd:cd05932 147 GTTGQPKGVMLTFGSFAWAAQAGI----EHIGTEENDRMLSYLPLAHVTERVfVEGGSLYGGVLV-AFAESLDTFVEDVQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 308 VLQPTVFPVVPRLLNRMFDRIFgqanttlkrwlldfaSKRKEAELRsgIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGA 386
Cdd:cd05932 222 RARPTLFFSVPRLWTKFQQGVQ---------------DKIPQQKLN--LLLKIPVVNSLVKRKVLKGLGlDQCRLAGCGS 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 387 APVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEGEVCVKGPNV 466
Cdd:cd05932 285 APVPPALLEWYRS-LGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE-----------DGEILVRSPAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 467 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQA 546
Cdd:cd05932 353 MMGYYKDPEATAEAFTADGFLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 547 FLIAIVVPDVETLCSWAQKRG-FEGSFeelcrnkdvkKAILEDMvrlgkDSGLKPFEQVKGITLHPELFSIDNGLLTPTM 625
Cdd:cd05932 433 PLALVVLSEEARLRADAFARAeLEASL----------RAHLARV-----NSTLDSHEQLAGIVVVKDPWSIDNGILTPTL 497
|
....
gi 1832481686 626 KAKR 629
Cdd:cd05932 498 KIKR 501
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
63-566 |
3.44e-76 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 250.50 E-value: 3.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 63 RKPDQP-----YEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 137
Cdd:COG0318 11 RHPDRPalvfgGRRLTYAELDARARRLAAALRALGVG--PGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 138 TYIVNKAELSLVFVdkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppa 217
Cdd:COG0318 89 AYILEDSGARALVT------------------------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 pedlAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI---- 292
Cdd:COG0318 103 ----ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT----PGDVVLVALPLFHVFGLTVGLLApLLAGATLvllp 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELRSgiirnnslwdrlifhkvq 372
Cdd:COG0318 175 RF---DPERVLELIERERVTVLFGVPTMLARLLRH-----------------PEFARYDLSS------------------ 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 sslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNY 450
Cdd:COG0318 217 ------LRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERrpGSVGRPLPGVEVRIVD-EDGRE 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 451 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMR 530
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISG-GENVYPAEVEEVLAA 367
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1832481686 531 SEPVAQVFV-------HGESLQAFLI--AIVVPDVETLCSWAQKR 566
Cdd:COG0318 368 HPGVAEAAVvgvpdekWGERVVAFVVlrPGAELDAEELRAFLRER 412
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
73-629 |
7.05e-73 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 245.41 E-value: 7.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 73 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIE---QGCFAYSMvivPLYDTLGNEAITYIVNKAELSLV 149
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVG--RGDVVAILGDNRPEWVWAElaaQAIGALSL---GIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 150 FVDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVERGQrcgveVTSMKAMEDLGRA-NRRKPK-------PPAPEDL 221
Cdd:cd17641 88 IAEDEEQVDKLLEIADR--IPSVRYVIYCDPRGMRKYDDPR-----LISFEDVVALGRAlDRRDPGlyerevaAGKGEDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 222 AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQgDIR 300
Cdd:cd17641 161 AVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADPLG----PGDEYVSVLPLPWIGEQMYSVGQaLVCGFIVNFPE-EPE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 301 LLMDDLKVLQPTVFPVVPRLLNRM--FDRIFGQANTTLKRWLLDF--------ASKRKEAELRSGIIRNNS-LWDRLIFH 369
Cdd:cd17641 236 TMMEDLREIGPTFVLLPPRVWEGIaaDVRARMMDATPFKRFMFELgmklglraLDRGKRGRPVSLWLRLASwLADALLFR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 370 KVQSSLG-GRVRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVeem 448
Cdd:cd17641 316 PLRDRLGfSRLRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDEV--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 nymaaegeGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIY 528
Cdd:cd17641 392 --------GEILVRSPGVFVGYYKNPEATAEDFDEDGWLHTGDAGYFKENGHLVVIDRAKDVGTTSDGTRFSPQFIENKL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 529 MRSEPVAQVFVHGESlQAFLIAIVVPDVETLCSWAQKRGFE-GSFEELCRNKDVKKAILEDMVRLGKDsgLKPFEQV-KG 606
Cdd:cd17641 464 KFSPYIAEAVVLGAG-RPYLTAFICIDYAIVGKWAEQRGIAfTTYTDLASRPEVYELIRKEVEKVNAS--LPEAQRIrRF 540
|
570 580
....*....|....*....|...
gi 1832481686 607 ITLHPELfSIDNGLLTPTMKAKR 629
Cdd:cd17641 541 LLLYKEL-DADDGELTRTRKVRR 562
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
64-644 |
7.27e-73 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 246.11 E-value: 7.27e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 64 KPDQPYEWLSYKQVAELseCIGSAliqKGF-KTAPDQF--IGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYI 140
Cdd:cd05933 1 KRGDKWHTLTYKEYYEA--CRQAA---KAFlKLGLERFhgVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 141 VNKAELSLVFVDKPEKAKLLLEgVENKLiPGLKIIVvmdAYGSELVERGQRcgveVTSMKAMEDLGR-----ANRRKPKP 215
Cdd:cd05933 76 AETSEANILVVENQKQLQKILQ-IQDKL-PHLKAII---QYKEPLKEKEPN----LYSWDEFMELGRsipdeQLDAIISS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 216 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVEcVMLC--HGAKIG 293
Cdd:cd05933 147 QKPNQCCTLIYTSGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVGQESVVSYLPLSHIAAQILD-IWLPikVGGQVY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 294 FFQGDIR--LLMDDLKVLQPTVFPVVPRLLNRMFDRI--FGQANTTLKRWLLDFAsKRKEAE-------LRSGIIRNNSL 362
Cdd:cd05933 226 FAQPDALkgTLVKTLREVRPTAFMGVPRVWEKIQEKMkaVGAKSGTLKRKIASWA-KGVGLEtnlklmgGESPSPLFYRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 363 WDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLrAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIK 441
Cdd:cd05933 305 AKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 442 LVDVEemnymaAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAP 521
Cdd:cd05933 384 IHNPD------ADGIGEICFWGRHVFMGYLNMEDKTEEAIDEDGWLHSGDLGKLDEDGFLYITGRIKELIITAGGENVPP 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 522 EKIEN-IYMRSEPVAQVFVHGESLQaFLIAIVV----PDVET----------LCSWAQKRGFEGS-FEELCRNKD--VKK 583
Cdd:cd05933 458 VPIEDaVKKELPIISNAMLIGDKRK-FLSMLLTlkceVNPETgepldelteeAIEFCRKLGSQATrVSEIAGGKDpkVYE 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832481686 584 AILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLY 644
Cdd:cd05933 537 AIEEGIKRVNKKAISNA-QKIQKWVILEKDFSVPGGELGPTMKLKRPVVAKKYKDEIDKLY 596
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
58-622 |
2.53e-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: 233.50 E-value: 2.53e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 58 PCLGSRK---PDQPYE-WLSYKQVAELSECIGSALIQKGFKTA----------PDQFIGIFAQNRPEWVIIEQGCFAYSM 123
Cdd:cd17632 39 PALGQRAtelVTDPATgRTTLRLLPRFETITYAELWERVGAVAaahdpeqpvrPGDFVAVLGFTSPDYATVDLALTRLGA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 124 VIVPLYDTLGNEAITYIVNKAELSLVFVDK---PEKAKLLLEGvenkliPGLKIIVVMDaYGSEL----------VERGQ 190
Cdd:cd17632 119 VSVPLQAGASAAQLAPILAETEPRLLAVSAehlDLAVEAVLEG------GTPPRLVVFD-HRPEVdahraalesaRERLA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 191 RCGVEVTSMKAMEDLGRANRRKPKPPAPED---LAVICFTSGTTGNPKGAMVTHRNIVSdcsAFVKATENTVNPCPDDTL 267
Cdd:cd17632 192 AVGIPVTTLTLIAVRGRDLPPAPLFRPEPDddpLALLIYTSGSTGTPKGAMYTERLVAT---FWLKVSSIQDIRPPASIT 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 268 ISFLPLAHMFERVVECVMLCHGAkIGFFQG--DIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIfgQAntTLKRWLLDFA- 344
Cdd:cd17632 269 LNFMPMSHIAGRISLYGTLARGG-TAYFAAasDMSTLFDDLALVRPTELFLVPRVCDMLFQRY--QA--ELDRRSVAGAd 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 345 ----SKRKEAELRsgiirnnslwdrlifhkvQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCL 420
Cdd:cd17632 344 aetlAERVKAELR------------------ERVLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE--AGAVI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 421 TmpgdwtAGHVGAPmPCNLIKLVDVEEMNYMAAEG---EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLP 497
Cdd:cd17632 404 L------DGVIVRP-PVLDYKLVDVPELGYFRTDRphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGFYRTGDVMAELG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 498 NGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRgfegsfeelcr 577
Cdd:cd17632 477 PDRLVYVDRRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTAR----------- 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1832481686 578 nkdVKKAILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLT 622
Cdd:cd17632 546 ---LRAALAESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
72-629 |
8.16e-68 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 228.87 E-value: 8.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKTAPDqfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDR--VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPEkaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapeDLAVICFTSGTT 231
Cdd:cd05914 86 SDED----------------------------------------------------------------DVALINYTSGTT 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVSD---CSAFVKATENtvnpcpdDTLISFLPLAHMFERVVECVM-LCHGAKIGFFQGDIRLLMDDLK 307
Cdd:cd05914 102 GNSKGVMLTYRNIVSNvdgVKEVVLLGKG-------DKILSILPLHHIYPLTFTLLLpLLNGAHVVFLDKIPSAKIIALA 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 308 VLQPTVFPVVPRLLNRMFDRIFGQAN-TTLKRWLLDFASKRKEAELRSgiirnnslwdrLIFHKVQSSLGGRVRLMVTGA 386
Cdd:cd05914 175 FAQVTPTLGVPVPLVIEKIFKMDIIPkLTLKKFKFKLAKKINNRKIRK-----------LAFKKVHEAFGGNIKEFVIGG 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 387 APVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPmpcnlIKLVDVEEMNYMAAEGEGEVCVKGPNV 466
Cdd:cd05914 244 AKINPDVEEFLRT-IGFPYTIGYGMTETAPIISYSPPNRIRLGSAGKV-----IDGVEVRIDSPDPATGEGEIIVRGPNV 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 467 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVA--QVFVHGESL 544
Cdd:cd05914 318 MKGYYKNPEATAEAFDKDGWFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKINNMPFVLesLVVVQEKKL 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 545 QAflIAIVVPDvetlcswaqkrgFEGSFEELCRNKdvKKAILEDmVRLGKDSGLKPFEQVKGITLHPELFSidnglLTPT 624
Cdd:cd05914 398 VA--LAYIDPD------------FLDVKALKQRNI--IDAIKWE-VRDKVNQKVPNYKKISKVKIVKEEFE-----KTPK 455
|
....*
gi 1832481686 625 MKAKR 629
Cdd:cd05914 456 GKIKR 460
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
220-566 |
6.84e-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: 217.15 E-value: 6.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKI----GFF 295
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL----AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVvllpKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 QGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiirnnslwdrlifhkvqssl 375
Cdd:cd04433 77 PEAALELIEREKV---TILLGVPTLLARLLKAP-----------------ESAGYDLSS--------------------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 376 ggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT--AGHVGAPMPCNLIKLVDVEEmNYMAA 453
Cdd:cd04433 116 ---LRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVATGPPDDDArkPGSVGRPVPGVEVRIVDPDG-GELPP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 454 EGEGEVCVKGPNVFQGYLKDPAKTAEAlDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEP 533
Cdd:cd04433 192 GEIGELVVRGPSVMKGYWNNPEATAAV-DEDGWYRTGDLGRLDEDGYLYIVGRLKDMIK-SGGENVYPAEVEAVLLGHPG 269
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832481686 534 VAQVFVHG---ESLQAFLIAIVVP------DVETLCSWAQKR 566
Cdd:cd04433 270 VAEAAVVGvpdPEWGERVVAVVVLrpgadlDAEELRAHVRER 311
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
72-541 |
1.40e-64 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 220.93 E-value: 1.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLK--KGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPEKAKLLleGVENKLIPGLKIIVvMDAYGSELVERGQrcGVEVTSMKAMEDlgranRRKPKPPAPEDLAVICFTSGTT 231
Cdd:cd05911 89 DPDGLEKVK--EAAKELGPKDKIIV-LDDKPDGVLSIED--LLSPTLGEEDED-----LPPPLKDGKDDTAAILYSSGTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVSDCSaFVKATEnTVNPCPDDTLISFLPLAHMFervveCVMLCHGAKIgffQG---------DIRLL 302
Cdd:cd05911 159 GLPKGVCLSHRNLIANLS-QVQTFL-YGNDGSNDVILGFLPLYHIY-----GLFTTLASLL---NGatviimpkfDSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 303 MDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRlifHKVQSslggrVRLM 382
Cdd:cd05911 229 LDLIEKYKITFLYLVPPIAAALA---------------------------------KSPLLDK---YDLSS-----LRVI 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 383 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCV 461
Cdd:cd05911 268 LSGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDSLGPNEPGEICV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 462 KGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:cd05911 348 RGPQVMKGYYNNPEATKETFDEDGWLHTGDIGYFDEDGYLYIVDRKKELIKY-KGFQVAPAELEAVLLEHPGVADAAVIG 426
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
61-566 |
2.73e-62 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 215.54 E-value: 2.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 61 GSRKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIieqGCFAYSM---VIVPLYDTL 132
Cdd:PRK07656 15 ARRFGDKEAyvfgdQRLTYAELNARVRRAAAALAALGIG--KGDRVAIWAPNSPHWVI---AALGALKagaVVVPLNTRY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 133 GNEAITYIVNKAELSLVFVdkpekAKLLLeGVENKL---IPGLKIIVVMDaygselVERGQRCGVEVTSMKAMedLGRAN 209
Cdd:PRK07656 90 TADEAAYILARGDAKALFV-----LGLFL-GVDYSAttrLPALEHVVICE------TEEDDPHTEKMKTFTDF--LAAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 210 RRKPKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMF---ERVVECVM 285
Cdd:PRK07656 156 PAERAPEvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLT----EGDRYLAANPFFHVFgykAGVNAPLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 286 lcHGAKIgffqgDIRLLMDDLKVLQ------PTVFPVVPrllnrmfdrifgqantTLKRWLLDFAsKRKEAELRSgiirn 359
Cdd:PRK07656 232 --RGATI-----LPLPVFDPDEVFRlieterITVLPGPP----------------TMYNSLLQHP-DRSAEDLSS----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 360 nslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTAGCCLTMPGD---WTAGHVGAPM 435
Cdd:PRK07656 283 -------------------LRLAVTGAASMPVALLERFESELGVDiVLTGYGLSEASGVTTFNRLDDdrkTVAGTIGTAI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 436 PCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 514
Cdd:PRK07656 344 AGVENKIVN--ELGEEVPVGEvGELLVRGPNVMKGYYDDPEATAAAIDADGWLHTGDLGRLDEEGYLYIVDRKKDMF-IV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832481686 515 QGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVP------DVETLCSWAQKR 566
Cdd:PRK07656 421 GGFNVYPAEVEEVLYEHPAVAEAAVigvpderLGEVGKAY----VVLkpgaelTEEELIAYCREH 481
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
63-554 |
1.53e-61 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 212.04 E-value: 1.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 63 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 137
Cdd:cd05936 11 RFPDKTAlifmgRKLTYRELDALAEAFAAGLQNLGVQ--PGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPREL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 138 TYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkaMEDLGRANRRKPKPPA 217
Cdd:cd05936 89 EHILNDSGAKALIVAVS-----------------------------------------------FTDLLAAGAPLGERVA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 --PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAfVKATENTVNPcPDDTLISFLPLAHMFERVVECV-MLCHGAKIGF 294
Cdd:cd05936 122 ltPEDVAVLQYTSGTTGVPKGAMLTHRNLVANALQ-IKAWLEDLLE-GDDVVLAALPLFHVFGLTVALLlPLALGATIVL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 295 FQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfASKRKEAELRSgiirnnslwdrlifhkvqs 373
Cdd:cd05936 200 IPRfRPIGVLKEIRKHRVTIFPGVPTMYIALLN-----------------APEFKKRDFSS------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 374 slggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMA 452
Cdd:cd05936 244 -----LRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVD-DDGEELP 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 453 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 532
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGWLRTGDIGYMDEDGYFFIVDRKKDMI-IVGGFNVYPREVEEVLYEHP 395
|
490 500
....*....|....*....|....*....
gi 1832481686 533 PVAQVFV-------HGESLQAFliaiVVP 554
Cdd:cd05936 396 AVAEAAVvgvpdpySGEAVKAF----VVL 420
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
73-542 |
8.38e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 211.58 E-value: 8.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 73 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIieqgC-FAYSM---VIVPLYDTLGNEAITYIVNKAELSL 148
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVK--KGDRVAVFDWNSHEYLE----AyFAVPKigaVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 149 VFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSElvergqRCGVEVTSMKAMedLGRANRRKPKPPAPE-DLAVICFT 227
Cdd:PRK06187 107 VLVD-SEFVPLL-AAILPQL-PTVRTVIVEGDGPAA------PLAPEVGEYEEL--LAAASDTFDFPDIDEnDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 228 SGTTGNPKGAMVTHRNIVSD---CSAFVKATentvnpcPDDTLISFLPLAHMFERVVECVMLCHGAKI---GFFqgDIRL 301
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHslaVCAWLKLS-------RDDVYLVIVPMFHVHAWGLPYLALMAGAKQvipRRF--DPEN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 302 LMDDLKVLQPTVFPVVPRLLNRMFdrifgQANTTLKRWLldfaskrkeaelrsgiirnnslwdrlifhkvqsslgGRVRL 381
Cdd:PRK06187 247 LLDLIETERVTFFFAVPTIWQMLL-----KAPRAYFVDF------------------------------------SSLRL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 382 MVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT-AGCCLT----MPGDWT-AGHVGAPMPCNLIKLVDvEEMNYMAAEG 455
Cdd:PRK06187 286 VIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqLPGQWTkRRSAGRPLPGVEARIVD-DDGDELPPDG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 456 E--GEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEP 533
Cdd:PRK06187 365 GevGEIIVRGPWLMQGYWNRPEATAETID-GGWLHTGDVGYIDEDGYLYITDRIKDVIISG-GENIYPRELEDALYGHPA 442
|
....*....
gi 1832481686 534 VAQVFVHGE 542
Cdd:PRK06187 443 VAEVAVIGV 451
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
220-566 |
1.54e-45 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 167.85 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVV----------ECVMLchg 289
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT----EDDVLLHVLPLHHVHGLVNallcplfagaSVEFL--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 290 akiGFF---QGDIRLLMDDLkvlqpTVFPVVPRllnrMFDRIFGQANTTLKrwllDFASKRKEAElrsgiirnnslwdrl 366
Cdd:cd05941 163 ---PKFdpkEVAISRLMPSI-----TVFMGVPT----IYTRLLQYYEAHFT----DPQFARAAAA--------------- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 367 ifhkvqsslgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMP--GDWTAGHVGAPMPCNLIKLVD 444
Cdd:cd05941 212 ----------ERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTE--IGMALSNPldGERRPGTVGMPLPGVQARIVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 445 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIFKlAQGEYIAPEK 523
Cdd:cd05941 280 EETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGWFKTGDLGVVDEDGYYWILGRSSvDIIK-SGGYKVSALE 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832481686 524 IENIYMRSEPVAQVFVHGESLQAF---LIAIVVP-------DVETLCSWAQKR 566
Cdd:cd05941 359 IERVLLAHPGVSECAVIGVPDPDWgerVVAVVVLragaaalSLEELKEWAKQR 411
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
72-567 |
1.52e-41 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 157.49 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAeLSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd05909 8 LTYRKLL-TGAIALARKLAKM--TKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKP--EKAKLL-------------LEGVENKLIPGLKIIVVMDAYgselvergqrcgveVTSMKAMEDLGRANRRkpkpp 216
Cdd:cd05909 85 SKQfiEKLKLHhlfdveydarivyLEDLRAKISKADKCKAFLAGK--------------FPPKWLLRIFGVAPVQ----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 aPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQ 296
Cdd:cd05909 146 -PDDPAVILFTSGSEGLPKGVVLSHKNLLAN----VEQITAIFDPNPEDVVFGALPFFHSF---------------GLTG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 297 GDIRLLMDDLKVLQ---PTVFPVVPRLLNRMFDRIFGQANTTLKRWLldfasKRKEAELRSGIirnnslwdrlifhkvqs 373
Cdd:cd05909 206 CLWLPLLSGIKVVFhpnPLDYKKIPELIYDKKATILLGTPTFLRGYA-----RAAHPEDFSSL----------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 374 slggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMA 452
Cdd:cd05909 264 ------RLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVETHEEVP 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 453 AEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSE 532
Cdd:cd05909 338 IGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGWYDTGDIGKIDGEGFLTITGRLSRFAKIA-GEMVSLEAIEDILSEIL 415
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1832481686 533 P----VAQVFV----HGESLQAFLIAIvVPDVETLCSWAQKRG 567
Cdd:cd05909 416 PedneVAVVSVpdgrKGEKIVLLTTTT-DTDPSSLNDILKNAG 457
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
183-527 |
4.51e-41 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 156.63 E-value: 4.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 183 SELVERGQRCGVEVTSMKAMEDLGRANRR------KPKPPAPE----DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV 252
Cdd:cd05904 112 AELAEKLASLALPVVLLDSAEFDSLSFSDllfeadEAEPPVVVikqdDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 253 KATENtvNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMfdr 327
Cdd:cd05904 192 AGEGS--NSDSEDVFLCVLPMFHIYGLSSFALgLLRLGATVvvmpRF---DLEELLAAIERYKVTHLPVVPPIVLAL--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 328 ifgqanttlkrwlldfaskrkeaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFY 406
Cdd:cd05904 264 ------------------------VKSPIVDKYDL----------SSL----RQIMSGAAPLGKELIEAFRAKFpNVDLG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 407 EGYGQTECTAGCCLTMPGDWTAGHVG-----APMPCnlIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL 481
Cdd:cd05904 306 QGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVPNVE--AKIVDPETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832481686 482 DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 527
Cdd:cd05904 384 DKEGWLHTGDLCYIDEDGYLFIVDRLKELIKY-KGFQVAPAELEAL 428
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
62-555 |
6.39e-41 |
|
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: 154.69 E-value: 6.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 62 SRKPDQP-YEW----LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA 136
Cdd:cd17631 6 RRHPDRTaLVFggrsLTYAELDERVNRLAHALRALGVA--KGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 137 ITYIVNKAElslvfvdkpekAKLLLEgvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkpp 216
Cdd:cd17631 84 VAYILADSG-----------AKVLFD------------------------------------------------------ 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 apeDLAVICFTSGTTGNPKGAMVTHRNIvsdcsafvkaTENTVN------PCPDDTLISFLPLAHMFERVVECVM-LCHG 289
Cdd:cd17631 99 ---DLALLMYTSGTTGRPKGAMLTHRNL----------LWNAVNalaaldLGPDDVLLVVAPLFHIGGLGVFTLPtLLRG 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 290 AKI----GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTlkrwllDFASkrkeaelrsgiirnnslwdr 365
Cdd:cd17631 166 GTVvilrKF---DPETVLDLIERHRVTSFFLVPTMIQALLQH--PRFATT------DLSS-------------------- 214
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 366 lifhkvqsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLV 443
Cdd:cd17631 215 -------------LRAVIYGGAPMPERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPEDHrrKLGSAGRPVFFVEVRIV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEK 523
Cdd:cd17631 281 D-PDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGWFHTGDLGRLDEDGYLYIVDRKKDMII-SGGENVYPAE 357
|
490 500 510
....*....|....*....|....*....|....*....
gi 1832481686 524 IENIYMRSEPVAQVFV-------HGESlqafLIAIVVPD 555
Cdd:cd17631 358 VEDVLYEHPAVAEVAVigvpdekWGEA----VVAVVVPR 392
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
218-642 |
1.11e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 152.57 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFVKatentVNPcpdDTLISFLPLAHMFERVVECVMLCHGAK 291
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLyntvvpLCKHSIFKK-----YNP---KTHLSYLPISHIYERVIAYLSFMLGGT 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 292 IGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQAN--TTLKRWLLdfaskRKEAELRSGiiRNNSLWDRL--- 366
Cdd:PTZ00342 375 INIWSKDINYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINnlPPLKRFLV-----KKILSLRKS--NNNGGFSKFleg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 367 IFH---KVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPM-PCNLIKL 442
Cdd:PTZ00342 448 ITHissKIKDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPIFVQHADDNNTESIGGPIsPNTKYKV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 443 VDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPE 522
Cdd:PTZ00342 528 RTWETYKATDTLPKGELLIKSDSIFSGYFLEKEQTKNAFTEDGYFKTGDIVQINKNGSLTFLDRSKGLVKLSQGEYIETD 607
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 523 KIENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETLCSWAQKRGF-------EGSFEELCRNKDVKKAILEDMVR---- 591
Cdd:PTZ00342 608 MLNNLYSQISFINFCVVYGDDSMDGPLAIISVDKYLLFKCLKDDNMlestginEKNYLEKLTDETINNNIYVDYVKgkml 687
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1832481686 592 -LGKDSGLKPFEQVKGITLHPELFSIDNgLLTPTMKAKRPELRNYFRSQIDD 642
Cdd:PTZ00342 688 eVYKKTNLNRYNIINDIYLTSKVWDTNN-YLTPTFKVKRFYVFKDYAFFIDQ 738
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
205-559 |
2.03e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 149.91 E-value: 2.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 205 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKAteNTVNPCpdDTLISFLPLAHMFERVV 281
Cdd:PRK05677 193 KGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmlqCRALMGS--NLNEGC--EILIAPLPLYHIYAFTF 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 282 ECVMLchgakigffqgdirLLMDDLKVLQPTvfpvvPRLLNRMFdrifgqanTTLKRWLLdfaskrkeaelrSGIIRNNS 361
Cdd:PRK05677 269 HCMAM--------------MLIGNHNILISN-----PRDLPAMV--------KELGKWKF------------SGFVGLNT 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 362 LWDRLI----FHKVQSSlggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 437
Cdd:PRK05677 310 LFVALCnneaFRKLDFS---ALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 438 NLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGE 517
Cdd:PRK05677 387 TLCKVID-DDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWLKTGDIALIQEDGYMRIVDRKKDMI-LVSGF 464
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1832481686 518 YIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaIVVPDVETL 559
Cdd:PRK05677 465 NVYPNELEDVLAALPGVLQCAAigvpdekSGEAIKVF---VVVKPGETL 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
66-566 |
3.85e-38 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 147.84 E-value: 3.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 66 DQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVI-----IEQGCfaysmVIVPLYDTLGNEAITYI 140
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAALGIK--KGDRVAIALPNGLEFVVaflaaARAGA-----VVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 141 VNKAELSLVFVDKPEkaklLLEGVENKLIPGLKII-VVMDAYGSELVERGQRCGVEvtsmkameDLGRANRRKPKPPAPE 219
Cdd:cd05926 82 LADLGSKLVLTPKGE----LGPASRAASKLGLAILeLALDVGVLIRAPSAESLSNL--------LADKKNAKSEGVPLPD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAHMFERVVECV-MLCHGAKI----GF 294
Cdd:cd05926 150 DLALILHTSGTTGRPKGVPLTHRNLAAS----ATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLsTLAAGGSVvlppRF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 295 fqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqss 374
Cdd:cd05926 226 ---SASTFWPDVRDYNATWYTAVP----------------TIHQILLNRPEPNPESPP---------------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 375 lgGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgcclTM------PGDWTAGHVGAPMPcNLIKLVDvEEM 448
Cdd:cd05926 265 --PKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAH----QMtsnplpPGPRKPGSVGKPVG-VEVRILD-EDG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 528
Cdd:cd05926 337 EILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGWFRTGDLGYLDADGYLFLTGRIKELINRG-GEKISPLEVDGVL 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1832481686 529 MRSEPVAQ--VF-----VHGESLQAFliaiVVP------DVETLCSWAQKR 566
Cdd:cd05926 416 LSHPAVLEavAFgvpdeKYGEEVAAA----VVLregasvTEEELRAFCRKH 462
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
218-550 |
1.42e-37 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 147.51 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcPDDTLISFLPLAHMFERVVECVMLCH-GAKigffq 296
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGPLLHP-GKELVVTALPLYHIFALTVNCLLFIElGGQ----- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 297 gdirllmdDLKVLQPTVFP-VVPRLLNRMFDRIFGqANTTLKRWLldfaskrkeaelrsgiirNNSLwdrliFHKVQSSl 375
Cdd:PRK08974 279 --------NLLITNPRDIPgFVKELKKYPFTAITG-VNTLFNALL------------------NNEE-----FQELDFS- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 376 ggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCcltmPGDWT--AGHVGAPMPCNLIKLVDvEEMNY 450
Cdd:PRK08974 326 --SLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECSplvSVN----PYDLDyySGSIGLPVPSTEIKLVD-DDGNE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 451 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMR 530
Cdd:PRK08974 399 VPPGEPGELWVKGPQVMLGYWQRPEATDEVI-KDGWLATGDIAVMDEEGFLRIVDRKKDMI-LVSGFNVYPNEIEDVVML 476
|
330 340
....*....|....*....|....*..
gi 1832481686 531 SEPVAQVF-------VHGESLQAFLIA 550
Cdd:PRK08974 477 HPKVLEVAavgvpseVSGEAVKIFVVK 503
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
73-527 |
5.39e-37 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 145.36 E-value: 5.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 73 SYKQVAELSECIGSALIQKGFKTapDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVD 152
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQ--NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 153 KPEKAKLLleGVENKLiPGLKIIVVMDaygSELVERGQRCgveVTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSG 229
Cdd:cd17642 124 KKGLQKVL--NVQKKL-KIIKTIIILD---SKEDYKGYQC---LYTFITQNLPPGFNEYDFKPPSfdrDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 230 TTGNPKGAMVTHRNIvsdCSAFVKATENTV--NPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGF---FQGDIRL-LM 303
Cdd:cd17642 195 STGLPKGVQLTHKNI---VARFSHARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLmykFEEELFLrSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 304 DDLKV----LQPTVFPVVPRllnrmfdrifgqanttlkrwlldfaskrkeaelrSGIIRNNSLwdrlifhkvqSSLggrv 379
Cdd:cd17642 272 QDYKVqsalLVPTLFAFFAK----------------------------------STLVDKYDL----------SNL---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 380 RLMVTGAAPVSATVLTFLRAALGCQFY-EGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGE 458
Cdd:cd17642 304 HEIASGGAPLSKEVGEAVAKRFKLPGIrQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTGKTLGPNERGE 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832481686 459 VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 527
Cdd:cd17642 384 LCVKGPMIMKGYVNNPEATKALIDKDGWLHSGDIAYYDEDGHFFIVDRLKSLIKY-KGYQVPPAELESI 451
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-579 |
2.16e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 139.72 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFV----KATENTVNPCPddtlisfLPLAHMFERVVEcVMLC--HGAK 291
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNN-GYFIgerlGLTEQDRLCIP-------VPLFHCFGSVLG-VLACltHGAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 292 IGFfqgdIRLLMDDLKVLQP------TVFPVVPRllnrMFDRIFGQAnttlKRWLLDFASkrkeaeLRSGIIrnnslwdr 365
Cdd:cd05917 72 MVF----PSPSFDPLAVLEAiekekcTALHGVPT----MFIAELEHP----DFDKFDLSS------LRTGIM-------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 366 lifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 441
Cdd:cd05917 126 -------------------AGAPCPPELMKRVIEVMNMkDVTIAYGMTETSPVSTQTRTDDSIekrVNTVGRIMPHTEAK 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 442 LVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIA 520
Cdd:cd05917 187 IVD-PEGGIVPPVGVpGELCIRGYSVMKGYWNDPEKTAEAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGENIY 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481686 521 PEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQ-KRGFEGSFEEL---CRNK 579
Cdd:cd05917 265 PREIEEFLHTHPKVSDVQVVG-----------VPDErygEEVCAWIRlKEGAELTEEDIkayCKGK 319
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
220-566 |
2.93e-36 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 138.79 E-value: 2.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVM-LCHGAKI---GFF 295
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLT----EDDRYLIINPFFHTFGYKAGIVAcLLTGATVvpvAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 qgDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRifgqanttlkrwlldfaSKRKEAELrsgiirnnslwdrlifhkvqSSL 375
Cdd:cd17638 77 --DVDAILEAIERERITVLPGPPTLFQSLLDH-----------------PGRKKFDL--------------------SSL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 376 ggrvRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTECTagcCLTM--PGD---WTAGHVGAPMPcnliklvDVEemn 449
Cdd:cd17638 118 ----RAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG---VATMcrPGDdaeTVATTCGRACP-------GFE--- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 450 yMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 529
Cdd:cd17638 181 -VRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGWLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVYPAEVEGALA 258
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1832481686 530 RSEPVAQVFV-------HGESLQAFLIA--IVVPDVETLCSWAQKR 566
Cdd:cd17638 259 EHPGVAQVAVigvpderMGEVGKAFVVArpGVTLTEEDVIAWCRER 304
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
74-566 |
3.53e-36 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 141.05 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 74 YKQVAELSECIGSALIQKGfktapdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDk 153
Cdd:TIGR01923 6 DCEAAHLAKALKAQGIRSG------SRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 154 pekAKLLLEGVENKLIPGLKiivvmdAYGselvergqRCGVEVTSMKAMEDLgranrrkpkppapedlAVICFTSGTTGN 233
Cdd:TIGR01923 79 ---SLLEEKDFQADSLDRIE------AAG--------RYETSLSASFNMDQI----------------ATLMFTSGTTGK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 234 PKGAMVTHRNIvsdcSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGDIRLLmDDLKVLQPTV 313
Cdd:TIGR01923 126 PKAVPHTFRNH----YASAVGSKENLGFTEDDNWLLSLPLYHISGLSILFRWLIEGATLRIVDKFNQLL-EMIANERVTH 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 314 FPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnnslwdrlifhkvqsslggrvrlmvtGAAPVSATV 393
Cdd:TIGR01923 201 ISLVPTQLNRLLDE--GGHNENLRKILL-------------------------------------------GGSAIPAPL 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 394 LTFLRAaLGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHVGAPMPCNLIKL-VDveemnymAAEGEGEVCVKGPNVFQGYL 471
Cdd:TIGR01923 236 IEEAQQ-YGLPIYLSYGMTEtCSQVTTATPEMLHARPDVGRPLAGREIKIkVD-------NKEGHGEIMVKGANLMKGYL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 472 kDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESL 544
Cdd:TIGR01923 308 -YQGELTPAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLI-ISGGENIYPEEIETVLYQHPGIQEAVVvpkpdaeWGQVP 385
|
490 500
....*....|....*....|..
gi 1832481686 545 QAFLIAIVVPDVETLCSWAQKR 566
Cdd:TIGR01923 386 VAYIVSESDISQAKLIAYLTEK 407
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
62-541 |
5.64e-36 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 142.00 E-value: 5.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 62 SRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIV 141
Cdd:cd12119 16 SRTHEGEVHRYTYAEVAERARRLANALRRLGVK--PGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 142 NKAELSLVFVDkPEKAKLLlEGVENKLiPGLKIIVVMDAYGSELVERGQRCGvevtsmkAMEDL-GRANRRKPKPPAPE- 219
Cdd:cd12119 94 NHAEDRVVFVD-RDFLPLL-EAIAPRL-PTVEHVVVMTDDAAMPEPAGVGVL-------AYEELlAAESPEYDWPDFDEn 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTlisFLPLAHMFErvVE-------CVMLchGAKI 292
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVL--HAMAALLTDGLGLSESDV---VLPVVPMFH--VNawglpyaAAMV--GAKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 ----GFFQGDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRifgqanttLKRWLLDFASKRkeaelrsgiirnnslwdrli 367
Cdd:cd12119 235 vlpgPYLDPASLAeLIEREGV---TFAAGVPTVWQGLLDH--------LEANGRDLSSLR-------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 368 fhkvqsslggrvRLMVTGAAPVSATVLTFlrAALGCQFYEGYGQTE-CTAGCCLTMPGDWTAGHV----------GAPMP 436
Cdd:cd12119 284 ------------RVVIGGSAVPRSLIEAF--EERGVRVIHAWGMTEtSPLGTVARPPSEHSNLSEdeqlalrakqGRPVP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 437 CNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAkTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLA 514
Cdd:cd12119 350 GVELRIVD-DDGRELPWDGKavGELQVRGPWVTKSYYKNDE-ESEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSG 427
|
490 500
....*....|....*....|....*..
gi 1832481686 515 qGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:cd12119 428 -GEWISSVELENAIMAHPAVAEAAVIG 453
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
205-510 |
6.59e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 142.83 E-value: 6.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 205 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCS---AFVKATentvnPCPDDTLISFLPLAHMF--ER 279
Cdd:PRK05605 205 GGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkAWVPGL-----GDGPERVLAALPMFHAYglTL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 280 VVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLlnrmFDRIfgqanttlkrwlldfaskRKEAELRsGIirn 359
Cdd:PRK05605 280 CLTLAVSIGGELVLLPAPDIDLILDAMKKHPPTWLPGVPPL----YEKI------------------AEAAEER-GV--- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 360 nslwdrlifhkvqsSLGGrVRLMVTGAA--PVSaTVLTFlRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMP 436
Cdd:PRK05605 334 --------------DLSG-VRNAFSGAMalPVS-TVELW-EKLTGGLLVEGYGLTETSPiIVGNPMSDDRRPGYVGVPFP 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832481686 437 CNLIKLVDVEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHI 510
Cdd:PRK05605 397 DTEVRIVDPEDPDETMPDGEeGELLVRGPQVFKGYWNRPEETAKSF-LDGWFRTGDVVVMEEDGFIRIVDRIKEL 470
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
198-550 |
6.87e-35 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 139.57 E-value: 6.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 198 SMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD------CSAFVKATENTVNPCPDDTLISFL 271
Cdd:PRK12492 186 PFKQALRQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANmlqvraCLSQLGPDGQPLMKEGQEVMIAPL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 272 PLAHMFERVVECVMLchgakigFFQGDIRLLMDDlkvlqptvfpvvPRLLNRMFDRifgqanttLKRWLLdfaskrkeae 351
Cdd:PRK12492 266 PLYHIYAFTANCMCM-------MVSGNHNVLITN------------PRDIPGFIKE--------LGKWRF---------- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 352 lrSGIIRNNSLWDRLIFHKVQSSLGGRvRLMVT---GAAPVSATVLTFlRAALGCQFYEGYGQTECTAGCCLTMPGDWTA 428
Cdd:PRK12492 309 --SALLGLNTLFVALMDHPGFKDLDFS-ALKLTnsgGTALVKATAERW-EQLTGCTIVEGYGLTETSPVASTNPYGELAR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 429 -GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRK 507
Cdd:PRK12492 385 lGTVGIPVPGTALKVID-DDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGWFKTGDIAVIDPDGFVRIVDRK 463
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1832481686 508 KHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFLIA 550
Cdd:PRK12492 464 KDLI-IVSGFNVYPNEIEDVVMAHPKVANCAAigvpderSGEAVKLFVVA 512
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
65-579 |
7.76e-35 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 139.18 E-value: 7.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 65 PDQPYEWlSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEqgcFAYS-----MV-IVPLYDTlgNEaIT 138
Cdd:PRK08315 38 RDQGLRW-TYREFNEEVDALAKGLLALGIE--KGDRVGIWAPNVPEWVLTQ---FATAkigaiLVtINPAYRL--SE-LE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 139 YIVNKAELS-LVFVDK--------------PEKAKLLLEGVENKLIPGLKIIVVMDAYGSelveRGQRCGVEVTSMKAME 203
Cdd:PRK08315 109 YALNQSGCKaLIAADGfkdsdyvamlyelaPELATCEPGQLQSARLPELRRVIFLGDEKH----PGMLNFDELLALGRAV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 204 DLGRANRRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFVkaTENtVNPCPDDTLISFLPLAHMFErvveC 283
Cdd:PRK08315 185 DDAELAARQATL-DPDDPINIQYTSGTTGFPKGATLTHRNILNN-GYFI--GEA-MKLTEEDRLCIPVPLYHCFG----M 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 284 VM-----LCHGAKI-----GFfqgdirllmDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwl 340
Cdd:PRK08315 256 VLgnlacVTHGATMvypgeGF---------DPLATLAaveeerctalygvPTMF--IAELDHPDFAR------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 341 LDFASkrkeaeLRSGI-------IRnnslwdrlIFHKVQSSLGgrvrlM--VTGAapvsatvltflraalgcqfyegYGQ 411
Cdd:PRK08315 312 FDLSS------LRTGImagspcpIE--------VMKRVIDKMH-----MseVTIA----------------------YGM 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 412 TECTAGCCLTMPGD------WTaghVGAPMPCNLIKLVDvEEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD 484
Cdd:PRK08315 351 TETSPVSTQTRTDDplekrvTT---VGRALPHLEVKIVD-PETGETVPRGEqGELCTRGYSVMKGYWNDPEKTAEAIDAD 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 485 GWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCS 561
Cdd:PRK08315 427 GWMHTGDLAVMDEEGYVNIVGRIKDMI-IRGGENIYPREIEEFLYTHPKIQDVQVVG-----------VPDEkygEEVCA 494
|
570 580
....*....|....*....|..
gi 1832481686 562 WAQKR-GFEGSFEEL---CRNK 579
Cdd:PRK08315 495 WIILRpGATLTEEDVrdfCRGK 516
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
205-634 |
2.25e-34 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 138.09 E-value: 2.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 205 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD---CSAFVKATENTVNPCpdDTLISFLPLAHMFERVV 281
Cdd:PRK08751 194 LGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANmqqAHQWLAGTGKLEEGC--EVVITALPLYHIFALTA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 282 ECVMLchgAKIGFFQG------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsg 355
Cdd:PRK08751 272 NGLVF---MKIGGCNHlisnprDMPGFVKELKKTRFTAFTGVNTLFNGLL------------------------------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 356 iirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT-MPGDWTAGHVGAP 434
Cdd:PRK08751 319 ---NTPGFDQIDFSSLKMTLGG-------GMA-VQRSVAERWKQVTGLTLVEAYGLTETSPAACINpLTLKEYNGSIGLP 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 435 MPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkL 513
Cdd:PRK08751 388 IPSTDACIKD--DAGTVLAIGEiGELCIKGPQVMKGYWKRPEETAKVMDADGWLHTGDIARMDEQGFVYIVDRKKDMI-L 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 514 AQGEYIAPEKIENIYMRSEPVAQVfvhgeslqaflIAIVVPDvetlcswaQKRGfegsfeELCRNKDVKK--AILEDMVR 591
Cdd:PRK08751 465 VSGFNVYPNEIEDVIAMMPGVLEV-----------AAVGVPD--------EKSG------EIVKVVIVKKdpALTAEDVK 519
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1832481686 592 LGKDSGLKPFEQVKGITLHPELFSIDNGlltptmKAKRPELRN 634
Cdd:PRK08751 520 AHARANLTGYKQPRIIEFRKELPKTNVG------KILRRELRD 556
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
206-588 |
1.36e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 134.35 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 206 GRANRRKPKPPaPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvecvm 285
Cdd:PRK07787 116 ARSWHRYPEPD-PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT----ADDVLVHGLPLFHV--------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 286 lcHGAKIGffqgdirllmddlkVLQPTvfpvvprllnrmfdRIFGQANTTLKrwlldFASKRKEAELRSGiirnNSL--- 362
Cdd:PRK07787 182 --HGLVLG--------------VLGPL--------------RIGNRFVHTGR-----PTPEAYAQALSEG----GTLyfg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 363 ----WDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCN 438
Cdd:PRK07787 223 vptvWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 439 LIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDR------KKHI 510
Cdd:PRK07787 303 ETRLVD-EDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGWFRTGDVAVVDPDGMHRIVGRestdliKSGG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 511 FKLAQGEyiapekIENIYMRSEPVAQVFVHGE---SLQAFLIAIVVPD-----------VETLCSwAQKRGFEGSF-EEL 575
Cdd:PRK07787 382 YRIGAGE------IETALLGHPGVREAAVVGVpddDLGQRIVAYVVGAddvaadelidfVAQQLS-VHKRPREVRFvDAL 454
|
410
....*....|....*.
gi 1832481686 576 CRN---KDVKKAILED 588
Cdd:PRK07787 455 PRNamgKVLKKQLLSE 470
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
72-579 |
2.28e-33 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 134.90 E-value: 2.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEqgcFAYSMV------IVPLYDTlgnEAITYIVNKAE 145
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQ--PGDRVGIWAPNCAEWLLTQ---FATARIgailvnINPAYRA---SELEYALGQSG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 146 LSLVFVDK---------------PEKAKLLLEGVENKLIPGLKIIVVMDAYGS-------ELVERGqrcgvEVTSMKAME 203
Cdd:PRK12583 118 VRWVICADafktsdyhamlqellPGLAEGQPGALACERLPELRGVVSLAPAPPpgflawhELQARG-----ETVSREALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 204 DLGRANRRkpkppapEDLAVICFTSGTTGNPKGAMVTHRNIVSDcSAFV----KATENtvnpcpdDTLISFLPLAHMFER 279
Cdd:PRK12583 193 ERQASLDR-------DDPINIQYTSGTTGFPKGATLSHHNILNN-GYFVaeslGLTEH-------DRLCVPVPLYHCFGM 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 280 VVeCVMLC--HGAKIgFFQGDirlLMDDLKVLQ-------------PTVFpvVPRLLNRMFDRifgqanttlkrwlLDFA 344
Cdd:PRK12583 258 VL-ANLGCmtVGACL-VYPNE---AFDPLATLQaveeerctalygvPTMF--IAELDHPQRGN-------------FDLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 345 SkrkeaeLRSGIIrnnslwdrlifhkvqsslggrvrlmvtGAAPVSATVLTFLRAALGC-QFYEGYGQTECTAGCCLTMP 423
Cdd:PRK12583 318 S------LRTGIM---------------------------AGAPCPIEVMRRVMDEMHMaEVQIAYGMTETSPVSLQTTA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 424 GD---WTAGHVGAPMPCNLIKLVDVEemNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNG 499
Cdd:PRK12583 365 ADdleRRVETVGRTQPHLEVKVVDPD--GATVPRGEiGELCTRGYSVMKGYWNNPEATAESIDEDGWMHTGDLATMDEQG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 500 TLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDV---ETLCSWAQKR-GFEGSFEEL 575
Cdd:PRK12583 443 YVRIVGRSKDMI-IRGGENIYPREIEEFLFTHPAVADVQVFG-----------VPDEkygEEIVAWVRLHpGHAASEEEL 510
|
....*..
gi 1832481686 576 ---CRNK 579
Cdd:PRK12583 511 refCKAR 517
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
73-559 |
3.10e-33 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 132.42 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 73 SYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVD 152
Cdd:cd05934 5 TYAELLRESARIAAALAALGIR--PGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 153 kpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapedLAVICFTSGTTG 232
Cdd:cd05934 83 --------------------------------------------------------------------PASILYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 233 NPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVEC-VMLCHGAKI--------GFFQGDIRllm 303
Cdd:cd05934 95 PPKGVVITHANLTFAGYYSARRFGLG----EDDVYLTVLPLFHINAQAVSVlAALSVGATLvllprfsaSRFWSDVR--- 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 304 ddlkVLQPTVF---PVVPRLLNRMFDRIFGQANttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslggRVR 380
Cdd:cd05934 168 ----RYGATVTnylGAMLSYLLAQPPSPDDRAH--------------------------------------------RLR 199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 381 LmVTGAAPVSATVLTFLRAaLGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVC 460
Cdd:cd05934 200 A-AYGAPNPPELHEEFEER-FGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVD-DDGQELPAGEPGELV 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 461 VK---GPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQV 537
Cdd:cd05934 277 IRglrGWGFFKGYYNMPEATAEAM-RNGWFHTGDLGYRDADGFFYFVDRKKDMIR-RRGENISSAEVERAILRHPAVREA 354
|
490 500
....*....|....*....|....*.
gi 1832481686 538 FVHG----ESLQAFLIAIVVPDVETL 559
Cdd:cd05934 355 AVVAvpdeVGEDEVKAVVVLRPGETL 380
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
72-508 |
3.46e-33 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 133.85 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAIT-----YIVNKAEL 146
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVK--PGDRVAVQVEKSPEALALYLATLRAGAVFLPL-----NTAYTlaeldYFIGDAEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 147 SLVFVDkPEKAKLLLEGVENKlipGLKIIVVMDAYGS-ELVERGQrcgvevtsmkamedlGRANRRKPKPPAPEDLAVIC 225
Cdd:PRK07514 102 ALVVCD-PANFAWLSKIAAAA---GAPHVETLDADGTgSLLEAAA---------------AAPDDFETVPRGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 226 FTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH---MFerVVECVMLCHGAKIGFFQG-DIRL 301
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFT----PDDVLIHALPIFHthgLF--VATNVALLAGASMIFLPKfDPDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 302 LMDDLKvlQPTVFPVVP----RLL-NRMFDRifgqanttlkrwlldfaskrkeaelrsgiirnnslwdrlifhkvqsSLG 376
Cdd:PRK07514 237 VLALMP--RATVMMGVPtfytRLLqEPRLTR----------------------------------------------EAA 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 377 GRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaGCCLTM-P--GDWTAGHVGAPMPCNLIKLVDVEEMNYMAA 453
Cdd:PRK07514 269 AHMRLFISGSAPLLAETHREFQERTGHAILERYGMTE---TNMNTSnPydGERRAGTVGFPLPGVSLRVTDPETGAELPP 345
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1832481686 454 EGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 508
Cdd:PRK07514 346 GEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGFFITGDLGKIDERGYVHIVGRGK 400
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
217-525 |
6.67e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 133.18 E-value: 6.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHMFErvVECVMLCH---GAKIG 293
Cdd:PLN02246 177 SPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYFHSDDVILCVLPMFHIYS--LNSVLLCGlrvGAAIL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 294 FFQG-DIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlLDFAskrkeaelRSGIIRNNSLwdrlifhkvq 372
Cdd:PLN02246 255 IMPKfEIGALLELIQRHKVTIAPFVPPIV-------------------LAIA--------KSPVVEKYDL---------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 SSlggrVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTM-------PGDWTAGHVGAPMPCNLIKLVD 444
Cdd:PLN02246 298 SS----IRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTE--AGPVLAMclafakePFPVKSGSCGTVVRNAELKIVD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 445 VEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 524
Cdd:PLN02246 372 PETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWLHTGDIGYIDDDDELFIVDRLKELIKY-KGFQVAPAEL 450
|
.
gi 1832481686 525 E 525
Cdd:PLN02246 451 E 451
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
72-558 |
8.62e-33 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 131.50 E-value: 8.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWV-----IIEQGCfAYsmviVPLYDTLGNEAITYIVNKAEL 146
Cdd:cd05930 13 LTYAELDARANRLARYLRERGVG--PGDLVAVLLERSLEMVvailaVLKAGA-AY----VPLDPSYPAERLAYILEDSGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 147 SLVFVDkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICF 226
Cdd:cd05930 86 KLVLTD-----------------------------------------------------------------PDDLAYVIY 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAH-MFerVVE-CVMLCHGAKI----GFFQGDIR 300
Cdd:cd05930 101 TSGSTGKPKGVMVEHRGLVN----LLLWMQEAYPLTPGDRVLQFTSFSFdVS--VWEiFGALLAGATLvvlpEEVRKDPE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 301 LLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslggrvr 380
Cdd:cd05930 175 ALADLLAEEGITVLHLTPSLLRLLLQELELAALPSLRL------------------------------------------ 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 381 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT--MPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGE 456
Cdd:cd05930 213 VLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYrvPPDDEEDGRVpiGRPIPNTRVYVLD-ENLRPVPPGVP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 457 GEVCVKGPNVFQGYLKDPAKTAEA-----LDKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMR 530
Cdd:cd05930 292 GELYIGGAGLARGYLNRPELTAERfvpnpFGPGERMYrTGDLVRWLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLA 370
|
490 500 510
....*....|....*....|....*....|.
gi 1832481686 531 SEPVAQVFV---HGESLQAFLIAIVVPDVET 558
Cdd:cd05930 371 HPGVREAAVvarEDGDGEKRLVAYVVPDEGG 401
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
171-539 |
1.99e-32 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 129.69 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 171 GLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSA 250
Cdd:TIGR01733 72 GARLLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 251 FVKATENTvnpcPDDTLISFLPLAHMFervveCVM-----LCHGAK--------IGFFQGDIRLLMDDLKVlqpTVFPVV 317
Cdd:TIGR01733 152 LARRYGLD----PDDRVLQFASLSFDA-----SVEeifgaLLAGATlvvppedeERDDAALLAALIAEHPV---TVLNLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 318 PrllnrmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGgrVRLMVTGA-APVSATVLTF 396
Cdd:TIGR01733 220 P------------------------------------------SLLALLAAALPPALAS--LRLVILGGeALTPALVDRW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 397 LRAALGCQFYEGYGQTECTAGCCLT-----MPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYL 471
Cdd:TIGR01733 256 RARGPGARLINLYGPTETTVWSTATlvdpdDAPRESPVPIGRPLANTRLYVLD-DDLRPVPVGVVGELYIGGPGVARGYL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481686 472 KDPAKTAE--------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFV 539
Cdd:TIGR01733 335 NRPELTAErfvpdpfaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKI-RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
50-554 |
2.20e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 131.65 E-value: 2.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 50 LHGQIYNGPCLGS---RKPDQP-YEW----LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPE-WVIIEQGCFA 120
Cdd:PRK06188 8 LHSGATYGHLLVSalkRYPDRPaLVLgdtrLTYGQLADRISRYIQAFEALGL--GTGDAVALLSLNRPEvLMAIGAAQLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 121 ySMVIVPLYDTLGNEAITYIVNKAELSLVFVDK---PEKAKLLLEGVenkliPGLKIIVVMDA--YGSELvergqrcgve 195
Cdd:PRK06188 86 -GLRRTALHPLGSLDDHAYVLEDAGISTLIVDPapfVERALALLARV-----PSLKHVLTLGPvpDGVDL---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 196 vtsmkamedLGRANRRKPKPP----APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATEntvnpCPDDtlISFL 271
Cdd:PRK06188 150 ---------LAAAAKFGPAPLvaaaLPPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWE-----WPAD--PRFL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 272 ---PLAHMFERVVECVMLCHGAKI---GFfqgDIRLLMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFAS 345
Cdd:PRK06188 214 mctPLSHAGGAFFLPTLLRGGTVIvlaKF---DPAEVLRAIEEQRITATFLVPTMIYA----------------LLDHPD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 346 KRKeAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGD 425
Cdd:PRK06188 275 LRT-RDL--------------------SSL----ETVYYGASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 426 WTAGHV------GAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPN 498
Cdd:PRK06188 330 HDPDDPkrltscGRPTPGLRVALLD-EDGREVAQ-GEvGEICVRGPLVMDGYWNRPEETAEAF-RDGWLHTGDVAREDED 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832481686 499 GTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQafliAIVVP 554
Cdd:PRK06188 407 GFYYIVDRKKDMI-VTGGFNVFPREVEDVLAEHPAVAQVAVigvpdekWGEAVT----AVVVL 464
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
64-529 |
1.54e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 129.48 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 64 KPDQPYEWlSYKQVAELSECIGSALIQKGFKTApdqfiGIFAQNRPEW---VIIEQGCFAYSMVIVPLYDTLGNEAITYI 140
Cdd:PRK06087 43 VDNHGASY-TYSALDHAASRLANWLLAKGIEPG-----DRVAFQLPGWcefTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 141 VNKAElSLVF-----VDKPEKAKLLLEGVENklIPGLKIIVVMDAYGSELVErgqrcgveVTSMKAMEDLGRANrrKPKP 215
Cdd:PRK06087 117 LNKCQ-AKMFfaptlFKQTRPVDLILPLQNQ--LPQLQQIVGVDKLAPATSS--------LSLSQIIADYEPLT--TAIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 216 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHmfervvecvmlchgaKIGFF 295
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLT----WQDVFMMPAPLGH---------------ATGFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 QGDIR-LLMDDLKVLQPTVFPVVP-RLLNRmfDRIFGQANTTlkRWLLDFASKRKEAELRSgiirnnslwdrlifhkvqS 373
Cdd:PRK06087 245 HGVTApFLIGARSVLLDIFTPDAClALLEQ--QRCTCMLGAT--PFIYDLLNLLEKQPADL------------------S 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 374 SLggrvRLMVTGAAPVSATVLtflRAAL--GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMN 449
Cdd:PRK06087 303 AL----RFFLCGGTTIPKKVA---RECQqrGIKLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVD-EARK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 450 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 529
Cdd:PRK06087 375 TLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGWYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILL 453
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
215-566 |
1.92e-31 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 127.43 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 215 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 292
Cdd:cd17653 101 TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVLN----YVSQPPARLDVGPGSRVAQVLSIA--FDACIGEIFstLCNGGTL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 gFFQGDIRLLMDDLKVLqpTVFPVVPRLLnrmfdrifgqanTTLKRWLLDfaskrkeaelrsgiirnnslwdrlifhkvq 372
Cdd:cd17653 175 -VLADPSDPFAHVARTV--DALMSTPSIL------------STLSPQDFP------------------------------ 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 sslggRVRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLT--MPGDWTagHVGAPMPCNLIKLVDVEEMNY 450
Cdd:cd17653 210 -----NLKTIFLGGEAVPPSLLD--RWSPGRRLYNAYGPTECTISSTMTelLPGQPV--TIGKPIPNSTCYILDADLQPV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 451 MAAEgEGEVCVKGPNVFQGYLKDPAKTAEAL----DKDGWLH--TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKI 524
Cdd:cd17653 281 PEGV-VGEICISGVQVARGYLGNPALTASKFvpdpFWPGSRMyrTGDYGRWTEDGGLEFLGREDNQVKV-RGFRINLEEI 358
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1832481686 525 ENIYMRSEPVAQ---VFVHGEslqaFLIAIVVP---DVETLCSWAQKR 566
Cdd:cd17653 359 EEVVLQSQPEVTqaaAIVVNG----RLVAFVTPetvDVDGLRSELAKH 402
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
70-555 |
2.59e-31 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 127.79 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 70 EWLSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLV 149
Cdd:cd12116 11 RSLSYAELDERANRLAARLRARG--VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 150 FVDkpekaklllegvenklipglkiivvmdaygSELVERGQRCGVevTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSG 229
Cdd:cd12116 89 LTD------------------------------DALPDRLPAGLP--VLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 230 TTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFFQGDI----RLLM 303
Cdd:cd12116 137 STGRPKGVVVSHRNLVN----FLHSMRERLGLGPGDRLLAVTTYA--FDiSLLELLLpLLAGARVVIAPRETqrdpEALA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 304 DDLKVLQPTVFpvvprllnrmfdrifgQANTTLKRWLLDfaskrkeaelrSGiirnnslWDRLifhkvqsslgGRVRLMV 383
Cdd:cd12116 211 RLIEAHSITVM----------------QATPATWRMLLD-----------AG-------WQGR----------AGLTALC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 384 TGAA--PVSATVLTflraALGCQFYEGYGQTECT--AGCCLTMPGDwTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 459
Cdd:cd12116 247 GGEAlpPDLAARLL----SRVGSLWNLYGPTETTiwSTAARVTAAA-GPIPIGRPLANTQVYVLD-AALRPVPPGVPGEL 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 460 CVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSE 532
Cdd:cd12116 321 YIGGDGVAQGYLGRPALTAERFVPDPFAGpgsrlyrTGDLVRRRADGRLEYLGRADGQVKI-RGHRIELGEIEAALAAHP 399
|
490 500
....*....|....*....|....*
gi 1832481686 533 PVAQ--VFVHGESLQAFLIAIVVPD 555
Cdd:cd12116 400 GVAQaaVVVREDGGDRRLVAYVVLK 424
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
206-549 |
1.28e-30 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 126.67 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 206 GRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC--------SAFVKatentvnPCPDDTLISF--LPLAH 275
Cdd:PRK07059 191 GARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeawlqPAFEK-------KPRPDQLNFVcaLPLYH 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 276 MFERVVECVMlchGAKIGffqG---------DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfask 346
Cdd:PRK07059 264 IFALTVCGLL---GMRTG---GrnilipnprDIPGFIKELKKYQVHIFPAVNTLYNALL--------------------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 347 rkeaelrsgiirNNSLWDRLIFHKVQSSLGGrvrlmvtGAApVSATVLTFLRAALGCQFYEGYG--QTECTAGCCLTMPG 424
Cdd:PRK07059 317 ------------NNPDFDKLDFSKLIVANGG-------GMA-VQRPVAERWLEMTGCPITEGYGlsETSPVATCNPVDAT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 425 DWTaGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKII 504
Cdd:PRK07059 377 EFS-GTIGLPLPSTEVSIRD-DDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGFFRTGDVGVMDERGYTKIV 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832481686 505 DRKKHIFkLAQGEYIAPEKIENIyMRSEP----VAQVFVH----GESLQAFLI 549
Cdd:PRK07059 455 DRKKDMI-LVSGFNVYPNEIEEV-VASHPgvleVAAVGVPdehsGEAVKLFVV 505
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
72-567 |
5.34e-30 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 123.26 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELslvfv 151
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVG--PGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 dkpekaklllegvenklipglKIIVVMDAYGSelvergqrcgvevTSMKAMedlgranrrkpkppaPEDLAVICFTSGTT 231
Cdd:cd05903 75 ---------------------KVFVVPERFRQ-------------FDPAAM---------------PDAVALLLFTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVvecvmlcHGAKIGFFQGDIRLLMDdlkVLQP 311
Cdd:cd05903 106 GEPKGVMHSHNTLSASIRQYAERLGLG----PGDVFLVASPMAHQTGFV-------YGFTLPLLLGAPVVLQD---IWDP 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 312 TVfpvVPRLLNRmfDRI-FGQANTTLKRWLLDfaskrkeAELRSGiirnnslwDRLifhkvqsslgGRVRLMVTGAAPVS 390
Cdd:cd05903 172 DK---ALALMRE--HGVtFMMGATPFLTDLLN-------AVEEAG--------EPL----------SRLRTFVCGGATVP 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 391 ATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGD-WTAGHV-GAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQ 468
Cdd:cd05903 222 RSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPeDRRLYTdGRPLPGVEIKVVD-DTGATLAPGVEGELLSRGPSVFL 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 469 GYLKDPAKTAEALDkDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQ 545
Cdd:cd05903 301 GYLDRPDLTADAAP-EGWFRTGDLARLDEDGYLRITGRSKDII-IRGGENIPVLEVEDLLLGHPGVIEAAVVAlpdERLG 378
|
490 500
....*....|....*....|....*...
gi 1832481686 546 AFLIAIVV------PDVETLCSWAQKRG 567
Cdd:cd05903 379 ERACAVVVtksgalLTFDELVAYLDRQG 406
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
124-555 |
7.71e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 126.19 E-value: 7.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 124 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAKLLLEGVENKLIPGLKIIVVMDaygseLVERgqrcgveVTSMKAME 203
Cdd:PRK08633 691 VPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKLKNKGFDLELPENVKVIYLED-----LKAK-------ISKVDKLT 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 204 DLGRA--------NRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAH 275
Cdd:PRK08633 759 ALLAArllparllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSN----IEQISDVFNLRNDDVILSSLPFFH 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 276 MFERVVECVM-LCHGAKIGFFQGDirllMDDLKVLQ-------------PTVFpvvprllnRMFDRifgqaNTTLKRwlL 341
Cdd:PRK08633 835 SFGLTVTLWLpLLEGIKVVYHPDP----TDALGIAKlvakhratillgtPTFL--------RLYLR-----NKKLHP--L 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 342 DFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLT 421
Cdd:PRK08633 896 MFAS---------------------------------LRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATETSPVASVN 942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 422 MP-----GDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL---DKDGWLH 488
Cdd:PRK08633 943 LPdvlaaDFKRqtgskEGSVGMPLPGVAVRIVDPETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIkdiDGIGWYV 1022
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832481686 489 TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEniymrsEPVAQVFvHGESLQafLIAIVVPD 555
Cdd:PRK08633 1023 TGDKGHLDEDGFLTITDRYSRFAKIG-GEMVPLGAVE------EELAKAL-GGEEVV--FAVTAVPD 1079
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
71-579 |
4.38e-29 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 121.25 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 71 WLSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVF 150
Cdd:cd12118 29 RYTWRQTYDRCRRLASALAALGI--SRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 151 VDKPekakLLLEgvenklipglkiivvmdaygsELVERGQRcgvevtsmkamedlgranRRKPKPPAPE-DLAVICFTSG 229
Cdd:cd12118 107 VDRE----FEYE---------------------DLLAEGDP------------------DFEWIPPADEwDPIALNYTSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 230 TTGNPKGAMVTHRnivsdcSAFVKATENTV----NPCPddTLISFLPLAHmfervveCVMLCHGAKIGFFQG-------- 297
Cdd:cd12118 144 TTGRPKGVVYHHR------GAYLNALANILewemKQHP--VYLWTLPMFH-------CNGWCFPWTVAAVGGtnvclrkv 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 298 DIRLLMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrwlldfaskrkeaelrsgIIRNNSlwdrlifHKVQSSLGG 377
Cdd:cd12118 209 DAKAIYDLIEKHKVTHFCGAPTVLN---------------------------------MLANAP-------PSDARPLPH 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 378 RVRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDWTAGHV----------GAPMPCNL-IKLV 443
Cdd:cd12118 249 RVHVMTAGAPP-PAAVL-AKMEELGFDVTHVYGLTE-TYGpatVCAWKP-EWDELPTeerarlkarqGVRYVGLEeVDVL 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 DVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAP 521
Cdd:cd12118 325 DPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGWFHSGDLAVIHPDGYIEIKDRSKDII-ISGGENISS 402
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832481686 522 EKIENIymrsepvaqVFVHGESLQAFLIAivVPD---VETLCSW-AQKRGFEGSFEEL---CRNK 579
Cdd:cd12118 403 VEVEGV---------LYKHPAVLEAAVVA--RPDekwGEVPCAFvELKEGAKVTEEEIiafCREH 456
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
220-539 |
6.18e-29 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 121.62 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVSD-CSAFVKATENTVNPCpddTLISFLPLAHMFERVVEC--VMLCHGAKIGFFQ 296
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANlCSSLFSVGPEMIGQV---VTLGLIPFFHIYGITGICcaTLRNKGKVVVMSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 297 GDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWDRLIFHKVqsslg 376
Cdd:PLN02330 262 FELRTFLNALITQEVSFAPIVPPIILNLV---------------------------------KNPIVEEFDLSKL----- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 377 gRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECTagcCLTMP-GDWTAGH-------VGAPMPCNLIKLVDVEE 447
Cdd:PLN02330 304 -KLQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHS---CITLThGDPEKGHgiakknsVGFILPNLEVKFIDPDT 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 448 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 527
Cdd:PLN02330 380 GRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWLHTGDIGYIDDDGDIFIVDRIKELIKY-KGFQVAPAELEAI 458
|
330
....*....|..
gi 1832481686 528 YMRSEPVAQVFV 539
Cdd:PLN02330 459 LLTHPSVEDAAV 470
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
72-554 |
9.08e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 120.81 E-value: 9.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:PRK08316 37 WTYAELDAAVNRVAAALLDLGLK--KGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DkPEKAKLLLEGVENKlipglkiivVMDAYGSELVERGQrcgVEVTSMKAMEDLGRANRRKPKPPAP--EDLAVICFTSG 229
Cdd:PRK08316 115 D-PALAPTAEAALALL---------PVDTLILSLVLGGR---EAPGGWLDFADWAEAGSVAEPDVELadDDLAQILYTSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 230 TTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVecvmlchgakigffqgdirLLMDDLKVL 309
Cdd:PRK08316 182 TESLPKGAMLTHRALIAEYVSCIVAGDMS----ADDIPLHALPLYHCAQLDV-------------------FLGPYLYVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 310 QPTVFPVVPRLlNRMFDRIFGQANTTLkrwlldFASKrkeaelrsgiirnnSLWDRLIFHKV-----QSSLggrvRLMVT 384
Cdd:PRK08316 239 ATNVILDAPDP-ELILRTIEAERITSF------FAPP--------------TVWISLLRHPDfdtrdLSSL----RKGYY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 385 GAAPVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCLTMPGDwTAGHVG-APMPC-NL-IKLVDvEEMNYMAAeGE-GEV 459
Cdd:PRK08316 294 GASIMPVEVLKELRERLpGLRFYNCYGQTEIAPLATVLGPEE-HLRRPGsAGRPVlNVeTRVVD-DDGNDVAP-GEvGEI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 460 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV 539
Cdd:PRK08316 371 VHRSPQLMLGYWDDPEKTAEAF-RGGWFHSGDLGVMDEEGYITVVDRKKDMIKTG-GENVASREVEEALYTHPAVAEVAV 448
|
490
....*....|....*....
gi 1832481686 540 ----HGESLQAfLIAIVVP 554
Cdd:PRK08316 449 iglpDPKWIEA-VTAVVVP 466
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
124-526 |
1.77e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 119.08 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 124 VIVPLYDTLGNEAITYIVNKAELSLVFVDKPekaklllegvenklipglkiivvmdaYGSELVERGQRCGVEVTSMKAME 203
Cdd:cd05922 48 VFVPLNPTLKESVLRYLVADAGGRIVLADAG--------------------------AADRLRDALPASPDPGTVLDADG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 204 DLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVEC 283
Cdd:cd05922 102 IRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT----ADDRALTVLPLSYDYGLSVLN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 284 VMLCHGAKIgFFQGDIRL---LMDDLKVLQPTVFPVVPRLLNrMFDRIfgqanttlkrwlldfasKRKEAELrsgiirnN 360
Cdd:cd05922 178 THLLRGATL-VLTNDGVLddaFWEDLREHGATGLAGVPSTYA-MLTRL-----------------GFDPAKL-------P 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 361 SLwdRLIfhkvqSSLGGRVRlmvtgaapvSATVLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTA---GHVGAPMPC 437
Cdd:cd05922 232 SL--RYL-----TQAGGRLP---------QETIARLRELLPGAQVYVMYGQTEATRRMT-YLPPERILekpGSIGLAIPG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 438 NLIKLVDVEEMNYmaAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqG 516
Cdd:cd05922 295 GEFEILDDDGTPT--PPGEpGEIVHRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLF-G 371
|
410
....*....|
gi 1832481686 517 EYIAPEKIEN 526
Cdd:cd05922 372 NRISPTEIEA 381
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
65-508 |
3.27e-28 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 119.31 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 65 PDQPYEWLSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAQNRpEWVIIEQGC----FAYSMVIVPLYDTLGNEAITYI 140
Cdd:cd05906 33 ADGSEEFQSYQDLLEDARRLAAGLRQLGLR-PGDSVILQFDDNE-DFIPAFWACvlagFVPAPLTVPPTYDEPNARLRKL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 141 VNKAELslvfVDKPekakLLLegVENKLIPGLKiivvmdaygsELVERGQRCGVEVTSMkamEDLGRANRRKPKPPA-PE 219
Cdd:cd05906 111 RHIWQL----LGSP----VVL--TDAELVAEFA----------GLETLSGLPGIRVLSI---EELLDTAADHDLPQSrPD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHmferVVECVMlCHGAkigffqgDI 299
Cdd:cd05906 168 DLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLT----PQDVFLNWVPLDH----VGGLVE-LHLR-------AV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 300 RLLMDDLKVLQPTVFPVVPRLLnRMFDRIfgQANTTlkrWLLDFA-SKRKEAELRsgiiRNNSLWDrlifhkvQSSLggr 378
Cdd:cd05906 232 YLGCQQVHVPTEEILADPLRWL-DLIDRY--RVTIT---WAPNFAfALLNDLLEE----IEDGTWD-------LSSL--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 379 vRLMVTGAAPVSA-TVLTFLR--AALGCQ---FYEGYGQTECTAGC--CLTMP-GDWTAGH----VGAPMPCNLIKLVDv 445
Cdd:cd05906 292 -RYLVNAGEAVVAkTIRRLLRllEPYGLPpdaIRPAFGMTETCSGViySRSFPtYDHSQALefvsLGRPIPGVSMRIVD- 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832481686 446 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 508
Cdd:cd05906 370 DEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGWFRTGDLG-FLDNGNLTITGRTK 431
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
78-525 |
4.02e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 118.37 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 78 AELSECIG-SALIQKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFvdkpek 156
Cdd:PRK09088 26 AELDALVGrLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 157 aklllegvenklipglkiivvmdayGSELVERGQRCGVEVTSMKAMEDLGRANRRKPKPPapEDLAVICFTSGTTGNPKG 236
Cdd:PRK09088 100 -------------------------GDDAVAAGRTDVEDLAAFIASADALEPADTPSIPP--ERVSLILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 237 AMVTHRNIVSDCSAFVKATENTVNPcpddtliSFLPLAHMFERV--VECV--MLCHGAKIGFFQGdirllmddlkvLQPT 312
Cdd:PRK09088 153 VMLSERNLQQTAHNFGVLGRVDAHS-------SFLCDAPMFHIIglITSVrpVLAVGGSILVSNG-----------FEPK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 313 vfpvvpRLLNRMFDRIFGQANTtlkrwlldFASKRKEAELRSGIIRNNSLWDRLIfhkvqsslggrvrLMVTGAAP-VSA 391
Cdd:PRK09088 215 ------RTLGRLGDPALGITHY--------FCVPQMAQAFRAQPGFDAAALRHLT-------------ALFTGGAPhAAE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 392 TVLTFLraALGCQFYEGYGQTEctAGCCLTMPGDWT-----AGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCVKGPNV 466
Cdd:PRK09088 268 DILGWL--DDGIPMVDGFGMSE--AGTVFGMSVDCDvirakAGAAGIPTPTVQTRVVDDQGNDCPAGV-PGELLLRGPNL 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1832481686 467 FQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 525
Cdd:PRK09088 343 SPGYWRRPQATARAFTGDGWFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIE 400
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
135-535 |
1.18e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 118.13 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 135 EAITYIVNKAELSLVFVDKPE-------KAKLLLEGVenkliPGLKIIVVMDayGSELVERGQRCGVEVTSMKAME---D 204
Cdd:PRK07529 119 EQIAELLRAAGAKVLVTLGPFpgtdiwqKVAEVLAAL-----PELRTVVEVD--LARYLPGPKRLAVPLIRRKAHArilD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 205 LGRANRRKP-------KPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC---SAFVKATentvnpcPDDTLISFLPLA 274
Cdd:PRK07529 192 FDAELARQPgdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAwlgALLLGLG-------PGDTVFCGLPLF 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 275 HMFERVVEC-VMLCHGAKIGFF--QG--DIRLLMDDLKVL---QPTVFPVVPRLLNRMFDRIFGQANTtlkrwlldfask 346
Cdd:PRK07529 265 HVNALLVTGlAPLARGAHVVLAtpQGyrGPGVIANFWKIVeryRINFLSGVPTVYAALLQVPVDGHDI------------ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 347 rkeaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GD 425
Cdd:PRK07529 333 --------------------------SSL----RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVSSVNPPdGE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 426 WTAGHVGAPMPCNLIKLVDVEEM-NYM--AAEGE-GEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTL 501
Cdd:PRK07529 383 RRIGSVGLRLPYQRVRVVILDDAgRYLrdCAVDEvGVLCIAGPNVFSGYL-EAAHNKGLWLEDGWLNTGDLGRIDADGYF 461
|
410 420 430
....*....|....*....|....*....|....
gi 1832481686 502 KIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 535
Cdd:PRK07529 462 WLTGRAKDLI-IRGGHNIDPAAIEEALLRHPAVA 494
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
215-549 |
1.31e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 117.83 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 215 PPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpDDTLISFLPLAHMF-ERVVECVMLCHGAKI 292
Cdd:PRK06710 201 PCDPEnDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEG--EEVVLGVLPFFHVYgMTAVMNLSIMQGYKM 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 GFF-QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqaNTTLkrwlldfaskRKEAELRSgiirnnslwdrlifhkv 371
Cdd:PRK06710 279 VLIpKFDMKMVFEAIKKHKVTLFPGAPTIYIALL-------NSPL----------LKEYDISS----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 372 qsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPgdW---TAGHVGAPMPCNLIKLVDVEEM 448
Cdd:PRK06710 325 -------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFL--WekrVPGSIGVPWPDTEAMIMSLETG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 528
Cdd:PRK06710 396 EALPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-QDGWLHTGDVGYMDEDGFFYVKDRKKDMI-VASGFNVYPREVEEVL 473
|
330 340
....*....|....*....|....*...
gi 1832481686 529 MRSEPVAQVFV-------HGESLQAFLI 549
Cdd:PRK06710 474 YEHEKVQEVVTigvpdpyRGETVKAFVV 501
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
218-555 |
2.17e-27 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 116.10 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLplAHMFE-RVVECVM-LCHGAKIGff 295
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT----SESRVLQFA--SYTFDvSILEIFTtLAAGGCLC-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 qgdI---RLLMDDLkvlqptvfpvvPRLLNRMfdrifgQANTtlkrwlldfaskrkeAELRSGIIRnnslwdrLIFHKVQ 372
Cdd:cd05918 177 ---IpseEDRLNDL-----------AGFINRL------RVTW---------------AFLTPSVAR-------LLDPEDV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 SSLggrvRLMVTGAAPVSATVLTflRAALGCQFYEGYGQTECTAGCCLTMPG-DWTAGHVGAPMPCNLIkLVDVEEMNYM 451
Cdd:cd05918 215 PSL----RTLVLGGEALTQSDVD--TWADRVRLINAYGPAECTIAATVSPVVpSTDPRNIGRPLGATCW-VVDPDNHDRL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 452 AAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKD-GWLH------------TGDIGKWLPNGTLKIIDRKKHIFKLaQGE 517
Cdd:cd05918 288 VPIGAvGELLIEGPILARGYLNDPEKTAAAFIEDpAWLKqegsgrgrrlyrTGDLVRYNPDGSLEYVGRKDTQVKI-RGQ 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1832481686 518 YIAPEKIENIYMRSEP-----VAQVFVH-GESLQAFLIAIVVPD 555
Cdd:cd05918 367 RVELGEIEHHLRQSLPgakevVVEVVKPkDGSSSPQLVAFVVLD 410
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
58-622 |
2.45e-27 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 116.76 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 58 PCLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCF---AYSMVIVPLYDTLGN 134
Cdd:cd05921 12 TWLAEREGNGGWRRVTYAEALRQVRAIAQGLLDLGLS--AERPLLILSGNSIEHALMALAAMyagVPAAPVSPAYSLMSQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 135 E--AITYIVNKAELSLVFVDKPEKAKLLLEGVenkLIPGLKIIVVmdaygselveRGQRCGVEVTSMK---AMEDLGRAN 209
Cdd:cd05921 90 DlaKLKHLFELLKPGLVFAQDAAPFARALAAI---FPLGTPLVVS----------RNAVAGRGAISFAelaATPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 210 RRKPKPpAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchG 289
Cdd:cd05921 157 AAFAAV-GPDTVAKFLFTSGSTGLPKAVINTQRMLCA--NQAMLEQTYPFFGEEPPVLVDWLPWNHTF-----------G 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 290 AKIGF-----------------FQGDIRLLMDDLKVLQPTVFPVVPR----LLNRMfdrifgQANTTLKRWLLdfasKRK 348
Cdd:cd05921 223 GNHNFnlvlynggtlyiddgkpMPGGFEETLRNLREISPTVYFNVPAgwemLVAAL------EKDEALRRRFF----KRL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 349 EAELRSGIIRNNSLWDRLIFHKVQSSlGGRVRlmvtgaapvsatvltflraalgcqFYEGYGQTECTAGCCLTMPGDWTA 428
Cdd:cd05921 293 KLMFYAGAGLSQDVWDRLQALAVATV-GERIP------------------------MMAGLGATETAPTATFTHWPTERS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 429 GHVGAPMPCNLIKLVdveemnymAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PNGTLKII 504
Cdd:cd05921 348 GLIGLPAPGTELKLV--------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGFYCLGDAAKLAdpddPAKGLVFD 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 505 DRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVETLcsWAQKRGFEGSFEELCRNKDVK 582
Cdd:cd05921 420 GRVAEDFKLASGTWVSvgPLRARAVAACAPLVHDAVVAGED-RAEVGALVFPDLLAC--RRLVGLQEASDAEVLRHAKVR 496
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1832481686 583 KAILEDMVRLGKDSGLKPfEQVKGITLHPELFSIDNGLLT 622
Cdd:cd05921 497 AAFRDRLAALNGEATGSS-SRIARALLLDEPPSIDKGEIT 535
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
219-542 |
3.99e-27 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 114.37 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 219 EDLAVICFTSGTTGNPKGAMVTHRNIvsdcSAFVKATENTVNPCPDDTLISFLPLAH------MFERVVE-CVMLCHGAk 291
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFGNH----WWSAIGSALNLGLTEDDNWLCALPLFHisglsiLMRSVIYgMTVYLVDK- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 292 igFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLkrwlldfaskrkeaelrsgiirnnslwdrlifhkv 371
Cdd:cd05912 152 --FDAEQVLHLINSGKV---TIISVVPTMLQRLLEILGEGYPNNL----------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 372 qsslggrvRLMVTGAAPVSATVLTFLRAaLGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPMPCNLIKLVDveem 448
Cdd:cd05912 192 --------RCILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTE-TCSQIVTLSPEDALnkiGSAGKPLFPVELKIED---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 528
Cdd:cd05912 258 DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF-ENGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVL 335
|
330
....*....|....
gi 1832481686 529 MRSEPVAQVFVHGE 542
Cdd:cd05912 336 LSHPAIKEAGVVGI 349
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
70-541 |
6.11e-27 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.96 E-value: 6.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 70 EWLSYKQVAELSECIGSALIQKgFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLydtlgNEAITyivnKAELSLV 149
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIYE-LNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL-----NIRLT----ENELIFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 150 FVDKpekaklllegvenklipGLKIIVVMDAYGSELVERGQRCGVE----VTSMKAMEDLGRANRrkpKPPAPEDLAVIC 225
Cdd:PRK06839 96 LKDS-----------------GTTVLFVEKTFQNMALSMQKVSYVQrvisITSLKEIEDRKIDNF---VEKNESASFIIC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 226 FTSGTTGNPKGAMVTHRNIvsdcsaFVKATEN--TVNPCPDDTLISFLPLAHMfervvecvmlchgAKIGFFQgdirllm 303
Cdd:PRK06839 156 YTSGTTGKPKGAVLTQENM------FWNALNNtfAIDLTMHDRSIVLLPLFHI-------------GGIGLFA------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 304 ddlkvlQPTVFP----VVPRLLN-----RMFDR-----IFGQAntTLKRWLLDfASKRKEAELRSgiirnnslwdrlifh 369
Cdd:PRK06839 210 ------FPTLFAggviIVPRKFEptkalSMIEKhkvtvVMGVP--TIHQALIN-CSKFETTNLQS--------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 370 kvqsslggrVRLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTECTAGCCLTMPGDW--TAGHVGAPMPCNLIKLVDvEE 447
Cdd:PRK06839 266 ---------VRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELID-EN 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 448 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENI 527
Cdd:PRK06839 335 KNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI-QDGWLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIYPLEVEQV 412
|
490
....*....|....
gi 1832481686 528 YMRSEPVAQVFVHG 541
Cdd:PRK06839 413 INKLSDVYEVAVVG 426
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
213-527 |
6.19e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 115.71 E-value: 6.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 213 PKPP-APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVK-ATENTVNPCPDDTLISFLPLAHMFERVVECV-MLCHG 289
Cdd:PLN02574 191 PKPViKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfEASQYEYPGSDNVYLAALPMFHIYGLSLFVVgLLSLG 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 290 AKI----GFFQGDIRLLMDDLKVlqpTVFPVVPRLLNRMFDRIFGQANTTLKrwlldfaskrkeaelrsgiirnnslwdr 365
Cdd:PLN02574 271 STIvvmrRFDASDMVKVIDRFKV---THFPVVPPILMALTKKAKGVCGEVLK---------------------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 366 lifhkvqsSLggrvRLMVTGAAPVSA-TVLTFLRAALGCQFYEGYGQTECTA----GCCLTMPGDWTAghVGAPMPCNLI 440
Cdd:PLN02574 320 --------SL----KQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAvgtrGFNTEKLSKYSS--VGLLAPNMQA 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 441 KLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIA 520
Cdd:PLN02574 386 KVVDWSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWLRTGDIAYFDEDGYLYIVDRLKEIIKY-KGFQIA 464
|
....*..
gi 1832481686 521 PEKIENI 527
Cdd:PLN02574 465 PADLEAV 471
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
72-575 |
9.71e-27 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 114.82 E-value: 9.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVK--KGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 D----KPEKAKLLLEGVEN--KLIPGLKIIVVMDAYGSELVERGQRcgvevtsmkAMEDLgRANRRKPKPPAP---EDLA 222
Cdd:COG0365 118 AdgglRGGKVIDLKEKVDEalEELPSLEHVIVVGRTGADVPMEGDL---------DWDEL-LAAASAEFEPEPtdaDDPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 223 VICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLA----HMFervveCVM--LCHGAKIGFFQ 296
Cdd:COG0365 188 FILYTSGTTGKPKGVVHTHGGYLVHAATTAK---YVLDLKPGDVFWCTADIGwatgHSY-----IVYgpLLNGATVVLYE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 297 GDI------RL--LMDDLKVlqpTVFPVVPRLLnRMfdrifgqanttLKRWLLDFASKrkeaelrsgiirnnslWDRlif 368
Cdd:COG0365 260 GRPdfpdpgRLweLIEKYGV---TVFFTAPTAI-RA-----------LMKAGDEPLKK----------------YDL--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 369 hkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWT-AGHVGAPMPCNLIKLVDvEE 447
Cdd:COG0365 306 ----SSL----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFISNLPGLPVkPGSMGKPVPGYDVAVVD-ED 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 448 MNYMAAEGEGEVCVKG--PNVFQGYLKDPAKTAEAL--DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 523
Cdd:COG0365 377 GNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVS-GHRIGTAE 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1832481686 524 IENIYMRSEPVAQVFV----HGESLQAfLIAIVVPdvetlcswaqKRGFEGSfEEL 575
Cdd:COG0365 456 IESALVSHPAVAEAAVvgvpDEIRGQV-VKAFVVL----------KPGVEPS-DEL 499
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
72-549 |
1.09e-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: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKTApdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAelslvfv 151
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKG--DRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 dkpekaklllegvenklipGLKIIVVmdayGSELvergqrcgvevtsmkamedlgranrrkpkppapEDLAVICFTSGTT 231
Cdd:cd05935 73 -------------------GAKVAVV----GSEL---------------------------------DDLALIPYTSGTT 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHM--FERVVECVMLCHGAKIGFFQGDIRLLMDDLKVL 309
Cdd:cd05935 97 GLPKGCMHTHFSAAANALQSAVWTGLT----PSDVILACLPLFHVtgFVGSLNTAVYVGGTYVLMARWDRETALELIEKY 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 310 QPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhkvqsslggrVRLMVTGAAPV 389
Cdd:cd05935 173 KVTFWTNIPTMLVDLL--------ATPEFKTRDLSS---------------------------------LKVLTGGGAPM 211
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 390 SATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQG 469
Cdd:cd05935 212 PPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKG 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 470 YLKDPAKTAEALDKDG---WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV------- 539
Cdd:cd05935 292 YWNRPEETEESFIEIKgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS-GFKVWPAEVEAKLYKHPAI*EVCVisvpder 370
|
490
....*....|
gi 1832481686 540 HGESLQAFLI 549
Cdd:cd05935 371 VGEEVKAFIV 380
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
103-566 |
1.30e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 114.49 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 103 IFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDKPEKAklLLEGVENkLIPGLKIIVVMDAYG 182
Cdd:PRK07786 72 ILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAP--VATAVRD-IVPLLSTVVVAGGSS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 183 SELVergqrcgvevtsmKAMEDLGRANRrKPKPPA--PEDL-AVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTV 259
Cdd:PRK07786 149 DDSV-------------LGYEDLLAEAG-PAHAPVdiPNDSpALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADI 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 260 NpcpDDtlISFL--PLAHM--FERVVECVMLchGAKIgffqgdirllmddlkVLQPTvfpvvprllnRMFDrifgqANTT 335
Cdd:PRK07786 215 N---SD--VGFVgvPLFHIagIGSMLPGLLL--GAPT---------------VIYPL----------GAFD-----PGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 336 LKRWlldfaskrkEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEC 414
Cdd:PRK07786 258 LDVL---------EAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFpEAQILAAFGQTEM 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 415 TAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDkDGWLHTGDI 492
Cdd:PRK07786 329 SPVTCMLLGEDAIRklGSVGKVIPTVAARVVD-ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFA-GGWFHSGDL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 493 GKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAF---LIAIVVPD-------VETLCSW 562
Cdd:PRK07786 407 VRQDEEGYVWVVDRKKDMI-ISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWgevPVAVAAVRnddaaltLEDLAEF 485
|
....
gi 1832481686 563 AQKR 566
Cdd:PRK07786 486 LTDR 489
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
63-597 |
2.42e-26 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 114.21 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 63 RKPDQPY--------EW--LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---Y 129
Cdd:PRK08180 51 EAPDRVFlaergadgGWrrLTYAEALERVRAIAQALLDRGL--SAERPLMILSGNSIEHALLALAAMYAGVPYAPVspaY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 130 DTLGN--EAITYIVNKAELSLVFVDKPEKAKLLLEGVEnklIPGLKIIVVmdaygselveRGQRCGVEVTSMKAMEDLGR 207
Cdd:PRK08180 129 SLVSQdfGKLRHVLELLTPGLVFADDGAAFARALAAVV---PADVEVVAV----------RGAVPGRAATPFAALLATPP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 208 ANRRKPKPPA--PEDLAVICFTSGTTGNPKGAMVTHRNIVS------DCSAFVKATEntvnpcPddTLISFLPLAHMFER 279
Cdd:PRK08180 196 TAAVDAAHAAvgPDTIAKFLFTSGSTGLPKAVINTHRMLCAnqqmlaQTFPFLAEEP------P--VLVDWLPWNHTFGG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 280 VVEC-VMLCHGAKI---------GFFQGDIRllmdDLKVLQPTVFPVVPR--------------LLNRMFDRifgqantt 335
Cdd:PRK08180 268 NHNLgIVLYNGGTLyiddgkptpGGFDETLR----NLREISPTVYFNVPKgwemlvpalerdaaLRRRFFSR-------- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 336 LKrwLLDFASkrkeAELRSgiirnnSLWDRLifHKV-QSSLGGRVRLMVtgaapvsatvltflraalgcqfyeGYGQTEc 414
Cdd:PRK08180 336 LK--LLFYAG----AALSQ------DVWDRL--DRVaEATCGERIRMMT------------------------GLGMTE- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 415 TAGCCL--TMPGDwTAGHVGAPMPCNLIKLVDVEemnymaaeGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDI 492
Cdd:PRK08180 377 TAPSATftTGPLS-RAGNIGLPAPGCEVKLVPVG--------GKLEVRVKGPNVTPGYWRAPELTAEAFDEEGYYRSGDA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 493 GKWL----PNGTLKIIDRKKHIFKLAQGEYIA--PEKIENIYMRSEPVAQVFVHGESlQAFLIAIVVPDVEtLCSWAQKR 566
Cdd:PRK08180 448 VRFVdpadPERGLMFDGRIAEDFKLSSGTWVSvgPLRARAVSAGAPLVQDVVITGHD-RDEIGLLVFPNLD-ACRRLAGL 525
|
570 580 590
....*....|....*....|....*....|.
gi 1832481686 567 GFEGSFEELCRNKDVKKAILEDMVRLGKDSG 597
Cdd:PRK08180 526 LADASLAEVLAHPAVRAAFRERLARLNAQAT 556
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
72-554 |
4.25e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.84 E-value: 4.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAElSLVFV 151
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLG--VGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 --------DKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERgqrcgveVTSMKAME---DLGR--ANRRkpkpPAP 218
Cdd:PRK13295 133 vpktfrgfDHAAMARRLRPE-----LPALRHVVVVGGDGADSFEA-------LLITPAWEqepDAPAilARLR----PGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 219 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvecvmlchgakIGFFQGD 298
Cdd:PRK13295 197 DDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLG----ADDVILMASPMAHQ---------------TGFMYGL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 299 IRLLMDDLK-VLQPTVFPVvprllnRMFDRI------FGQANTTlkrWLLDFASKRKEAElrsgiirnnslwdrlifhKV 371
Cdd:PRK13295 258 MMPVMLGATaVLQDIWDPA------RAAELIrtegvtFTMASTP---FLTDLTRAVKESG------------------RP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 372 QSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLTMPGD---WTAGHVGAPMPCNLIKLVDVEEM 448
Cdd:PRK13295 311 VSSL----RTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDpdeRASTTDGCPLPGVEVRVVDADGA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEalDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIY 528
Cdd:PRK13295 386 PLPAGQ-IGRLQVRGCSNFGGYLKRPQLNGT--DADGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALL 461
|
490 500
....*....|....*....|....*....
gi 1832481686 529 MRSEPVAQVFVHG---ESLQAFLIAIVVP 554
Cdd:PRK13295 462 YRHPAIAQVAIVAypdERLGERACAFVVP 490
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
59-645 |
5.99e-26 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 114.18 E-value: 5.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 59 CLGSRKPDQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTlgNEAIT 138
Cdd:PTZ00297 445 CLGQTSESGESEWLTYGTVDARARELGSGLLALGVR--PGDVIGVDCEASRNIVILEVACALYGFTTLPLVGK--GSTMR 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 139 YIVNKAELSLVFVDKPEKAKLL------LEGVENklipglkiivVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRRK 212
Cdd:PTZ00297 521 TLIDEHKIKVVFADRNSVAAILtcrsrkLETVVY----------THSFYDEDDHAVARDLNITLIPYEFVEQKGRLCPVP 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 213 PKPPAPED----LAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVkATENTVNPCPDDTLISFLPLAHMFERVVECVMLCH 288
Cdd:PTZ00297 591 LKEHVTTDtvftYVVDNTTSASGDGLAVVRVTHADVLRDISTLV-MTGVLPSSFKKHLMVHFTPFAMLFNRVFVLGLFAH 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 289 GAKIGffQGDIRLLMDDLKVLQPTVFPVVPRLlnrmfdriFGQANTTLKR----------WLLDfaskrKEAELRSGII- 357
Cdd:PTZ00297 670 GSAVA--TVDAAHLQRAFVKFQPTILVAAPSL--------FSTSRLQLSRanerysavysWLFE-----RAFQLRSRLIn 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 358 --RNNSLWDRLIFHK-VQSSLGGRVRLMVTGAAPVSATvltflraalgcqfyegYGQTECTAGCCltmpgdwtaghvgap 434
Cdd:PTZ00297 735 ihRRDSSLLRFIFFRaTQELLGGCVEKIVLCVSEESTS----------------FSLLEHISVCY--------------- 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 435 MPCnliklvdVEEMNYMAAegEGEVCVKG---PNVfQGYLK---DPAKTAE----ALDKDGWL-HTGDI-GKWLPNGTLK 502
Cdd:PTZ00297 784 VPC-------LREVFFLPS--EGVFCVDGtpaPSL-QVDLEpfdEPSDGAGigqlVLAKKGEPrRTLPIaAQWKRDRTLR 853
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 503 IIDRKKHIFKLAQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAfLIAIVVPDVETL-CSWAQKRGFE---GSFEELCRN 578
Cdd:PTZ00297 854 LLGPPLGILLPVAYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNRDTVeFEWRQSHCMGeggGPARQLGWT 932
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 579 KDVKKA---ILEDMVRLGKDSGLKPFEQVKGITLHPELFSIDNGLLTPTMKAKRPELRNYFRSQIDDLYS 645
Cdd:PTZ00297 933 ELVAYAsslLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFYS 1002
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
70-559 |
1.54e-25 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 112.64 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 70 EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCF----AYsmviVPLYDTLGNEAITYIVNKAE 145
Cdd:COG1020 500 QSLTYAELNARANRLAHHLRALGVG--PGDLVGVCLERSLEMVVALLAVLkagaAY----VPLDPAYPAERLAYMLEDAG 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 146 LSLVFVDKPEKAKLLLEGVEnklipglkiIVVMDAygselvergqrcgvevtsmkamEDLGRANRRKPKPPA-PEDLAVI 224
Cdd:COG1020 574 ARLVLTQSALAARLPELGVP---------VLALDA----------------------LALAAEPATNPPVPVtPDDLAYV 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 225 CFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAH------MFervvecVMLCHGAKIGFFQGD 298
Cdd:COG1020 623 IYTSGSTGRPKGVMVEHRALV----NLLAWMQRRYGLGPGDRVLQFASLSFdasvweIF------GALLSGATLVLAPPE 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 299 IRLLMDDLKVL----QPTVFPVVPRLLNRMFDrifgqanttlkrwlldfaskrkeaelrsgiirnnSLWDRLifhkvqss 374
Cdd:COG1020 693 ARRDPAALAELlarhRVTVLNLTPSLLRALLD----------------------------------AAPEAL-------- 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 375 lgGRVRLMVTG--AAPVsATVLTFLRAALGCQFYEGYGQTECTAGCCL--TMPGDWTAGHV--GAPMPCNLIKLVDvEEM 448
Cdd:COG1020 731 --PSLRLVLVGgeALPP-ELVRRWRARLPGARLVNLYGPTETTVDSTYyeVTPPDADGGSVpiGRPIANTRVYVLD-AHL 806
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-----LDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 521
Cdd:COG1020 807 QPVPVGVPGELYIGGAGLARGYLNRPELTAERfvadpFGFPGarLYRTGDLARWLPDGNLEFLGRADDQVKI-RGFRIEL 885
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1832481686 522 EKIENIYMRSEPVAQ--VFVHGESLQA-FLIAIVVPDVETL 559
Cdd:COG1020 886 GEIEAALLQHPGVREavVVAREDAPGDkRLVAYVVPEAGAA 926
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
220-557 |
4.36e-25 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 106.59 E-value: 4.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFvkATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK---IGFFQ 296
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLI--AANL--QLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 297 GDIRL-LMDDLKVlqpTVFPVVPRLLNRMFDRIfgqanttlkrwlldfasKRKEAELRSgiIRNnslwdrlifhkvqssl 375
Cdd:cd17637 77 PAEALeLIEEEKV---TLMGSFPPILSNLLDAA-----------------EKSGVDLSS--LRH---------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 376 ggrvrlmVTGA-APvsATVLTFLrAALGCQFYEGYGQTEcTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 454
Cdd:cd17637 119 -------VLGLdAP--ETIQRFE-ETTGATFWSLYGQTE-TSGLVTLSPYRERPGSAGRPGPLVRVRIVD-DNDRPVPAG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 455 GEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK--KHIFKlAQGEYIAPEKIENIYMRSE 532
Cdd:cd17637 187 ETGEIVVRGPLVFQGYWNLPELTAYTF-RNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK-PGGENVYPAEVEKVILEHP 264
|
330 340
....*....|....*....|....*
gi 1832481686 533 PVAQVFVHGeslqafliaivVPDVE 557
Cdd:cd17637 265 AIAEVCVIG-----------VPDPK 278
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
70-534 |
6.54e-25 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 109.25 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 70 EWLSYKQVAELSECIGSALIQKGfktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEA---ITYIVNKAEL 146
Cdd:cd05931 23 ETLTYAELDRRARAIAARLQAVG---KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 147 SLVFVDKPEKAKLLLEGVENKLIPGLKIIVVmDAYGSELVERGQrcgvevtsmkamedlgranrrkPKPPAPEDLAVICF 226
Cdd:cd05931 100 RVVLTTAAALAAVRAFAASRPAAGTPRLLVV-DLLPDTSAADWP----------------------PPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH-MfervvecvmlchgakiGFFQGdirllmdd 305
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLD----PGDVVVSWLPLYHdM----------------GLIGG-------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 306 lkVLQPTV--FPVV---PR-LLNRMFdrifgqanttlkRWL-----------------LDFASKRKEAELRSGIirnnsl 362
Cdd:cd05931 209 --LLTPLYsgGPSVlmsPAaFLRRPL------------RWLrlisryratisaapnfaYDLCVRRVRDEDLEGL------ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 363 wdRLifhkvqsslgGRVRLMVTGAAPVSATVLT-FLRAALGCQF-----YEGYGQTECT----------AGCCLTMPGDW 426
Cdd:cd05931 269 --DL----------SSWRVALNGAEPVRPATLRrFAEAFAPFGFrpeafRPSYGLAEATlfvsggppgtGPVVLRVDRDA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 427 TAGHV----------------GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE------ALDKD 484
Cdd:cd05931 337 LAGRAvavaaddpaarelvscGRPLPDQEVRIVDPETGRELPDGEVGEIWVRGPSVASGYWGRPEATAEtfgalaATDEG 416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1832481686 485 GWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 534
Cdd:cd05931 417 GWLRTGDLG-FLHDGELYITGRLKDLIIVR-GRNHYPQDIEATAEEAHPA 464
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
62-555 |
6.54e-25 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 108.57 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 62 SRKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTL 132
Cdd:cd17655 8 EKTPDHTAvvfedQTLTYRELNERANQLARTLREKGVG--PDTIVGIMAERSLEMIVgilgILKAGGAY----LPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 133 GNEAITYIVNKAELSLVFVDKPEKAKLLLEGvenklipglkIIVVMDAygselvergqrcgvEVTSMKAMEDLGRANRrk 212
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPPIAFIG----------LIDLLDE--------------DTIYHEESENLEPVSK-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 213 pkppaPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGA 290
Cdd:cd17655 136 -----SDDLAYVIYTSGSTGKPKGVMIEHRGVVN----LVEWANKVIYQGEHLRVALFASIS--FDASVTEIFasLLSGN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 291 KIgffqgdirllmddLKVLQPTVFPVVPrllnrmFDRIFGQANTTLkrwlldfaSKRKEAELRsgiirnnslwdrlIFHK 370
Cdd:cd17655 205 TL-------------YIVRKETVLDGQA------LTQYIRQNRITI--------IDLTPAHLK-------------LLDA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 371 VQSSLGGRVRLMVTGAAPVSATVLTFL--RAALGCQFYEGYGQTECTAGCC--LTMPGDWTAGHV--GAPMPCNLIKLVD 444
Cdd:cd17655 245 ADDSEGLSLKHLIVGGEALSTELAKKIieLFGTNPTITNAYGPTETTVDASiyQYEPETDQQVSVpiGKPLGNTRIYILD 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 445 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 518
Cdd:cd17655 325 -QYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVpgermyRTGDLARWLPDGNIEFLGRIDHQVKI-RGYR 402
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1832481686 519 IAPEKIENIYMRSEPVAQ--VFVH-GESLQAFLIAIVVPD 555
Cdd:cd17655 403 IELGEIEARLLQHPDIKEavVIARkDEQGQNYLCAYIVSE 442
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
72-633 |
3.58e-24 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 105.50 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAqNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLR-KGDRVAVLLP-RVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppapEDLAVICFTSGTT 231
Cdd:cd05972 79 DA-----------------------------------------------------------------EDPALIYFTSGTT 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVS---DCSAFVKATENTVNPCPDDT------LISFL-PLAHMFervveCVMLCHGAKIgffqgDIRL 301
Cdd:cd05972 94 GLPKGVLHTHSYPLGhipTAAYWLGLRPDDIHWNIADPgwakgaWSSFFgPWLLGA-----TVFVYEGPRF-----DAER 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 302 LMDDLKVLQPTVFPVVPrllnrmfdrifgqanTTLKRWL-LDFASKRKeaelrsgiirnnslwdrlifhkvqsslgGRVR 380
Cdd:cd05972 164 ILELLERYGVTSFCGPP---------------TAYRMLIkQDLSSYKF----------------------------SHLR 200
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 381 LMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTA--GCCLTMPgdWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGE 458
Cdd:cd05972 201 LVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLtvGNFPDMP--VKPGSMGRPTPGYDVAIID-DDGRELPPGEEGD 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 459 VCVKGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQ 536
Cdd:cd05972 278 IAIKLPPPglFLGYVGDPEKTEASI-RGDYYLTGDRAYRDEDGYFWFVGRADDIIK-SSGYRIGPFEVESALLEHPAVAE 355
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 537 VFV-------HGESLQAFLIAivvpdvetlcswaqKRGFEGSfEELcrnkdvkkaiLEDMVRLGKdSGLKPFEQVKGITL 609
Cdd:cd05972 356 AAVvgspdpvRGEVVKAFVVL--------------TSGYEPS-EEL----------AEELQGHVK-KVLAPYKYPREIEF 409
|
570 580
....*....|....*....|....
gi 1832481686 610 HPELfsidngLLTPTMKAKRPELR 633
Cdd:cd05972 410 VEEL------PKTISGKIRRVELR 427
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
72-555 |
8.35e-24 |
|
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: 105.36 E-value: 8.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWV-----IIEQGCfAYsmviVPLYDTLGNEAITYIVNKAEL 146
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGV--GPGDVVGVLAERSPELVvallaVLKAGA-AY----VPLDPELPAERLAFMLADAGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 147 SLVFVDKPEKAklllegvenkLIPGLKIIVVMDAYGSELVERGQRCgvevtsmkamedlgranrrkpkPPAPEDLAVICF 226
Cdd:cd12117 96 KVLLTDRSLAG----------RAGGLEVAVVIDEALDAGPAGNPAV----------------------PVSPDDLAYVMY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRNIVSdcsaFVKATeNTVNPCPDDTLISFLPL---AHMFERVVEcvmLCHGAKIgffqgdirllm 303
Cdd:cd12117 144 TSGSTGRPKGVAVTHRGVVR----LVKNT-NYVTLGPDDRVLQTSPLafdASTFEIWGA---LLNGARL----------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 304 ddlkVLQPtvfPVVPRLLNRMFDRIFGQANTTLkrWLldfaskrkeaelrsgiirNNSLWdRLIFHKVQSSLGGrVRLMV 383
Cdd:cd12117 205 ----VLAP---KGTLLDPDALGALIAEEGVTVL--WL------------------TAALF-NQLADEDPECFAG-LRELL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 384 TGAAPVS-ATVLTFLRAALGCQFYEGYGQTECT--AGCCLTMPGDWTAGHV--GAPMPcNLIKLVdVEEMNYMAAEGE-G 457
Cdd:cd12117 256 TGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTtfTTSHVVTELDEVAGSIpiGRPIA-NTRVYV-LDEDGRPVPPGVpG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 458 EVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRS 531
Cdd:cd12117 334 ELYVGGDGLALGYLNRPALTAERFVADPFGpgerlyRTGDLARWLPDGRLEFLGRIDDQVKI-RGFRIELGEIEAALRAH 412
|
490 500
....*....|....*....|....*..
gi 1832481686 532 EPVAQVFV---HGESLQAFLIAIVVPD 555
Cdd:cd12117 413 PGVREAVVvvrEDAGGDKRLVAYVVAE 439
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
217-558 |
1.05e-23 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 104.64 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAHMFervveCVM-----LCHGAk 291
Cdd:cd05945 95 DGDDNAYIIFTSGSTGRPKGVQISHDNLVS----FTNWMLSDFPLGPGDVFLNQAPFSFDL-----SVMdlypaLASGA- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 292 igffqgdirllmddlkvlqpTVFPVvPRLLNRMFDRIF-GQANTTLKRWLldfaskrkeaelrsgiiRNNSLWDRLIFHK 370
Cdd:cd05945 165 --------------------TLVPV-PRDATADPKQLFrFLAEHGITVWV-----------------STPSFAAMCLLSP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 371 --VQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTmpgDWT----AGH----VGAPMPCNLI 440
Cdd:cd05945 207 tfTPESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYI---EVTpevlDGYdrlpIGYAKPGAKL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 441 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD---GWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGE 517
Cdd:cd05945 284 VILD-EDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDegqRAYRTGDLVRLEADGLLFYRGRLDFQVKL-NGY 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1832481686 518 YIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDVET 558
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVvpkyKGEKVTE-LIAFVVPKPGA 405
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
72-633 |
1.34e-23 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 104.76 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVK--REERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DkPEKAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgqrcgvevtsmKAMEDL--GRANRRKPKPPAPEDLAVICFTSG 229
Cdd:cd05959 108 S-GELAPVLAAALT-KSEHTLVVLIVSGGAGPEAGA------------LLLAELvaAEAEQLKPAATHADDPAFWLYSSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 230 TTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLAHMFErvvecvmLCHGAKIGFFQGDIRLLM------ 303
Cdd:cd05959 174 STGRPKGVVHLHADIYWTAELYAR---NVLGIREDDVCFSAAKLFFAYG-------LGNSLTFPLSVGATTVLMperptp 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 304 ----DDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfaskrkeaelrsgiirNNSLWdrlifhkvQSSLGGRV 379
Cdd:cd05959 244 aavfKRIRRYRPTVFFGVPTLYAAML---------------------------------AAPNL--------PSRDLSSL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 380 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 459
Cdd:cd05959 283 RLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRD-EDGGDVADGEPGEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 460 CVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV 539
Cdd:cd05959 362 YVRGPSSATMYWNNRDKTRDTF-QGEWTRTGDKYVRDDDGFYTYAGRADDMLK-VSGIWVSPFEVESALVQHPAVLEAAV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 540 HGESLQAFLI---AIVVPdvetlcswaqKRGFEGSfeelcrnkdvkkAILEDMVRLGKDSGLKPFEQVKGITLHPELFSi 616
Cdd:cd05959 440 VGVEDEDGLTkpkAFVVL----------RPGYEDS------------EALEEELKEFVKDRLAPYKYPRWIVFVDELPK- 496
|
570
....*....|....*..
gi 1832481686 617 dngllTPTMKAKRPELR 633
Cdd:cd05959 497 -----TATGKIQRFKLR 508
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
46-566 |
2.07e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 104.74 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 46 WPWGL-------HGQIYNGPCL---GSRKPDQP-YEW----LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPE 110
Cdd:PRK06178 18 WPAGIprepeypHGERPLTEYLrawARERPQRPaIIFyghvITYAELDELSDRFAALLRQRG--VGAGDRVAVFLPNCPQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 111 WVIIEQGCFAYSMVIVPlydtlgneaITYIVNKAELSLVFVDKpekaklllegvenklipGLKIIVVMDAYgSELVER-G 189
Cdd:PRK06178 96 FHIVFFGILKLGAVHVP---------VSPLFREHELSYELNDA-----------------GAEVLLALDQL-APVVEQvR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 190 QRCGVE---VTSMKAM-----------------------EDLGRANRRKPKP-----PAPEDLAVICFTSGTTGNPKGAM 238
Cdd:PRK06178 149 AETSLRhviVTSLADVlpaeptlplpdslraprlaaagaIDLLPALRACTAPvplppPALDALAALNYTGGTTGMPKGCE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 239 VTHRNIVSDCSAFVKATentVNPCPDDTLISFLPlahMFervvecvmlchgakigFFQGDirllmdDLKVLQPTVF--PV 316
Cdd:PRK06178 229 HTQRDMVYTAAAAYAVA---VVGGEDSVFLSFLP---EF----------------WIAGE------NFGLLFPLFSgaTL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 317 VprLLNRmfdrifgqanttlkrwlldfaskrkeaelrsgiirnnslWDRLIF------HKVQSSLG---GRVRLMVTGAa 387
Cdd:PRK06178 281 V--LLAR---------------------------------------WDAVAFmaaverYRVTRTVMlvdNAVELMDHPR- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 388 pVSATVLTFL--------------------RAALGCQFYEG-YGQTEcTAGCcltmpGDWTAG-------------HVGA 433
Cdd:PRK06178 319 -FAEYDLSSLrqvrvvsfvkklnpdyrqrwRALTGSVLAEAaWGMTE-THTC-----DTFTAGfqdddfdllsqpvFVGL 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 434 PMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKL 513
Cdd:PRK06178 392 PVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEAL-RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832481686 514 aQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVP------DVETLCSWAQKR 566
Cdd:PRK06178 471 -NGMSVFPSEVEALLGQHPAVLGSAVVGrpdPDKGQVPVAFVQLkpgadlTAAALQAWCREN 531
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
74-566 |
2.91e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 103.50 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 74 YKQVAELSECIGSALIQKGfktapdQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFVDk 153
Cdd:PRK03640 34 HEAVVSVAGKLAALGVKKG------DRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITD- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 154 pekaklllEGVENKLIPGLKIIVvmdaygSELVErgqrcgvevtsmkamedlGRANRRKPKPPAPED-LAVICFTSGTTG 232
Cdd:PRK03640 107 --------DDFEAKLIPGISVKF------AELMN------------------GPKEEAEIQEEFDLDeVATIMYTSGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 233 NPKGAMVTHRNivsdcsAFVKATENTVNP--CPDDTLISFLPLAH------MFERVVE-CVMLCH----GAKIgffqgdI 299
Cdd:PRK03640 155 KPKGVIQTYGN------HWWSAVGSALNLglTEDDCWLAAVPIFHisglsiLMRSVIYgMRVVLVekfdAEKI------N 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 300 RLLMDDlKVlqpTVFPVVPRLLNRMFDRIfGQANTtlkrwlldfaskrkeaelrsgiirNNSLwdrlifhkvqsslggrv 379
Cdd:PRK03640 223 KLLQTG-GV---TIISVVSTMLQRLLERL-GEGTY------------------------PSSF----------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 380 RLMVTGAAPVSATVLTFLRAAlGCQFYEGYGQTEcTAGCCLTMPGDWTA---GHVGAPM-PCNlIKLVDveEMNYMAAEG 455
Cdd:PRK03640 257 RCMLLGGGPAPKPLLEQCKEK-GIPVYQSYGMTE-TASQIVTLSPEDALtklGSAGKPLfPCE-LKIEK--DGVVVPPFE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 456 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 535
Cdd:PRK03640 332 EGEIVVKGPNVTKGYLNREDATRETF-QDGWFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIEEVLLSHPGVA 409
|
490 500 510
....*....|....*....|....*....|....*...
gi 1832481686 536 QVFVHGESLQ-------AFLIAIVVPDVETLCSWAQKR 566
Cdd:PRK03640 410 EAGVVGVPDDkwgqvpvAFVVKSGEVTEEELRHFCEEK 447
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
72-554 |
3.13e-23 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 103.71 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALiqKGFKTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfV 151
Cdd:TIGR03098 26 LTYAALSERVLALASGL--RGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLL-V 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPEKAKLLLEGvenklIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRANRrkPKPPAPEDLAVICFTSGTT 231
Cdd:TIGR03098 103 TSSERLDLLHPA-----LPGCHDLRTLIIVGDPAHASEGHPGEEPASWPKLLALGDADP--PHPVIDSDMAAILYTSGST 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmfervvecvmlchgakigffqgdirllmddlkvlqp 311
Cdd:TIGR03098 176 GRPKGVVLSHRNLVAGAQSVATYLENR----PDDRLLAVLPLS------------------------------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 312 tvfpvvprllnrmFDRIFGQANTTL----KRWLLDFASKRK-----EAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLM 382
Cdd:TIGR03098 215 -------------FDYGFNQLTTAFyvgaTVVLHDYLLPRDvlkalEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 383 VTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTmPG--DWTAGHVGAPMPcNLIKLVDVEEMNYMAAEGEGEV 459
Cdd:TIGR03098 282 TNSGGAMPRATLSRLRSFLPnARLFLMYGLTEAFRSTYLP-PEevDRRPDSIGKAIP-NAEVLVLREDGSECAPGEEGEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 460 CVKGPNVFQGYLKDPAKTAEALDK----DGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 528
Cdd:TIGR03098 360 VHRGALVAMGYWNDPEKTAERFRPlppfPGELHlpelavwSGDTVRRDEEGFLYFVGRRDEMIKTS-GYRVSPTEVEEVA 438
|
490 500 510
....*....|....*....|....*....|
gi 1832481686 529 MRSEPVAQVFVHG----ESLQAfLIAIVVP 554
Cdd:TIGR03098 439 YATGLVAEAVAFGvpdpTLGQA-IVLVVTP 467
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
220-566 |
3.35e-23 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 100.87 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATENTVNPCPDDTLISFLPLAHM--FERVVECVMLchGAKIGFFQG 297
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLA--SA--AGLHSRLGFGGGDSWLLSLPLYHVggLAILVRSLLA--GAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 298 DiRLLMDDLKVLQPTVFPVVPRLLNRMFDRifGQANTTLKRwlldfaskrkeaelrsgiirnnslwdrlifhkvqsslgg 377
Cdd:cd17630 75 N-QALAEDLAPPGVTHVSLVPTQLQRLLDS--GQGPAALKS--------------------------------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 378 rVRLMVTGAAPVSAtVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDveemnymaaegEG 457
Cdd:cd17630 113 -LRAVLLGGAPIPP-ELLERAADRGIPLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVE-----------DG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 458 EVCVKGPNVFQGYLKDPakTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQV 537
Cdd:cd17630 180 EIWVGGASLAMGYLRGQ--LVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQPEEIEAALAAHPAVRDA 256
|
330 340 350
....*....|....*....|....*....|....*.
gi 1832481686 538 FVHG---ESLQAFLIAIVV----PDVETLCSWAQKR 566
Cdd:cd17630 257 FVVGvpdEELGQRPVAVIVgrgpADPAELRAWLKDK 292
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
218-575 |
8.15e-23 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 100.63 E-value: 8.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECVMLchgakigFFQG 297
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFD----PDDVLLCGLPLFHVNGSVVTLLTP-------LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 298 DIRLLMDDLKVLQPTVFPVVPRLLNRMfdRIfgQANTTLKRWLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLgg 377
Cdd:cd05944 70 AHVVLAGPAGYRNPGLFDNFWKLVERY--RI--TSLSTVPTVYAALLQVPVNADI--------------------SSL-- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 378 rvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMP-GDWTAGHVGAPMPCNLIKLVDVE-EMNYM--AA 453
Cdd:cd05944 124 --RFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNPPdGPKRPGSVGLRLPYARVRIKVLDgVGRLLrdCA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 454 EGE-GEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSE 532
Cdd:cd05944 202 PDEvGEICVAGPGVFGGYLYTEGNK-NAFVADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNIDPALIEEALLRHP 279
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1832481686 533 PVaqvfvhgeslqAFLIAIVVPDV---ETLCSWAQ-KRGFEGSFEEL 575
Cdd:cd05944 280 AV-----------AFAGAVGQPDAhagELPVAYVQlKPGAVVEEEEL 315
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
72-555 |
4.30e-22 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 101.58 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGsALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:PRK06814 659 LTYRKLLTGAFVLG-RKLKKN--TPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKP--EKAKL--LLEGVENklipGLKIIVVMDaygselVERGQRCGVEVTSMKAmedlGRANRRKPKPPAPEDLAVICFT 227
Cdd:PRK06814 736 SRAfiEKARLgpLIEALEF----GIRIIYLED------VRAQIGLADKIKGLLA----GRFPLVYFCNRDPDDPAVILFT 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 228 SGTTGNPKGAMVTHRNIVSDC---SAFVKATentvnpcPDDTLISFLPLAHMFervvecvmlchgakiGFFQGDIRLLMD 304
Cdd:PRK06814 802 SGSEGTPKGVVLSHRNLLANRaqvAARIDFS-------PEDKVFNALPVFHSF---------------GLTGGLVLPLLS 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 305 DLKVL---QPTVFPVVPRLLnrmFDR----IFGqANTTLKRWL-----LDFASkrkeaelrsgiirnnslwdrlifhkvq 372
Cdd:PRK06814 860 GVKVFlypSPLHYRIIPELI---YDTnatiLFG-TDTFLNGYAryahpYDFRS--------------------------- 908
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 sslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNyma 452
Cdd:PRK06814 909 ------LRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGIEYRLEPVPGID--- 979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 453 aEGeGEVCVKGPNVFQGYLK-DPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRS 531
Cdd:PRK06814 980 -EG-GRLFVRGPNVMLGYLRaENPGVLEPP-ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIA-GEMISLAAVEELAAEL 1055
|
490 500
....*....|....*....|....
gi 1832481686 532 EPvaqvfvhgESLQAfliAIVVPD 555
Cdd:PRK06814 1056 WP--------DALHA---AVSIPD 1068
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
63-557 |
5.67e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 100.03 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 63 RKPDQPYEW-----LSYKQVAELSECIGSAL-----IQKGfktapDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTL 132
Cdd:PRK08314 22 RYPDKTAIVfygraISYRELLEEAERLAGYLqqecgVRKG-----DR-VLLYMQNSPQFVIAYYAILRANAVVVPVNPMN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 133 GNEAITYIVNKAELSLVFVdkpekAKLLLEGVEnKLI--PGLKIIVV------MDAYGSE-----LVERGQRCGVEVTSM 199
Cdd:PRK08314 96 REEELAHYVTDSGARVAIV-----GSELAPKVA-PAVgnLRLRHVIVaqysdyLPAEPEIavpawLRAEPPLQALAPGGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 200 KAMEDLGRANRRkpkPPA----PEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPcpDDTLISFLPLAH 275
Cdd:PRK08314 170 VAWKEALAAGLA---PPPhtagPDDLAVLPYTSGTTGVPKGCMHTHRTVM--ANAVGSVLWSNSTP--ESVVLAVLPLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 276 mferVVECVMLCHGAkigFFQGDIRLLMddlkvlqptvfpvvPR----LLNRMFDR---IFGQANTTLkrwLLDFaskrk 348
Cdd:PRK08314 243 ----VTGMVHSMNAP---IYAGATVVLM--------------PRwdreAAARLIERyrvTHWTNIPTM---VVDF----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 349 eaeLRSGIIRNNSLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG----------- 417
Cdd:PRK08314 294 ---LASPGLAERDL----------SSL----RYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTETMAQthsnppdrpkl 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 418 CCLTMPgdwTAGhVGApmpcnliKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA---LDKDGWLHTGDIGK 494
Cdd:PRK08314 357 QCLGIP---TFG-VDA-------RVIDPETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAfieIDGKRFFRTGDLGR 425
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 495 WLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFV-------HGESLQAFliaiVVPDVE 557
Cdd:PRK08314 426 MDEEGYFFITDRLKRMIN-ASGFKVWPAEVENLLYKHPAIQEACViatpdprRGETVKAV----VVLRPE 490
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
219-550 |
1.13e-21 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 98.30 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 219 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISflpLAHMFErvveCVMLCHGAKIGFFQGD 298
Cdd:cd05919 91 DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR---EALGLTPGDRVFS---SAKMFF----GYGLGNSLWFPLAVGA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 299 IRLLMDD----------LKVLQPTVFPVVPRLlnrmfdrifgqanttlkrwlldFASKRKEAELRSGIIRNnslwdrlif 368
Cdd:cd05919 161 SAVLNPGwptaervlatLARFRPTVLYGVPTF----------------------YANLLDSCAGSPDALRS--------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 369 hkvqsslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEM 448
Cdd:cd05919 210 ----------LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVD-EEG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTaEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 528
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKS-RATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVG-GQWVSPVEVESLI 356
|
330 340
....*....|....*....|....*....
gi 1832481686 529 MRSEPVAQVFV------HGES-LQAFLIA 550
Cdd:cd05919 357 IQHPAVAEAAVvavpesTGLSrLTAFVVL 385
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
72-577 |
1.17e-21 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 98.74 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVF- 150
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLR--PGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVi 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 151 -VDKPekakllleGVENKLIPGLKIIVVMDAYGSelvergqrcGVEVTSMKAMEDlgranrrkpKPPAPEDLAVICFTSG 229
Cdd:cd05923 107 aVDAQ--------VMDAIFQSGVRVLALSDLVGL---------GEPESAGPLIED---------PPREPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 230 TTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMfervvecvmlchgakIGFFQgdirLLMDDLkVL 309
Cdd:cd05923 161 TTGLPKGAVIPQRAAES--RVLFMSTQAGLRHGRHNVVLGLMPLYHV---------------IGFFA----VLVAAL-AL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 310 QPTVFPVvprllnRMFDRIFgqanttlkrwlldfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLG-GRVRLMVTGAAP 388
Cdd:cd05923 219 DGTYVVV------EEFDPAD--------------ALKLIEQERVTSLFATPTHLDALAAAAEFAGLKlSSLRHVTFAGAT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 389 VSATVLTFLRAALGCQFYEGYGQTEctAGCCLTMPgDWTAGHVGAPMPCNLIKLVDV-EEMNYMAAEG-EGEVCVK--GP 464
Cdd:cd05923 279 MPDAVLERVNQHLPGEKVNIYGTTE--AMNSLYMR-DARTGTEMRPGFFSEVRIVRIgGSPDEALANGeEGELIVAaaAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 465 NVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG--- 541
Cdd:cd05923 356 AAFTGYLNQPEATAKKL-QDGWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSRHPGVTEVVVIGvad 433
|
490 500 510
....*....|....*....|....*....|....*.
gi 1832481686 542 ESLQAFLIAIVVPDVETLCswaqkrgfEGSFEELCR 577
Cdd:cd05923 434 ERWGQSVTACVVPREGTLS--------ADELDQFCR 461
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
217-647 |
1.32e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 99.10 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHM--FERVVECVML--CHGAKI 292
Cdd:PLN02860 170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAKIAI----VGYGEDDVYLHTAPLCHIggLSSALAMLMVgaCHVLLP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 GFfqgDIRLLMDDLKVLQPTVFPVVPRLL------NRMfdRIFGQANTTLKRWLldfaskrkeaelrSGiirNNSLWDRL 366
Cdd:PLN02860 246 KF---DAKAALQAIKQHNVTSMITVPAMMadlislTRK--SMTWKVFPSVRKIL-------------NG---GGSLSSRL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 367 IfhKVQSSLGGRVRLMVTGAAPVSATVLTFLRaaLGCQFYEGYGQTECTAGCCLTMPGDWTAGH-VGAPMPcnliklvDV 445
Cdd:PLN02860 305 L--PDAKKLFPNAKLFSAYGMTEACSSLTFMT--LHDPTLESPKQTLQTVNQTKSSSVHQPQGVcVGKPAP-------HV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 446 EEMNYM-AAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKI 524
Cdd:PLN02860 374 ELKIGLdESSRVGRILTRGPHVMLGYWGQNSETASVLSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIK-TGGENVYPEEV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 525 ENIYMRSEPVAQVFVHGeSLQAFLIAIVVPDVETLCSW--------AQKRGFEGSFEEL---CRNKdvkkailedmvrlg 593
Cdd:PLN02860 453 EAVLSQHPGVASVVVVG-VPDSRLTEMVVACVRLRDGWiwsdnekeNAKKNLTLSSETLrhhCREK-------------- 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1832481686 594 kdsGLKPFEQVKGITLHPELFSidnglLTPTMKAKRPELRNYFRSQIDDLYSTI 647
Cdd:PLN02860 518 ---NLSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVRREVLSHLQSLPSNL 563
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
217-633 |
1.60e-21 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 97.89 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPlahmfervvecvmlchgAKIGFFQ 296
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHRVLLGH----LPGVQFPFNLFPRDGDLYWTP-----------------ADWAWIG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 297 GdirlLMDdlkVLQPTVFPVVPRLLNRM--FDRifGQANTTLKRWLLDFASKRKEAeLRsgIIRnnslwdrliFHKVQSS 374
Cdd:cd05971 145 G----LLD---VLLPSLYFGVPVLAHRMtkFDP--KAALDLMSRYGVTTAFLPPTA-LK--MMR---------QQGEQLK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 375 LGG-RVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEC---TAGCCLTMPGDwtAGHVGAPMPCNLIKLVDvEEMNY 450
Cdd:cd05971 204 HAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnlvIGNCSALFPIK--PGSMGKPIPGHRVAIVD-DNGTP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 451 MAAEGEGEVCVKGPN--VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIY 528
Cdd:cd05971 281 LPPGEVGEIAVELPDpvAFLGYWNNPSATEKKM-AGDWLLTGDLGRKDSDGYFWYVGRDDDVITSS-GYRIGPAEIEECL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 529 MRSEPVAQVFV-------HGESLQAFliaIVVpdvetlcswaqKRGFEGSfEELCRNkdvkkaiLEDMVRlgkdSGLKPF 601
Cdd:cd05971 359 LKHPAVLMAAVvgipdpiRGEIVKAF---VVL-----------NPGETPS-DALARE-------IQELVK----TRLAAH 412
|
410 420 430
....*....|....*....|....*....|..
gi 1832481686 602 EQVKGITLHPELfsidngLLTPTMKAKRPELR 633
Cdd:cd05971 413 EYPREIEFVNEL------PRTATGKIRRRELR 438
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
72-554 |
2.78e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.03 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGL--LPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKpekaklllEGVENKLIPGLKIIVVMDAYGSElveRGQRCG-VEVTsmkamedLGRANRRKPKPPAPEDL----AVICF 226
Cdd:PRK05852 122 DA--------DGPHDRAEPTTRWWPLTVNVGGD---SGPSGGtLSVH-------LDAATEPTPATSTPEGLrpddAMIMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVECV-MLCHGAKI-----GFFQGdiR 300
Cdd:PRK05852 184 TGGTTGLPKMVPWTHANIASSVRAIITGYRLS----PRDATVAVMPLYHGHGLIAALLaTLASGGAVllparGRFSA--H 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 301 LLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFA----SKRKEAELRsgIIRNNSlwdrlifhkvqsslg 376
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVP----------------TIHQILLERAatepSGRKPAALR--FIRSCS--------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 377 grvrlmvtgaAPVSATVLTFLRAALGCQFYEGYGQTECT----------AGCCLTmPGDWT--AGHVGAPMpcnlIKLVD 444
Cdd:PRK05852 305 ----------APLTAETAQALQTEFAAPVVCAFGMTEAThqvtttqiegIGQTEN-PVVSTglVGRSTGAQ----IRIVG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 445 VEEMNYMAAEgEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 524
Cdd:PRK05852 370 SDGLPLPAGA-VGEVWLRGTTVVRGYLGDPTITAANF-TDGWLRTGDLGSLSAAGDLSIRGRIKELINRG-GEKISPERV 446
|
490 500 510
....*....|....*....|....*....|...
gi 1832481686 525 ENIYMRSEPVAQVFVHGESLQAF---LIAIVVP 554
Cdd:PRK05852 447 EGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVP 479
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
215-555 |
2.95e-21 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 97.41 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 215 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKI 292
Cdd:cd17651 132 ALDADDLAYVIYTSGSTGRPKGVVMPHRSLAN----LVAWQARASSLGPGARTLQFAGLG--FDVSVQEIFstLCAGATL 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 GFFQGDIRllMDDlkvlqptvfpvvprllnrmfdrifgqanTTLKRWLldfaskrkeAELR-SGIIRNNSLWDRLIFH-K 370
Cdd:cd17651 206 VLPPEEVR--TDP----------------------------PALAAWL---------DEQRiSRVFLPTVALRALAEHgR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 371 VQSSLGGRVRLMVTGAAPVSATVLT--FLRAALGCQFYEGYGQTECTAGCCLTMPGD---WTA-GHVGAPMPCNLIKLVD 444
Cdd:cd17651 247 PLGVRLAALRYLLTGGEQLVLTEDLreFCAGLPGLRLHNHYGPTETHVVTALSLPGDpaaWPApPPIGRPIDNTRVYVLD 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 445 vEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 518
Cdd:cd17651 327 -AALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpgarmyRTGDLARWLPDGELEFLGRADDQVKI-RGFR 404
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1832481686 519 IAPEKIENIYMRSEPVAQ--VFVHGE-SLQAFLIAIVVPD 555
Cdd:cd17651 405 IELGEIEAALARHPGVREavVLAREDrPGEKRLVAYVVGD 444
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
219-527 |
7.36e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 94.25 E-value: 7.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 219 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDTLISFLPLAHMFERVVECVMLCHGAKIGFFQGD 298
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVV---GDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 299 IRL--LMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwlldfaskrkeaELRSGIIRNNSLwdRLIfhkvqsslg 376
Cdd:cd17635 78 TTYksLFKILTTNAVTTTCLVPTLLSKLVS------------------------ELKSANATVPSL--RLI--------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 377 grvrlMVTGAAPVSATVLTFLRAALgCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMAAeG 455
Cdd:cd17635 123 -----GYGGSRAIAADVRFIEATGL-TNTAQVYGLSETGTALCLpTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSA-S 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832481686 456 EGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENI 527
Cdd:cd17635 196 FGTIWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLGERREDGFLFITGRSSESINCG-GVKIAPDEVERI 265
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
210-536 |
1.65e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 96.32 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 210 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchG 289
Cdd:PRK08043 356 RLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALPLFHSF-----------G 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 290 AKIGFFQGdirlLMDDLKVL---QPTVFPVVPRLLnrmFDR----IFGQAnTTLKRWL-----LDFAskrkeaelrsgii 357
Cdd:PRK08043 421 LTVGLFTP----LLTGAEVFlypSPLHYRIVPELV---YDRnctvLFGTS-TFLGNYArfanpYDFA------------- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 358 rnnslwdrlifhkvqsslggRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPC 437
Cdd:PRK08043 480 --------------------RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 438 NLIKLVDVEEMnymaaEGEGEVCVKGPNVFQGYLK--DP-------AKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK 508
Cdd:PRK08043 540 MDARLLSVPGI-----EQGGRLQLKGPNIMNGYLRveKPgvlevptAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAK 614
|
330 340
....*....|....*....|....*...
gi 1832481686 509 HIFKLAqGEYIAPEKIENIYMRSEPVAQ 536
Cdd:PRK08043 615 RFAKIA-GEMVSLEMVEQLALGVSPDKQ 641
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
124-541 |
1.69e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 95.34 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 124 VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekaklllegvENKLIPGLKI-IVVMDAYGSELVERGQRCGVEVTSMKam 202
Cdd:PRK06145 78 VFLPINYRLAADEVAYILGDAGAKLLLVDE-----------EFDAIVALETpKIVIDAAAQADSRRLAQGGLEIPPQA-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 203 edlgranrrkpkPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpcpDDTLISFLPLAHmferVVE 282
Cdd:PRK06145 145 ------------AVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGLTA----SERLLVVGPLYH----VGA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 283 C-----VMLCHGAKIGFFQG-DIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanTTLKRWLLDFASKRkeaelrsgi 356
Cdd:PRK06145 205 FdlpgiAVLWVGGTLRIHREfDPEAVLAAIERHRLTCAWMAPVMLSRVL--------TVPDRDRFDLDSLA--------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 357 irnnslWdrlifhkvqsSLGGrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTA--GHVGAP 434
Cdd:PRK06145 268 ------W----------CIGG-------GEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEkiGSTGRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 435 MPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLA 514
Cdd:PRK06145 325 LAHVEIRIAD-GAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAF-YGDWFRSGDVGYLDEEGFLYLTDRKKDMI-IS 401
|
410 420
....*....|....*....|....*..
gi 1832481686 515 QGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:PRK06145 402 GGENIASSEVERVIYELPEVAEAAVIG 428
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
171-534 |
2.34e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 95.06 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 171 GLKIIVV---MDAYGSELVERGQRcGVEVTSMKAMEDLgranrrKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSD 247
Cdd:PRK07768 108 GAKAVVVgepFLAAAPVLEEKGIR-VLTVADLLAADPI------DPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYAN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 248 CSAFVKATENTVNpcpDDTLISFLPLAH-MfervvecvmlchgAKIGFFQGDIRLLMDDLKVlQPTVFPVVPRLLNRMFD 326
Cdd:PRK07768 181 AEAMFVAAEFDVE---TDVMVSWLPLFHdM-------------GMVGFLTVPMYFGAELVKV-TPMDFLRDPLLWAELIS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 327 RIFGQ-------ANTTLKRwLLDFASKRKEAELrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVS-ATVLTFLR 398
Cdd:PRK07768 244 KYRGTmtaapnfAYALLAR-RLRRQAKPGAFDL--------------------SSL----RFALNGAEPIDpADVEDLLD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 399 A---------ALGCqfyeGYGQTECTAGCCLTMPGD--------------------WTAGHV------GAPMPCNLIKLV 443
Cdd:PRK07768 299 AgarfglrpeAILP----AYGMAEATLAVSFSPCGAglvvdevdadllaalrravpATKGNTrrlatlGPPLPGLEVRVV 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 DvEEMNYMAAEGEGEVCVKGPNVFQGYLkDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 523
Cdd:PRK07768 375 D-EDGQVLPPRGVGVIELRGESVTPGYL-TMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMA-GRNIYPTD 451
|
410
....*....|.
gi 1832481686 524 IENIYMRSEPV 534
Cdd:PRK07768 452 IERAAARVEGV 462
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
63-539 |
3.00e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 94.83 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 63 RKPDQPY-----EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAI 137
Cdd:PRK06155 33 RYPDRPLlvfggTRWTYAEAARAAAAAAHALAAAGVK--RGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 138 TYIVNKAELSLVFVDkpekAKLL--LEGVENKLIPgLKIIVVMDAYGSELVERGQRcgveVTSMKAMedlgrANRRKPKP 215
Cdd:PRK06155 111 EHILRNSGARLLVVE----AALLaaLEAADPGDLP-LPAVWLLDAPASVSVPAGWS----TAPLPPL-----DAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 216 PAPEDLAVICFTSGTTGNPKGAMVTH-------RNIVSDcsafvkatentVNPCPDDTLISFLPLAH-----MFERVvec 283
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHaqfywwgRNSAED-----------LEIGADDVLYTTLPLFHtnalnAFFQA--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 284 vmLCHGAKI---------GFFqgdirllmDDLKVLQPTVF----PVVPRLLnrmfdrifgqanttlkrwlldfaSKRKEA 350
Cdd:PRK06155 243 --LLAGATYvleprfsasGFW--------PAVRRHGATVTyllgAMVSILL-----------------------SQPARE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 351 ELRSgiirnnslwdrlifHKVQSSLGGrvrlmvtgaaPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDwTAGH 430
Cdd:PRK06155 290 SDRA--------------HRVRVALGP----------GVPAALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 431 VGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKG--PNVF-QGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRK 507
Cdd:PRK06155 345 MGRLAPGFEARVVD-EHDQELPDGEPGELLLRAdePFAFaTGYFGMPEKTVEAW-RNLWFHTGDRVVRDADGWFRFVDRI 422
|
490 500 510
....*....|....*....|....*....|...
gi 1832481686 508 KHIFKlAQGEYIAPEKIENIyMRSEP-VAQVFV 539
Cdd:PRK06155 423 KDAIR-RRGENISSFEVEQV-LLSHPaVAAAAV 453
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-555 |
6.21e-20 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 95.41 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARG--VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLT 2106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPEKAKLLLEGvenklipglkiivvmdaygselvergqrcGVEVTSMKAMEDLGRANRRKPKPP-APEDLAVICFTSGT 230
Cdd:PRK12316 2107 QRHLLERLPLPA-----------------------------GVARLPLDRDAEWADYPDTAPAVQlAGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 231 TGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigffqgdiRLLMDDLKV 308
Cdd:PRK12316 2158 TGLPKGVAVSHGALVAHCQAAGERYELS----PADCELQFMSFS--FDGAHEQWFhpLLNGA---------RVLIRDDEL 2222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 309 LQPtvfpvvprllNRMFDRIFGQANTtlkrwLLDFASkrkeaelrsgiirnnSLWDRLIFHKVQSSLGGRVRLMVTGAAP 388
Cdd:PRK12316 2223 WDP----------EQLYDEMERHGVT-----ILDFPP---------------VYLQQLAEHAERDGRPPAVRVYCFGGEA 2272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 389 VSATVLTFLRAALGCQF-YEGYGQTECTA-----GCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVK 462
Cdd:PRK12316 2273 VPAASLRLAWEALRPVYlFNGYGPTEAVVtpllwKCRPQDPCGAAYVPIGRALGNRRAYILD-ADLNLLAPGMAGELYLG 2351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 463 GPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVA 535
Cdd:PRK12316 2352 GEGLARGYLNRPGLTAERFVPDPFSAsgerlyrTGDLARYRADGVVEYLGRIDHQVKI-RGFRIELGEIEARLQAHPAVR 2430
|
490 500
....*....|....*....|...
gi 1832481686 536 QVFV---HGESLQAfLIAIVVPD 555
Cdd:PRK12316 2431 EAVVvaqDGASGKQ-LVAYVVPD 2452
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
135-577 |
8.91e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 93.09 E-value: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 135 EAITYIVNKAELSLVFVDkPEKAKLLLEGVEnkLIPGLKIIVV---MDAYGselveRGQRCG-VEVTSMKAMEDLGRAnr 210
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIVD-TEFAEVAREALA--LLPGPKPLVIdvdDPEYP-----GGRFIGaLDYEAFLASGDPDFA-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 211 rkPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRnivsdcSAFVKATENTV--NPCPDDTLISFLPLAHmfervveCVMLC 287
Cdd:PRK08162 175 --WTLPADEwDAIALNYTSGTTGNPKGVVYHHR------GAYLNALSNILawGMPKHPVYLWTLPMFH-------CNGWC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 288 H--------GAKIGFFQGDIRLLMDDLKVLQPTVF---PVVPRLLnrmfdrifgqANTtlkrwlldfaskrkEAELRSGI 356
Cdd:PRK08162 240 FpwtvaaraGTNVCLRKVDPKLIFDLIREHGVTHYcgaPIVLSAL----------INA--------------PAEWRAGI 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 357 irnnslwdrlifhkvqsslGGRVRLMVTGAAPVSAtVLTFLRAAlGCQFYEGYGQTEC--TAGCCLTMPGdWTA------ 428
Cdd:PRK08162 296 -------------------DHPVHAMVAGAAPPAA-VIAKMEEI-GFDLTHVYGLTETygPATVCAWQPE-WDAlplder 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 429 ----GHVGAPMPC-NLIKLVDVEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTL 501
Cdd:PRK08162 354 aqlkARQGVRYPLqEGVTVLDPDTMQPVPADGEtiGEIMFRGNIVMKGYLKNPKATEEAF-AGGWFHTGDLAVLHPDGYI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 502 KIIDRKKHIFkLAQGEYIAPEKIENIYMRsepvaqvfvHgeslQAFLIAIVV--PDV---ETLCSWAQ-KRGFEGSFEEL 575
Cdd:PRK08162 433 KIKDRSKDII-ISGGENISSIEVEDVLYR---------H----PAVLVAAVVakPDPkwgEVPCAFVElKDGASATEEEI 498
|
....*
gi 1832481686 576 ---CR 577
Cdd:PRK08162 499 iahCR 503
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
72-577 |
2.34e-19 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 91.75 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKTA-------PdqfigifaqNRPEWVIIeqgCFAYSMV-IVPLYdTL----GNEaITY 139
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGdrvvvqlP---------NVAEFVIV---FFALFRAgAIPVF-ALpahrRAE-ISH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 140 IVNKAELS-LVFVDKPEK------AKLLLEGVenkliPGLKIIVVMDAYGSELvergqrcgvevtsmkAMEDLGRANRRK 212
Cdd:COG1021 117 FAEQSEAVaYIIPDRHRGfdyralARELQAEV-----PSLRHVLVVGDAGEFT---------------SLDALLAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 213 PKP-PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPcpDDTLISFLPLAHMFervvecVMLCHGAk 291
Cdd:COG1021 177 SEPrPDPDDVAFFQLSGGTTGLPKLIPRTHDDYL--YSVRASAEICGLDA--DTVYLAALPAAHNF------PLSSPGV- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 292 IGFFQ--GDIRL-----------LMDDLKVlqpTVFPVVPRLLNRMfdrifgqanttlkrwlLDFASKRKeAELrsgiir 358
Cdd:COG1021 246 LGVLYagGTVVLapdpspdtafpLIERERV---TVTALVPPLALLW----------------LDAAERSR-YDL------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 359 nnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGD---WTAGHVGAP 434
Cdd:COG1021 300 --------------SSL----RVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE---GlVNYTRLDDpeeVILTTQGRP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 435 M-PCNLIKLVDVEEMNymAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKK-HIF 511
Cdd:COG1021 359 IsPDDEVRIVDEDGNP--VPPGEvGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRAKdQIN 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 512 KlaQGEYIAPEKIENIYMRSEPVAQVfvhgeslqafliAIV-VPDV---ETLCSWAQKRGFEGSFEELCR 577
Cdd:COG1021 437 R--GGEKIAAEEVENLLLAHPAVHDA------------AVVaMPDEylgERSCAFVVPRGEPLTLAELRR 492
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
72-556 |
7.92e-19 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 91.76 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAITYIVNKAELS 147
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAG--VGPDVLVGIAVERSIEMVVgllaVLKAGGAY----VPLDPEYPQDRLAYMLDDSGVR 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 148 LVFVDkPEKAKLLlegvenKLIPGLKIIVvMDAYGSELVergqrcgvevtsmkamedlGRANRRKPKPPAPEDLAVICFT 227
Cdd:PRK12467 612 LLLTQ-SHLLAQL------PVPAGLRSLC-LDEPADLLC-------------------GYSGHNPEVALDPDNLAYVIYT 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 228 SGTTGNPKGAMVTHRNIVSdcsaFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqgdirLLMDDLK 307
Cdd:PRK12467 665 SGSTGQPKGVAISHGALAN----YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--------HLLPPDC 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 308 VLQPTVFpvvprllnrmFDRIFGQANTTLKRwlldfaskrkeaelrsgiirNNSLWDRLIFHKVQSSLGGRVRLMVTGAA 387
Cdd:PRK12467 733 ARDAEAF----------AALMADQGVTVLKI--------------------VPSHLQALLQASRVALPRPQRALVCGGEA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 388 -PVSATVLTFlRAALGCQFYEGYGQTECTAGC----CLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVK 462
Cdd:PRK12467 783 lQVDLLARVR-ALGPGARLINHYGPTETTVGVstyeLSDEERDFGNVPIGQPLANLGLYILD-HYLNPVPVGVVGELYIG 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 463 GPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVA 535
Cdd:PRK12467 861 GAGLARGYHRRPALTAERFVPDpfgadgGRLYrTGDLARYRADGVIEYLGRMDHQVKI-RGFRIELGEIEARLLAQPGVR 939
|
490 500
....*....|....*....|...
gi 1832481686 536 QVFV--HGESLQAFLIAIVVPDV 556
Cdd:PRK12467 940 EAVVlaQPGDAGLQLVAYLVPAA 962
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
66-534 |
9.45e-19 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 89.85 E-value: 9.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 66 DQPYEWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPlydtlgneaityivnkae 145
Cdd:cd05908 10 DKKEKFVSYRHLREEALGYLGALQELGIK--PGQEVVFQITHNNKFLYLFWACLLGGMIAVP------------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 146 lslVFVDKPEKAKLLLEGVENKLI-PGLkiivvmdaygselvergqrcgveVTSMKAMEDLgranrrkpkppaPEDLAVI 224
Cdd:cd05908 70 ---VSIGSNEEHKLKLNKVWNTLKnPYL-----------------------ITEEEVLCEL------------ADELAFI 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 225 CFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVnpcpDDTLISFLPLAHMFErvvecVMLCHGAKIgfFQGDIRLLMd 304
Cdd:cd05908 112 QFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKT----KDRILSWMPLTHDMG-----LIAFHLAPL--IAGMNQYLM- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 305 dlkvlqPT-VFPVVPRLlnrmfdrifgqanttlkrWLLDfASKRKEAELRSGIIRNNSLWDRLIFHKVQSSLGGRVRLMV 383
Cdd:cd05908 180 ------PTrLFIRRPIL------------------WLKK-ASEHKATIVSSPNFGYKYFLKTLKPEKANDWDLSSIRMIL 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 384 TGAAPVSAT---VLTFLRAALGCQ---FYEGYGQTECTAGCCL----------------------------TMPGDWTAG 429
Cdd:cd05908 235 NGAEPIDYElchEFLDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvthgepepevdkKDSECLTFV 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 430 HVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKK 508
Cdd:cd05908 315 EVGKPIDETDIRICD--EDNKILPDGYiGHIQIRGKNVTPGYYNNPEATAKVFTDDGWLKTGDLG-FIRNGRLVITGREK 391
|
490 500
....*....|....*....|....*.
gi 1832481686 509 HIFkLAQGEYIAPEKIENIYMRSEPV 534
Cdd:cd05908 392 DII-FVNGQNVYPHDIERIAEELEGV 416
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
58-622 |
9.69e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 90.11 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 58 PCLGSRKPDQ-PYEWLSYKQVAELSECIGSALIQKGFktAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL---YDTLG 133
Cdd:PRK12582 66 PWLAQREPGHgQWRKVTYGEAKRAVDALAQALLDLGL--DPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVspaYSLMS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 134 NE--AITYIVNKAELSLVFVDKPEK-----AKLLLEGVEnklipglkiIVVMDAYG--------SELVERGQRCGVEvts 198
Cdd:PRK12582 144 HDhaKLKHLFDLVKPRVVFAQSGAPfaralAALDLLDVT---------VVHVTGPGegiasiafADLAATPPTAAVA--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 199 mKAMEDLGranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRNIvsdCSAfVKATENTVNPCPDD---TLISFLPLAH 275
Cdd:PRK12582 212 -AAIAAIT-----------PDTVAKYLFTSGSTGMPKAVINTQRMM---CAN-IAMQEQLRPREPDPpppVSLDWMPWNH 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 276 MFervvecvmlchGAKIGFfQGDIR----LLMDDLKVLqPTVFPVVPRLLNRMFDRIFGQANTTLKrwLLDFASKRKEAE 351
Cdd:PRK12582 276 TM-----------GGNANF-NGLLWgggtLYIDDGKPL-PGMFEETIRNLREISPTVYGNVPAGYA--MLAEAMEKDDAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 352 LRSgiirnnslwdrliFHKvqsslggRVRLMVTGAAPVSATVLTFLRA----ALGCQ--FYEGYGQTEcTAGccLTMPGD 425
Cdd:PRK12582 341 RRS-------------FFK-------NLRLMAYGGATLSDDLYERMQAlavrTTGHRipFYTGYGATE-TAP--TTTGTH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 426 WTA---GHVGAPMPCNLIKLVDVEEmNYmaaegegEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWL----PN 498
Cdd:PRK12582 398 WDTervGLIGLPLPGVELKLAPVGD-KY-------EVRVKGPNVTPGYHKDPELTAAAFDEEGFYRLGDAARFVdpddPE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 499 GTLKIIDRKKHIFKLAQGEYIAPEKIE-NIYMRSEPVAQ-VFVHGESlQAFLIAIVVPDVETLCSWAQKRGfeGSFEELC 576
Cdd:PRK12582 470 KGLIFDGRVAEDFKLSTGTWVSVGTLRpDAVAACSPVIHdAVVAGQD-RAFIGLLAWPNPAACRQLAGDPD--AAPEDVV 546
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1832481686 577 RNKDVKKAILEDMVRLGKDSGlKPFEQVKGITLHPELFSIDNGLLT 622
Cdd:PRK12582 547 KHPAVLAILREGLSAHNAEAG-GSSSRIARALLMTEPPSIDAGEIT 591
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
89-549 |
2.55e-18 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 88.59 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 89 IQKGFKTApdqfigIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVfVDKPEKAKLLLEGVENKL 168
Cdd:PRK08008 59 IRKGDKVA------LHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLL-VTSAQFYPMYRQIQQEDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 169 IPgLKIIVVMDAYGSElvERGqrcgveVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdc 248
Cdd:PRK08008 132 TP-LRHICLTRVALPA--DDG------VSSFTQLKAQQPATLCYAPPLSTDDTAEILFTSGTTSRPKGVVITHYNLRF-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 249 SAFVKATENTVNPcpDDTLISFLPLAHM-FERVVECVMLCHGAKIGF--------FQGDIRLLmddlkvlQPTVFPVVPR 319
Cdd:PRK08008 201 AGYYSAWQCALRD--DDVYLTVMPAFHIdCQCTAAMAAFSAGATFVLlekysaraFWGQVCKY-------RATITECIPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 320 LLNRM-------FDRifgqaNTTLKRWL--LDFASKRKEA-ELRSGiirnnslwdrlifhkvqsslggrVRLMVTgaapv 389
Cdd:PRK08008 272 MIRTLmvqppsaNDR-----QHCLREVMfyLNLSDQEKDAfEERFG-----------------------VRLLTS----- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 390 satvltflraalgcqfyegYGQTECTAGCCLTMPGD---WTAghVGAPMPCNLIKLVDveEMNYMAAEGE-GEVCVKG-- 463
Cdd:PRK08008 319 -------------------YGMTETIVGIIGDRPGDkrrWPS--IGRPGFCYEAEIRD--DHNRPLPAGEiGEICIKGvp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 464 -PNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFVHG- 541
Cdd:PRK08008 376 gKTIFKEYYLDPKATAKVLEADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRG-GENVSCVELENIIATHPKIQDIVVVGi 454
|
490
....*....|....
gi 1832481686 542 ------ESLQAFLI 549
Cdd:PRK08008 455 kdsirdEAIKAFVV 468
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
72-555 |
2.99e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 88.10 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd12114 13 LTYGELAERARRVAGALKAAG--VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPekakllleGVENKLIPGLKIIVVMDAygselvergqrcgvevtsmkamedLGRANRRKPKPPAPEDLAVICFTSGTT 231
Cdd:cd12114 91 DGP--------DAQLDVAVFDVLILDLDA------------------------LAAPAPPPPVDVAPDDLAYVIFTSGST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAH------MFErvvecvMLCHGAKIGFFQGDIR----L 301
Cdd:cd12114 139 GTPKGVMISHRAALNTILDINRRFAVG----PDDRVLALSSLSFdlsvydIFG------ALSAGATLVLPDEARRrdpaH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 302 LMDDLKVLQPTVFPVVPRLLNrMfdrifgqanttlkrwLLDfaskrkeaELRSGIIRNNSLwdRLIFHK---VQSSLGGR 378
Cdd:cd12114 209 WAELIERHGVTLWNSVPALLE-M---------------LLD--------VLEAAQALLPSL--RLVLLSgdwIPLDLPAR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 379 VRLMVTGAAPVSatvltflraaLGcqfyegyGQTECTAGCCL----TMPGDWTAGHVGAPMPCNLIKLVDveemnymaAE 454
Cdd:cd12114 263 LRALAPDARLIS----------LG-------GATEASIWSIYhpidEVPPDWRSIPYGRPLANQRYRVLD--------PR 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 455 GE-------GEVCVKGPNVFQGYLKDPAKTAEAL--DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 523
Cdd:cd12114 318 GRdcpdwvpGELWIGGRGVALGYLGDPELTAARFvtHPDGerLYRTGDLGRYRPDGTLEFLGRRDGQVKV-RGYRIELGE 396
|
490 500 510
....*....|....*....|....*....|....
gi 1832481686 524 IENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPD 555
Cdd:cd12114 397 IEAALQAHPGVARavVVVLGDPGGKRLAAFVVPD 430
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
218-568 |
7.74e-18 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 86.37 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPcpddtlISFLPLAHMFERVVE---CVMLCHGAKIGF 294
Cdd:cd17650 92 PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELDSFP------VRLLQMASFSFDVFAgdfARSLLNGGTLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 295 FQGDIRL----LMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLLDFASKRKE--AELRSGIIRNNSLWDRLiF 368
Cdd:cd17650 166 CPDEVKLdpaaLYDLILKSRITLMESTP----------------ALIRPVMAYVYRNGLdlSAMRLLIVGSDGCKAQD-F 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 369 HKVQSSLGGRVRLmvtgaapVSATVLTflRAALGCQFYEGYGQTECTAGcclTMPgdwtaghVGAPMPCNLIKLVDvEEM 448
Cdd:cd17650 229 KTLAARFGQGMRI-------INSYGVT--EATIDSTYYEEGRDPLGDSA---NVP-------IGRPLPNTAMYVLD-ERL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPE 522
Cdd:cd17650 289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFapgermYRTGDLARWRADGNVELLGRVDHQVKI-RGFRIELG 367
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1832481686 523 KIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETlcSWAQKRGF 568
Cdd:cd17650 368 EIESQLARHPAIDEAVVavrEDKGGEARLCAYVVAAATL--NTAELRAF 414
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
72-566 |
8.26e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 87.11 E-value: 8.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQG--VRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 dKPEKAKL----LLEGVENKLIPGLKIIVVMDAYGSELVERGQRCGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICFT 227
Cdd:PRK06164 114 -WPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQLFALPDPAPPAAA----GERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 228 -SGTTGNPK------GAMVTHRNIVSDCSAFVkatentvnpcPDDTLISFLPLahmfervveCVMLCHGAKIGFFQGDIR 300
Cdd:PRK06164 189 tSGTTSGPKlvlhrqATLLRHARAIARAYGYD----------PGAVLLAALPF---------CGVFGFSTLLGALAGGAP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 301 LLMDDlkvlqptVF--PVVPRLL-----------NRMFDRIFGQANTTLkrwllDFASKRkeaelrsgiirnnslwdRLI 367
Cdd:PRK06164 250 LVCEP-------VFdaARTARALrrhrvthtfgnDEMLRRILDTAGERA-----DFPSAR-----------------LFG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 368 FHKVQSSLGGRVRLMVTGAAPvsatvLTFLraalgcqfyegYGQTECTA-GCCLTMPGDWTAGHV--GAPM-PCNLIKLV 443
Cdd:PRK06164 301 FASFAPALGELAALARARGVP-----LTGL-----------YGSSEVQAlVALQPATDPVSVRIEggGRPAsPEARVRAR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 DVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 523
Cdd:PRK06164 365 DPQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLG-GFLVNPAE 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1832481686 524 IENIYMRSEPVAQVFVHGESLQ------AFLIAI--VVPDVETLCSWAQKR 566
Cdd:PRK06164 444 IEHALEALPGVAAAQVVGATRDgktvpvAFVIPTdgASPDEAGLMAACREA 494
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
119-541 |
1.06e-17 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 86.78 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 119 FAYSM--------VIVPLYDTLGNEAITYIVNKAELSLVFVDKpekAKLLLEGVEnKLIPGLKIIVVMDAYGSELVErgQ 190
Cdd:cd05970 85 FWYSLlalhklgaIAIPATHQLTAKDIVYRIESADIKMIVAIA---EDNIPEEIE-KAAPECPSKPKLVWVGDPVPE--G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 191 RCGVEVTSMKAMEDLGRanRRKPKPPAPEDLAVICFTSGTTGNPKgaMVTHRNIvsdcsafvkatentvnpcpddtlisf 270
Cdd:cd05970 159 WIDFRKLIKNASPDFER--PTANSYPCGEDILLVYFSSGTTGMPK--MVEHDFT-------------------------- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 271 LPLAHMFErvvecVMLCHGAKigffQGDIRLLMDDLKVLQPtvfpvvprllnrMFDRIFGQANTTLKRWLLDFasKRKEA 350
Cdd:cd05970 209 YPLGHIVT-----AKYWQNVR----EGGLHLTVADTGWGKA------------VWGKIYGQWIAGAAVFVYDY--DKFDP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 351 ELRSGIIRNN---------SLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAgCCLT 421
Cdd:cd05970 266 KALLEKLSKYgvttfcappTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTL-TIAT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 422 MPG-DWTAGHVGAPMPCNLIKLVDVEEMNYMAAEgEGEVCV---KGPNV--FQGYLKDPAKTAEALdKDGWLHTGDIGKW 495
Cdd:cd05970 345 FPWmEPKPGSMGKPAPGYEIDLIDREGRSCEAGE-EGEIVIrtsKGKPVglFGGYYKDAEKTAEVW-HDGYYHTGDAAWM 422
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1832481686 496 LPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:cd05970 423 DEDGYLWFVGRTDDLIK-SSGYRIGPFEVESALIQHPAVLECAVTG 467
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
98-541 |
1.73e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 85.99 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 98 DQFIGIFAQNRPEW--VIIEQGCFAysMVIVPLYDTLGNEAITYIVNKAELSLVFVDkPEKAKLLLEGVENklIPGLKII 175
Cdd:PRK05620 64 DQRVGSMMYNCAEHleVLFAVACMG--AVFNPLNKQLMNDQIVHIINHAEDEVIVAD-PRLAEQLGEILKE--CPCVRAV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 176 VVMDAYGSELVERGQRCGVEVTSMKAMEDlGRANRRkPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKA 254
Cdd:PRK05620 139 VFIGPSDADSAAAHMPEGIKVYSYEALLD-GRSTVY-DWPELDETTAAaICYSTGTTGAPKGVVYSHRSLYLQSLSLRTT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 255 TENTVNpcPDDTLISFLPLAHmfervvecvMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVprllnrmfdrifgqaNT 334
Cdd:PRK05620 217 DSLAVT--HGESFLCCVPIYH---------VLSWGVPLAAFMSGTPLVFPGPDLSAPTLAKII---------------AT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 335 TLKRwlldfaskrkeaeLRSGIirnNSLWDRLIFHKVQSSlGGRVRL--MVTGAAPVSATVLTFLRAALGCQFYEGYGQT 412
Cdd:PRK05620 271 AMPR-------------VAHGV---PTLWIQLMVHYLKNP-PERMSLqeIYVGGSAVPPILIKAWEERYGVDVVHVWGMT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 413 ECTAGCCLTMPGDWTAGHVGAP-------MPCNLIKLVdVEEMNYMAA--EGEGEVCVKGPNVFQGYLKDPAKT------ 477
Cdd:PRK05620 334 ETSPVGTVARPPSGVSGEARWAyrvsqgrFPASLEYRI-VNDGQVMEStdRNEGEIQVRGNWVTASYYHSPTEEgggaas 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832481686 478 ----------AEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:PRK05620 413 tfrgedvedaNDRFTADGWLRTGDVGSVTRDGFLTIHDRARDVIR-SGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
72-558 |
1.80e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 85.89 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKTAPDQFiGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:PRK07867 29 TSWREHIRGSAARAAALRARLDPTRPPHV-GVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPEKAklLLEGVEnkliPGLKIIVVMDAYGSELVergqrcgvevtsmkameDLGRANRRKPKPPAPEDLAVICFTSGTT 231
Cdd:PRK07867 108 ESAHAE--LLDGLD----PGVRVINVDSPAWADEL-----------------AAHRDAEPPFRVADPDDLFMLIFTSGTS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDTLISFLPLAHMFERVVE-CVMLCHGAKI---------GFfqgdirl 301
Cdd:PRK07867 165 GDPKAVRCTHRKVASAGVMLAQ----RFGLGPDDVCYVSMPLFHSNAVMAGwAVALAAGASIalrrkfsasGF------- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 302 lMDDLKVLQPTVFPVVPRLLNrmfdrifgqanttlkrWLLDFASKRKEAElrsgiirnNSLwdRLIFhkvqsslggrvrl 381
Cdd:PRK07867 234 -LPDVRRYGATYANYVGKPLS----------------YVLATPERPDDAD--------NPL--RIVY------------- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 382 mvtGAAPVSATVLTFlRAALGCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAPMPCnlIKLVDVE--------------E 447
Cdd:PRK07867 274 ---GNEGAPGDIARF-ARRFGCVVVDGFGSTE--GGVAITRTPDTPPGALGPLPPG--VAIVDPDtgtecppaedadgrL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 448 MNYMAAEGEgEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENI 527
Cdd:PRK07867 346 LNADEAIGE-LVNTAGPGGFEGYYNDPEADAERM-RGGVYWSGDLAYRDADGYAYFAGRLGDWMRV-DGENLGTAPIERI 422
|
490 500 510
....*....|....*....|....*....|.
gi 1832481686 528 YMRSEPVAQVFVHGeslqafliaivVPDVET 558
Cdd:PRK07867 423 LLRYPDATEVAVYA-----------VPDPVV 442
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
72-555 |
2.31e-17 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 85.40 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd17646 24 LTYRELDERANRLAHLLRARG--VGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPAVVLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPEKAKLllegvenklipglkiivvmdaygselvergqRCGVEVTSMKAMEDLGRANRRKPKPPAPEDLAVICFTSGTT 231
Cdd:cd17646 102 TADLAARL-------------------------------PAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVSD----CSAFVKATENTV---NPCPDDTLIS--FLPLAHMfERVVECVMLCHGaKIGFFQGdirlL 302
Cdd:cd17646 151 GRPKGVMVTHAGIVNRllwmQDEYPLGPGDRVlqkTPLSFDVSVWelFWPLVAG-ARLVVARPGGHR-DPAYLAA----L 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 303 MDDLKVlqpTVFPVVPRLLnrmfdRIFGQanttlkrwlldfaskrkeaELRSGIIRNnslwdrlifhkvqsslggrVRLM 382
Cdd:cd17646 225 IREHGV---TTCHFVPSML-----RVFLA-------------------EPAAGSCAS-------------------LRRV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 383 VTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGHV--GAPMPCNLIKLVDvEEMNYMAAEGEGEV 459
Cdd:cd17646 259 FCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHwPVRGPAETPSVpiGRPVPNTRLYVLD-DALRPVPVGVPGEL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 460 CVKGPNVFQGYLKDPAKTAEALDKDGWLH------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEP 533
Cdd:cd17646 338 YLGGVQLARGYLGRPALTAERFVPDPFGPgsrmyrTGDLARWRPDGALEFLGRSDDQVKI-RGFRVEPGEIEAALAAHPA 416
|
490 500
....*....|....*....|....*
gi 1832481686 534 VAQVFV---HGESLQAFLIAIVVPD 555
Cdd:cd17646 417 VTHAVVvarAAPAGAARLVGYVVPA 441
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
218-558 |
2.44e-17 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 85.05 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFErVVEcvM---LCHGAKIGF 294
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVL----ALFAATQRWFGFNEDDVWTLFHSYAFDFS-VWE--IwgaLLHGGRLVV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 295 FQGDIRLLMDDLkvlqptvfpvvPRLLNRMFDRIFGQANTTLKRWLldfaskrkEAELRsgiirnnslwdrliFHKVQSS 374
Cdd:cd17643 165 VPYEVARSPEDF-----------ARLLRDEGVTVLNQTPSAFYQLV--------EAADR--------------DGRDPLA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 375 LggrvRLMVTGAAPVSATVLTFLRAALGC---QFYEGYGQTECTAGCCL-----TMPGDWTAGHVGAPMPCNLIKLVDvE 446
Cdd:cd17643 212 L----RYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFrpldaADLPAAAASPIGRPLPGLRVYVLD-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 447 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-------ALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYI 519
Cdd:cd17643 287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAErfvanpfGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI-RGFRI 365
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1832481686 520 APEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVET 558
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVivrEDEPGDTRLVAYVVADDGA 407
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
218-566 |
2.91e-17 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 84.61 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVV-ECVM-LCHGAkigff 295
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG----PGSRVLQFASPS--FDASVwELLMaLLAGA----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 qgdiRLLMDDLKVLQPtvfpvvprllnrmfdrifGQAnttlkrwLLDFaskrkeaelrsgiirnnsLWDRLIFHKVQS-- 373
Cdd:cd17652 161 ----TLVLAPAEELLP------------------GEP-------LADL------------------LREHRITHVTLPpa 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 374 --------SLGGRVRLMVTGAAPVSATVLtflRAALGCQFYEGYGQTECTAgcCLTMPGDWTAGHV---GAPMPCNLIKL 442
Cdd:cd17652 194 alaalppdDLPDLRTLVVAGEACPAELVD---RWAPGRRMINAYGPTETTV--CATMAGPLPGGGVppiGRPVPGTRVYV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 443 VDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQ 515
Cdd:cd17652 269 LD-ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfgapgSRMYrTGDLARWRADGQLEFLGRADDQVKI-R 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 516 GEYIAPEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVV------PDVETLCSWAQKR 566
Cdd:cd17652 347 GFRIELGEVEAALTEHPGVAEavVVVRDDRPgDKRLVAYVVpapgaaPTAAELRAHLAER 406
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
101-589 |
6.63e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 84.30 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 101 IGIFAQNRPEwviIEQGCFAYSM---VIVPLYDTLGNEAITYIVNKAELSLVFVDKP-----EKAKLLLEGVENKLIPGL 172
Cdd:PLN03102 67 VSVLAPNTPA---MYEMHFAVPMagaVLNPINTRLDATSIAAILRHAKPKILFVDRSfeplaREVLHLLSSEDSNLNLPV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 173 KIIVVMD----AYGSE-----LVERGQRCGVEVTSMKAMEDlgranrrkpkppaPEDLAVICFTSGTTGNPKGAMVTHRN 243
Cdd:PLN03102 144 IFIHEIDfpkrPSSEEldyecLIQRGEPTPSLVARMFRIQD-------------EHDPISLNYTSGTTADPKGVVISHRG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 244 I-VSDCSAFVKATENTvnpCPddTLISFLPLAHmfervvecvmlCHGAKIGF---FQGDIRLLMDdlKVLQPTVFPVVpr 319
Cdd:PLN03102 211 AyLSTLSAIIGWEMGT---CP--VYLWTLPMFH-----------CNGWTFTWgtaARGGTSVCMR--HVTAPEIYKNI-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 320 llnRMFDRIFGQANTTLKRWLLdfaskrkeaelrsgiiRNNSLwdrlifhkVQSSLGGRVRLMVTGAAPVSATVLTFLRa 399
Cdd:PLN03102 271 ---EMHNVTHMCCVPTVFNILL----------------KGNSL--------DLSPRSGPVHVLTGGSPPPAALVKKVQR- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 400 aLGCQFYEGYGQTECTAGCCLTMPGD-WT------AGHVGAPMPCNLIKLVDVEEMNYMAAEGE-------GEVCVKGPN 465
Cdd:PLN03102 323 -LGFQVMHAYGLTEATGPVLFCEWQDeWNrlpenqQMELKARQGVSILGLADVDVKNKETQESVprdgktmGEIVIKGSS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 466 VFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIymrsepvaqVFVHGESLQ 545
Cdd:PLN03102 402 IMKGYLKNPKATSEAF-KHGWLNTGDVGVIHPDGHVEIKDRSKDII-ISGGENISSVEVENV---------LYKYPKVLE 470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1832481686 546 AFLIAIVVPDV-ETLCSW-AQKRGFEGSFEE----LCRNKDVKKAILEDM 589
Cdd:PLN03102 471 TAVVAMPHPTWgETPCAFvVLEKGETTKEDRvdklVTRERDLIEYCRENL 520
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
217-554 |
1.91e-16 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341304 [Multi-domain] Cd Length: 450 Bit Score: 82.42 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAkigf 294
Cdd:cd17649 92 HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT----PGDRELQFASFN--FDGAHEQLLppLICGA---- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 295 fqgdiRLLMDDLKVLQPtvfpvvPRLLNRMFDR----IFGQANTTLKRWLLDFASkrkeaelrsgiirnnslwdrlifhk 370
Cdd:cd17649 162 -----CVVLRPDELWAS------ADELAEMVRElgvtVLDLPPAYLQQLAEEADR------------------------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 371 VQSSLGGRVRLMVTGAAPVSAtvlTFLRAALGC--QFYEGYGQTEC--TAGCCLTMPGDWTAGH---VGAPMPCNLIKLV 443
Cdd:cd17649 206 TGDGRPPSLRLYIFGGEALSP---ELLRRWLKApvRLFNAYGPTEAtvTPLVWKCEAGAARAGAsmpIGRPLGGRSAYIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 DvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL--DKDG-----WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQG 516
Cdd:cd17649 283 D-ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFvpDPFGapgsrLYRTGDLARWRDDGVIEYLGRVDHQVKI-RG 360
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1832481686 517 EYIAPEKIENIYMRSEPVAQVFVHGES--LQAFLIAIVVP 554
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVALDgaGGKQLVAYVVL 400
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
220-550 |
3.48e-16 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 81.61 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRnivsDCSAFVKATENTVNPCPDDTLISFLPLAHMFerVVEC-----VMLChGAKIGF 294
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHN----DYAYNVRASAEVCGLDQDTVYLAVLPAAHNF--PLACpgvlgTLLA-GGRVVL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 295 FQ----GDIRLLMDDLKVlqpTVFPVVPRLLnrmfdrifgqanttlKRWLlDFASKRKEAElrsgiirnnslwdrlifhk 370
Cdd:cd05920 213 APdpspDAAFPLIEREGV---TVTALVPALV---------------SLWL-DAAASRRADL------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 371 vqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTM---PGDWTAGHVGAPM-PCNLIKLVDv 445
Cdd:cd05920 255 --SSL----RLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE---GlLNYTRlddPDEVIIHTQGRPMsPDDEIRVVD- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 446 EEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIE 525
Cdd:cd05920 325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGFYRTGDLVRRTPDGYLVVEGRIKDQINRG-GEKIAAEEVE 403
|
330 340 350
....*....|....*....|....*....|..
gi 1832481686 526 NIYMRSEPVAQVFV-------HGESLQAFLIA 550
Cdd:cd05920 404 NLLLRHPAVHDAAVvampdelLGERSCAFVVL 435
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
72-541 |
2.73e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 79.16 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPL-YDTLGNEaITYIVNKAELSLVF 150
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLG--PGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnYRYVEDE-LRYLLDDSDAVALV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 151 VDK---PEKAKLLLEgvenklIPGLKIIVVMDAYGSELVERGqrcGVEVTSMKAMEDLGRAnrrkPKPPAPEDLAVICfT 227
Cdd:PRK07798 106 YERefaPRVAEVLPR------LPKLRTLVVVEDGSGNDLLPG---AVDYEDALAAGSPERD----FGERSPDDLYLLY-T 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 228 SGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAK-----IGFFQGdirll 302
Cdd:PRK07798 172 GGTTGMPKGVMWRQEDIFR--VLLGGRDFATGEPIEDEEELAKRAAAGPGMRRFPAPPLMHGAGqwaafAALFSG----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 303 mddlkvlQPTVFPVVPRL-------------LNRMFdrIFGQAnttLKRWLLDFASKRKEAELrsgiirnnslwdrlifh 369
Cdd:PRK07798 245 -------QTVVLLPDVRFdadevwrtierekVNVIT--IVGDA---MARPLLDALEARGPYDL----------------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 370 kvqSSLggrvRLMVTGAAPVSATVLTFLRAAL-GCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAP--MPCNLIKLVDVE 446
Cdd:PRK07798 296 ---SSL----FAIASGGALFSPSVKEALLELLpNVVLTDSIGSSE--TGFGGSGTVAKGAVHTGGPrfTIGPRTVVLDED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 447 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 523
Cdd:PRK07798 367 GNPVEPGSGEIGWIARRGHIPLGYYKDPEKTAETFpTIDGvrYAIPGDRARVEADGTITLLGRGSVCINTG-GEKVFPEE 445
|
490
....*....|....*....
gi 1832481686 524 IENIyMRSEP-VAQVFVHG 541
Cdd:PRK07798 446 VEEA-LKAHPdVADALVVG 463
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
185-538 |
4.26e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 78.40 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 185 LVERGQRCGvevTSMKAMEDLGRANRRKPKPPA---PEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNP 261
Cdd:PRK09274 140 LVTVGGRLL---WGGTTLATLLRDGAAAPFPMAdlaPDDMAAILFTSGSTGTPKGVVYTHGMFE----AQIEALREDYGI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 262 CPDDTLISFLPLahmfervvecvMLCHGAKIGFfqGDIRLLMDDLKVLQptvfpVVPRllnRMFDRIFGQANTTLkrwll 341
Cdd:PRK09274 213 EPGEIDLPTFPL-----------FALFGPALGM--TSVIPDMDPTRPAT-----VDPA---KLFAAIERYGVTNL----- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 342 dFASKrkeaelrsgiirnnSLWDRLIFHKVQS--SLGGrVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTEC--- 414
Cdd:PRK09274 267 -FGSP--------------ALLERLGRYGEANgiKLPS-LRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpi 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 415 ---TAGCCLTMPGDWT---AGH-VGAPMPCNLIKLVDVEEM-------NYMAAEGE-GEVCVKGPNVFQGYLKDPAKTAE 479
Cdd:PRK09274 331 ssiESREILFATRAATdngAGIcVGRPVDGVEVRIIAISDApipewddALRLATGEiGEIVVAGPMVTRSYYNRPEATRL 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832481686 480 A--LDKDG--WLHTGDIGkWL-PNGTLKIIDRKKHIFKLAQGEYIapekieniymrSEPVAQVF 538
Cdd:PRK09274 411 AkiPDGQGdvWHRMGDLG-YLdAQGRLWFCGRKAHRVETAGGTLY-----------TIPCERIF 462
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
218-565 |
4.97e-15 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 77.59 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpDDTLI--SFLPLAHMFErvvecvMLCH---GAKI 292
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPA---DKSLVyaSFSFDASAWE------IFPHltaGAAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 GFFQGDIRLLMDDLkvlqptvfpvvprllnrmfDRIFGQANTTLKRWLLDFASKRKEAElrsgiirNNSLwdrlifhkvq 372
Cdd:cd17645 174 HVVPSERRLDLDAL-------------------NDYFNQEGITISFLPTGAAEQFMQLD-------NQSL---------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 sslggrvRLMVTGAAPVSATVLTflraalGCQFYEGYGQTECTAgCCLTMPGDWTAGHVGAPMPCNLIKLVDVEEMNYMA 452
Cdd:cd17645 218 -------RVLLTGGDKLKKIERK------GYKLVNNYGPTENTV-VATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 453 AEG-EGEVCVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIE 525
Cdd:cd17645 284 PIGvAGELCIAGEGLARGYLNRPELTAEKFIVHPFVpgermyRTGDLAKFLPDGNIEFLGRLDQQVKI-RGYRIEPGEIE 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1832481686 526 NIYMRSEPVAQVFV-------HGESLQAFLIAIVVPDVETLCSWAQK 565
Cdd:cd17645 363 PFLMNHPLIELAAVlakedadGRKYLVAYVTAPEEIPHEELREWLKN 409
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
217-554 |
1.75e-14 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 75.98 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKateNTVNPCPDDTLISFLPLAHMFER-VVECVMLCHGAKIGFF 295
Cdd:cd05958 95 ASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAV---NVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 QGDI-RLLMDDLKVLQPTVFPVVPRLLNRMfdrifgqanttlkrwlldFASKRKEAELRSGiirnnslwdrlifhkvqss 374
Cdd:cd05958 172 EEATpDLLLSAIARYKPTVLFTAPTAYRAM------------------LAHPDAAGPDLSS------------------- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 375 lggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAE 454
Cdd:cd05958 215 ----LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVD-DEGNPVPDG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 455 GEGEVCVKGPNvfqGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPV 534
Cdd:cd05958 290 TIGRLAVRGPT---GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDMIVSG-GYNIAPPEVEDVLLQHPAV 365
|
330 340
....*....|....*....|...
gi 1832481686 535 AQVFVHGESLQAFLI---AIVVP 554
Cdd:cd05958 366 AECAVVGHPDESRGVvvkAFVVL 388
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
218-529 |
1.86e-14 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 76.39 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAtentVNPCPDDTLISFLPLAHMFervvecvmlchgakiGFFQG 297
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKF----FSPKEDDVMMSFLPPFHAY---------------GFNSC 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 298 DIRLLMDDLkvlqPTVF---PVVPRLLNRMFDR----IFGQANTTLKrWLLDFASKRKEA--ELRSGIIRNNSLWDRLiF 368
Cdd:PRK06334 243 TLFPLLSGV----PVVFaynPLYPKKIVEMIDEakvtFLGSTPVFFD-YILKTAKKQESClpSLRFVVIGGDAFKDSL-Y 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 369 HKVQSslggrvrlmvtgaapvsatvlTFLRAALgcqfYEGYGQTECTAgcCLTMPGDWTAGH---VGAPMPCNLIKLVDv 445
Cdd:PRK06334 317 QEALK---------------------TFPHIQL----RQGYGTTECSP--VITINTVNSPKHescVGMPIRGMDVLIVS- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 446 EEMNYMAAEGE-GEVCVKGPNVFQGYL-KDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEK 523
Cdd:PRK06334 369 EETKVPVSSGEtGLVLTRGTSLFSGYLgEDFGQGFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIG-AEMVSLEA 447
|
....*.
gi 1832481686 524 IENIYM 529
Cdd:PRK06334 448 LESILM 453
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
408-564 |
2.05e-14 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 74.65 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 408 GYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAeGE-GEVCVKGPNVFQGYLKDPAKTAEALdKDGW 486
Cdd:cd17636 142 GYGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILD-EDGREVPD-GEvGEIVARGPTVMAGYWNRPEVNARRT-RGGW 218
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832481686 487 LHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIyMRSEP-VAQVFVhgeslqafliaIVVPDVetlcSWAQ 564
Cdd:cd17636 219 HHTNDLGRREPDGSLSFVGPKTRMIKSG-AENIYPAEVERC-LRQHPaVADAAV-----------IGVPDP----RWAQ 280
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
72-555 |
2.24e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 75.82 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVG--PESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DkpekaklllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICFTSGTT 231
Cdd:cd12115 103 D-----------------------------------------------------------------PDDLAYVIYTSGST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVsdcsAFVKATENTvnpCPDD--------TLISF-LPLAHMFervvecVMLCHGAKIgffqgdirll 302
Cdd:cd12115 118 GRPKGVAIEHRNAA----AFLQWAAAA---FSAEelagvlasTSICFdLSVFELF------GPLATGGKV---------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 303 mddlkVLQPTVFPvvprllnrmfdrifgqanttlkrwLLDFASkRKEAELrsgIIRNNSLWDRLIFHkvqSSLGGRVRLM 382
Cdd:cd12115 175 -----VLADNVLA------------------------LPDLPA-AAEVTL---INTVPSAAAELLRH---DALPASVRVV 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 383 VTGAAPVSATVLTFLRAAL-GCQFYEGYGQTECT--AGCCLTMPGDWTAGHVGAPMPCNLIKLVDvEEMNYMAAEGEGEV 459
Cdd:cd12115 219 NLAGEPLPRDLVQRLYARLqVERVVNLYGPSEDTtySTVAPVPPGASGEVSIGRPLANTQAYVLD-RALQPVPLGVPGEL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 460 CVKGPNVFQGYLKDPAKTAEALDKDGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEP 533
Cdd:cd12115 298 YIGGAGVARGYLGRPGLTAERFLPDPFGpgarlyRTGDLVRWRPDGLLEFLGRADNQVKV-RGFRIELGEIEAALRSIPG 376
|
490 500
....*....|....*....|....*
gi 1832481686 534 VAQ--VFVHGESL-QAFLIAIVVPD 555
Cdd:cd12115 377 VREavVVAIGDAAgERRLVAYIVAE 401
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
218-568 |
2.30e-14 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 75.93 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpdDTLISFLPLAhmFERVVE--CVMLCHGAKIgff 295
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSS----DRVLQFASIA--FDVAAEeiYVTLLSGATL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 qgdirllmddlkVLQPtvfpvvprllNRMFdrifgqanttlkRWLLDFASKRKEAELRSGIIrNNSLWDRLIFHKVQSSL 375
Cdd:cd17644 176 ------------VLRP----------EEMR------------SSLEDFVQYIQQWQLTVLSL-PPAYWHLLVLELLLSTI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 376 GG--RVRLMVTGAAPVSATVLTFLRAALG--CQFYEGYGQTECTAGCCLTMPGDWTAGH-----VGAPMPCNLIKLVDvE 446
Cdd:cd17644 221 DLpsSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIAATVCRLTQLTERNitsvpIGRPIANTQVYILD-E 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 447 EMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH--------TGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 518
Cdd:cd17644 300 NLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseserlykTGDLARYLPDGNIEYLGRIDNQVKI-RGFR 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832481686 519 IAPEKIENIYMRSEPVAQVFV---HGESLQAFLIAIVVPDVETLCSWAQKRGF 568
Cdd:cd17644 379 IELGEIEAVLSQHNDVKTAVVivrEDQPGNKRLVAYIVPHYEESPSTVELRQF 431
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
135-609 |
2.75e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 75.90 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 135 EAITYIVNKAELSLVFVD---KPekaklLLEGVENKLiPGLKIIVVM-DAygselvergQRCGVEVTSMKAMEDL-GRAN 209
Cdd:PRK07008 101 EQIAYIVNHAEDRYVLFDltfLP-----LVDALAPQC-PNVKGWVAMtDA---------AHLPAGSTPLLCYETLvGAQD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 210 RRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPCPDDTLisfLPLAHMFErvVECVMLCH 288
Cdd:PRK07008 166 GDYDWPRFDENQASsLCYTSGTTGNPKGALYSHRSTV--LHAYGAALPDAMGLSARDAV---LPVVPMFH--VNAWGLPY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 289 -----GAKIgffqgdirllmddlkvlqptVFPvvprllnrmfdrifGQAnttlkrwlLDFASKRK--EAELRSGIIRNNS 361
Cdd:PRK07008 239 sapltGAKL--------------------VLP--------------GPD--------LDGKSLYEliEAERVTFSAGVPT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 362 LWDRLIFHKVQSSLG-GRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECT---AGCCLT-----MPGD------W 426
Cdd:PRK07008 277 VWLGLLNHMREAGLRfSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSplgTLCKLKwkhsqLPLDeqrkllE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 427 TAGHV--GAPMpcnliKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDkDGWLHTGDIGKWLPNGTLK 502
Cdd:PRK07008 357 KQGRViyGVDM-----KIVG-DDGRELPWDGKafGDLQVRGPWVIDRYFR---GDASPLV-DGWFPTGDVATIDADGFMQ 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 503 IIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAqvfvhgeslQAFLIAIVVP--DVETLCSWAQKRGFEGSFEELCRNKD 580
Cdd:PRK07008 427 ITDRSKDVIK-SGGEWISSIDIENVAVAHPAVA---------EAACIACAHPkwDERPLLVVVKRPGAEVTREELLAFYE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1832481686 581 VKKA---ILEDMVRL--------GKDSGLKPFEQVKGITL 609
Cdd:PRK07008 497 GKVAkwwIPDDVVFVdaiphtatGKLQKLKLREQFRDYVL 536
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
215-559 |
3.51e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 215 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAhmFERVVECVM--LCHGAki 292
Cdd:PRK12316 4690 RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELT----PDDRVLQFMSFS--FDGSHEGLYhpLINGA-- 4761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 gffqgdiRLLMDDLKVLQPtvfpvvprllNRMFDRIFGQANTTlkrwlLDFASkrkeaelrsgiirnnSLWDRLIFHKVQ 372
Cdd:PRK12316 4762 -------SVVIRDDSLWDP----------ERLYAEIHEHRVTV-----LVFPP---------------VYLQQLAEHAER 4804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 SSLGGRVRLMVTG--AAPVSATVLTFlRAALGCQFYEGYGQTECTAG-CCLTMPGDWTAG----HVGAPMPCNLIKLVDV 445
Cdd:PRK12316 4805 DGEPPSLRVYCFGgeAVAQASYDLAW-RALKPVYLFNGYGPTETTVTvLLWKARDGDACGaaymPIGTPLGNRSGYVLDG 4883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 446 eEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEY 518
Cdd:PRK12316 4884 -QLNPLPVGVAGELYLGGEGVARGYLERPALTAErfvpdPFGAPGgrLYRTGDLARYRADGVIDYLGRVDHQVKI-RGFR 4961
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1832481686 519 IAPEKIEnIYMRSEP-------VAQVFVHGeslqAFLIAIVVPDVETL 559
Cdd:PRK12316 4962 IELGEIE-ARLREHPavreavvIAQEGAVG----KQLVGYVVPQDPAL 5004
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
219-549 |
1.25e-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: 73.65 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 219 EDLAVICFTSGTTGNPKgaMVTHrnivSDCSAFVKA----------TENTVNPCPDDTLISFLPLAHMFERVVE--CVML 286
Cdd:cd05928 174 QEPMAIYFTSGTTGSPK--MAEH----SHSSLGLGLkvngrywldlTASDIMWNTSDTGWIKSAWSSLFEPWIQgaCVFV 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 287 CHGAKIgffqgDIRLLMDDLKVLQPTVFPVVPrllnrmfdrifgqantTLKRWLL--DFASkrkeaelrsgiirnnslwd 364
Cdd:cd05928 248 HHLPRF-----DPLVILKTLSSYPITTFCGAP----------------TVYRMLVqqDLSS------------------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 365 rlifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG-DWTAGHVGAPMPCNLIKLV 443
Cdd:cd05928 288 ----YKFPS-----LQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE-TGLICANFKGmKIKPGSMGKASPPYDVQII 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 DvEEMNYMAAEGEGEVCVK-GPN----VFQGYLKDPAKTAEALDKDGWLhTGDIGKWLPNGTLKIIDRKKHIFkLAQGEY 518
Cdd:cd05928 358 D-DNGNVLPPGTEGDIGIRvKPIrpfgLFSGYVDNPEKTAATIRGDFYL-TGDRGIMDEDGYFWFMGRADDVI-NSSGYR 434
|
330 340 350
....*....|....*....|....*....|....*...
gi 1832481686 519 IAPEKIENIYMRSEPVAQVFV-------HGESLQAFLI 549
Cdd:cd05928 435 IGPFEVESALIEHPAVVESAVvsspdpiRGEVVKAFVV 472
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
215-557 |
1.67e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.98 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 215 PPAPEDLAVICFTSGTTGNPKGAMVTHRNI------VSDCSAFvkatenTVNpcpDDTLISfLPLAHmfervvecV---- 284
Cdd:PRK09029 131 AWQPQRLATMTLTSGSTGLPKAAVHTAQAHlasaegVLSLMPF------TAQ---DSWLLS-LPLFH--------Vsgqg 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 285 ----MLCHGAKIGFfqGDIRLLMDDLkvLQPTVFPVVPRLLNRMFDRifGQANTTLKRWLLdfaskrkeaelrsgiirnn 360
Cdd:PRK09029 193 ivwrWLYAGATLVV--RDKQPLEQAL--AGCTHASLVPTQLWRLLDN--RSEPLSLKAVLL------------------- 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 361 slwdrlifhkvqsslGGrvrlmvtGAAPVSatvLTFLRAALGCQFYEGYGQTECTAGCClTMPGDWTAGhVGAPMPCNLI 440
Cdd:PRK09029 248 ---------------GG-------AAIPVE---LTEQAEQQGIRCWCGYGLTEMASTVC-AKRADGLAG-VGSPLPGREV 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 441 KLVDveemnymaaegeGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLpNGTLKIIDRKKHIFkLAQGEYIA 520
Cdd:PRK09029 301 KLVD------------GEIWLRGASLALGYWRQ-GQLVPLVNDEGWFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQ 365
|
330 340 350
....*....|....*....|....*....|....*..
gi 1832481686 521 PEKIENIYMRSEPVAQVFVhgeslqafliaIVVPDVE 557
Cdd:PRK09029 366 PEEIERVINQHPLVQQVFV-----------VPVADAE 391
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
203-555 |
2.96e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 72.77 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 203 EDLGRANRRKPKPPAPEDLAVIC---FTSGTTGNPKGAMVTHRNIvsdcsAFVkATENTVNPCPD----DTLISFLPLAH 275
Cdd:PRK07470 144 EALVARHLGARVANAAVDHDDPCwffFTSGTTGRPKAAVLTHGQM-----AFV-ITNHLADLMPGtteqDASLVVAPLSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 276 MfERVVECVMLCHGAKigffqgDIRLLMDDLKVlqPTVFPVVPRL-LNRMFdrifgQANTTLKRWLLDFASKRKEaelrs 354
Cdd:PRK07470 218 G-AGIHQLCQVARGAA------TVLLPSERFDP--AEVWALVERHrVTNLF-----TVPTILKMLVEHPAVDRYD----- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 355 giirnnslwdrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTaGC------CLTMPGDWTA 428
Cdd:PRK07470 279 -----------------HSSL----RYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVT-GNitvlppALHDAEDGPD 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 429 GHVGapmPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLK 502
Cdd:PRK07470 337 ARIG---TCGFertgmeVQIQD-DEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF-RDGWFRTGDLGHLDARGFLY 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1832481686 503 IIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPD 555
Cdd:PRK07470 412 ITGRASDMY-ISGGSNVYPREIEEKLLTHPAVSEVAVLG-----------VPD 452
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
216-590 |
5.37e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 72.89 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 216 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAhmFERVVECVM--LCHGAKIG 293
Cdd:PRK12467 1715 LAPQNLAYVIYTSGSTGRPKGAGNRHGALV----NRLCATQEAYQLSAADVVLQFTSFA--FDVSVWELFwpLINGARLV 1788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 294 FFQGDIRL----LMDDLKVLQPTVFPVVPRLLNRmfdrifgqanttlkrwLLDFAskrkEAELRSGIIRnnslwdRLIFh 369
Cdd:PRK12467 1789 IAPPGAHRdpeqLIQLIERQQVTTLHFVPSMLQQ----------------LLQMD----EQVEHPLSLR------RVVC- 1841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 370 kvqsslGGRvrlmvtgAAPVSATVLTFlrAALG-CQFYEGYGQTECTAG-----CCLTMPGDWTAGHVGAPMPcNLIKLV 443
Cdd:PRK12467 1842 ------GGE-------ALEVEALRPWL--ERLPdTGLFNLYGPTETAVDvthwtCRRKDLEGRDSVPIGQPIA-NLSTYI 1905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 DVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL------DKDGWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQG 516
Cdd:PRK12467 1906 LDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFvadpfgTVGSRLYrTGDLARYRADGVIEYLGRIDHQVKI-RG 1984
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832481686 517 EYIAPEKIENIYMRSEPVAQ--VFVHGESLQAFLIAIVVPDVETLCSWAQKRGfeGSFEELcrnKDVKKAILED-MV 590
Cdd:PRK12467 1985 FRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDEAQV--ALRAIL---KNHLKASLPEyMV 2056
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
216-538 |
5.66e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 71.34 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 216 PAPEDLAVICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAHMFervvecvmlchGAKIGff 295
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFA----AQIDALRQLYGIRPGEVDLATFPLFALF-----------GPALG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 qgdirllmddLKVLQPTVFPVVPrllnrmfdrifGQANttlKRWLLDFASKRKEaelrSGIIRNNSLWDRLIFHKVQSSL 375
Cdd:cd05910 145 ----------LTSVIPDMDPTRP-----------ARAD---PQKLVGAIRQYGV----SIVFGSPALLERVARYCAQHGI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 376 G-GRVRLMVTGAAPVSATVLTFLRAAL--GCQFYEGYGQTECTAGCC------LTMPGDWTAGH----VGAPMPCNLIKL 442
Cdd:cd05910 197 TlPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSSigsrelLATTTAATSGGagtcVGRPIPGVRVRI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 443 VDVEEMNYMAAEGE--------GEVCVKGPNVFQGYLKDPAKTAEALDKDG----WLHTGDIGKWLPNGTLKIIDRKKHI 510
Cdd:cd05910 277 IEIDDEPIAEWDDTlelprgeiGEITVTGPTVTPTYVNRPVATALAKIDDNsegfWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
330 340
....*....|....*....|....*...
gi 1832481686 511 FKLAQGEYIapekieniymrSEPVAQVF 538
Cdd:cd05910 357 VITTGGTLY-----------TEPVERVF 373
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
361-539 |
1.10e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 70.29 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 361 SLWdRLIFHKVQSSLGGRVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLI 440
Cdd:cd05974 185 TVW-RMLIQQDLASFDVKLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRV 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 441 KLVDVEEmnymAAEGEGEVCV-----KGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKlAQ 515
Cdd:cd05974 264 ALLDPDG----APATEGEVALdlgdtRPVGLMKGYAGDPDKTAHAM-RGGYYRTGDIAMRDEDGYLTYVGRADDVFK-SS 337
|
170 180
....*....|....*....|....
gi 1832481686 516 GEYIAPEKIENIYMRSEPVAQVFV 539
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAEAAV 361
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
212-537 |
1.56e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 212 KPKPPAPEDLAVIcFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPDDTLISFLPLAHM--FERVVECVMlcHG 289
Cdd:PRK05857 163 NADQGSEDPLAMI-FTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIggLWWILTCLM--HG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 290 AKI---GFFQGDIRLLMDDLKVLQPTVfpvVPRLLNRMFdrifgqanttlkrwlldfaskrkeAELRSGIIRNNSLwdrl 366
Cdd:PRK05857 240 GLCvtgGENTTSLLEILTTNAVATTCL---VPTLLSKLV------------------------SELKSANATVPSL---- 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 367 ifhkvqsslggrvRLMVTGAAPVSATVLTFLRAA--LGCQFYeGYGQTECTAGCCLTMPGDWT---AGHVGAPMPCNLIK 441
Cdd:PRK05857 289 -------------RLVGYGGSRAIAADVRFIEATgvRTAQVY-GLSETGCTALCLPTDDGSIVkieAGAVGRPYPGVDVY 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 442 LVDVEEMNYMAAEGE-----GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQG 516
Cdd:PRK05857 355 LAATDGIGPTAPGAGpsasfGTLWIKSPANMLGYWNNPERTAEVL-IDGWVNTGDLLERREDGFFYIKGRSSEMI-ICGG 432
|
330 340
....*....|....*....|.
gi 1832481686 517 EYIAPEKIENIymrSEPVAQV 537
Cdd:PRK05857 433 VNIAPDEVDRI---AEGVSGV 450
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
201-554 |
1.69e-12 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 70.10 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 201 AMEDLGRANRRKPKPPAPEDLA--VICFTSGTTGNPKGAMVTHrnivsDCsafvkatentvNPCPDDTLISF-LPLAHMF 277
Cdd:cd05929 105 GLEDYEAAEGGSPETPIEDEAAgwKMLYSGGTTGRPKGIKRGL-----PG-----------GPPDNDTLMAAaLGFGPGA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 278 ERVVECVM-LCHGAKIGFFQGDIRL-----LM---DDLKVLQP------TVFPVVPRLLNRMfdrifgqanttLK----- 337
Cdd:cd05929 169 DSVYLSPApLYHAAPFRWSMTALFMggtlvLMekfDPEEFLRLieryrvTFAQFVPTMFVRL-----------LKlpeav 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 338 RWLLDFASkrkeaeLRSgiirnnslwdrlIFHkvqsslggrvrlmvtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAG 417
Cdd:cd05929 238 RNAYDLSS------LKR------------VIH---------------AAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQGL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 418 CCLTmPGDWTA--GHVGAPMPCNLiKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDGWLHTGDIGKW 495
Cdd:cd05929 285 TIIN-GEEWLThpGSVGRAVLGKV-HILD-EDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWSTLGDVGYL 360
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832481686 496 LPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVP 554
Cdd:cd05929 361 DEDGYLYLTDRRSDMI-ISGGVNIYPQEIENALIAHPKVLDAAVVGvpdEELGQRVHAVVQP 421
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
72-549 |
1.83e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 69.85 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtAPDQFIGIFAQNrPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd05973 1 LTFGELRALSARFANALQELGVG-PGDVVAGLLPRT-PELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 DKPEKAKLllegvenklipglkiivvmdaygselvergqrcgvevtsmkamedlgranrrkpkppaPEDLAVICFTSGTT 231
Cdd:cd05973 79 DAANRHKL----------------------------------------------------------DSDPFVMMFTSGTT 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 232 GNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDtliSFLPLAH------MFERVVECVMLCHGAKI---GFFQGDIRLL 302
Cdd:cd05973 101 GLPKGVPVPLRALA----AFGAYLRDAVDLRPED---SFWNAADpgwaygLYYAITGPLALGHPTILlegGFSVESTWRV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 303 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkeaeLRSGIirnnslwdrlifhKVQSSLGGRVRLM 382
Cdd:cd05973 174 IERLGVTNLAGSPTAYRLL------------------------------MAAGA-------------EVPARPKGRLRRV 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 383 VTGAAPVSATVLTFLRAALGCQFYEGYGQTEctagccLTMP--GDWTAGHV------GAPMP---CNLIKLVDVEemnym 451
Cdd:cd05973 211 SSAGEPLTPEVIRWFDAALGVPIHDHYGQTE------LGMVlaNHHALEHPvhagsaGRAMPgwrVAVLDDDGDE----- 279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 452 AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEAldkdGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIEN 526
Cdd:cd05973 280 LGPGEpGRLAIDIANSplmwFRGYQLPDTPAIDG----GYYLTGDTVEFDPDGSFSFIGRADDVITMS-GYRIGPFDVES 354
|
490 500 510
....*....|....*....|....*....|
gi 1832481686 527 IYMRSEPVAQVFV-------HGESLQAFLI 549
Cdd:cd05973 355 ALIEHPAVAEAAVigvpdpeRTEVVKAFVV 384
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-536 |
3.61e-12 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 70.20 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNrPEWVIIEQGCFaYSMVI-VPLYDTLGN-----EAITYIVNKAE 145
Cdd:PRK05691 41 LSYRDLDLRARTIAAALQARA--SFGDRAVLLFPSG-PDYVAAFFGCL-YAGVIaVPAYPPESArrhhqERLLSIIADAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 146 LSLVFVDkpekAKLL--LEGVENKLIPGLKIIVVMDAYGSELVERGQrcgvevtsmkamedlgranrrKPKPPaPEDLAV 223
Cdd:PRK05691 117 PRLLLTV----ADLRdsLLQMEELAAANAPELLCVDTLDPALAEAWQ---------------------EPALQ-PDDIAF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 224 ICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcPDDTLISFLPLAHmfervvecvmlchgaKIGFFQGdirllm 303
Cdd:PRK05691 171 LQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLN--PDDVIVSWLPLYH---------------DMGLIGG------ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 304 ddlkVLQPtVFPVVPRLLnrMFDRIFGQANTtlkRWLldfaskrkEA--ELRSGIIRNNSLWDRLIFHKV-QSSLGG--- 377
Cdd:PRK05691 228 ----LLQP-IFSGVPCVL--MSPAYFLERPL---RWL--------EAisEYGGTISGGPDFAYRLCSERVsESALERldl 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 378 -RVRLMVTGAAPVSATVL-TFLRAALGC-----QFYEGYGQTECT---AGC-------CLTMPGDWTAGHV--------- 431
Cdd:PRK05691 290 sRWRVAYSGSEPIRQDSLeRFAEKFAACgfdpdSFFASYGLAEATlfvSGGrrgqgipALELDAEALARNRaepgtgsvl 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 432 ---GAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEA-LDKDG--WLHTGDIGkWLPNGTLKIID 505
Cdd:PRK05691 370 mscGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTfVEHDGrtWLRTGDLG-FLRDGELFVTG 448
|
490 500 510
....*....|....*....|....*....|.
gi 1832481686 506 RKKHIFkLAQGEYIAPEKIENIYMRSEPVAQ 536
Cdd:PRK05691 449 RLKDML-IVRGHNLYPQDIEKTVEREVEVVR 478
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
63-541 |
5.33e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.56 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 63 RKPDQPY-------EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNE 135
Cdd:PRK13391 9 TTPDKPAvimastgEVVTYRELDERSNRLAHLFRSLGLK--RGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 136 AITYIVNKAELSLVF--VDKPEKAKLLLegvenKLIPGLKIIVVMDAYGSelvergqrcgvevtsMKAMEDLGRANRRKP 213
Cdd:PRK13391 87 EAAYIVDDSGARALItsAAKLDVARALL-----KQCPGVRHRLVLDGDGE---------------LEGFVGYAEAVAGLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 214 KPPAPEDL--AVICFTSGTTGNPKGamvthrnivsdcsafVKAtentvnPCPDDTLISFLPLAHMFERVV----ECVMLC 287
Cdd:PRK13391 147 ATPIADESlgTDMLYSSGTTGRPKG---------------IKR------PLPEQPPDTPLPLTAFLQRLWgfrsDMVYLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 288 -----HGAKIGFFQGDIRL-----LMDD------LKVLQP---TVFPVVPRllnrMFDRIFGQANTTLKRWLLdfaskrk 348
Cdd:PRK13391 206 paplyHSAPQRAVMLVIRLggtviVMEHfdaeqyLALIEEygvTHTQLVPT----MFSRMLKLPEEVRDKYDL------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 349 eaelrsgiirnnslwdrlifhkvqSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDWTA 428
Cdd:PRK13391 275 ------------------------SSL----EVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATE-GLGFTACDSEEWLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 429 --GHVGAPMpCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQgYLKDPAKTAEALDKDG-WLHTGDIGKWLPNGTLKIID 505
Cdd:PRK13391 326 hpGTVGRAM-FGDLHILD-DDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDGtWSTVGDIGYVDEDGYLYLTD 402
|
490 500 510
....*....|....*....|....*....|....*.
gi 1832481686 506 RKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:PRK13391 403 RAAFMI-ISGGVNIYPQEAENLLITHPKVADAAVFG 437
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
379-548 |
5.87e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 68.72 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 379 VRLMVTGAAPvSATVLtFLRAALGCQFYEGYGQTEcTAG---CCLTMPgDW------TAGHVGAPMPCNLIKL-----VD 444
Cdd:PLN02479 313 VHVMTAGAAP-PPSVL-FAMSEKGFRVTHTYGLSE-TYGpstVCAWKP-EWdslppeEQARLNARQGVRYIGLegldvVD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 445 VEEMNYMAAEGE--GEVCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPE 522
Cdd:PLN02479 389 TKTMKPVPADGKtmGEIVMRGNMVMKGYLKNPKANEEAF-ANGWFHSGDLGVKHPDGYIEIKDRSKDII-ISGGENISSL 466
|
170 180 190
....*....|....*....|....*....|...
gi 1832481686 523 KIENIYMRSEPVAQVFV-------HGESLQAFL 548
Cdd:PLN02479 467 EVENVVYTHPAVLEASVvarpderWGESPCAFV 499
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
135-541 |
2.45e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 66.70 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 135 EAITYIVNKAELSLVFVDK---PekaklLLEGVENKLiPGLKIIVVMdaygselverGQRCGVEVTSMK---AMED-LGR 207
Cdd:PRK06018 101 EQIAWIINHAEDRVVITDLtfvP-----ILEKIADKL-PSVERYVVL----------TDAAHMPQTTLKnavAYEEwIAE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 208 ANRRKPKPPAPEDLAV-ICFTSGTTGNPKGAMVTHRNIVsdCSAFVKATENTVNPCPDDTLISFLPLAH-------MFER 279
Cdd:PRK06018 165 ADGDFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHRSNV--LHALMANNGDALGTSAADTMLPVVPLFHanswgiaFSAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 280 VVECVMLCHGAKIGffQGDIRLLMDDLKVlqpTVFPVVPrllnrmfdrifgqantTLKRWLLDF--ASKRKEAELRSGII 357
Cdd:PRK06018 243 SMGTKLVMPGAKLD--GASVYELLDTEKV---TFTAGVP----------------TVWLMLLQYmeKEGLKLPHLKMVVC 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 358 rnnslwdrlifhkvqsslGGrvrlmvtgaapvSATVLTFLRA--ALGCQFYEGYGQTECT---AGCCLTMPGDWTAGHV- 431
Cdd:PRK06018 302 ------------------GG------------SAMPRSMIKAfeDMGVEVRHAWGMTEMSplgTLAALKPPFSKLPGDAr 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 432 -------GAPMPCNLIKLVDvEEMNYMAAEGE--GEVCVKGPNVFQGYLKdpaKTAEALDKDGWLHTGDIGKWLPNGTLK 502
Cdd:PRK06018 352 ldvlqkqGYPPFGVEMKITD-DAGKELPWDGKtfGRLKVRGPAVAAAYYR---VDGEILDDDGFFDTGDVATIDAYGYMR 427
|
410 420 430
....*....|....*....|....*....|....*....
gi 1832481686 503 IIDRKKHIFKlAQGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:PRK06018 428 ITDRSKDVIK-SGGEWISSIDLENLAVGHPKVAEAAVIG 465
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
218-559 |
3.30e-11 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 65.88 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpCPDDTLISFLPlAHMFERVVE--CVMLCHGAKIGFF 295
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGR---DNGDEAVLFFS-NYVFDFFVEqmTLALLNGQKLVVP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 QGDIRL-------LMDDLKVlqpTVFPVVPRLLNRM-FDRIfgqanTTLKRWLL---DFASKRkeaelrsgiirnnslwd 364
Cdd:cd17648 169 PDEMRFdpdrfyaYINREKV---TYLSGTPSVLQQYdLARL-----PHLKRVDAageEFTAPV----------------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 365 rliFHKVQSSLGGRVrlmVTGAAPVSATVLTFLRaalgcqFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIklvd 444
Cdd:cd17648 224 ---FEKLRSRFAGLI---INAYGPTETTVTNHKR------FFPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAV---- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 445 veemnymaaegeGEVCVKGPNVFQGYLKDPAKTAE-------------ALDKDGWLH-TGDIGKWLPNGTLKIIDRKKHI 510
Cdd:cd17648 288 ------------GELYLGGDGVARGYLNRPELTAErflpnpfqteqerARGRNARLYkTGDLVRWLPSGELEYLGRNDFQ 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1832481686 511 FKLaQGEYIAPEKIENIYMRSEPVAQVFV--------HGESLQAFLIAIVVPDVETL 559
Cdd:cd17648 356 VKI-RGQRIEPGEVEAALASYPGVRECAVvakedasqAQSRIQKYLVGYYLPEPGHV 411
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
60-559 |
5.07e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 65.43 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 60 LGSRKPDQPYEWlsyKQVAELSECIGSALIQKGFKTAPDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITY 139
Cdd:PRK13388 18 IAVRYGDRTWTW---REVLAEAAARAAALIALADPDRPLH-VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 140 IVNKAELSLVFVDKPEKAklLLEGVEnklIPGLKIIVVMDAYGSELVERGQRCgvevtsmkamedlgranrrKP-KPPAP 218
Cdd:PRK13388 94 DIRRADCQLLVTDAEHRP--LLDGLD---LPGVRVLDVDTPAYAELVAAAGAL-------------------TPhREVDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 219 EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMfervvECVM------LCHGAKI 292
Cdd:PRK13388 150 MDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT----RDDVCYVSMPLFHS-----NAVMagwapaVASGAAV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 293 ---------GFfqgdirllMDDLKVLQPTVFPVVPRLL-------NRMFDrifgqANTTLKRWLLDFASKRKEAElrsgi 356
Cdd:PRK13388 221 alpakfsasGF--------LDDVRRYGATYFNYVGKPLayilatpERPDD-----ADNPLRVAFGNEASPRDIAE----- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 357 irnnslwdrlifhkvqsslggrvrlmvtgaapvsatvltFLRAaLGCQFYEGYGQTEctAGCCLTMPGDWTAGHVGAPMP 436
Cdd:PRK13388 283 ---------------------------------------FSRR-FGCQVEDGYGSSE--GAVIVVREPGTPPGSIGRGAP 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 437 CnlIKLVDVEEM---------------NymAAEGEGE-VCVKGPNVFQGYLKDPAKTAEALdKDGWLHTGDIGKWLPNGT 500
Cdd:PRK13388 321 G--VAIYNPETLtecavarfdahgallN--ADEAIGElVNTAGAGFFEGYYNNPEATAERM-RHGMYWSGDLAYRDADGW 395
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832481686 501 LKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHG----ESLQAFLIAIVVPDVETL 559
Cdd:PRK13388 396 IYFAGRTADWMRV-DGENLSAAPIERILLRHPAINRVAVYAvpdeRVGDQVMAALVLRDGATF 457
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
380-555 |
6.14e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 65.40 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 380 RLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEctaG-CCLTMPGDwTAGHV----GAPM-PCNLIKLVDvEEMNYMAa 453
Cdd:PRK10946 303 KLLQVGGARLSETLARRIPAELGCQLQQVFGMAE---GlVNYTRLDD-SDERIfttqGRPMsPDDEVWVAD-ADGNPLP- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 454 EGE-GEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHifklaQ----GEYIAPEKIENIY 528
Cdd:PRK10946 377 QGEvGRLMTRGPYTFRGYYKSPQHNASAFDANGFYCSGDLVSIDPDGYITVVGREKD-----QinrgGEKIAAEEIENLL 451
|
170 180
....*....|....*....|....*..
gi 1832481686 529 MRsepvaqvfvHGESLQAFLIAIvvPD 555
Cdd:PRK10946 452 LR---------HPAVIHAALVSM--ED 467
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
220-541 |
8.39e-11 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 64.68 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 220 DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTvnpcPDDTLISFLPLAHMFERVVE-CVMLCHGAKIGF---F 295
Cdd:cd05940 82 DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL----PSDVLYTCLPLYHSTALIVGwSACLASGATLVIrkkF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 QGdiRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfASKRKEAELRsgiirnnslwdrlifHKVQSSL 375
Cdd:cd05940 158 SA--SNFWDDIRKYQATIFQYIGELC----------------RYLL--NQPPKPTERK---------------HKVRMIF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 376 GGRVRLMVTGaapvsatvlTFL-RAALGcQFYEGYGQTECTAGCCLTMPGDWTAGHVGA----PMPCNLIKlVDVEEMN- 449
Cdd:cd05940 203 GNGLRPDIWE---------EFKeRFGVP-RIAEFYAATEGNSGFINFFGKPGAIGRNPSllrkVAPLALVK-YDLESGEp 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 450 ------YMAAEGEGEV--CV-----KGPnvFQGYLkDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHI 510
Cdd:cd05940 272 irdaegRCIKVPRGEPglLIsrinpLEP--FDGYT-DPAATEKKIlrdvfkKGDAWFNTGDLMRLDGEGFWYFVDRLGDT 348
|
330 340 350
....*....|....*....|....*....|.
gi 1832481686 511 FKLaQGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:cd05940 349 FRW-KGENVSTTEVAAVLGAFPGVEEANVYG 378
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-557 |
1.05e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 65.36 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 3 MSQHYTKVSRGEYRCQDRSGPSVSTVTFPESVPKLTGPSRCSL-WPWGLH-GQIYNGPCLgsRKPDQPY-----EWLSYK 75
Cdd:PRK12316 3009 LARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAeYPLERGvHRLFEEQVE--RTPDAVAlafgeQRLSYA 3086
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 76 QVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELsLVFVDKPE 155
Cdd:PRK12316 3087 ELNRRANRLAHRLIERG--VGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGA-QLLLSQSH 3163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 156 KAKLLLEGVENKLipglkiivvmdaygselVERGQrcgvevtsmkamEDLGRANrrKPKPPAPEDLAVICFTSGTTGNPK 235
Cdd:PRK12316 3164 LRLPLAQGVQVLD-----------------LDRGD------------ENYAEAN--PAIRTMPENLAYVIYTSGSTGKPK 3212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 236 GAMVTHrnivSDCSAFVKATENTVNPCPDDTLISFLPLAHMFERVVECVMLCHGAKIgffqgdirllmddlkVLQPTVFP 315
Cdd:PRK12316 3213 GVGIRH----SALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV---------------VLAGPEDW 3273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 316 VVPRLLNRMFDRifGQANTTLKRWlldfaskrkeaelrsgiirnnSLWDRLIFHKVQSSLGGRVRLMVTGAAPVSATVlt 395
Cdd:PRK12316 3274 RDPALLVELINS--EGVDVLHAYP---------------------SMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQ-- 3328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 396 fLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGH--VGAPMPCNLIKLVDVeEMNYMAAEGEGEVCVKGPNVFQGYLKD 473
Cdd:PRK12316 3329 -QQVFAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDG-SLEPVPVGALGELYLGGEGLARGYHNR 3406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 474 PAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHGESLQAf 547
Cdd:PRK12316 3407 PGLTAERFVPDPFvpgerlYRTGDLARYRADGVIEYIGRVDHQVKI-RGFRIELGEIEARLLEHPWVREAVVLAVDGRQ- 3484
|
570
....*....|
gi 1832481686 548 LIAIVVPDVE 557
Cdd:PRK12316 3485 LVAYVVPEDE 3494
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
373-557 |
1.49e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 63.77 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 SSLggrvRLMVTGAAPVSATVLtflRAAL---GCQFYEGYGQTEcTAGCCLTMPGDWTA--GHVGAPMPCNlIKLVDvEE 447
Cdd:PRK08276 262 SSL----RVAIHAAAPCPVEVK---RAMIdwwGPIIHEYYASSE-GGGVTVITSEDWLAhpGSVGKAVLGE-VRILD-ED 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 448 MNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGkWL-PNGTLKIIDRKKHIFkLAQGEYIAPEKIEN 526
Cdd:PRK08276 332 GNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVTVGDVG-YLdEDGYLYLTDRKSDMI-ISGGVNIYPQEIEN 409
|
170 180 190
....*....|....*....|....*....|.
gi 1832481686 527 IYMRSEPVAQVFVHGeslqafliaivVPDVE 557
Cdd:PRK08276 410 LLVTHPKVADVAVFG-----------VPDEE 429
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
218-565 |
1.77e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 64.80 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNpcpdDTLISFLPLAhmFERVVECVM--LCHGAKIGFF 295
Cdd:PRK12467 3236 GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN----DRVLLFMSFS--FDGAQERFLwtLICGGCLVVR 3309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 QGDIRllmDDLKVLQptvfpvvprLLNRmfDRIfgqanTTlkrwlLDFASkrkeaelrsgiirnNSLWDRLIFHKVQSsl 375
Cdd:PRK12467 3310 DNDLW---DPEELWQ---------AIHA--HRI-----SI-----ACFPP--------------AYLQQFAEDAGGAD-- 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 376 GGRVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKL---VDVEEMNY 450
Cdd:PRK12467 3350 CASLDIYVFGGEAVPPAAFEQVKRKLKpRGLTNGYGPTEAVVTVTLwKCGGDAVCEAPYAPIGRPVAGRsiyVLDGQLNP 3429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 451 MAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKD------GWLH-TGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEK 523
Cdd:PRK12467 3430 VPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfsgsgGRLYrTGDLARYRADGVIEYLGRIDHQVKI-RGFRIELGE 3508
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1832481686 524 IENIYMRSEPVAQVFVHGESLQA--FLIAIVVPDVETlCSWAQK 565
Cdd:PRK12467 3509 IEARLLQHPSVREAVVLARDGAGgkQLVAYVVPADPQ-GDWRET 3551
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
135-555 |
1.80e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.56 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 135 EAITYIVN--KAELSLVFVDkpekaklLLEGVENKLIPGLKIIVV------MDAYGSELVERGQRCGvevtsMKAMEDLG 206
Cdd:PRK12406 73 EEIAYILEdsGARVLIAHAD-------LLHGLASALPAGVTVLSVptppeiAAAYRISPALLTPPAG-----AIDWEGWL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 207 RANRRKPKPPAPEDLAVIcFTSGTTGNPKGamvthrnivsdcsafVKATentvNPCPDDTL--ISFLPLAHMFERVVECV 284
Cdd:PRK12406 141 AQQEPYDGPPVPQPQSMI-YTSGTTGHPKG---------------VRRA----APTPEQAAaaEQMRALIYGLKPGIRAL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 285 M---LCHGAKIGFFQGDIRLlmDDLKVLQP-----------------TVFpVVPRllnrMFDRifgqanttlkrwLLDFA 344
Cdd:PRK12406 201 LtgpLYHSAPNAYGLRAGRL--GGVLVLQPrfdpeellqlierhritHMH-MVPT----MFIR------------LLKLP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 345 SKRKEAelrsgiirnnslWDrlifhkvQSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPG 424
Cdd:PRK12406 262 EEVRAK------------YD-------VSSL----RHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTE-SGAVTFATSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 425 DWTA--GHVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNV--FQgYLKDPAKTAEaLDKDGWLHTGDIGKWLPNGT 500
Cdd:PRK12406 318 DALShpGTVGKAAPGAELRFVD-EDGRPLPQGEIGEIYSRIAGNpdFT-YHNKPEKRAE-IDRGGFITSGDVGYLDADGY 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832481686 501 LKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 555
Cdd:PRK12406 395 LFLCDRKRDMV-ISGGVNIYPAEIEAVLHAVPGVHDCAVFGipdAEFGEALMAVVEPQ 451
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
180-537 |
2.89e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.25 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 180 AYGSELvergQRCGVEVTSMkAMEDL---GRANRRKPKPPAP-EDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKAT 255
Cdd:PRK05851 114 SHGSHL----ERLRAVDSSV-TVHDLataAHTNRSASLTPPDsGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 256 ENTVnpcPDDTLISFLPLAH-MFERVVECVMLChGAKIGffqgdirllmddlkvLQPT-VFPVVP-RLLNrmfdrifgqa 332
Cdd:PRK05851 189 GLDA---ATDVGCSWLPLYHdMGLAFLLTAALA-GAPLW---------------LAPTtAFSASPfRWLS---------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 333 nttlkrWLLDF-ASKRKEAELRSGIIRNNSlwdrlifHKVQSSLGGRVRLMVTGAAPVSATVLT-FLRAALGCQFYEG-- 408
Cdd:PRK05851 240 ------WLSDSrATLTAAPNFAYNLIGKYA-------RRVSDVDLGALRVALNGGEPVDCDGFErFATAMAPFGFDAGaa 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 409 ---YGQTECTagCCLTMP---------------GDWTAGH--VGAPMPCNLIKLVDVEEMNYMAAEGEGEVCVKGPNVFQ 468
Cdd:PRK05851 307 apsYGLAEST--CAVTVPvpgiglrvdevttddGSGARRHavLGNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMS 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832481686 469 GYLKDPAktaeaLDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIymrsepVAQV 537
Cdd:PRK05851 385 GYLGQAP-----IDPDDWFPTGDLG-YLVDGGLVVCGRAKELITVA-GRNIFPTEIERV------AAQV 440
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
72-558 |
8.27e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 61.87 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRpEWVIIEQGCFAYSMVIVPLYDT-LGNEAITYIVNKAELSLVF 150
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVR--AGDGVAVLARNH-RGFVLALYAAGKVGARIILLNTgFSGPQLAEVAAREGVKALV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 151 VDKpEKAKLLlEGVENKLIPGLKIIVVMDAygselvERGQRCGVEVtsmkaMEDLGRANRRKPKPPAPEDLAVICFTSGT 230
Cdd:PRK07788 152 YDD-EFTDLL-SALPPDLGRLRAWGGNPDD------DEPSGSTDET-----LDDLIAGSSTAPLPKPPKPGGIVILTSGT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 231 TGNPKGAMVTHRNIVSDCSAFV-----KATENTVNPCPddtlisflplahMFervvecvmlcHG-----AKIGFFQG--- 297
Cdd:PRK07788 219 TGTPKGAPRPEPSPLAPLAGLLsrvpfRAGETTLLPAP------------MF----------HAtgwahLTLAMALGstv 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 298 ------DIRLLMDDLKVLQPTVFPVVPRLLNRMFDrifgqanttlkrwLLDFASKRKEAelrsgiirnnslwdrlifhkv 371
Cdd:PRK07788 277 vlrrrfDPEATLEDIAKHKATALVVVPVMLSRILD-------------LGPEVLAKYDT--------------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 372 qSSLggrvRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTECtAGCCLTMPGDWTA--GHVGAPMPCNLIKLVDvEEMN 449
Cdd:PRK07788 323 -SSL----KIIFVSGSALSPELATRALEAFGPVLYNLYGSTEV-AFATIATPEDLAEapGTVGRPPKGVTVKILD-ENGN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 450 YMAAEGEGEVCVKGPNVFQGYLKDPAKTAealdKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYM 529
Cdd:PRK07788 396 EVPRGVVGRIFVGNGFPFEGYTDGRDKQI----IDGLLSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAEVEDLLA 470
|
490 500
....*....|....*....|....*....
gi 1832481686 530 RSEPVAQVFVHGeslqafliaivVPDVET 558
Cdd:PRK07788 471 GHPDVVEAAVIG-----------VDDEEF 488
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
64-589 |
1.29e-09 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 61.06 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 64 KPDQP-YEWL----SYKQVAELSECIGSALIQKGF-KTAPdqfIGIFAQNRPEWVI-----IEQGCfAYsmviVPLYDTL 132
Cdd:PRK04813 15 QPDFPaYDYLgeklTYGQLKEDSDALAAFIDSLKLpDKSP---IIVFGHMSPEMLAtflgaVKAGH-AY----IPVDVSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 133 GNEAITYIVNKAELSLVFvdkpEKAKLLLEGVENKLIpglkiivvmdayGSELVERGQRCGVEVTSMKAMEDlgranrrk 212
Cdd:PRK04813 87 PAERIEMIIEVAKPSLII----ATEELPLEILGIPVI------------TLDELKDIFATGNPYDFDHAVKG-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 213 pkppapEDLAVICFTSGTTGNPKGAMVTHRNIVS----DCSAFVKATENTV-NPCPddtlISFlplahmfervvecvmlc 287
Cdd:PRK04813 143 ------DDNYYIIFTSGTTGKPKGVQISHDNLVSftnwMLEDFALPEGPQFlNQAP----YSF----------------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 288 hgakigffqgdirllmdDLKV--LQP------TVFPVVPRLLNRmfdriFGQANTTLKR-----W----------LLD-- 342
Cdd:PRK04813 196 -----------------DLSVmdLYPtlasggTLVALPKDMTAN-----FKQLFETLPQlpinvWvstpsfadmcLLDps 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 343 FASKrKEAELRsgiirnnslwdRLIF------HKVQSSLGGRVrlmvtgaaPvSATVltflraalgcqfYEGYGQTECTA 416
Cdd:PRK04813 254 FNEE-HLPNLT-----------HFLFcgeelpHKTAKKLLERF--------P-SATI------------YNTYGPTEATV 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 417 GC------------CLTMPgdwtaghVGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEAL-DK 483
Cdd:PRK04813 301 AVtsieitdemldqYKRLP-------IGYAKPDSPLLIID-EEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFfTF 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 484 DGW--LHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKIENIYMRSEPVAQVFV----HGESLQAfLIAIVVPDve 557
Cdd:PRK04813 373 DGQpaYHTGDAGY-LEDGLLFYQGRIDFQIKLN-GYRIELEEIEQNLRQSSYVESAVVvpynKDHKVQY-LIAYVVPK-- 447
|
570 580 590
....*....|....*....|....*....|..
gi 1832481686 558 tlcswaqkrgfEGSFEelcRNKDVKKAILEDM 589
Cdd:PRK04813 448 -----------EEDFE---REFELTKAIKKEL 465
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
219-557 |
2.54e-09 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341311 [Multi-domain] Cd Length: 479 Bit Score: 59.80 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 219 EDLAVICFTSGTTGNPKGAMVTHRNIVSdcsafvkatentvnpcpddtlisflPLAHMFERvvecvmlchgAKIGFFQGd 298
Cdd:cd17656 128 DDLLYIIYTSGTTGKPKGVQLEHKNMVN-------------------------LLHFEREK----------TNINFSDK- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 299 irllmddlkVLQPTVFPvvprllnrmFDRIFGQANTTL----KRWLLDFASKRKEAELRSGIIRNN--------SLWdRL 366
Cdd:cd17656 172 ---------VLQFATCS---------FDVCYQEIFSTLlsggTLYIIREETKRDVEQLFDLVKRHNievvflpvAFL-KF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 367 IFHKVQ--SSLGGRVRLMVTGAAP--VSATVLTFLRAAlGCQFYEGYGQTEC-TAGCCLTMPGDWTAGH--VGAPMPCNL 439
Cdd:cd17656 233 IFSEREfiNRFPTCVKHIITAGEQlvITNEFKEMLHEH-NVHLHNHYGPSEThVVTTYTINPEAEIPELppIGKPISNTW 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 440 IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW------LHTGDIGKWLPNGTLKIIDRKKHIFKL 513
Cdd:cd17656 312 IYILD-QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFdpnermYRTGDLARYLPDGNIEFLGRADHQVKI 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1832481686 514 aQGEYIAPEKIENIYMRSEPVAQ--VFVHGESL-QAFLIAIVVPDVE 557
Cdd:cd17656 391 -RGYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQE 436
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
215-525 |
5.11e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 59.25 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 215 PPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkaTENTVNPCPDDTLISFLPLAH-MfervvecvmlchgAKIG 293
Cdd:PRK09192 172 RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI---SHDGLKVRPGDRCVSWLPFYHdM-------------GLVG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 294 FFQGDI--RLLMDDLKVLQptvFPVVPRLLNRMFDR---------IFG------------QANTTLKRW----------- 339
Cdd:PRK09192 236 FLLTPVatQLSVDYLPTRD---FARRPLQWLDLISRnrgtisyspPFGyelcarrvnskdLAELDLSCWrvagigadmir 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 340 ---LLDFASKRKEA-----------------------ELRSGIIRNNSLWDRLIFHKVQSSLGGRVRlmvtgaaPVSATV 393
Cdd:PRK09192 313 pdvLHQFAEAFAPAgfddkafmpsyglaeatlavsfsPLGSGIVVEEVDRDRLEYQGKAVAPGAETR-------RVRTFV 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 394 LtflraalgcqfyegygqtectagcCltmpgdwtaghvGAPMPCNLIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKD 473
Cdd:PRK09192 386 N------------------------C------------GKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFRD 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1832481686 474 PAkTAEALDKDGWLHTGDIGkWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIE 525
Cdd:PRK09192 429 EE-SQDVLAADGWLDTGDLG-YLLDGYLYITGRAKDLI-IINGRNIWPQDIE 477
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
216-559 |
5.65e-09 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 58.64 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 216 PAPEDLAVICFTSGTTGNPKGAMVTHR----NIVSDCSAFvkatentvNPCPDDTLIsFLPLAHMFERVVECVM-LCHGA 290
Cdd:cd17654 115 RTDECLAYVIHTSGTTGTPKIVAVPHKcilpNIQHFRSLF--------NITSEDILF-LTSPLTFDPSVVEIFLsLSSGA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 291 KIgffqgdirllmddlkVLQPTVFPVVPRLLNRMFDRIFG----QANTTLKRwllDFASKRKEAELRSGIirnnslwdrl 366
Cdd:cd17654 186 TL---------------LIVPTSVKVLPSKLADILFKRHRitvlQATPTLFR---RFGSQSIKSTVLSAT---------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 367 ifhkvqSSLggRVrLMVTGAAPVSATVLTFLRAA-LGCQFYEGYGQTECTAGCCL-TMPGDWTAGHVGAPMPCNLIKLVD 444
Cdd:cd17654 238 ------SSL--RV-LALGGEPFPSLVILSSWRGKgNRTRIFNIYGITEVSCWALAyKVPEEDSPVQLGSPLLGTVIEVRD 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 445 VEemnymAAEGEGEVCVKGPNVfQGYLKDPAKTAEALdkdgWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAPEKI 524
Cdd:cd17654 309 QN-----GSEGTGQVFLGGLNR-VCILDDEVTVPKGT----MRATGDFVT-VKDGELFFLGRKDSQIKRR-GKRINLDLI 376
|
330 340 350
....*....|....*....|....*....|....*
gi 1832481686 525 ENIYMRSEPVAQVFVHGESLQAFLIAIVVPDVETL 559
Cdd:cd17654 377 QQVIESCLGVESCAVTLSDQQRLIAFIVGESSSSR 411
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
224-555 |
5.11e-08 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 55.10 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 224 ICFTSGTTGNPKGAMVTHRNIVsdcsAFVKATENTVNPCPDDTLISFLPLAH-MFERVVECVMLCHGAKIGFFQGDIRLL 302
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWI----ESFVCNEDLFNISGEDAILAPGPLSHsLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 303 MDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkrwlldfaskrkEAELRSGIIRnnslwdrlifHKVQSSLGGrvrlm 382
Cdd:cd17633 81 IRKINQYNATVIYLVPTML---------------------------QALARTLEPE----------SKIKSIFSS----- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 383 vtGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCnliklVDVEEMNymAAEGE-GEVCV 461
Cdd:cd17633 119 --GQKLFESTKKKLKNIFPKANLIEFYGTSELSFITYNFNQESRPPNSVGRPFPN-----VEIEIRN--ADGGEiGKIFV 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 462 KGPNVFQGYLKdpaktAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHG 541
Cdd:cd17633 190 KSEMVFSGYVR-----GGFSNPDGWMSVGDIGYVDEEGYLYLVGRESDMI-IIGGINIFPTEIESVLKAIPGIEEAIVVG 263
|
330
....*....|....*..
gi 1832481686 542 ESLQAF---LIAIVVPD 555
Cdd:cd17633 264 IPDARFgeiAVALYSGD 280
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
219-550 |
5.25e-08 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 56.72 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 219 EDLAVICFTSGTTGNPKGAMVTHRNIVSDcsafVKATENTVNPCPDDTLISFLPLAhmFE-RVVECVM-LCHGAKIGFF- 295
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAER----LQWMQATYALDDSDVLMQKAPIS--FDvSVWECFWpLITGCRLVLAg 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 296 ---QGDIRLLMDDLKVLQPTVFPVVPRLLNRMFDRIFGQANTTLKRwlLDFASKRKEAELRsgiirnnslwDRLIFHKVQ 372
Cdd:PRK05691 1347 pgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLRR--LFSGGEALPAELR----------NRVLQRLPQ 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 373 SSLGGRvrlmvtgaapvsatvltflraalgcqfyegYGQTE----CTAGCCLTMPGDWTAghVGAPMPCNLIKLVDvEEM 448
Cdd:PRK05691 1415 VQLHNR------------------------------YGPTEtainVTHWQCQAEDGERSP--IGRPLGNVLCRVLD-AEL 1461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 449 NYMAAEGEGEVCVKGPNVFQGYLKDPAKTAE-----ALDKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAP 521
Cdd:PRK05691 1462 NLLPPGVAGELCIGGAGLARGYLGRPALTAErfvpdPLGEDGarLYRTGDRARWNADGALEYLGRLDQQVKL-RGFRVEP 1540
|
330 340 350
....*....|....*....|....*....|.
gi 1832481686 522 EKIENIYMRSEPVAQ--VFVHGESLQAFLIA 550
Cdd:PRK05691 1541 EEIQARLLAQPGVAQaaVLVREGAAGAQLVG 1571
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
194-275 |
7.44e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 55.33 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 194 VEVTSMkameDLGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSDC----SAFVKATENTvnPCPDDTLIS 269
Cdd:PRK05850 139 IEVDLL----DLDSPRGSDARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeqlmSDYFGDTGGV--PPPDTTVVS 212
|
....*.
gi 1832481686 270 FLPLAH 275
Cdd:PRK05850 213 WLPFYH 218
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
45-557 |
1.20e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 54.63 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 45 LWPwGLHGQIyngpclgsrKPDQPY-------EWLSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPE-----WV 112
Cdd:PRK13390 1 MYP-GTHAQI---------APDRPAvivaetgEQVSYRQLDDDSAALARVLYDAGLR--TGDVVALLSDNSPEalvvlWA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 113 IIEQGcfaysmvivpLYDTlgneAITYIVNKAELSLVFVDKPEK---AKLLLEGVENKLIPGLKIIVvmdAYGSELVERG 189
Cdd:PRK13390 69 ALRSG----------LYIT----AINHHLTAPEADYIVGDSGARvlvASAALDGLAAKVGADLPLRL---SFGGEIDGFG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 190 QrcgVEVTsmkamedLGRANRRKPKPPAPedlAVICFTSGTTGNPKGAM--VTHRNIVSDCSAFVKATENTVNPCPDDTL 267
Cdd:PRK13390 132 S---FEAA-------LAGAGPRLTEQPCG---AVMLYSSGTTGFPKGIQpdLPGRDVDAPGDPIVAIARAFYDISESDIY 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 268 ISFLPLAHMFE-RVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPRLLNRMFdrifgqanttlkrwlldfask 346
Cdd:PRK13390 199 YSSAPIYHAAPlRWCSMVHALGGTVVLAKRFDAQATLGHVERYRITVTQMVPTMFVRLL--------------------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 347 RKEAELRSGiirnnslwdrlifHKVQSslggrVRLMVTGAAPVSATVLTFLRAALGCQFYEGYGQTEcTAGCCLTMPGDW 426
Cdd:PRK13390 258 KLDADVRTR-------------YDVSS-----LRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE-AHGMTFIDSPDW 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 427 TA--GHVGAPMPCNLiKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDG--WLHTGDIGKWLPNGTLK 502
Cdd:PRK13390 319 LAhpGSVGRSVLGDL-HICD-DDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAQHPAHpfWTTVGDLGSVDEDGYLY 396
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1832481686 503 IIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVAQVFVHGeslqafliaivVPDVE 557
Cdd:PRK13390 397 LADRKSFMI-ISGGVNIYPQETENALTMHPAVHDVAVIG-----------VPDPE 439
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
212-605 |
1.93e-07 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 53.97 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 212 KPKPPAPE-DLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKATENTVNPCPddTLISFLPLAHmfervveCVMLCHGA 290
Cdd:cd05915 145 ADPVRVPErAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKD--VVLPVVPMFH-------VNAWCLPY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 291 KIGFFQGDIRLLMDdlkVLQPTVfpvvprllnrMFDRIFGQANTTL--KRWLLDFASKRKEAelrsgiirnnslwdrlif 368
Cdd:cd05915 216 AATLVGAKQVLPGP---RLDPAS----------LVELFDGEGVTFTagVPTVWLALADYLES------------------ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 369 hkVQSSLGGRVRLMVTGAAPvsATVLTFLRAALGCQFYEGYGQTEC--TAGCCLTMPgDWT------AGHVGAPMPCN-L 439
Cdd:cd05915 265 --TGHRLKTLRRLVVGGSAA--PRSLIARFERMGVEVRQGYGLTETspVVVQNFVKS-HLEslseeeKLTLKAKTGLPiP 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 440 IKLVDVEEMNYMAAEGEGE----VCVKGPNVFQGYLKDPAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAq 515
Cdd:cd05915 340 LVRLRVADEEGRPVPKDGKalgeVQLKGPWITGGYYGNEEATRSALTPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSG- 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 516 GEYIAPEKIENIYMRSEPVAQVFVHGEslqafliaivvPDV---ETLCSWAQKRGFEGSFEEL---CRNKDVKKAILEDM 589
Cdd:cd05915 419 GEWISSVDLENALMGHPKVKEAAVVAI-----------PHPkwqERPLAVVVPRGEKPTPEELnehLLKAGFAKWQLPDA 487
|
410
....*....|....*.
gi 1832481686 590 VRLGKDSGLKPFEQVK 605
Cdd:cd05915 488 YVFAEEIPRTSAGKFL 503
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
216-541 |
4.61e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 52.38 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 216 PAPEDLAVICfTSGTTGNPKGAMVTHRNIVSdcSAFVKATENTVNPCPDD---------TLISFLPLAHmfervvecvmL 286
Cdd:cd05924 1 RSADDLYILY-TGGTTGMPKGVMWRQEDIFR--MLMGGADFGTGEFTPSEdahkaaaaaAGTVMFPAPP----------L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 287 CHGAK-----IGFFQGDiRLLMDDLKVLQPTVFPVVPR-LLNRMFdrIFGQAnttLKRWLLDfaskrkeaELRSGiiRNN 360
Cdd:cd05924 68 MHGTGswtafGGLLGGQ-TVVLPDDRFDPEEVWRTIEKhKVTSMT--IVGDA---MARPLID--------ALRDA--GPY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 361 SLwdrlifhkvqSSLggrvRLMVTGAAPVSATVLT-FLRAALGCQFYEGYGQTECTA-GCCLTMPGDWTAGHVGAPMPcn 438
Cdd:cd05924 132 DL----------SSL----FAISSGGALLSPEVKQgLLELVPNITLVDAFGSSETGFtGSGHSAGSGPETGPFTRANP-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 439 LIKLVDvEEMNYM--AAEGEGEVCVKGpNVFQGYLKDPAKTAEAL-DKDG--WLHTGDIGKWLPNGTLKIIDRKKHIFKL 513
Cdd:cd05924 196 DTVVLD-DDGRVVppGSGGVGWIARRG-HIPLGYYGDEAKTAETFpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINT 273
|
330 340
....*....|....*....|....*....
gi 1832481686 514 AqGEYIAPEKIENIyMRSEP-VAQVFVHG 541
Cdd:cd05924 274 G-GEKVFPEEVEEA-LKSHPaVYDVLVVG 300
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
64-241 |
5.75e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.59 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 64 KPDQPYEWLSYKQVAELSECIGSALIQKGFKTAPDQFIgiFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNK 143
Cdd:PRK04319 66 LDASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFI--FMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLED 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 144 AElSLVFVDKPEkaklLLEGVENKLIPGLKIIVVMDAYGSELvergqrcGVEVTSMKAMEDlgrANRRKPKPP-APEDLA 222
Cdd:PRK04319 144 SE-AKVLITTPA----LLERKPADDLPSLKHVLLVGEDVEEG-------PGTLDFNALMEQ---ASDEFDIEWtDREDGA 208
|
170 180
....*....|....*....|....*
gi 1832481686 223 VICFTSGTTGNPKG------AMVTH 241
Cdd:PRK04319 209 ILHYTSGSTGKPKGvlhvhnAMLQH 233
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
205-540 |
6.47e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 52.74 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 205 LGRANRRKPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIV------------SDCSAFVKATentvnPCPDDtlIS--- 269
Cdd:PRK10252 584 LAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVnrllwmqnhyplTADDVVLQKT-----PCSFD--VSvwe 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 270 -FLPlahmfervvecvMLChGAKIGFFQGD-------IRLLMDDLKVlqpTVFPVVPRLL----NRMFDRIFGQANTTLK 337
Cdd:PRK10252 657 fFWP------------FIA-GAKLVMAEPEahrdplaMQQFFAEYGV---TTTHFVPSMLaafvASLTPEGARQSCASLR 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 338 RWlldFASKRK-EAELRsgiirnnSLWDRLIfhkvqsslggrvrlmvtgAAPVsatvltflraalgcqfYEGYGQTECT- 415
Cdd:PRK10252 721 QV---FCSGEAlPADLC-------REWQQLT------------------GAPL----------------HNLYGPTEAAv 756
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 416 ------AGccltmpGDWTAGHVGAPMPCNL------IKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDK 483
Cdd:PRK10252 757 dvswypAF------GEELAAVRGSSVPIGYpvwntgLRILD-ARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIA 829
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1832481686 484 DGWL------HTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVH 540
Cdd:PRK10252 830 DPFApgermyRTGDVARWLDDGAVEYLGRSDDQLKI-RGQRIELGEIDRAMQALPDVEQAVTH 891
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
72-241 |
1.09e-06 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 51.72 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKTApDQfIGIFAQNRPEWVIIEQGCFAYSMVIVPLYDTLGNEAITYIVNKAELSLVFV 151
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKG-DR-VGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 152 -------DKP-------EKAKLLLEGVEnklipglKIIVVmdaygselvergQRCGVEVTSMKAmEDLGRANRRKPKPPA 217
Cdd:cd05968 170 adgftrrGREvnlkeeaDKACAQCPTVE-------KVVVV------------RHLGNDFTPAKG-RDLSYDEEKETAGDG 229
|
170 180
....*....|....*....|....*....
gi 1832481686 218 -----PEDLAVICFTSGTTGNPKGAMVTH 241
Cdd:cd05968 230 aerteSEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
72-275 |
1.11e-06 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 51.80 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGFKtaPDQFIGIFAQNRPEWVIIEQGcFAYSMVIVPLYDT-LGNEAITYIVNKAELSLVF 150
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVG--KGDVVALLMENRPEYLAAWLG-LAKLGAVVALLNTqQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 151 VDkPEKAKLLlEGVENKLIPGLKIIVVMDAYGSELVergqrcgvevtsmkAMEDLGRANRRKPKPPAP-------EDLAV 223
Cdd:PRK08279 140 VG-EELVEAF-EEARADLARPPRLWVAGGDTLDDPE--------------GYEDLAAAAAGAPTTNPAsrsgvtaKDTAF 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1832481686 224 ICFTSGTTGNPKGAMVTHRNIVSDCSAFVkateNTVNPCPDDTLISFLPLAH 275
Cdd:PRK08279 204 YIYTSGTTGLPKAAVMSHMRWLKAMGGFG----GLLRLTPDDVLYCCLPLYH 251
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
197-552 |
2.17e-06 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 50.80 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 197 TSMKAMEDLGRANRRKP---KPPAPEDLAVICFTSGTTGNPKGAMvtHRNivSDCSAFVKAT-ENTVNPCPDDtlisflp 272
Cdd:PRK06060 120 RVAEAAELMSEAARVAPggyEPMGGDALAYATYTSGTTGPPKAAI--HRH--ADPLTFVDAMcRKALRLTPED------- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 273 lahmfervvecVMLChGAKIGFFQGDIRLLMDDLKVLQPTVFPVVPrllnrmfdrIFGQANTTLkrwlldfaSKRKEAEL 352
Cdd:PRK06060 189 -----------TGLC-SARMYFAYGLGNSVWFPLATGGSAVINSAP---------VTPEAAAIL--------SARFGPSV 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 353 RSGIirnNSLWDRLIFHKVQSSLGGrVRLMVTGAAPVSATVLTFLRAALG-CQFYEGYGQTECTAGCCLTMPGDWTAGHV 431
Cdd:PRK06060 240 LYGV---PNFFARVIDSCSPDSFRS-LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTEVGQTFVSNRVDEWRLGTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 432 GAPMPCNLIKLVdVEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTaeaLDKDGWLHTGDIGKWLPNGTLKIIDRKKHIf 511
Cdd:PRK06060 316 GRVLPPYEIRVV-APDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSP---VANEGWLDTRDRVCIDSDGWVTYRCRADDT- 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1832481686 512 KLAQGEYIAPEKIENIYMRSEPVAQVFVHG-------ESLQAFLIAIV 552
Cdd:PRK06060 391 EVIGGVNVDPREVERLIIEDEAVAEAAVVAvrestgaSTLQAFLVATS 438
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
217-550 |
2.48e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 217 APEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFV--------KATENTVNPCPDDTLISFLPlAHMFERVVECV--ML 286
Cdd:PRK05691 3867 GPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVpylalseaDVIAQTASQSFDISVWQFLA-APLFGARVEIVpnAI 3945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 287 CHgakigffqgDIRLLMDDLKVLQPTVFPVVPRLLNRMF--DRifgQANTTLkRWLLDfaskrkeaelrsgiirnnslwd 364
Cdd:PRK05691 3946 AH---------DPQGLLAHVQAQGITVLESVPSLIQGMLaeDR---QALDGL-RWMLP---------------------- 3990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 365 rlifhkvqsslggrvrlmvTGAAPVSATVLTFLRAALGCQFYEGYGQTECTAGCCL-TMPGDWTAGH---VGAPMPCNLI 440
Cdd:PRK05691 3991 -------------------TGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFfRVDLASTRGSylpIGSPTDNNRL 4051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 441 KLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGW-------LHTGDIGKWLPNGTLKIIDRKKHIFKL 513
Cdd:PRK05691 4052 YLLD-EALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgapgerlYRTGDLARRRSDGVLEYVGRIDHQVKI 4130
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1832481686 514 aQGEYIAPEKIENIYMRSEPV------AQVFVHGESLQAFLIA 550
Cdd:PRK05691 4131 -RGYRIELGEIEARLHEQAEVreaavaVQEGVNGKHLVGYLVP 4172
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
72-566 |
3.33e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.73 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 72 LSYKQVAELSECIGSALIQKGfkTAPDQFIGIFAQNRPEWVI----IEQGCFAYsmviVPLYDTLGNEAITYIVNKAELS 147
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERG--VGPDVLVGVAMERSIEMVVallaILKAGGAY----VPLDPEYPAERLAYMLEDSGVQ 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 148 LVFVDKPEKAKL-LLEGVENklipglkiiVVMDAYGSELveRGQRCGVEVTSMkamedlgranrrkpkppAPEDLAVICF 226
Cdd:PRK12316 611 LLLSQSHLGRKLpLAAGVQV---------LDLDRPAAWL--EGYSEENPGTEL-----------------NPENLAYVIY 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 227 TSGTTGNPKGAMVTHRNIVSDCSAFVKATEntvnpcpddtlisfLPLAhmfERVVECVMLCHGAKIGFFQGDirlLMDDL 306
Cdd:PRK12316 663 TSGSTGKPKGAGNRHRALSNRLCWMQQAYG--------------LGVG---DTVLQKTPFSFDVSVWEFFWP---LMSGA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 307 KVLqptvfpVVPRLLNRMFDRIFGQANTTLKRwLLDFASKRKEAELRSGiirnnslwdrlifhKVQSSLGgrVRLMVTGA 386
Cdd:PRK12316 723 RLV------VAAPGDHRDPAKLVELINREGVD-TLHFVPSMLQAFLQDE--------------DVASCTS--LRRIVCSG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 387 APVSATVLTFLRAAL-GCQFYEGYGQTECTAGCCltmpgDWTAGH-------VGAPMPCNLIKLVDVeEMNYMAAEGEGE 458
Cdd:PRK12316 780 EALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVT-----HWTCVEeggdsvpIGRPIANLACYILDA-NLEPVPVGVLGE 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 459 VCVKGPNVFQGYLKDPAKTAEAL------DKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLaQGEYIAPEKIENIYMRSE 532
Cdd:PRK12316 854 LYLAGRGLARGYHGRPGLTAERFvpspfvAGERMYRTGDLARYRADGVIEYAGRIDHQVKL-RGLRIELGEIEARLLEHP 932
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1832481686 533 PVAQVFVHGESLQAfLIAIVVPD------VETLCSWAQKR 566
Cdd:PRK12316 933 WVREAAVLAVDGKQ-LVGYVVLEseggdwREALKAHLAAS 971
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
184-276 |
6.79e-06 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 49.21 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 184 ELVERGQRCGV--EVTSMKAMEDLGRANRRKPKPPAPEDL---------AVICFTSGTTGNPKGAMVTHRNIVSdCSAFV 252
Cdd:cd05938 98 ALRADGVSVWYlsHTSNTEGVISLLDKVDAASDEPVPASLrahvtikspALYIYTSGTTGLPKAARISHLRVLQ-CSGFL 176
|
90 100
....*....|....*....|....
gi 1832481686 253 KATentvNPCPDDTLISFLPLAHM 276
Cdd:cd05938 177 SLC----GVTADDVIYITLPLYHS 196
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| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
218-545 |
6.15e-05 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 45.89 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFvkatENTVNPCPDDTLISFLPLAH---MFERVVECVMlcHGAKIGF 294
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLL----SHDLNLKNGDRTYTCMPLYHgtaAFLGACNCLM--SGGTLAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 295 ---FQgdIRLLMDDLKVLQPTVFPVVPRLLnrmfdrifgqanttlkRWLLdfaskrkeaelrSGIIrnnSLWDRLifHKV 371
Cdd:cd05937 160 srkFS--ASQFWKDVRDSGATIIQYVGELC----------------RYLL------------STPP---SPYDRD--HKV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 372 QSSLGGRVRLMVTGAapvsatvltfLRAALGC-QFYEGYGQTECTAGCCLTMPGDWTAGHVGAPMPCNLIKLVDVE---- 446
Cdd:cd05937 205 RVAWGNGLRPDIWER----------FRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRWKFENQVvlvk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 447 -----EMNYM---------AAEGE-GEVCVKGPNV----FQGYLKDPAKTAEALDK------DGWLHTGDIGKWLPNGTL 501
Cdd:cd05937 275 mdpetDDPIRdpktgfcvrAPVGEpGEMLGRVPFKnreaFQGYLHNEDATESKLVRdvfrkgDIYFRTGDLLRQDADGRW 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1832481686 502 KIIDRKKHIFKLaQGEYIAPEKIENIYMRSEPVAQVFVHGESLQ 545
Cdd:cd05937 355 YFLDRLGDTFRW-KSENVSTTEVADVLGAHPDIAEANVYGVKVP 397
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| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
456-541 |
7.72e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 45.54 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 456 EGEVCVKGPNVFQGYLKDpAKTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFkLAQGEYIAPEKIENIYMRSEPVA 535
Cdd:PRK07638 333 IGTVYVKSPQFFMGYIIG-GVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMI-LFGGINIFPEEIESVLHEHPAVD 410
|
....*.
gi 1832481686 536 QVFVHG 541
Cdd:PRK07638 411 EIVVIG 416
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
212-555 |
8.94e-05 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 212 KPKPPAPEDLAVICFTSGTTGNPKGAMVTHRNIVSdcSAfvKATENTVNPcPDDTLISfLPLAHmfervvecvmlchgak 291
Cdd:PRK07824 28 RVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTA--SA--DATHDRLGG-PGQWLLA-LPAHH---------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 292 IGFFQGDIRLLM---DDLKVLQPTVF--PVVPRLLNRM-FDRIF-GQANTTLKRWLLDFASKRKEAELRSGIIrnnslwd 364
Cdd:PRK07824 86 IAGLQVLVRSVIagsEPVELDVSAGFdpTALPRAVAELgGGRRYtSLVPMQLAKALDDPAATAALAELDAVLV------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 365 rlifhkvqsslggrvrlmvtGAAPVSATVLTflRA-ALGCQFYEGYGQTEcTAGCCLtmpgdwtagHVGAPMPCNLIKLV 443
Cdd:PRK07824 159 --------------------GGGPAPAPVLD--AAaAAGINVVRTYGMSE-TSGGCV---------YDGVPLDGVRVRVE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 444 DveemnymaaegeGEVCVKGPNVFQGY--LKDPAKTAEaldkDGWLHTGDIGKwLPNGTLKIIDRKKHIFKLAqGEYIAP 521
Cdd:PRK07824 207 D------------GRIALGGPTLAKGYrnPVDPDPFAE----PGWFRTDDLGA-LDDGVLTVLGRADDAISTG-GLTVLP 268
|
330 340 350
....*....|....*....|....*....|....*..
gi 1832481686 522 EKIENIYMRSEPVAQVFVHG---ESLQAFLIAIVVPD 555
Cdd:PRK07824 269 QVVEAALATHPAVADCAVFGlpdDRLGQRVVAAVVGD 305
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
218-513 |
8.52e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.85 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 218 PEDLAVICFTSGTTGNPKGAMVTHRNIVSDCSAFVKatenTVNPCPDDtlisflplahmfervveCVMlcHGAKIGFFQG 297
Cdd:PRK05691 2332 PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIE----RFGMRADD-----------------CEL--HFYSINFDAA 2388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 298 DIRLLmddlkvlqptvfpvVPRLLN-RMFDRIFGQanttlkrWlldfaskrkEAELRSGIIRNNSLwDRLIFHKVQSS-- 374
Cdd:PRK05691 2389 SERLL--------------VPLLCGaRVVLRAQGQ-------W---------GAEEICQLIREQQV-SILGFTPSYGSql 2437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 375 ---LGGR-----VRLMVTGAAPVSATVLTFLRAALGCQ-FYEGYGQTE-------CTAGccLTMPGDWTAGHVGAPMPCN 438
Cdd:PRK05691 2438 aqwLAGQgeqlpVRMCITGGEALTGEHLQRIRQAFAPQlFFNAYGPTEtvvmplaCLAP--EQLEEGAASVPIGRVVGAR 2515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832481686 439 LIKLVDvEEMNYMAAEGEGEVCVKGPNVFQGYLKDPAKTAEALDKDGWLH-------TGDIGKWLPNGTLKIIDRKKHIF 511
Cdd:PRK05691 2516 VAYILD-ADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdggrlyrTGDLVRLRADGLVEYVGRIDHQV 2594
|
..
gi 1832481686 512 KL 513
Cdd:PRK05691 2595 KI 2596
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
210-241 |
1.59e-03 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 41.41 E-value: 1.59e-03
10 20 30
....*....|....*....|....*....|..
gi 1832481686 210 RRKPKPPAPEDLAVICFTSGTTGNPKGAMVTH 241
Cdd:cd17634 223 EHQPEAMNAEDPLFILYTSGTTGKPKGVLHTT 254
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