|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
30-717 |
0e+00 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 824.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 30 ISLYTILTYIPFYFFSESRQEKSNRIKAKPVNSKPDSAYRSVNS-LDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTR 108
Cdd:PLN02387 1 MGAYIVGVLVPLLLTLLLRGSKKGKKRGVPVDVGGEPGYAIRNArFPELVETPWEGATTLAALFEQSCKKYSDKRLLGTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 109 EVLNEEDEVQPNGKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVT 188
Cdd:PLN02387 81 KLISREFETSSDGRKFEKLHLGEYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 189 LYATLGGPAIVHALNETEVTNIIT-SKELlqTKLKDIVSLVPRLRHIITVDGKP---PTWSEFPKGIIVHTMAAVEALGA 264
Cdd:PLN02387 161 IYASLGEEALCHSLNETEVTTVICdSKQL--KKLIDISSQLETVKRVIYMDDEGvdsDSSLSGSSNWTVSSFSEVEKLGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 265 KASMenQPHSkPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLS 344
Cdd:PLN02387 239 ENPV--DPDL-PSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVPKLGKNDVYLAYLPLAHILELAAESVMAA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 345 HGCRIGYSSPQTLADQSSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQI---- 420
Cdd:PLN02387 316 VGAAIGYGSPLTLTDTSNKIKKGTKGDASALKPTLMTAVPAILDRVRDGVRKKVDAKGGLAKKLFDIAYKRRLAAIegsw 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 421 --SKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVG 498
Cdd:PLN02387 396 fgAWGLEKLLWDALVFKKIRAVLGGRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFSEWDDTSVGRVG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 499 APLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIID 578
Cdd:PLN02387 476 PPLPCCYVKLVSWEEGGYLISDKPMPRGEIVIGGPSVTLGYFKNQEKTDEVYKVDERGMRWFYTGDIGQFHPDGCLEIID 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 579 RKKDLVKLQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLK-GTWEELCNSCEMENE 657
Cdd:PLN02387 556 RKKDIVKLQHGEYVSLGKVEAALSVSPYVDNIMVHADPFHSYCVALVVPSQQALEKWAKKAGIDySNFAELCEKEEAVKE 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 658 VLKVLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMY 717
Cdd:PLN02387 636 VQQSLSKAAKAARLEKFEIPAKIKLLPEPWTPESGLVTAALKLKREQIRKKFKDDLKKLY 695
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
130-705 |
0e+00 |
|
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: 805.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 130 GQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTN 209
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 210 IITSKEllqtklkdivslvprlrhiitvdgkpptwsefpkgiivhtmaavealgakasmenqphskplPSDIAVIMYTSG 289
Cdd:cd17639 81 IFTDGK--------------------------------------------------------------PDDLACIMYTSG 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 290 STGLPKGVMISHSNIIAGITGMAERIPE-LGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADqssKIKKGS 368
Cdd:cd17639 99 STGNPKGVMLTHGNLVAGIAGLGDRVPElLGPDDRYLAYLPLAHIFELAAENVCLYRGGTIGYGSPRTLTD---KSKRGC 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 369 KGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKGRNTPLCDSFVFRKVRSLLGGNIRLL 448
Cdd:cd17639 176 KGDLTEFKPTLMVGVPAIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTPLLDELVFKKVRAALGGRLRYM 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 449 LCGGAPLSATTQRFMNIcFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFnTDKPHPRGEI 528
Cdd:cd17639 256 LSGGAPLSADTQEFLNI-VLCPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDWEEGGYS-TDKPPPRGEI 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 529 LIGGQSVTMGYYKNEAKTKADFfedeNGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLVD 608
Cdd:cd17639 334 LIRGPNVFKGYYKNPEKTKEAF----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQNGEYIALEKLESIYRSNPLVN 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 609 NICAYANSYHSYVIGFVVPNQKELTELARKKGLK-GTWEELCNSCEMENEVLKVLSEAAISASLEKFEIPVKIRLSPEPW 687
Cdd:cd17639 410 NICVYADPDKSYPVAIVVPNEKHLTKLAEKHGVInSEWEELCEDKKLQKAVLKSLAETARAAGLEKFEIPQGVVLLDEEW 489
|
570
....*....|....*...
gi 115502350 688 TPETGLVTDAFKLKRKEL 705
Cdd:cd17639 490 TPENGLVTAAQKLKRKEI 507
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
130-717 |
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: 540.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 130 GQYNWLSYEDVFVRAFNFGNGLQMLGQK--PKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEV 207
Cdd:cd05927 1 GPYEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 208 TniitskellqtklkdivslvprlrhIITVDgkpptwsefpKGIIVHTMAAVEALGAKAsmeNQPHSKPLPSDIAVIMYT 287
Cdd:cd05927 81 S-------------------------IVFCD----------AGVKVYSLEEFEKLGKKN---KVPPPPPKPEDLATICYT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 288 SGSTGLPKGVMISHSNIIAGITGM---AERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSS--PQTLADqss 362
Cdd:cd05927 123 SGTTGNPKGVMLTHGNIVSNVAGVfkiLEILNKINPTDVYISYLPLAHIFERVVEALFLYHGAKIGFYSgdIRLLLD--- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 363 kikkgskgDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKG--RNTPLCDSFVFRKVRSL 440
Cdd:cd05927 200 --------DIKALKPTVFPGVPRVLNRIYDKIFNKVQAKGPLKRKLFNFALNYKLAELRSGvvRASPFWDKLVFNKIKQA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 441 LGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTD 520
Cdd:cd05927 272 LGGNVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKLVDVPEMNYDAKD 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 521 kPHPRGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAA 600
Cdd:cd05927 352 -PNPRGEVCIRGPNVFSGYYKDPEKTAEAL--DEDG--WLHTGDIGEWLPNGTLKIIDRKKNIFKLSQGEYVAPEKIENI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 601 LKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGL-KGTWEELCNSCEMENEVLKVLSEAAISASLEKFEIPVK 679
Cdd:cd05927 427 YARSPFVAQIFVYGDSLKSFLVAIVVPDPDVLKEWAASKGGgTGSFEELCKNPEVKKAILEDLVRLGKENGLKGFEQVKA 506
|
570 580 590
....*....|....*....|....*....|....*...
gi 115502350 680 IRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMY 717
Cdd:cd05927 507 IHLEPEPFSVENGLLTPTFKLKRPQLKKYYKKQIDEMY 544
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
68-717 |
2.28e-153 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 459.95 E-value: 2.28e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 68 YRSVNSLDGLASVL--YPGCDTLDKVFTYAKNKFKNKRLLGTRevlneedeVQPNGKIfkkvilGQYNWLSYEDVFVRAF 145
Cdd:PLN02736 24 YRSARSPLKLVSRFpdHPEIGTLHDNFVYAVETFRDYKYLGTR--------IRVDGTV------GEYKWMTYGEAGTART 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 146 NFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIv 225
Cdd:PLN02736 90 AIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEVAAIFCVPQTLNTLLSCL- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 226 SLVPRLRHIITVDGKPPTWSEFPK--GIIVHTMAAVEALGakaSMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSN 303
Cdd:PLN02736 169 SEIPSVRLIVVVGGADEPLPSLPSgtGVEIVTYSKLLAQG---RSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 304 IIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLadqsskikkGSKGDTSMLKPTLMAAV 383
Cdd:PLN02736 246 LIANVAGSSLSTK-FYPSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYQGDNL---------KLMDDLAALRPTIFCSV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 384 PEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKGRN-TPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRF 462
Cdd:PLN02736 316 PRLYNRIYDGITNAVKESGGLKERLFNAAYNAKKQALENGKNpSPMWDRLVFNKIKAKLGGRVRFMSSGASPLSPDVMEF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 463 MNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYKN 542
Cdd:PLN02736 396 LRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDVPEMNYTSEDQPYPRGEICVRGPIIFKGYYKD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 543 EAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVI 622
Cdd:PLN02736 476 EVQTREVI--DEDG--WLHTGDIGLWLPGGRLKIIDRKKNIFKLAQGEYIAPEKIENVYAKCKFVAQCFVYGDSLNSSLV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 623 GFVVPNQKELTELARKKGLK-GTWEELCNSCEMENEVLKVLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLK 701
Cdd:PLN02736 552 AVVVVDPEVLKAWAASEGIKyEDLKQLCNDPRVRAAVLADMDAVGREAQLRGFEFAKAVTLVPEPFTVENGLLTPTFKVK 631
|
650
....*....|....*.
gi 115502350 702 RKELKTHYQADIERMY 717
Cdd:PLN02736 632 RPQAKAYFAKAISDMY 647
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
130-720 |
3.71e-148 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 444.93 E-value: 3.71e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 130 GQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTN 209
Cdd:COG1022 36 GIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 210 IITSKELLQTKLKDIVSLVPRLRHIITVDGKPPtwsefPKGIIVHTMAAVEALGAKASMEN---QPHSKPLPSDIAVIMY 286
Cdd:COG1022 116 LFVEDQEQLDKLLEVRDELPSLRHIVVLDPRGL-----RDDPRLLSLDELLALGREVADPAeleARRAAVKPDDLATIIY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 287 TSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYS-SPQTLADQSSKIK 365
Cdd:COG1022 191 TSGTTGRPKGVMLTHRNLLSNARALLERLP-LGPGDRTLSFLPLAHVFERTVSYYALAAGATVAFAeSPDTLAEDLREVK 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 366 kgskgdtsmlkPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYN--YKM-EQISKGRNTP--------LCDSFVF 434
Cdd:COG1022 270 -----------PTFMLAVPRVWEKVYAGIQAKAEEAGGLKRKLFRWALAvgRRYaRARLAGKSPSlllrlkhaLADKLVF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 435 RKVRSLLGGNIRLLLCGGAPLSATTQRF---MNIcfccPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLknw 511
Cdd:COG1022 339 SKLREALGGRLRFAVSGGAALGPELARFfraLGI----PVLEGYGLTETSPVITVNRPGDNRIGTVGPPLPGVEVKI--- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 512 eeggyfntdkpHPRGEILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEY 591
Cdd:COG1022 412 -----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADG----WLHTGDIGELDEDGFLRITGRKKDLIVTSGGKN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 592 VSLGKVEAALKNLPLVDNICAYANSyHSYVIGFVVPNQKELTELARKKGLK-GTWEELCNSCEMENEVLKVLseAAISAS 670
Cdd:COG1022 477 VAPQPIENALKASPLIEQAVVVGDG-RPFLAALIVPDFEALGEWAEENGLPyTSYAELAQDPEVRALIQEEV--DRANAG 553
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 115502350 671 LEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK 720
Cdd:COG1022 554 LSRAEQIKRFRLLPKEFTIENGELTPTLKLKRKVILEKYADLIEALYAGA 603
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
101-717 |
6.13e-146 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 442.49 E-value: 6.13e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 101 NKRLLGTREVLNEEDEVQPNGKIFKKVI----LGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAA 176
Cdd:PTZ00216 84 DRRALAYRPVERVEKEVVKDADGKERTMevthFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASI 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 177 QACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKEllqtKLKDIVSLVP--RLRH--IITVDGKPPtwSEFPKGII 252
Cdd:PTZ00216 164 YGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGK----NVPNLLRLMKsgGMPNttIIYLDSLPA--SVDTEGCR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 253 VHTMAAVEALGAKASMEnqpHSKPLPS---DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPEL----GEEDVYI 325
Cdd:PTZ00216 238 LVAWTDVVAKGHSAGSH---HPLNIPEnndDLALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLigppEEDETYC 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 326 GYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKikkgSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQ 405
Cdd:PTZ00216 315 SYLPLAHIMEFGVTNIFLARGALIGFGSPRTLTDTFAR----PHGDLTEFRPVFLIGVPRIFDTIKKAVEAKLPPVGSLK 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 406 RNLFILAYNYKMEQISKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFcCPVGQGYGLTESAGAGT 485
Cdd:PTZ00216 391 RRVFDHAYQSRLRALKEGKDTPYWNEKVFSAPRAVLGGRVRAMLSGGGPLSAATQEFVNVVF-GMVIQGWGLTETVCCGG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 486 ISEVWDYNTGRVGAPLVCCEIKLKNWEEggYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDI 565
Cdd:PTZ00216 470 IQRTGDLEPNAVGQLLKGVEMKLLDTEE--YKHTDTPEPRGEILLRGPFLFKGYYKQEELTREVL--DEDG--WFHTGDV 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 566 GEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLVDN--ICAYANSYHSYVIGFVVPNQKELTELARKKGLKG 643
Cdd:PTZ00216 544 GSIAANGTLRIIGRVKALAKNCLGEYIALEALEALYGQNELVVPngVCVLVHPARSYICALVLTDEAKAMAFAKEHGIEG 623
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115502350 644 TWEELCNSCEMENEVLKVLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMY 717
Cdd:PTZ00216 624 EYPAILKDPEFQKKATESLQETARAAGRKSFEIVRHVRVLSDEWTPENGVLTAAMKLKRRVIDERYADLIKELF 697
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
130-705 |
5.74e-139 |
|
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: 415.84 E-value: 5.74e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 130 GQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTN 209
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 210 IITSKellqtklkdivslvprlrhiitvdgkpptwsefpkgiivhtmaavealgakasmenqphskplPSDIAVIMYTSG 289
Cdd:cd05907 81 LFVED---------------------------------------------------------------PDDLATIIYTSG 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 290 STGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLE-LSAELVCLSHGCRIGY-SSPQTLADQSSKIKkg 367
Cdd:cd05907 98 TTGRPKGVMLSHRNILSNALALAERLP-ATEGDRHLSFLPLAHVFErRAGLYVPLLAGARIYFaSSAETLLDDLSEVR-- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 368 skgdtsmlkPTLMAAVPEIMDRIYKNVmnKVSEMSSFQRNLFILAYnykmeqiskgrntplcdsfvfrkvrsllGGNIRL 447
Cdd:cd05907 175 ---------PTVFLAVPRVWEKVYAAI--KVKAVPGLKRKLFDLAV----------------------------GGRLRF 215
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 448 LLCGGAPLSATTQRFMNIcFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLknweeggyfntdkpHPRGE 527
Cdd:cd05907 216 AASGGAPLPAELLHFFRA-LGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRI--------------ADDGE 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 528 ILIGGQSVTMGYYKNEAKTKADFFEDengqRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLV 607
Cdd:cd05907 281 ILVRGPNVMLGYYKNPEATAEALDAD----GWLHTGDLGEIDEDGFLHITGRKKDLIITSGGKNISPEPIENALKASPLI 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 608 DNICAYANSyHSYVIGFVVPNQKELTELARKKGLKG-TWEELCNSCEMENEVLKVLSEAaiSASLEKFEIPVKIRLSPEP 686
Cdd:cd05907 357 SQAVVIGDG-RPFLVALIVPDPEALEAWAEEHGIAYtDVAELAANPAVRAEIEAAVEAA--NARLSRYEQIKKFLLLPEP 433
|
570
....*....|....*....
gi 115502350 687 WTPETGLVTDAFKLKRKEL 705
Cdd:cd05907 434 FTIENGELTPTLKLKRPVI 452
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
46-717 |
1.58e-126 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 391.10 E-value: 1.58e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 46 ESRQEKSNRIKAKPVnskpdsaYRSVNSLDGLASvLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEdevqpngkifk 125
Cdd:PLN02430 10 EGVKGKDGKPSVGPV-------YRNLLSKKGFPP-IDSDITTAWDIFSKSVEKYPDNKMLGWRRIVDGK----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 126 kviLGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNET 205
Cdd:PLN02430 71 ---VGPYMWKTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSLICVPLYDTLGPGAVDYIVDHA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 206 EVTNIITS----KELLQ------TKLKDIVSLVPRLRHIIT----VDGKPPTWSEFPKgiivhtmaaveaLGAKASMENQ 271
Cdd:PLN02430 148 EIDFVFVQdkkiKELLEpdcksaKRLKAIVSFTSVTEEESDkasqIGVKTYSWIDFLH------------MGKENPSETN 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 272 PhskPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITG----MAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGC 347
Cdd:PLN02430 216 P---PKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGvdlfMEQFEDKMTHDDVYLSFLPLAHILDRMIEEYFFRKGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 348 RIGYSSPQTLAdqsskikkgSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKG---- 423
Cdd:PLN02430 293 SVGYYHGDLNA---------LRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAWMNRGyshk 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 424 RNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNT-GRVGAPLV 502
Cdd:PLN02430 364 KASPMADFLAFRKVKAKLGGRLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTETLGPTTLGFPDEMCMlGTVGAPAV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 503 CCEIKLKNWEEGGYFNTDKPhPRGEILIGGQSVTMGYYKNEAKTkadffEDENGQRWLCTGDIGEFEPDGCLKIIDRKKD 582
Cdd:PLN02430 444 YNELRLEEVPEMGYDPLGEP-PRGEICVRGKCLFSGYYKNPELT-----EEVMKDGWFHTGDIGEILPNGVLKIIDRKKN 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 583 LVKLQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLKVL 662
Cdd:PLN02430 518 LIKLSQGEYVALEYLENVYGQNPIVEDIWVYGDSFKSMLVAVVVPNEENTNKWAKDNGFTGSFEELCSLPELKEHILSEL 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 115502350 663 SEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMY 717
Cdd:PLN02430 598 KSTAEKNKLRGFEYIKGVILETKPFDVERDLVTATLKKRRNNLLKYYQVEIDEMY 652
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
41-717 |
5.20e-126 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 389.77 E-value: 5.20e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 41 FYFFSESRQEKSN-RIKAKPVnskpdsaYRSVNSLDGLASVLyPGCDTLDKVFTYAKNKFKNKRLLGTREVLNeedevqp 119
Cdd:PLN02614 7 FIFQVEEGKEGSDgRPSVGPV-------YRSIFAKDGFPNPI-EGMDSCWDVFRMSVEKYPNNPMLGRREIVD------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 120 nGKIfkkvilGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIV 199
Cdd:PLN02614 72 -GKP------GKYVWQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 200 HALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGKPPTWSEFPK--GIIVHTMAAVEALGakasmENQPHSKPL 277
Cdd:PLN02614 145 FIISHSEVSIVFVEEKKISELFKTCPNSTEYMKTVVSFGGVSREQKEEAEtfGLVIYAWDEFLKLG-----EGKQYDLPI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 --PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERI----PELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGY 351
Cdd:PLN02614 220 kkKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLksanAALTVKDVYLSYLPLAHIFDRVIEECFIQHGAAIGF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 352 SSpqtlADQSSKIKkgskgDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKGRN----TP 427
Cdd:PLN02614 300 WR----GDVKLLIE-----DLGELKPTIFCAVPRVLDRVYSGLQKKLSDGGFLKKFVFDSAFSYKFGNMKKGQShveaSP 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 428 LCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAgAGTISEVWDY--NTGRVGAPLVCCE 505
Cdd:PLN02614 371 LCDKLVFNKVKQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESC-AGTFVSLPDEldMLGTVGPPVPNVD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 506 IKLKNWEEGGYfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDengqrWLCTGDIGEFEPDGCLKIIDRKKDLVK 585
Cdd:PLN02614 450 IRLESVPEMEY-DALASTPRGEICIRGKTLFSGYYKREDLTKEVLIDG-----WLHTGDVGEWQPNGSMKIIDRKKNIFK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 586 LQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLKVLSEA 665
Cdd:PLN02614 524 LSQGEYVAVENIENIYGEVQAVDSVWVYGNSFESFLVAIANPNQQILERWAAENGVSGDYNALCQNEKAKEFILGELVKM 603
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 115502350 666 AISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMY 717
Cdd:PLN02614 604 AKEKKMKGFEIIKAIHLDPVPFDMERDLLTPTFKKKRPQLLKYYQSVIDEMY 655
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
46-717 |
8.60e-118 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 368.40 E-value: 8.60e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 46 ESRQEKSNRIKAKPVnskpdsaYRSVNSLDGLAsVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNeedevqpnGKIfk 125
Cdd:PLN02861 11 ESRPATGGKPSAGPV-------YRSIYAKDGLL-DLPADIDSPWQFFSDAVKKYPNNQMLGRRQVTD--------SKV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 126 kvilGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNET 205
Cdd:PLN02861 73 ----GPYVWLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 206 EVTNIITSkellQTKLKDIVSLVPR----LRHIITVDGKPPTWSEFPKGIIVHTMAAVEAlgakASMENQPHSKP--LPS 279
Cdd:PLN02861 149 EVSIAFVQ----ESKISSILSCLPKcssnLKTIVSFGDVSSEQKEEAEELGVSCFSWEEF----SLMGSLDCELPpkQKT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPE----LGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGY--SS 353
Cdd:PLN02861 221 DICTIMYTSGTTGEPKGVILTNRAIIAEVLSTDHLLKVtdrvATEEDSYFSYLPLAHVYDQVIETYCISKGASIGFwqGD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 354 PQTLADqsskikkgskgDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKG----RNTPLC 429
Cdd:PLN02861 301 IRYLME-----------DVQALKPTIFCGVPRVYDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGlkqeEASPRL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 430 DSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGA--GTISEVWDYnTGRVGAPLVCCEIK 507
Cdd:PLN02861 370 DRLVFDKIKEGLGGRVRLLLSGAAPLPRHVEEFLRVTSCSVLSQGYGLTESCGGcfTSIANVFSM-VGTVGVPMTTIEAR 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNWEEGGYfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDengqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQ 587
Cdd:PLN02861 449 LESVPEMGY-DALSDVPRGEICLRGNTLFSGYHKRQDLTEEVLIDG-----WFHTGDIGEWQPNGAMKIIDRKKNIFKLS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 588 AGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLKVLSEAAI 667
Cdd:PLN02861 523 QGEYVAVENLENTYSRCPLIASIWVYGNSFESFLVAVVVPDRQALEDWAANNNKTGDFKSLCKNLKARKYILDELNSTGK 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 115502350 668 SASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMY 717
Cdd:PLN02861 603 KLQLRGFEMLKAIHLEPNPFDIERDLITPTFKLKRPQLLKYYKDCIDQLY 652
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
130-587 |
9.97e-112 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 344.30 E-value: 9.97e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 130 GQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTN 209
Cdd:pfam00501 17 GEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 210 IITSKELLQTKLKDIVSLVPRLRHIITVDGKPPTWSEfpkgiivhtmaAVEALGAKASMENQPHSKPLPSDIAVIMYTSG 289
Cdd:pfam00501 97 LITDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEE-----------PLPEEAKPADVPPPPPPPPDPDDLAYIIYTSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 290 STGLPKGVMISHSNIIAGITG---MAERIPELGEEDVYIGYLPLAHVLELSAE-LVCLSHGCRIGYSSPQTLADQsskik 365
Cdd:pfam00501 166 TTGKPKGVMLTHRNLVANVLSikrVRPRGFGLGPDDRVLSTLPLFHDFGLSLGlLGPLLAGATVVLPPGFPALDP----- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 366 KGSKGDTSMLKPTLMAAVPEIMDRIYknvmnkvsEMSSFQRNLFilaynykmeqiskgrntplcdsfvfrkvrsllgGNI 445
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLL--------EAGAPKRALL---------------------------------SSL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 446 RLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDY---NTGRVGAPLVCCEIKLKNWEEGGYFNTDKP 522
Cdd:pfam00501 280 RLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEdlrSLGSVGRPLPGTEVKIVDDETGEPVPPGEP 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115502350 523 hprGEILIGGQSVTMGYYKNEAKTKADFFEDengqRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQ 587
Cdd:pfam00501 360 ---GELCVRGPGVMKGYLNDPELTAEAFDED----GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
135-702 |
8.37e-69 |
|
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: 233.02 E-value: 8.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMynfqlvtlyatLGGPAIVHAlnetevtNIITSK 214
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMA-----------LGAVDVVRG-------SDSSVE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQTklkdivslvprLRHiitvdgkpptwSEfPKGIIVhtmaavealgakasmENQPhskplpSDIAVIMYTSGSTGLP 294
Cdd:cd17640 68 ELLYI-----------LNH-----------SE-SVALVV---------------ENDS------DDLATIIYTSGTTGNP 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 295 KGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLadqsskikkgsKGDTSM 374
Cdd:cd17640 104 KGVMLTHANLLHQIRSLSDIVP-PQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTL-----------KDDLKR 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 375 LKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAynykmeqiskgrntplcdsfvfrkvrsLLGGNIRLLLCGGAP 454
Cdd:cd17640 172 VKPHYIVSVPRLWESLYSGIQKQVSKSSPIKQFLFLFF---------------------------LSGGIFKFGISGGGA 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 455 LSATTQRFMNIcFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNwEEGGyfNTDKPHPRGEILIGGQS 534
Cdd:cd17640 225 LPPHVDTFFEA-IGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVD-PEGN--VVLPPGEKGIVWVRGPQ 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 535 VTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLVDNIcaya 614
Cdd:cd17640 301 VMKGYYKNPEATSKVL--DSDG--WFNTGDLGWLTCGGELVLTGRAKDTIVLSNGENVEPQPIEEALMRSPFIEQI---- 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 615 nsyhsYVIG--------FVVPNQKELTELARKKGLKGTWEELCNSCEME------NEVLKVLSEAAISASLEKFeipVKI 680
Cdd:cd17640 373 -----MVVGqdqkrlgaLIVPNFEELEKWAKESGVKLANDRSQLLASKKvlklykNEIKDEISNRPGFKSFEQI---APF 444
|
570 580
....*....|....*....|..
gi 115502350 681 RLSPEPWTpETGLVTDAFKLKR 702
Cdd:cd17640 445 ALLEEPFI-ENGEMTQTMKIKR 465
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
130-709 |
1.80e-60 |
|
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: 211.94 E-value: 1.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 130 GQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEvtn 209
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 210 iitSKELLQTKLKDIVSLVPrlrhiiTVDGKPPTWSEFPKGiivhTMAAVEALGAKASMENQPHSKPLPSD--IAVIMYT 287
Cdd:cd05932 79 ---SKALFVGKLDDWKAMAP------GVPEGLISISLPPPS----AANCQYQWDDLIAQHPPLEERPTRFPeqLATLIYT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 288 SGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVLELSA-ELVCLSHGCRIGYS-SPQTLADqsskik 365
Cdd:cd05932 146 SGTTGQPKGVMLTFGSFAWAAQAGIEHI-GTEENDRMLSYLPLAHVTERVFvEGGSLYGGVLVAFAeSLDTFVE------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 366 kgskgDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEmSSFQRNLFIlaynykmeqiskgrntPLCDSFVFRKVRSLLGGN- 444
Cdd:cd05932 219 -----DVQRARPTLFFSVPRLWTKFQQGVQDKIPQ-QKLNLLLKI----------------PVVNSLVKRKVLKGLGLDq 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 445 IRLLLCGGAPLS-ATTQRFMNICFccPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKnweeggyfntdkph 523
Cdd:cd05932 277 CRLAGCGSAPVPpALLEWYRSLGL--NILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRIS-------------- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 524 PRGEILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKN 603
Cdd:cd05932 341 EDGEILVRSPALMMGYYKDPEATAEAFTADG----FLRTGDKGELDADGNLTITGRVKDIFKTSKGKYVAPAPIENKLAE 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 604 LPLVDNICAyANSYHSYVIGFVVPNqkeltELARKKGLKGTWEELcnscemENEVLKVLseAAISASLEKFEIPVKIRLS 683
Cdd:cd05932 417 HDRVEMVCV-IGSGLPAPLALVVLS-----EEARLRADAFARAEL------EASLRAHL--ARVNSTLDSHEQLAGIVVV 482
|
570 580
....*....|....*....|....*.
gi 115502350 684 PEPWTPETGLVTDAFKLKRKELKTHY 709
Cdd:cd05932 483 KDPWSIDNGILTPTLKIKRNVLEKAY 508
|
|
| carboxyl_red |
NF041592 |
carboxylic acid reductase; |
204-717 |
8.36e-59 |
|
carboxylic acid reductase;
Pssm-ID: 469476 [Multi-domain] Cd Length: 1161 Bit Score: 215.97 E-value: 8.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 204 ETEVTNIITSKELLQtklkDIVSLV---PRLRHIITVDGKPPT-------------WSEFPkGIIVHTMAAVEALGAKAS 267
Cdd:NF041592 147 ETEPRVLAASVDLLD----DAVELVltgPAPRRLVVFDYHPEVddhrealeaararLADAG-PVVVETLAEVLERGRALP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 268 MENQPHSKPlPSDIAVIMYTSGSTGLPKGVMISHSNIiagiTGMAERIPELGEED-----VYIGYLPLAHVLELSAELVC 342
Cdd:NF041592 222 AAPPPASDD-DDPLALLIYTSGSTGAPKGAMYTERLV----ANMWRGSARAGWGPravpsITLNFMPMSHVMGRGTLYGT 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 343 LSHGcRIGYSSPQtlADQSSKIKkgskgDTSMLKPTLMAAVPEIMDRIYKNVMnkvSEMSSfqrnlfilaynykmeQISK 422
Cdd:NF041592 297 LARG-GTAYFAAR--SDLSTLLE-----DLALVRPTELNFVPRVWDMLFQEYQ---SELDR---------------RAAD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 423 GRNTPLCDSFVFRKVR-SLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEsAGAGTISevwdyntGRVGAPL 501
Cdd:NF041592 351 GADRAAAEAAVKAELReDLLGGRFVSAMTGSAPISAEMKAFVESLLDLHLHDGYGSTE-AGGVFID-------GRVRRPP 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 502 VCcEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTkADFFeDENGqrWLCTGDI-GEFEPDGcLKIIDRK 580
Cdd:NF041592 423 VL-DYKLVDVPELGYFGTDRPHPRGELLVKTTTMFPGYYKRPEVT-AEVF-DEDG--FYRTGDIvAELGPDQ-LVYVDRR 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 581 KDLVKLQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEElcnscemenevlk 660
Cdd:NF041592 497 NNVLKLSQGEFVTVSKLEAVFGDSPLVRQIYVYGNSARAYLLAVVVPTEEALARHGDAAELKALIAE------------- 563
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 115502350 661 VLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMY 717
Cdd:NF041592 564 SLQRVAREAGLQSYEIPRDFLIETTPFTLENGLLTGIRKLARPKLKERYGERLEQLY 620
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
135-712 |
2.13e-58 |
|
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: 204.66 E-value: 2.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEvtniitsk 214
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSG-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ellqtklkdivslvprlrhiitvdgkpptwsefPKGIIVhtmaavealgakasmenqphskplpsdiAVIMYTSGSTGLP 294
Cdd:COG0318 97 ---------------------------------ARALVT----------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 295 KGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAE-LVCLSHGCRI---GYSSPQTLADQsskIKKGskg 370
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAALG-LTPGDVVLVALPLFHVFGLTVGlLAPLLAGATLvllPRFDPERVLEL---IERE--- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 371 dtsmlKPTLMAAVPEIMDRIYknvmnkvsemssfqrnlfilaynykmeqiskgrNTPLCDSFVFRkvrsllggNIRLLLC 450
Cdd:COG0318 189 -----RVTVLFGVPTMLARLL---------------------------------RHPEFARYDLS--------SLRLVVS 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 451 GGAPLSATT-QRFMNiCFCCPVGQGYGLTESAGAGTIS--EVWDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGE 527
Cdd:COG0318 223 GGAPLPPELlERFEE-RFGVRIVEGYGLTETSPVVTVNpeDPGERRPGSVGRPLPGVEVRIVD-EDG---RELPPGEVGE 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 528 ILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLV 607
Cdd:COG0318 298 IVVRGPNVMKGYWNDPEATAEAF---RDG--WLRTGDLGRLDEDGYLYIVGRKKDMIIS-GGENVYPAEVEEVLAAHPGV 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 608 DNICAYA---NSYHSYVIGFVVPNQ-KELTElarkkglkgtwEELcnscemenevlkvlsEAAISASLEKFEIPVKIRLS 683
Cdd:COG0318 372 AEAAVVGvpdEKWGERVVAFVVLRPgAELDA-----------EEL---------------RAFLRERLARYKVPRRVEFV 425
|
570 580 590
....*....|....*....|....*....|
gi 115502350 684 PE-PWTPeTGlvtdafKLKRKELKTHYQAD 712
Cdd:COG0318 426 DElPRTA-SG------KIDRRALRERYAAG 448
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
135-634 |
1.42e-56 |
|
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: 200.52 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMynfqlvtlyatLGGPA-----------IVHALN 203
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLF-----------AGGIFsaanpiytadeLAHQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 204 ETEVTNIITSKELLQtKLKDIVSLVPRLRHIITVDGKPPTwsefpKGIIVHTMAAVealgAKASMENQP-HSKPLPSDIA 282
Cdd:cd05911 80 ISKPKVIFTDPDGLE-KVKEAAKELGPKDKIIVLDDKPDG-----VLSIEDLLSPT----LGEEDEDLPpPLKDGKDDTA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 283 VIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPE-LGEEDVYIGYLPLAHVLELSAELVCLSHGCRIgYSSPqtladqs 361
Cdd:cd05911 150 AILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGnDGSNDVILGFLPLYHIYGLFTTLASLLNGATV-IIMP------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 362 skikkgsKGDT-SML------KPTLMAAVPEIMDRIYKNvmnkvsemssfqrnlfilaynykmeqiskgrntPLCDSFVF 434
Cdd:cd05911 222 -------KFDSeLFLdliekyKITFLYLVPPIAAALAKS---------------------------------PLLDKYDL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 435 RKVRSLLggnirlllCGGAPLSATTQRFMNICFC-CPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEE 513
Cdd:cd05911 262 SSLRVIL--------SGGAPLSKELQELLAKRFPnATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 GgyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDengqRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVS 593
Cdd:cd05911 334 K---DSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDED----GWLHTGDIGYFDEDGYLYIVDRKKELIKYK-GFQVA 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 115502350 594 LGKVEAALKNLPLVDNICayansyhsyVIG------------FVVPNQ-KELTE 634
Cdd:cd05911 406 PAELEAVLLEHPGVADAA---------VIGipdevsgelpraYVVRKPgEKLTE 450
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
280-685 |
3.81e-56 |
|
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: 194.81 E-value: 3.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLAD 359
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG-LTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 360 QSSKIKKgskgdtsmLKPTLMAAVPEIMDRIyknvmnkVSEMSSFQRNLfilaynykmeqiskgrntplcdsfvfrkvRS 439
Cdd:cd04433 80 ALELIER--------EKVTILLGVPTLLARL-------LKAPESAGYDL-----------------------------SS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 440 LlggniRLLLCGGAPLS-ATTQRFMNIcFCCPVGQGYGLTESAGAGTISEVWDYNTGR--VGAPLVCCEIKLKNwEEGGy 516
Cdd:cd04433 116 L-----RALVSGGAPLPpELLERFEEA-PGIKLVNGYGLTETGGTVATGPPDDDARKPgsVGRPVPGVEVRIVD-PDGG- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 517 fnTDKPHPRGEILIGGQSVTMGYYKNEAKTkADFFEDengqRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGK 596
Cdd:cd04433 188 --ELPPGEIGELVVRGPSVMKGYWNNPEAT-AAVDED----GWYRTGDLGRLDEDGYLYIVGRLKDMIKSG-GENVYPAE 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 597 VEAALKNLPLVDnicayansyHSYVIGfvVPNQKELTELArkkglkgTWEELCNSCEMENEVLKvlseAAISASLEKFEI 676
Cdd:cd04433 260 VEAVLLGHPGVA---------EAAVVG--VPDPEWGERVV-------AVVVLRPGADLDAEELR----AHVRERLAPYKV 317
|
....*....
gi 115502350 677 PVKIRLSPE 685
Cdd:cd04433 318 PRRVVFVDA 326
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
198-695 |
1.59e-54 |
|
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: 197.29 E-value: 1.59e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 198 IVHALNETEVTNIITSKELLQTKLKdIVSLVPRLRHIITVDGKPPT-------------WSEFPKGIIVHTMAAVEALGA 264
Cdd:cd17632 132 LAPILAETEPRLLAVSAEHLDLAVE-AVLEGGTPPRLVVFDHRPEVdahraalesarerLAAVGIPVTTLTLIAVRGRDL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 265 KAS--MENQPHSKPLpsdiAVIMYTSGSTGLPKGVMISHSNIIA---GITGMAERIPELGeedVYIGYLPLAHVLELSAE 339
Cdd:cd17632 211 PPAplFRPEPDDDPL----ALLIYTSGSTGTPKGAMYTERLVATfwlKVSSIQDIRPPAS---ITLNFMPMSHIAGRISL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 340 LVCLSHGcRIGYSSPQtlADQSSKIKkgskgDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEq 419
Cdd:cd17632 284 YGTLARG-GTAYFAAA--SDMSTLFD-----DLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAE- 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 420 iskgrntplcdsfvFRKVrsLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEsAGAGTISevwdyntGRVGA 499
Cdd:cd17632 355 --------------LRER--VLGGRLLAAVCGSAPLSAEMKAFMESLLDLDLHDGYGSTE-AGAVILD-------GVIVR 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PLVCcEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYKnEAKTKADFFEDENGQRwlcTGDI-GEFEPDGcLKIID 578
Cdd:cd17632 411 PPVL-DYKLVDVPELGYFRTDRPHPRGELLVKTDTLFPGYYK-RPEVTAEVFDEDGFYR---TGDVmAELGPDR-LVYVD 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 579 RKKDLVKLQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKkglkgtweelcnscEMENEV 658
Cdd:cd17632 485 RRNNVLKLSQGEFVTVARLEAVFAASPLVRQIFVYGNSERAYLLAVVVPTQDALAGEDTA--------------RLRAAL 550
|
490 500 510
....*....|....*....|....*....|....*..
gi 115502350 659 LKVLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVT 695
Cdd:cd17632 551 AESLQRIAREAGLQSYEIPRDFLIETEPFTIANGLLS 587
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
130-609 |
7.70e-53 |
|
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: 192.57 E-value: 7.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 130 GQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVtN 209
Cdd:cd05933 4 DKWHTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEA-N 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 210 II---TSKELlqTKLKDIVSLVPRLRHIITVDGKPP-------TWSEF---PKGIIVHTMAAVealgakasMENQPhskp 276
Cdd:cd05933 83 ILvveNQKQL--QKILQIQDKLPHLKAIIQYKEPLKekepnlySWDEFmelGRSIPDEQLDAI--------ISSQK---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 277 lPSDIAVIMYTSGSTGLPKGVMISHSNI----IAGITGMAERIPELGEEDVyIGYLPLAHVlelSAEL----VCLSHGCR 348
Cdd:cd05933 149 -PNQCCTLIYTSGTTGMPKGVMLSHDNItwtaKAASQHMDLRPATVGQESV-VSYLPLSHI---AAQIldiwLPIKVGGQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 IGYSSPQTLadqsskikKGSKGDT-SMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISK----G 423
Cdd:cd05933 224 VYFAQPDAL--------KGTLVKTlREVRPTAFMGVPRVWEKIQEKMKAVGAKSGTLKRKIASWAKGVGLETNLKlmggE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 424 RNTPLC----DSFVFRKVRSLLG-GNIRLLLCGGAPLSATTQRF---MNIcfccPVGQGYGLTESAGAGTISEVWDYNTG 495
Cdd:cd05933 296 SPSPLFyrlaKKLVFKKVRKALGlDRCQKFFTGAAPISRETLEFflsLNI----PIMELYGMSETSGPHTISNPQAYRLL 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 496 RVGAPLVCCEIKLKNWEEGGYfntdkphprGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLK 575
Cdd:cd05933 372 SCGKALPGCKTKIHNPDADGI---------GEICFWGRHVFMGYLNMEDKTEEAI--DEDG--WLHSGDLGKLDEDGFLY 438
|
490 500 510
....*....|....*....|....*....|....*
gi 115502350 576 IIDRKKDLVKLQAGEYVSLGKVEAALKN-LPLVDN 609
Cdd:cd05933 439 ITGRIKELIITAGGENVPPVPIEDAVKKeLPIISN 473
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
136-712 |
5.48e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 180.38 E-value: 5.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 136 SYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKE 215
Cdd:PRK06187 33 TYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 216 LLQTkLKDIVSLVPRLRHIITVDGKP-----PTWSEFpkgiivhtmaaVEALGAKASMENQPHSKPlpSDIAVIMYTSGS 290
Cdd:PRK06187 113 FVPL-LAAILPQLPTVRTVIVEGDGPaaplaPEVGEY-----------EELLAAASDTFDFPDIDE--NDAAAMLYTSGT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 291 TGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYS---SPQTLADQsskIKKg 367
Cdd:PRK06187 179 TGHPKGVVLSHRNLFLHSLAVCAWL-KLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIPrrfDPENLLDL---IET- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 368 skgdtsmLKPTLMAAVPEIMDriyknvmnkvsemssfqrnlFILAYnykmeqiskgrntPLCDsfvFRKVRSLlggniRL 447
Cdd:PRK06187 254 -------ERVTFFFAVPTIWQ--------------------MLLKA-------------PRAY---FVDFSSL-----RL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 448 LLCGGAPLSATT-QRFMNIcFCCPVGQGYGLTESAGAGTIS-------EVWDY--NTGRVgAPLVccEIKLKNwEEGgyf 517
Cdd:PRK06187 286 VIYGGAALPPALlREFKEK-FGIDLVQGYGMTETSPVVSVLppedqlpGQWTKrrSAGRP-LPGV--EARIVD-DDG--- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 518 ntdKPHPR-----GEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKlQAGEYV 592
Cdd:PRK06187 358 ---DELPPdggevGEIIVRGPWLMQGYWNRPEATAETI---DGG--WLHTGDVGYIDEDGYLYITDRIKDVII-SGGENI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 593 SLGKVEAALKNLPLVDNICayansyhsyVIGfvVPNQKeltelarkkglkgtWEElcnscemenEVL--------KVLSE 664
Cdd:PRK06187 429 YPRELEDALYGHPAVAEVA---------VIG--VPDEK--------------WGE---------RPVavvvlkpgATLDA 474
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 115502350 665 AAISASLE----KFEIPVKIRLSPE-PWTPeTGlvtdafKLKRKELKTHYQAD 712
Cdd:PRK06187 475 KELRAFLRgrlaKFKLPKRIAFVDElPRTS-VG------KILKRVLREQYAEG 520
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
129-605 |
5.98e-49 |
|
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: 181.08 E-value: 5.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 129 LGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEW---MIAAQACFMYNfqlVTLYATLGGPAIVHALNET 205
Cdd:cd17641 6 FGIWQEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWvwaELAAQAIGALS---LGIYQDSMAEEVAYLLNYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 206 EVTNIITSKELLQTKLKDIVSLVPRLRHIITVDgkpptwsefPKGIIVHT---MAAVEALGAKASMENQPHSKPL----- 277
Cdd:cd17641 83 GARVVIAEDEEQVDKLLEIADRIPSVRYVIYCD---------PRGMRKYDdprLISFEDVVALGRALDRRDPGLYereva 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 ---PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLE----LSAELVClshGCRIG 350
Cdd:cd17641 154 agkGEDVAVLCTTSGTTGKPKLAMLSHGNFLGHCAAYLAADP-LGPGDEYVSVLPLPWIGEqmysVGQALVC---GFIVN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 351 Y-SSPQTLadqsskikkgsKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLF---------ILAYNYKMEQI 420
Cdd:cd17641 230 FpEEPETM-----------MEDLREIGPTFVLLPPRVWEGIAADVRARMMDATPFKRFMFelgmklglrALDRGKRGRPV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 421 SKGRNTP--LCDSFVFRKVRSLLG-GNIRLLLCGGAPLSATTQRF---MNIcfccPVGQGYGLTESAGAGTISEVWDYNT 494
Cdd:cd17641 299 SLWLRLAswLADALLFRPLRDRLGfSRLRSAATGGAALGPDTFRFfhaIGV----PLKQLYGQTELAGAYTVHRDGDVDP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 495 GRVGAPLVCCEIKLKNweeggyfntdkphpRGEILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCL 574
Cdd:cd17641 375 DTVGVPFPGTEVRIDE--------------VGEILVRSPGVFVGYYKNPEATAEDFDEDG----WLHTGDAGYFKENGHL 436
|
490 500 510
....*....|....*....|....*....|.
gi 115502350 575 KIIDRKKDLVKLQAGEYVSLGKVEAALKNLP 605
Cdd:cd17641 437 VVIDRAKDVGTTSDGTRFSPQFIENKLKFSP 467
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
135-607 |
9.05e-49 |
|
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: 178.40 E-value: 9.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 EllqtklkdivslvprlrhiitvdgkpptwsefpkgiivhtmaavealgakasmenqphskplpSDIAVIMYTSGSTGLP 294
Cdd:cd05914 88 E---------------------------------------------------------------DDVALINYTSGTTGNS 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 295 KGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVC-LSHGCRIGY----SSPQTLADQSSKIkkgsk 369
Cdd:cd05914 105 KGVMLTYRNIVSNVDGVKEVVL-LGKGDKILSILPLHHIYPLTFTLLLpLLNGAHVVFldkiPSAKIIALAFAQV----- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 370 gdtsmlKPTLMAAVPEIMDRIYKNV-MNKVsemsSFQRNLFILAYNYKMEQISKgrntplcdsFVFRKVRSLLGGNIRLL 448
Cdd:cd05914 179 ------TPTLGVPVPLVIEKIFKMDiIPKL----TLKKFKFKLAKKINNRKIRK---------LAFKKVHEAFGGNIKEF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 449 LCGGAPLSATTQRF---MNICFCcpvgQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKlknweeggyfnTDKPHPR 525
Cdd:cd05914 240 VIGGAKINPDVEEFlrtIGFPYT----IGYGMTETAPIISYSPPNRIRLGSAGKVIDGVEVR-----------IDSPDPA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 526 ---GEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALK 602
Cdd:cd05914 305 tgeGEIIVRGPNVMKGYYKNPEATAEAF--DKDG--WFHTGDLGKIDAEGYLYIRGRKKEMIVLSSGKNIYPEEIEAKIN 380
|
....*
gi 115502350 603 NLPLV 607
Cdd:cd05914 381 NMPFV 385
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
134-584 |
1.28e-40 |
|
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: 155.41 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 134 WLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAaqacfmynfqlvtLYATLGGPAIVHALNEtevtnIITS 213
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIA-------------YFGALKAGAVVVPLNP-----LYTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 214 KELlqtklkdivslvprlRHIITvDGKPPTwsefpkGIIVHTMAAVEALGAKASMENQPHskplPSDIAVIMYTSGSTGL 293
Cdd:cd05936 86 REL---------------EHILN-DSGAKA------LIVAVSFTDLLAAGAPLGERVALT----PEDVAVLQYTSGTTGV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 294 PKGVMISHSNIIAGITGMAERIPELGE-EDVYIGYLPLAHVLELSaelVCLSHGCRIGYS-------SPQTLADQsskIK 365
Cdd:cd05936 140 PKGAMLTHRNLVANALQIKAWLEDLLEgDDVVLAALPLFHVFGLT---VALLLPLALGATivliprfRPIGVLKE---IR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 366 KGskgdtsmlKPTLMAAVPEImdriyknvmnkvsemssfqrnlfilaYNYkmeqiskgrntpLCDSFVFRKVRSllgGNI 445
Cdd:cd05936 214 KH--------RVTIFPGVPTM--------------------------YIA------------LLNAPEFKKRDF---SSL 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 446 RLLLCGGAPLS-ATTQRFMNIcFCCPVGQGYGLTESAGAGTISEVWDYN-TGRVGAPLVCCEIKLKNwEEGgyfNTDKPH 523
Cdd:cd05936 245 RLCISGGAPLPvEVAERFEEL-TGVPIVEGYGLTETSPVVAVNPLDGPRkPGSIGIPLPGTEVKIVD-DDG---EELPPG 319
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115502350 524 PRGEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDLV 584
Cdd:cd05936 320 EVGELWVRGPQVMKGYWNRPEETAEAF---VDG--WLRTGDIGYMDEDGYFFIVDRKKDMI 375
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
278-615 |
9.14e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 156.80 E-value: 9.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAE-RIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIgysspqt 356
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKhSIFKKYNPKTHLSYLPISHIYERVIAYLSFMLGGTI------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 357 laDQSSK-IKKGSKgDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLfilaynykMEQISKGRNTPLCDSF--- 432
Cdd:PTZ00342 376 --NIWSKdINYFSK-DIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFL--------VKKILSLRKSNNNGGFskf 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 433 ------VFRKVRSLLGGNIRLLLCGGAPLSATTQR----FMNICFCcpvgQGYGLTESAGAGTISEVWDYNTGRVGAPLV 502
Cdd:PTZ00342 445 legithISSKIKDKVNPNLEVILNGGGKLSPKIAEelsvLLNVNYY----QGYGLTETTGPIFVQHADDNNTESIGGPIS 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 503 -CCEIKLKNWEEggYFNTDKPhPRGEILIGGQSVTMGYYKNEAKTKADFFEDengqRWLCTGDIGEFEPDGCLKIIDRKK 581
Cdd:PTZ00342 521 pNTKYKVRTWET--YKATDTL-PKGELLIKSDSIFSGYFLEKEQTKNAFTED----GYFKTGDIVQINKNGSLTFLDRSK 593
|
330 340 350
....*....|....*....|....*....|....
gi 115502350 582 DLVKLQAGEYVSLGKVEAALKNLPLVDNICAYAN 615
Cdd:PTZ00342 594 GLVKLSQGEYIETDMLNNLYSQISFINFCVVYGD 627
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
135-584 |
1.08e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 138.88 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQTkLKDIVSLVPRLRHIITVdgkpPTWSEFPKGIIVHTMAAVEALGAKASMENQPHskplPSDIAVIMYTSGSTGLP 294
Cdd:PRK07656 111 LFLGV-DYSATTRLPALEHVVIC----ETEEDDPHTEKMKTFTDFLAAGDPAERAPEVD----PDDVADILFTSGTTGRP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 295 KGVMISHSNIIAGITGMAErIPELGEEDVYIGYLPLAHVLELSAELV-CLSHGCRI----GYSSPQTLAdqssKIKKGsk 369
Cdd:PRK07656 182 KGAMLTHRQLLSNAADWAE-YLGLTEGDRYLAANPFFHVFGYKAGVNaPLMRGATIlplpVFDPDEVFR----LIETE-- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 370 gdtsmlKPTLMAAVPEImdriyknvmnkvsemssfqrnlfilaYNYkMEQISKGRNTPLcdsfvfrkvRSLlggniRLLL 449
Cdd:PRK07656 255 ------RITVLPGPPTM--------------------------YNS-LLQHPDRSAEDL---------SSL-----RLAV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 450 CGGA--PLsATTQRFMNICFCCPVGQGYGLTESAGAGTIS---EVWDYNTGRVGAPLVCCEIKLKNwEEGGYFNTDKPhp 524
Cdd:PRK07656 288 TGAAsmPV-ALLERFESELGVDIVLTGYGLSEASGVTTFNrldDDRKTVAGTIGTAIAGVENKIVN-ELGEEVPVGEV-- 363
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 525 rGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLV 584
Cdd:PRK07656 364 -GELLVRGPNVMKGYYDDPEATAAAI--DADG--WLHTGDLGRLDEEGYLYIVDRKKDMF 418
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
278-585 |
1.26e-34 |
|
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: 138.52 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITG-MAERIPELGEEDVYIGYLPLAHVLELSAELVCLSH-GCRI----GY 351
Cdd:cd05904 157 QDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQfVAGEGSNSDSEDVFLCVLPMFHIYGLSSFALGLLRlGATVvvmpRF 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 352 SSPQTL-ADQSSKIkkgskgdtsmlkpTLMAAVPEIMDRIYKNvmnkvsemssfqrnlfilaynykmeqiskgrntPLCD 430
Cdd:cd05904 237 DLEELLaAIERYKV-------------THLPVVPPIVLALVKS---------------------------------PIVD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 431 SFVFRKVRSLLggnirlllCGGAPLSATT-----QRFMNicfcCPVGQGYGLTESAGAGTISEVWDYNTGRVG-----AP 500
Cdd:cd05904 271 KYDLSSLRQIM--------SGAAPLGKELieafrAKFPN----VDLGQGYGMTESTGVVAMCFAPEKDRAKYGsvgrlVP 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 LVccEIKLKNWEEGgyfntdKPHP---RGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKII 577
Cdd:cd05904 339 NV--EAKIVDPETG------ESLPpnqTGELWIRGPSIMKGYLNNPEATAATI--DKEG--WLHTGDLCYIDEDGYLFIV 406
|
....*...
gi 115502350 578 DRKKDLVK 585
Cdd:cd05904 407 DRLKELIK 414
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
127-706 |
3.15e-32 |
|
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: 131.28 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 127 VILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAaqacfmynfqlvtLYATLGGPAIVHALN--- 203
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVA-------------FLAAARAGAVVAPLNpay 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 204 -ETEVTN---------IITSKELLQTKLKDIVSLVPRLRHIitvdgkpptwsEFPKGIIVHTMAAVE-ALGAKASMENQP 272
Cdd:cd05926 74 kKAEFEFyladlgsklVLTPKGELGPASRAASKLGLAILEL-----------ALDVGVLIRAPSAESlSNLLADKKNAKS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 273 HSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAeRIPELGEEDVYIGYLPLAHVLELSAelVCLShgcrigys 352
Cdd:cd05926 143 EGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAASATNIT-NTYKLTPDDRTLVVMPLFHVHGLVA--SLLS-------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 353 spqTLADQSSKIK----KGSK--GDTSMLKPTLMAAVPEIMDRIYKNVM-NKVSEMSSFqrnlfilaynykmeqiskgrn 425
Cdd:cd05926 212 ---TLAAGGSVVLpprfSASTfwPDVRDYNATWYTAVPTIHQILLNRPEpNPESPPPKL--------------------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 426 tplcdsfvfRKVRSllggnirlllcGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTIS--EVWDYNTGRVGAPlVC 503
Cdd:cd05926 268 ---------RFIRS-----------CSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSNplPPGPRKPGSVGKP-VG 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 504 CEIKLKNwEEGgyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDengqRWLCTGDIGEFEPDGCLKIIDRKKDL 583
Cdd:cd05926 327 VEVRILD-EDG---EILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKD----GWFRTGDLGYLDADGYLFLTGRIKEL 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 584 VKlQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSY---VIGFVVPnqkeltelarKKGLKGTWEELCNSCEMEnevlk 660
Cdd:cd05926 399 IN-RGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYgeeVAAAVVL----------REGASVTEEELRAFCRKH----- 462
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 115502350 661 vlseaaisasLEKFEIPVKIRLSPE-PWTPeTGlvtdafKLKRKELK 706
Cdd:cd05926 463 ----------LAAFKVPKKVYFVDElPKTA-TG------KIQRRKVA 492
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
274-634 |
3.57e-32 |
|
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: 130.04 E-value: 3.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 274 SKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAG--ITGMAEripELGEEDVYIGYLPLAHVLELSaelvclshgcriGY 351
Cdd:cd17631 93 AKVLFDDLALLMYTSGTTGRPKGAMLTHRNLLWNavNALAAL---DLGPDDVLLVVAPLFHIGGLG------------VF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 352 SSPQTLADQSSKIKKGSKGDTSML-----KPTLMAAVPEIMDRiyknvmnkvsemssfqrnlfilaynykmeqiskgrnt 426
Cdd:cd17631 158 TLPTLLRGGTVVILRKFDPETVLDlierhRVTSFFLVPTMIQA------------------------------------- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 427 pLCDSFVFRKVR--SLlggniRLLLCGGAPLSATTQRFMnICFCCPVGQGYGLTESAGAGTISEVWDYNT--GRVGAPLV 502
Cdd:cd17631 201 -LLQHPRFATTDlsSL-----RAVIYGGAPMPERLLRAL-QARGVKFVQGYGMTETSPGVTFLSPEDHRRklGSAGRPVF 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 503 CCEIKLKNwEEGgyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTkADFFEDenGqrWLCTGDIGEFEPDGCLKIIDRKKD 582
Cdd:cd17631 274 FVEVRIVD-PDG---REVPPGEVGEIVVRGPHVMAGYWNRPEAT-AAAFRD--G--WFHTGDLGRLDEDGYLYIVDRKKD 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115502350 583 LVKlQAGEYVSLGKVEAALKNLPLVDNiCAyansyhsyVIG------------FVVPNQK-ELTE 634
Cdd:cd17631 345 MII-SGGENVYPAEVEDVLYEHPAVAE-VA--------VIGvpdekwgeavvaVVVPRPGaELDE 399
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
274-707 |
2.32e-31 |
|
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: 127.08 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 274 SKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAEripELG--EEDVYIGYLPLAHVLELSAELVCLSHGCRIgY 351
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSAL---NLGltEDDNWLCALPLFHISGLSILMRSVIYGMTV-Y 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 352 SSPQTLADQSSKIKKGSKGdtsmlkpTLMAAVPEIMDRIYKNVMNKVSEmssfqrnlfilaynykmeqiskgrntplcds 431
Cdd:cd05912 148 LVDKFDAEQVLHLINSGKV-------TIISVVPTMLQRLLEILGEGYPN------------------------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 432 fvfrkvrsllggNIRLLLCGGAPLSATT-----QRfmNIcfccPVGQGYGLTESAgagtiSEVWDYN-------TGRVGA 499
Cdd:cd05912 190 ------------NLRCILLGGGPAPKPLleqckEK--GI----PVYQSYGMTETC-----SQIVTLSpedalnkIGSAGK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PLVCCEIKLKNweeggyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDR 579
Cdd:cd05912 247 PLFPVELKIED-------DGQPPYEVGEILLKGPNVTKGYLNRPDATEESF---ENG--WFKTGDIGYLDEEGFLYVLDR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 580 KKDLVkLQAGEYVSLGKVEAALKNLPLVDNICAYA---NSYHSYVIGFVVPNQkELTElarkkglkgtwEELCNSCemen 656
Cdd:cd05912 315 RSDLI-ISGGENIYPAEIEEVLLSHPAIKEAGVVGipdDKWGQVPVAFVVSER-PISE-----------EELIAYC---- 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 115502350 657 evlkvlseaaiSASLEKFEIPVKIRLSPEpwTPETGlvtdAFKLKRKELKT 707
Cdd:cd05912 378 -----------SEKLAKYKVPKKIYFVDE--LPRTA----SGKLLRHELKQ 411
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
278-642 |
2.91e-31 |
|
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: 127.36 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIgYSSPQTL 357
Cdd:cd05945 96 GDDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFP-LGPGDVFLNQAPFSFDLSVMDLYPALASGATL-VPVPRDA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 ADqsskikkgskgdtsmlKPTLMAAvpeimdRIYKNVMNKVSEMSSFQRNLFilaynykMEQISKGRNTPLCDSFVFrkv 437
Cdd:cd05945 174 TA----------------DPKQLFR------FLAEHGITVWVSTPSFAAMCL-------LSPTFTPESLPSLRHFLF--- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 438 rsllggnirlllCGGAPLSATTQRFMNiCF-CCPVGQGYGLTESAGAGTISEV-----WDYNTGRVGAPLVCCEIKLknW 511
Cdd:cd05945 222 ------------CGEVLPHKTARALQQ-RFpDARIYNTYGPTEATVAVTYIEVtpevlDGYDRLPIGYAKPGAKLVI--L 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 512 EEGGyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDEnGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEY 591
Cdd:cd05945 287 DEDG--RPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLN-GYR 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 115502350 592 VSLGKVEAALKNLPLVDNICA---YANSYHSYVIGFVVPnqKELTELARKKGLK 642
Cdd:cd05945 363 IELEEIEAALRQVPGVKEAVVvpkYKGEKVTELIAFVVP--KPGAEAGLTKAIK 414
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
276-614 |
2.40e-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: 124.42 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 276 PLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVlelsaelvclshgcrIGYSSPQ 355
Cdd:cd05903 90 AMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG-LGPGDVFLVASPMAHQ---------------TGFVYGF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 356 TLAdqsskikkgskgdtsmlkptLMAAVPEIMDRIYKnvMNKVSEMSSFQRNLFILAYNYKMEQI---SKGRNTPLCDsf 432
Cdd:cd05903 154 TLP--------------------LLLGAPVVLQDIWD--PDKALALMREHGVTFMMGATPFLTDLlnaVEEAGEPLSR-- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 433 vfrkvrsllggnIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWD-----YNTGRVGAPLvccEIK 507
Cdd:cd05903 210 ------------LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPedrrlYTDGRPLPGV---EIK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNweegGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDengqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQ 587
Cdd:cd05903 275 VVD----DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-----WFRTGDLARLDEDGYLRITGRSKDII-IR 344
|
330 340
....*....|....*....|....*..
gi 115502350 588 AGEYVSLGKVEAALKNLPLVDNICAYA 614
Cdd:cd05903 345 GGENIPVLEVEDLLLGHPGVIEAAVVA 371
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
135-613 |
4.36e-30 |
|
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: 124.89 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:TIGR03098 26 LTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQtKLKDIVSLVPRLRHIITVDGKPPTwSEFPKGIIVHTMAAVEALGAKasmenQPHSKPLPSDIAVIMYTSGSTGLP 294
Cdd:TIGR03098 106 ERLD-LLHPALPGCHDLRTLIIVGDPAHA-SEGHPGEEPASWPKLLALGDA-----DPPHPVIDSDMAAILYTSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 295 KGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVLELSAELVCLSHGCRI---GYSSPQTLADqsSKIKKGSKGd 371
Cdd:TIGR03098 179 KGVVLSHRNLVAGAQSVATYL-ENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVvlhDYLLPRDVLK--ALEKHGITG- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 372 tsmlkptlMAAVPEIMDRiyknvmnkvsemssfqrnLFILAYnykmeqiskgrntPLCDsfvFRKVRsllggniRLLLCG 451
Cdd:TIGR03098 255 --------LAAVPPLWAQ------------------LAQLDW-------------PESA---APSLR-------YLTNSG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 452 GAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTIS-EVWDYNTGRVGAPLVCCEIKLKNwEEGGYFntdKPHPRGEILI 530
Cdd:TIGR03098 286 GAMPRATLSRLRSFLPNARLFLMYGLTEAFRSTYLPpEEVDRRPDSIGKAIPNAEVLVLR-EDGSEC---APGEEGELVH 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 531 GGQSVTMGYYKNEAKTKADF-----FEDEN--GQRWLCTGDIGEFEPDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKN 603
Cdd:TIGR03098 362 RGALVAMGYWNDPEKTAERFrplppFPGELhlPELAVWSGDTVRRDEEGFLYFVGRRDEMIK-TSGYRVSPTEVEEVAYA 440
|
490
....*....|
gi 115502350 604 LPLVDNICAY 613
Cdd:TIGR03098 441 TGLVAEAVAF 450
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
278-631 |
1.66e-29 |
|
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: 122.25 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLA---HVLEL------SAELVCLSHGCR 348
Cdd:cd05930 92 PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYP-LTPGDRVLQFTSFSfdvSVWEIfgallaGATLVVLPEEVR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 igySSPQTLAD--QSSKIkkgskgdtsmlkpTLMAAVPeimdriyknvmnkvSEMSSFqrnlfilaynykMEQISKGRNT 426
Cdd:cd05930 171 ---KDPEALADllAEEGI-------------TVLHLTP--------------SLLRLL------------LQELELAALP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 427 PLcdsfvfrkvrsllggniRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTESAGAGTISEV----WDYNTGRVGAPL 501
Cdd:cd05930 209 SL-----------------RLVLVGGEALPPDLvRRWRELLPGARLVNLYGPTEATVDATYYRVppddEEDGRVPIGRPI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 502 VCCEIKLKNweEGGyfntdKPHPR---GEILIGGQSVTMGYYKNEAKTKADFFED-ENGQRWLC-TGDIGEFEPDGCLKI 576
Cdd:cd05930 272 PNTRVYVLD--ENL-----RPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPNpFGPGERMYrTGDLVRWLPDGNLEF 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 115502350 577 IDRKKDLVKLqAGEYVSLGKVEAALKNLPLVDN---ICAYANSYHSYVIGFVVPNQKE 631
Cdd:cd05930 345 LGRIDDQVKI-RGYRIELGEIEAALLAHPGVREaavVAREDGDGEKRLVAYVVPDEGG 401
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
135-610 |
5.88e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 121.22 E-value: 5.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQTKLKDIVSLVPRLrhiITVDGKPPTW-SEFPKgiivhtmaavealgakasmenqphskplpSDIAVIMYTSGSTGL 293
Cdd:PRK03640 108 DFEAKLIPGISVKFAEL---MNGPKEEAEIqEEFDL-----------------------------DEVATIMYTSGTTGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 294 PKGVMISHSNIIAGITGMAEripELG--EEDVYIGYLPLAHVLELSAELVCLSHGCRIgYSSPQTLADQSSKIKKGSKGd 371
Cdd:PRK03640 156 PKGVIQTYGNHWWSAVGSAL---NLGltEDDCWLAAVPIFHISGLSILMRSVIYGMRV-VLVEKFDAEKINKLLQTGGV- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 372 tsmlkpTLMAAVPEIMDRIyknvmnkvsemssfqrnlfilaynykMEQISKGRntplCDSfvfrkvrsllggNIRLLLCG 451
Cdd:PRK03640 231 ------TIISVVSTMLQRL--------------------------LERLGEGT----YPS------------SFRCMLLG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 452 GAPLSATT-----QRfmNIcfccPVGQGYGLTESAgagtiSEV----WDY---NTGRVGAPLVCCEIKL-KNWEEGgyfn 518
Cdd:PRK03640 263 GGPAPKPLleqckEK--GI----PVYQSYGMTETA-----SQIvtlsPEDaltKLGSAGKPLFPCELKIeKDGVVV---- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 519 tdKPHPRGEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVE 598
Cdd:PRK03640 328 --PPFEEGEIVVKGPNVTKGYLNREDATRETF---QDG--WFKTGDIGYLDEEGFLYVLDRRSDLI-ISGGENIYPAEIE 399
|
490
....*....|..
gi 115502350 599 AALKNLPLVDNI 610
Cdd:PRK03640 400 EVLLSHPGVAEA 411
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
280-607 |
6.74e-29 |
|
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: 120.47 E-value: 6.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVlelsaelvclsHGCRIGYSSPqtLAD 359
Cdd:cd05941 90 DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAW-RWTEDDVLLHVLPLHHV-----------HGLVNALLCP--LFA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 360 QSSKIKKG----SKGDTSMLKP--TLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFilaynykmeqiskgrntplcdsfv 433
Cdd:cd05941 156 GASVEFLPkfdpKEVAISRLMPsiTVFMGVPTIYTRLLQYYEAHFTDPQFARAAAA------------------------ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 434 frkvrsllgGNIRLLLCGGAPLSATT-QRFMNIcfccpVGQG----YGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKL 508
Cdd:cd05941 212 ---------ERLRLMVSGSAALPVPTlEEWEAI-----TGHTllerYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARI 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 509 KNWEEGGYFNTDKPhprGEILIGGQSVTMGYYKNEAKTKADFFEDengqRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQA 588
Cdd:cd05941 278 VDEETGEPLPRGEV---GEIQVRGPSVFKEYWNKPEATKEEFTDD----GWFKTGDLGVVDEDGYYWILGRSSVDIIKSG 350
|
330
....*....|....*....
gi 115502350 589 GEYVSLGKVEAALKNLPLV 607
Cdd:cd05941 351 GYKVSALEIERVLLAHPGV 369
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
181-641 |
1.64e-28 |
|
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: 120.13 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 181 MYNFqlvtlyaTLGGPAIVHALNETEVTNIITSKELLQtKLKdivslvprLRHIITVdgkpptwsEFPKGII-------- 252
Cdd:cd05909 60 MLNY-------TAGLRELRACIKLAGIKTVLTSKQFIE-KLK--------LHHLFDV--------EYDARIVyledlrak 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 253 ------VHTMAAVEALgAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIG 326
Cdd:cd05909 116 iskadkCKAFLAGKFP-PKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIF-DPNPEDVVFG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 327 YLPLAHVLelsaelvclshgcrigysspqtladqsskikkgskGDTSMLKPTLMAAVPEIMdriYKNVMN--KVSEMssf 404
Cdd:cd05909 194 ALPFFHSF-----------------------------------GLTGCLWLPLLSGIKVVF---HPNPLDykKIPEL--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 405 qrnlfilaynykmeqISKGRNTPLCDSFVF-----RKVRSLLGGNIRLLLCGGAPLSATT-QRFMNIcFCCPVGQGYGLT 478
Cdd:cd05909 233 ---------------IYDKKATILLGTPTFlrgyaRAAHPEDFSSLRLVVAGAEKLKDTLrQEFQEK-FGIRILEGYGTT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 479 ESAGAGTISEVW-DYNTGRVGAPLVCCEIKLKNWEeggyfnTDKPHPRGE---ILIGGQSVTMGYYKNEAKTKADFfede 554
Cdd:cd05909 297 ECSPVISVNTPQsPNKEGTVGRPLPGMEVKIVSVE------THEEVPIGEgglLLVRGPNVMLGYLNEPELTSFAF---- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 555 nGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLVDNICAYANSYHSY----VIGFVVP--- 627
Cdd:cd05909 367 -GDGWYDTGDIGKIDGEGFLTITGRLSRFAKI-AGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRkgekIVLLTTTtdt 444
|
490
....*....|....
gi 115502350 628 NQKELTELARKKGL 641
Cdd:cd05909 445 DPSSLNDILKNAGI 458
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
232-612 |
3.01e-28 |
|
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: 117.75 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 232 RHIITVDGKPPTWSEFPKGIIVHTMAAVEALGAkASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGM 311
Cdd:TIGR01733 74 RLLLTDSALASRLAGLVLPVILLDPLELAALDD-APAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 312 AERIPeLGEEDVYIGYLPLAH---VLELsaeLVCLSHG-CRIGYSSPQTLADqsskikkgskgdtsmlkptlmAAVPEIM 387
Cdd:TIGR01733 153 ARRYG-LDPDDRVLQFASLSFdasVEEI---FGALLAGaTLVVPPEDEERDD---------------------AALLAAL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 388 DRIYknvmnKVSEMSSfqrnlfilaynykmeqiskgrnTP-LCDSFVFRKVRSLLGgnIRLLLCGGAPLSATT-----QR 461
Cdd:TIGR01733 208 IAEH-----PVTVLNL----------------------TPsLLALLAAALPPALAS--LRLVILGGEALTPALvdrwrAR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 462 FMNICFCcpvgQGYGLTESAGAGTISEVWDYNTGR-----VGAPLVCCEIKLKNweeggyfNTDKPHPR---GEILIGGQ 533
Cdd:TIGR01733 259 GPGARLI----NLYGPTETTVWSTATLVDPDDAPRespvpIGRPLANTRLYVLD-------DDLRPVPVgvvGELYIGGP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 534 SVTMGYYKNEAKTKADFFED----ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDN 609
Cdd:TIGR01733 328 GVARGYLNRPELTAERFVPDpfagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIR-GYRIELGEIEAALLRHPGVRE 406
|
...
gi 115502350 610 ICA 612
Cdd:TIGR01733 407 AVV 409
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
272-609 |
5.02e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 119.33 E-value: 5.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 272 PHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIA-GITGMAeRIPELGEED-VYIGYLPLAHVLELSaelVCLSHGCRI 349
Cdd:PRK05605 212 SHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFAnAAQGKA-WVPGLGDGPeRVLAALPMFHAYGLT---LCLTLAVSI 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 350 G-----YSSPQtlADQSSKIKKGSKgdtsmlkPTLMAAVPEIMDRIYKnvmnkvsemssfqrnlfilaynykmeqISKGR 424
Cdd:PRK05605 288 GgelvlLPAPD--IDLILDAMKKHP-------PTWLPGVPPLYEKIAE---------------------------AAEER 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 425 NTPLcdsfvfrkvrsllgGNIRLLLCGGAPLSATTqrfmnicfccpVGQ-----------GYGLTES---AGAGTISEvw 490
Cdd:PRK05605 332 GVDL--------------SGVRNAFSGAMALPVST-----------VELwekltggllveGYGLTETspiIVGNPMSD-- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 491 DYNTGRVGAPLVCCEIKLKNWEeggyfNTDKPHP---RGEILIGGQSVTMGYYKNEAKTkADFFEDEngqrWLCTGDIGE 567
Cdd:PRK05605 385 DRRPGYVGVPFPDTEVRIVDPE-----DPDETMPdgeEGELLVRGPQVFKGYWNRPEET-AKSFLDG----WFRTGDVVV 454
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 115502350 568 FEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLVDN 609
Cdd:PRK05605 455 MEEDGFIRIVDRIKELI-ITGGFNVYPAEVEEVLREHPGVED 495
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
280-614 |
1.11e-27 |
|
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: 116.24 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHV--LELSAeLVCLSHGCRIgysspqTL 357
Cdd:cd05934 82 DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFG-LGEDDVYLTVLPLFHInaQAVSV-LAALSVGATL------VL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 ADQSSKikkgskgdtsmlkptlmaavpeimdriyknvmnkvsemSSFQRnlfilaynykmeQISKGRNTplcdsfvfrkV 437
Cdd:cd05934 154 LPRFSA--------------------------------------SRFWS------------DVRRYGAT----------V 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 438 RSLLGGNIRLLL----------------CGGAPLSATTQRFMNIcFCCPVGQGYGLTEsAGAGTISEVWDYN-TGRVGAP 500
Cdd:cd05934 174 TNYLGAMLSYLLaqppspddrahrlraaYGAPNPPELHEEFEER-FGVRLLEGYGMTE-TIVGVIGPRDEPRrPGSIGRP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 LVCCEIKLKNWEeggyfntDKPHPR---GEILI---GGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCL 574
Cdd:cd05934 252 APGYEVRIVDDD-------GQELPAgepGELVIrglRGWGFFKGYYNMPEATAEAM---RNG--WFHTGDLGYRDADGFF 319
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 115502350 575 KIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLVDNICAYA 614
Cdd:cd05934 320 YFVDRKKDMIR-RRGENISSAEVERAILRHPAVREAAVVA 358
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
188-584 |
7.91e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 116.21 E-value: 7.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 188 TLYATLGG---------------PAIVHALNETEVTNIITSKELLQT----KLKDIVSLVPRLRHIITVDGKPPTWSefP 248
Cdd:PRK07529 96 THFALWGGeaagianpinpllepEQIAELLRAAGAKVLVTLGPFPGTdiwqKVAEVLAALPELRTVVEVDLARYLPG--P 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 249 KGIIVHTM---AAVEALGAKASMENQPH------SKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGiTGMAERIPELG 319
Cdd:PRK07529 174 KRLAVPLIrrkAHARILDFDAELARQPGdrlfsgRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLGALLLGLG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 320 EEDVYIGYLPLAHVLELSAE-LVCLSHGCRIGYSSPQtladqsskikkGSKGdtsmlkptlmaavPEIMDRIYKNVMN-K 397
Cdd:PRK07529 253 PGDTVFCGLPLFHVNALLVTgLAPLARGAHVVLATPQ-----------GYRG-------------PGVIANFWKIVERyR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 398 VSEMSSFQRnlfilAYNYKMEQISKGRNtplcdsfvfrkVRSLlggniRLLLCGGAPLS-ATTQRFMN---IcfccPVGQ 473
Cdd:PRK07529 309 INFLSGVPT-----VYAALLQVPVDGHD-----------ISSL-----RYALCGAAPLPvEVFRRFEAatgV----RIVE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 474 GYGLTESAGAGTISEV-WDYNTGRVGAPLVCCEIK-LKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYkNEAKTKADFF 551
Cdd:PRK07529 364 GYGLTEATCVSSVNPPdGERRIGSVGLRLPYQRVRvVILDDAGRYLRDCAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWL 442
|
410 420 430
....*....|....*....|....*....|...
gi 115502350 552 EDengqRWLCTGDIGEFEPDGCLKIIDRKKDLV 584
Cdd:PRK07529 443 ED----GWLNTGDLGRIDADGYFWLTGRAKDLI 471
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
173-601 |
9.91e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.95 E-value: 9.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 173 MIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQT-KLKDIVSLVPRLRHIITVDGKPPTWSEFPKgi 251
Cdd:PRK08633 679 ALANLALLLAGKVPVNLNYTASEAALKSAIEQAQIKTVITSRKFLEKlKNKGFDLELPENVKVIYLEDLKAKISKVDK-- 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 252 ivhTMAAVEALGAKASM-ENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPL 330
Cdd:PRK08633 757 ---LTALLAARLLPARLlKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFN-LRNDDVILSSLPF 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 331 AHVLELSAEL-VCLSHGCRIGYSSPQTLADQSSK-IKKgskgdtsmLKPTLMAAVPEIMdRIY-KNvmNKVS-EMssFQR 406
Cdd:PRK08633 833 FHSFGLTVTLwLPLLEGIKVVYHPDPTDALGIAKlVAK--------HRATILLGTPTFL-RLYlRN--KKLHpLM--FAS 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 407 NLFILAYNYKMeqiskgrNTPLCDSFVFRKvrsllggNIRLLlcggaplsattqrfmnicfccpvgQGYGLTESAGAGTI 486
Cdd:PRK08633 900 LRLVVAGAEKL-------KPEVADAFEEKF-------GIRIL------------------------EGYGATETSPVASV 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 487 S-------EVW---DYNTGRVGAPLVCCEIKLKNWEeggyfnTDKPHPRGE---ILIGGQSVTMGYYKNEAKTkADFFED 553
Cdd:PRK08633 942 NlpdvlaaDFKrqtGSKEGSVGMPLPGVAVRIVDPE------TFEELPPGEdglILIGGPQVMKGYLGDPEKT-AEVIKD 1014
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 115502350 554 ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAAL 601
Cdd:PRK08633 1015 IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKI-GGEMVPLGAVEEEL 1061
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
136-601 |
3.05e-26 |
|
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: 113.39 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 136 SYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKE 215
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 216 LLQtKLKDIVSLVPRLRHIITVDGKPP--TWSEFPKGIIVHTMAAVEALGAKasmenqPHSKPLPSDIAVIMYTSGSTGL 293
Cdd:cd17642 126 GLQ-KVLNVQKKLKIIKTIIILDSKEDykGYQCLYTFITQNLPPGFNEYDFK------PPSFDRDEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 294 PKGVMISHSNIIAGITgmAERIPELG----EEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSP-------QTLADQss 362
Cdd:cd17642 199 PKGVQLTHKNIVARFS--HARDPIFGnqiiPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKfeeelflRSLQDY-- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 363 kikkgsKGDTSMLKPTLMAAVPEimdriyknvmnkvsemssfqrnlfilaynykmeqiskgrnTPLCDSFVFrkvrsllg 442
Cdd:cd17642 275 ------KVQSALLVPTLFAFFAK----------------------------------------STLVDKYDL-------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 443 GNIRLLLCGGAPLSATTQRFMNICFCCP-VGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGgyfNTDK 521
Cdd:cd17642 301 SNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDTG---KTLG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 522 PHPRGEILIGGQSVTMGYYKNEAKTKAdfFEDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAAL 601
Cdd:cd17642 378 PNERGELCVKGPMIMKGYVNNPEATKA--LIDKDG--WLHSGDIAYYDEDGHFFIVDRLKSLIKYK-GYQVPPAELESIL 452
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
136-593 |
1.61e-25 |
|
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: 111.18 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 136 SYEDVFVRAFNFGNGLQMLGQKPKTNIAIFcetraewmiaaqacfMYNFQ--LVTLYATLGGPAIVHALN---------- 203
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATL---------------AWNTHrhLELYYAVPGMGAVLHTINprlfpeqiay 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 204 -----ETEVtnIITSKELLQtKLKDIVSLVPRLRHIITVDGKPPTWSEFPKGIIvhtmaAVEALGAKASMEnqphsKPLP 278
Cdd:cd12119 92 iinhaEDRV--VFVDRDFLP-LLEAIAPRLPTVEHVVVMTDDAAMPEPAGVGVL-----AYEELLAAESPE-----YDWP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 279 S----DIAVIMYTSGSTGLPKGVMISHSNII--AGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYS 352
Cdd:cd12119 159 DfdenTAAAICYTSGTTGNPKGVVYSHRSLVlhAMAALLTDGLG-LSESDVVLPVVPMFHVNAWGLPYAAAMVGAKLVLP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 353 SPQTLADQSSKIKKGSKgdtsmlkPTLMAAVPEImdriYKNVMNkvsEMSSFQRNLFILaynykmeqiskgrntplcdsf 432
Cdd:cd12119 238 GPYLDPASLAELIEREG-------VTFAAGVPTV----WQGLLD---HLEANGRDLSSL--------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 433 vfrkvrsllggniRLLLCGGA--PLS---ATTQRFMNICfccpvgQGYGLTESAGAGTIS------------EVWDY--N 493
Cdd:cd12119 283 -------------RRVVIGGSavPRSlieAFEERGVRVI------HAWGMTETSPLGTVArppsehsnlsedEQLALraK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 494 TGRVgAPLVccEIKLKNwEEGGyfntDKPH---PRGEILIGGQSVTMGYYKNEAKTKadfFEDENGqrWLCTGDIGEFEP 570
Cdd:cd12119 344 QGRP-VPGV--ELRIVD-DDGR----ELPWdgkAVGELQVRGPWVTKSYYKNDEESE---ALTEDG--WLRTGDVATIDE 410
|
490 500
....*....|....*....|...
gi 115502350 571 DGCLKIIDRKKDLVKlQAGEYVS 593
Cdd:cd12119 411 DGYLTITDRSKDVIK-SGGEWIS 432
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
134-609 |
1.00e-24 |
|
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: 108.15 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 134 WLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITS 213
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 214 KELLQtklkdivslvpRLRHIITVdgkpptwsefpkgiivhTMAAVEALGAKASmenQPHSKPLPSDIAVIMYTSGSTGL 293
Cdd:cd12116 92 DALPD-----------RLPAGLPV-----------------LLLALAAAAAAPA---APRTPVSPDDLAYVIYTSGSTGR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 294 PKGVMISHSNIIAGITGMAERiPELGEEDVYIGYLPLA---HVLELsaeLVCLSHGCRIGYSSPQTLADqsskiKKGSKG 370
Cdd:cd12116 141 PKGVVVSHRNLVNFLHSMRER-LGLGPGDRLLAVTTYAfdiSLLEL---LLPLLAGARVVIAPRETQRD-----PEALAR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 371 DTSMLKPTLMAAVPeimdriyknvmnkvsemsSFQRNLFilaynykmeqiSKGrntplcdsfvFRKVRSLlggnirLLLC 450
Cdd:cd12116 212 LIEAHSITVMQATP------------------ATWRMLL-----------DAG----------WQGRAGL------TALC 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 451 GGAPLSATTQRFmnicFCCPVGQG---YGLTESAGAGTISEVWDYNTG-RVGAPLVcceiklknweeggyfNTD------ 520
Cdd:cd12116 247 GGEALPPDLAAR----LLSRVGSLwnlYGPTETTIWSTAARVTAAAGPiPIGRPLA---------------NTQvyvlda 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 521 --KPHPR---GEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYV 592
Cdd:cd12116 308 alRPVPPgvpGELYIGGDGVAQGYLGRPALTAERFVPDpfaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIR-GHRI 386
|
490
....*....|....*..
gi 115502350 593 SLGKVEAALKNLPLVDN 609
Cdd:cd12116 387 ELGEIEAALAAHPGVAQ 403
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
257-627 |
2.24e-24 |
|
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: 107.36 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 257 AAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAH---- 332
Cdd:cd12114 104 VLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRF-AVGPDDRVLALSSLSFdlsv 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 333 -----VLELSAELVCLSHGCRigySSPQTLAD--QSSKIkkgskgdtsmlkpTLMAAVPEIMdriyknvmnkvsEMssfq 405
Cdd:cd12114 183 ydifgALSAGATLVLPDEARR---RDPAHWAEliERHGV-------------TLWNSVPALL------------EM---- 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 406 rnlfilaynykmeqiskgrntpLCDsfVFRKVRSLLGGnIRLLLCGG--APLS---ATTQRFMNicfCCPVGQGyGLTES 480
Cdd:cd12114 231 ----------------------LLD--VLEAAQALLPS-LRLVLLSGdwIPLDlpaRLRALAPD---ARLISLG-GATEA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 481 AGAGTISEVWDYNTGRV----GAPLvcceiklknweEGGYFNTDKPHPR-------GEILIGGQSVTMGYYKNEAKTKAD 549
Cdd:cd12114 282 SIWSIYHPIDEVPPDWRsipyGRPL-----------ANQRYRVLDPRGRdcpdwvpGELWIGGRGVALGYLGDPELTAAR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 550 FFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDNICA--YANSYHSYVIGFVVP 627
Cdd:cd12114 351 FVTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR-GYRIELGEIEAALQAHPGVARAVVvvLGDPGGKRLAAFVVP 429
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
150-688 |
3.57e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.17 E-value: 3.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 150 GLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK--------ELLQTKL 221
Cdd:PRK12583 61 GLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafktsdyhAMLQELL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 222 KDIVSL---------VPRLRHIITVDGKPP----TWSEFPKGIIVHTMAAVEALGAKASmenqphskplPSDIAVIMYTS 288
Cdd:PRK12583 141 PGLAEGqpgalacerLPELRGVVSLAPAPPpgflAWHELQARGETVSREALAERQASLD----------RDDPINIQYTS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 289 GSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAH----VLelsAELVCLSHGCRIGYssPQTLADQSSKI 364
Cdd:PRK12583 211 GTTGFPKGATLSHHNILNNGYFVAESL-GLTEHDRLCVPVPLYHcfgmVL---ANLGCMTVGACLVY--PNEAFDPLATL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 365 KKGSKGdtsmlKPTLMAAVPEIMdriyknvmnkVSEMSSFQRNLFILAynykmeqiskgrntplcdsfvfrkvrsllggN 444
Cdd:PRK12583 285 QAVEEE-----RCTALYGVPTMF----------IAELDHPQRGNFDLS-------------------------------S 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 445 IRLLLCGGAP-LSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGR---VGAPLVCCEIKLKNwEEGgyfNTD 520
Cdd:PRK12583 319 LRTGIMAGAPcPIEVMRRVMDEMHMAEVQIAYGMTETSPVSLQTTAADDLERRvetVGRTQPHLEVKVVD-PDG---ATV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 521 KPHPRGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAA 600
Cdd:PRK12583 395 PRGEIGELCTRGYSVMKGYWNNPEATAESI--DEDG--WMHTGDLATMDEQGYVRIVGRSKDMI-IRGGENIYPREIEEF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 601 LKNLPLVDNIcayansyhsYVIGfvVPNQKELTELAR----KKGLKGTWEELCNSCEmenevlkvlseaaisASLEKFEI 676
Cdd:PRK12583 470 LFTHPAVADV---------QVFG--VPDEKYGEEIVAwvrlHPGHAASEEELREFCK---------------ARIAHFKV 523
|
570
....*....|...
gi 115502350 677 PVKIRLSPE-PWT 688
Cdd:PRK12583 524 PRYFRFVDEfPMT 536
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
280-630 |
8.33e-24 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 103.12 E-value: 8.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNII-AGITGMAerIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCR---IGYSSPQ 355
Cdd:cd17637 1 DPFVIIHTAAVAGRPRGAVLSHGNLIaANLQLIH--AMGLTEADVYLNMLPLFHIAGLNLALATFHAGGAnvvMEKFDPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 356 TLAD--QSSKIkkgskgdtsmlkpTLMAAVPEIMDRIyknvmnkvsemssfqrnlfilaynykMEQISKGRntplcdsfv 433
Cdd:cd17637 79 EALEliEEEKV-------------TLMGSFPPILSNL--------------------------LDAAEKSG--------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 434 fRKVRSLlggniRLLLCGGAPlsATTQRFMNIC---FCCpvgqGYGLTESAGAGTISEVWDyNTGRVGAPLVCCEIKLKN 510
Cdd:cd17637 111 -VDLSSL-----RHVLGLDAP--ETIQRFEETTgatFWS----LYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVD 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 511 weeggyfNTDKPHPR---GEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRK--KDLVK 585
Cdd:cd17637 178 -------DNDRPVPAgetGEIVVRGPLVFQGYWNLPELTAYTF---RNG--WHHTGDLGRFDEDGYLWYAGRKpeKELIK 245
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 115502350 586 lQAGEYVSLGKVEAALKNLPLVDNICayansyhsyVIGfvVPNQK 630
Cdd:cd17637 246 -PGGENVYPAEVEKVILEHPAIAEVC---------VIG--VPDPK 278
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
276-607 |
6.61e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 103.30 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 276 PLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITG----MAERIPElGEEdVYIGYLPLAHVLELS----AELVCLSHGC 347
Cdd:PRK05677 204 PQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQcralMGSNLNE-GCE-ILIAPLPLYHIYAFTfhcmAMMLIGNHNI 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 348 RIgySSPQTLAdqsskikkgskgdtSMLKptlmaavpeimdriyknvmnkvsEMSSFQRNLFIlaynykmeqiskGRNT- 426
Cdd:PRK05677 282 LI--SNPRDLP--------------AMVK-----------------------ELGKWKFSGFV------------GLNTl 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 427 --PLCDSFVFRKvrsLLGGNIRLLLCGGAPL-SATTQRFMNICfCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVC 503
Cdd:PRK05677 311 fvALCNNEAFRK---LDFSALKLTLSGGMALqLATAERWKEVT-GCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPS 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 504 CEIKLKNwEEGGYFNTDKPhprGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDL 583
Cdd:PRK05677 387 TLCKVID-DDGNELPLGEV---GELCVKGPQVMKGYWQRPEATDEIL--DSDG--WLKTGDIALIQEDGYMRIVDRKKDM 458
|
330 340
....*....|....*....|....
gi 115502350 584 VkLQAGEYVSLGKVEAALKNLPLV 607
Cdd:PRK05677 459 I-LVSGFNVYPNELEDVLAALPGV 481
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
134-584 |
8.82e-23 |
|
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: 103.09 E-value: 8.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 134 WLSYEDVFVRAFNFGNGLQMLGqKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPA---IVHALNETEVTNI 210
Cdd:cd05931 24 TLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRHaerLAAILADAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 211 ITSKELLqtklkdivSLVPRLRHIITVDGKPPTWsefpkgiivhTMAAVEALGAKASMENQPHskplPSDIAVIMYTSGS 290
Cdd:cd05931 103 LTTAAAL--------AAVRAFAASRPAAGTPRLL----------VVDLLPDTSAADWPPPSPD----PDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 291 TGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAH----VLELSAELVClshgcriGYSSpqtladqsskikk 366
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAY-GLDPGDVVVSWLPLYHdmglIGGLLTPLYS-------GGPS------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 367 gskgdtsmlkpTLMAAVpeimdriyknvmnkvsemsSF-QRNLFILaynykmEQISKGRNT----PlcdSFVF----RKV 437
Cdd:cd05931 220 -----------VLMSPA-------------------AFlRRPLRWL------RLISRYRATisaaP---NFAYdlcvRRV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 438 RS--LLG---GNIRLLLCGGAPLSATT-QRFMNiCFcCPVG-------QGYGLTES--------AGAGTISEVWDY---- 492
Cdd:cd05931 261 RDedLEGldlSSWRVALNGAEPVRPATlRRFAE-AF-APFGfrpeafrPSYGLAEAtlfvsggpPGTGPVVLRVDRdala 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 493 NTGRVGAP-------LVCC-------EIKLKNWEeggyfnTDKPHPR---GEILIGGQSVTMGYYKNEAKTKADFF---- 551
Cdd:cd05931 339 GRAVAVAAddpaareLVSCgrplpdqEVRIVDPE------TGRELPDgevGEIWVRGPSVASGYWGRPEATAETFGalaa 412
|
490 500 510
....*....|....*....|....*....|...
gi 115502350 552 EDENGqrWLCTGDIGeFEPDGCLKIIDRKKDLV 584
Cdd:cd05931 413 TDEGG--WLRTGDLG-FLHDGELYITGRLKDLI 442
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
280-709 |
1.04e-22 |
|
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: 99.71 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVCLSHGcrigysSPQTLAD 359
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLG-FGGGDSWLLSLPLYHVGGLAILVRSLLAG------AELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 360 QSSKIKKgskgDTSMLKPTLMAAVPEIMDRIyknvmnkvsemssfqrnlfilaynykmeqiskgrntpLCDSFVFRKVRS 439
Cdd:cd17630 74 RNQALAE----DLAPPGVTHVSLVPTQLQRL-------------------------------------LDSGQGPAALKS 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 440 LlggniRLLLCGGAPLS------ATTQRFmnicfccPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLknwee 513
Cdd:cd17630 113 L-----RAVLLGGAPIPpellerAADRGI-------PLYTTYGMTETASQVATKRPDGFGRGGVGVLLPGRELRI----- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 ggyfntdkpHPRGEILIGGQSVTMGYYKNEakTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVS 593
Cdd:cd17630 176 ---------VEDGEIWVGGASLAMGYLRGQ--LVPEFNEDG----WFTTKDLGELHADGRLTVLGRADNMI-ISGGENIQ 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 594 LGKVEAALKNLPLVDNICAYA---NSYHSYVIGFVVPNQKELTelarkkglkgtwEELcnscemenevlkvlsEAAISAS 670
Cdd:cd17630 240 PEEIEAALAAHPAVRDAFVVGvpdEELGQRPVAVIVGRGPADP------------AEL---------------RAWLKDK 292
|
410 420 430
....*....|....*....|....*....|....*....
gi 115502350 671 LEKFEIPVKIRlsPEPWTPETGLVtdafKLKRKELKTHY 709
Cdd:cd17630 293 LARFKLPKRIY--PVPELPRTGGG----KVDRRALRAWL 325
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
272-637 |
6.33e-22 |
|
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: 101.86 E-value: 6.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 272 PHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAH---VLELsaeLVCLSHGCR 348
Cdd:COG1020 610 PPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYG-LGPGDRVLQFASLSFdasVWEI---FGALLSGAT 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 I------GYSSPQTLAD--QSSKIkkgskgdtsmlkpTLMAAVPeimdriyknvmnkvsemSSFQrnlfilaynykmeqi 420
Cdd:COG1020 686 LvlappeARRDPAALAEllARHRV-------------TVLNLTP-----------------SLLR--------------- 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 421 skgrntPLCDSfVFRKVRSLlggniRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGR--- 496
Cdd:COG1020 721 ------ALLDA-APEALPSL-----RLVLVGGEALPPELvRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGgsv 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 497 -VGAPLVcceiklknweeggyfNT-----DK---PHP---RGEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLC 561
Cdd:COG1020 789 pIGRPIA---------------NTrvyvlDAhlqPVPvgvPGELYIGGAGLARGYLNRPELTAERFVADpfgFPGARLYR 853
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115502350 562 TGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDNICAYA---NSYHSYVIGFVVPNQKELTELAR 637
Cdd:COG1020 854 TGDLARWLPDGNLEFLGRADDQVKIR-GFRIELGEIEAALLQHPGVREAVVVAredAPGDKRLVAYVVPEAGAAAAAAL 931
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
262-653 |
5.32e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 97.59 E-value: 5.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 262 LGAKASMenQPHSKPLpSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEE---------DVYIGYLPLAH 332
Cdd:PRK12492 193 QGRGLSL--KPVPVGL-DDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDgqplmkegqEVMIAPLPLYH 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 333 VLELSAELVCL----SHGCRIgySSPqtladqsskikkgskgdtsmlkptlmaavpeimdriyKNVMNKVSEMSSFQRNL 408
Cdd:PRK12492 270 IYAFTANCMCMmvsgNHNVLI--TNP-------------------------------------RDIPGFIKELGKWRFSA 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 409 FIlaynykmeqiskGRNT---PLCDSFVFRKVRSllgGNIRLLLCGGAPL-SATTQRFMNICfCCPVGQGYGLTESAGA- 483
Cdd:PRK12492 311 LL------------GLNTlfvALMDHPGFKDLDF---SALKLTNSGGTALvKATAERWEQLT-GCTIVEGYGLTETSPVa 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 484 -----GTISEVwdyntGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKadffEDENGQR 558
Cdd:PRK12492 375 stnpyGELARL-----GTVGIPVPGTALKVID-DDG---NELPLGERGELCIKGPQVMKGYWQQPEATA----EALDAEG 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 559 WLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLVDNiCAyansyhsyVIGfvVPNQK-----ELT 633
Cdd:PRK12492 442 WFKTGDIAVIDPDGFVRIVDRKKDLI-IVSGFNVYPNEIEDVVMAHPKVAN-CA--------AIG--VPDERsgeavKLF 509
|
410 420
....*....|....*....|
gi 115502350 634 ELARKKGLkgTWEELCNSCE 653
Cdd:PRK12492 510 VVARDPGL--SVEELKAYCK 527
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-630 |
7.91e-21 |
|
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: 94.65 E-value: 7.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNII--AGITGMAERipeLGEEDVYIGYLPLAHVLELS-AELVCLSHGCRIGYssP 354
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVnnGYFIGERLG---LTEQDRLCIPVPLFHCFGSVlGVLACLTHGATMVF--P 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 355 QTLADQSSKIKKGSKGdtsmlKPTLMAAVPEImdriyknvmnkvsemssFQRNLfilaynykmeqiskgrNTPLCDSFVF 434
Cdd:cd05917 76 SPSFDPLAVLEAIEKE-----KCTALHGVPTM-----------------FIAEL----------------EHPDFDKFDL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 435 rkvrsllgGNIRLLLCGGAPL-SATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWD-----YNTgrVGAPLVCCEIKL 508
Cdd:cd05917 118 --------SSLRTGIMAGAPCpPELMKRVIEVMNMKDVTIAYGMTETSPVSTQTRTDDsiekrVNT--VGRIMPHTEAKI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 509 KNwEEGGyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKadffEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVkLQA 588
Cdd:cd05917 188 VD-PEGG--IVPPVGVPGELCIRGYSVMKGYWNDPEKTA----EAIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRG 259
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 115502350 589 GEYVSLGKVEAALKNLPLVDNICayansyhsyVIGfvVPNQK 630
Cdd:cd05917 260 GENIYPREIEEFLHTHPKVSDVQ---------VVG--VPDER 290
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
135-634 |
9.31e-21 |
|
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: 96.58 E-value: 9.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFmynfqLVTLYATLGGPAIVHALNETEVTNIitsK 214
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACV-----LAGFVPAPLTVPPTYDEPNARLRKL---R 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQTKLKDIV----SLVPRLRHIITVDGKPptwsefpkgiiVHTMAAVEALGAKASMENQPHSkpLPSDIAVIMYTSGS 290
Cdd:cd05906 112 HIWQLLGSPVVltdaELVAEFAGLETLSGLP-----------GIRVLSIEELLDTAADHDLPQS--RPDDLALLMLTSGS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 291 TGLPKGVMISHSNIIAGITGmAERIPELGEEDVYIGYLPLAHV---LELSAELVCLshGCR-IGYSSPQTLADqsskikk 366
Cdd:cd05906 179 TGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFLNWVPLDHVgglVELHLRAVYL--GCQqVHVPTEEILAD------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 367 gskgdtsmlkPTLMAavpEIMDRiyknvmNKVSEmsSFQRNlFILAYnykmeqiskgrntpLCDSFVFRKVRSLLGGNIR 446
Cdd:cd05906 249 ----------PLRWL---DLIDR------YRVTI--TWAPN-FAFAL--------------LNDLLEEIEDGTWDLSSLR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 447 LLLCGGAPLSA-TTQRFMNICFCCPVGQ-----GYGLTESAgAGTIsevWD-----YNTGR------VGAPLVCCEIKLK 509
Cdd:cd05906 293 YLVNAGEAVVAkTIRRLLRLLEPYGLPPdairpAFGMTETC-SGVI---YSrsfptYDHSQalefvsLGRPIPGVSMRIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 510 NWEEGGyfntdKPHPR-GEILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGeFEPDGCLKIIDRKKDLVKLQA 588
Cdd:cd05906 369 DDEGQL-----LPEGEvGRLQVRGPVVTKGYYNNPEANAEAFTEDG----WFRTGDLG-FLDNGNLTITGRTKDTIIVNG 438
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 115502350 589 GEYvSLGKVEAALKNLPLVDnicayansyHSYVIGFVVPNQKELTE 634
Cdd:cd05906 439 VNY-YSHEIEAAVEEVPGVE---------PSFTAAFAVRDPGAETE 474
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
278-605 |
1.81e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 95.82 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIagiTGMAERI----PELG--EEDVYIGYLPLAHVLELSAELVClshGCRIGy 351
Cdd:PLN02246 178 PDDVVALPYSSGTTGLPKGVMLTHKGLV---TSVAQQVdgenPNLYfhSDDVILCVLPMFHIYSLNSVLLC---GLRVG- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 352 sspqtladqsSKIKKGSKGDTSML-------KPTLMAAVPEIMDRIYKNVMNKVSEMSSfqrnlfilaynykmeqiskgr 424
Cdd:PLN02246 251 ----------AAILIMPKFEIGALleliqrhKVTIAPFVPPIVLAIAKSPVVEKYDLSS--------------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 425 ntplcdsfvfrkvrsllggnIRLLLCGGAPL-----SATTQRFMNICFccpvGQGYGLTEsagAGTI--------SEVWD 491
Cdd:PLN02246 300 --------------------IRMVLSGAAPLgkeleDAFRAKLPNAVL----GQGYGMTE---AGPVlamclafaKEPFP 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 492 YNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPD 571
Cdd:PLN02246 353 VKSGSCGTVVRNAELKIVDPETGASLPRNQP---GEICIRGPQIMKGYLNDPEATANTI--DKDG--WLHTGDIGYIDDD 425
|
330 340 350
....*....|....*....|....*....|....
gi 115502350 572 GCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 605
Cdd:PLN02246 426 DELFIVDRLKELIKYK-GFQVAPAELEALLISHP 458
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
286-692 |
2.16e-20 |
|
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: 95.06 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 286 YTSGSTGLPKGVMISH--------SNIIAGitgmaeripELGEEDVYIGYLPLAHvlelsaelvclshgCRiGYSSPQTL 357
Cdd:cd12118 140 YTSGTTGRPKGVVYHHrgaylnalANILEW---------EMKQHPVYLWTLPMFH--------------CN-GWCFPWTV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 AdqsskikkgSKGDTSMLKPTLMAavPEIMDRIYKNvmnKVSEMSSFQRNLFILAynykmeqiskgrNTPLCDsfvfrkv 437
Cdd:cd12118 196 A---------AVGGTNVCLRKVDA--KAIYDLIEKH---KVTHFCGAPTVLNMLA------------NAPPSD------- 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 438 RSLLGGNIRLLLCGGAPLSATTQRFMNICFCcpVGQGYGLTESAGAGTISEvW--DYNT----------GRVGAPLVcce 505
Cdd:cd12118 243 ARPLPHRVHVMTAGAPPPAAVLAKMEELGFD--VTHVYGLTETYGPATVCA-WkpEWDElpteerarlkARQGVRYV--- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 506 ikLKNWEEGGYFNTDKPHPR-----GEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRK 580
Cdd:cd12118 317 --GLEEVDVLDPETMKPVPRdgktiGEIVFRGNIVMKGYLKNPEATAEAF---RGG--WFHSGDLAVIHPDGYIEIKDRS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 581 KDLVkLQAGEYVSLGKVEAALKNLPLVdnicayansYHSYVIGfvVPNQKeLTE-----LARKKGLKGTWEELCNSCEme 655
Cdd:cd12118 390 KDII-ISGGENISSVEVEGVLYKHPAV---------LEAAVVA--RPDEK-WGEvpcafVELKEGAKVTEEEIIAFCR-- 454
|
410 420 430
....*....|....*....|....*....|....*..
gi 115502350 656 nevlkvlseaaisASLEKFEIPVKIRLSPEPWTPeTG 692
Cdd:cd12118 455 -------------EHLAGFMVPKTVVFGELPKTS-TG 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
278-612 |
2.20e-20 |
|
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: 94.92 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDvyigylplaHVLELSAelvclshgcrigYSSpqtl 357
Cdd:cd05918 105 PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALG-LTSES---------RVLQFAS------------YTF---- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 adqsskikkgskgDTSMLK--PTLMA----AVPEIMDRiyknvMNKVSE-MSSFQRNLFILaynykmeqiskgrnTPlcd 430
Cdd:cd05918 159 -------------DVSILEifTTLAAggclCIPSEEDR-----LNDLAGfINRLRVTWAFL--------------TP--- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 431 SFVF----RKVRSLlggniRLLLCGGAPLSATTQ-------RFMNicfccpvgqGYGLTESAGAGTISEVWDYNTGR-VG 498
Cdd:cd05918 204 SVARlldpEDVPSL-----RTLVLGGEALTQSDVdtwadrvRLIN---------AYGPAECTIAATVSPVVPSTDPRnIG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 499 APL-VCCEIKLKNweeggyfNTDKPHPR---GEILIGGQSVTMGYYKNEAKTKADFFEDengQRWLC------------T 562
Cdd:cd05918 270 RPLgATCWVVDPD-------NHDRLVPIgavGELLIEGPILARGYLNDPEKTAAAFIED---PAWLKqegsgrgrrlyrT 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 115502350 563 GDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKN-LPLVDNICA 612
Cdd:cd05918 340 GDLVRYNPDGSLEYVGRKDTQVKIR-GQRVELGEIEHHLRQsLPGAKEVVV 389
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
272-627 |
8.33e-20 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 93.11 E-value: 8.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 272 PHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLA---HVLELsaeLVCLSHGCR 348
Cdd:cd17646 131 PLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYP-LGPGDRVLQKTPLSfdvSVWEL---FWPLVAGAR 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 IGYSSPQTLADqsskikkgskgdtsmlkptlMAAVPEIMDRIYKNVMNKVSEMssfqrnLFILaynykMEQISKGRNTPL 428
Cdd:cd17646 207 LVVARPGGHRD--------------------PAYLAALIREHGVTTCHFVPSM------LRVF-----LAEPAAGSCASL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 429 cdsfvfrkvrsllggniRLLLCGGAPLSA-TTQRFMNIcFCCPVGQGYGLTESagagTISEVWDYNTGRVGAPLVccEIK 507
Cdd:cd17646 256 -----------------RRVFCSGEALPPeLAARFLAL-PGAELHNLYGPTEA----AIDVTHWPVRGPAETPSV--PIG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNWEEGGYFNTD--KPHPRG---EILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGCLKIIDRK 580
Cdd:cd17646 312 RPVPNTRLYVLDDalRPVPVGvpgELYLGGVQLARGYLGRPALTAERFVPDpfGPGSRMYRTGDLARWRPDGALEFLGRS 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 115502350 581 KDLVKLQaGEYVSLGKVEAALKNLPLVDNICAYA---NSYHSYVIGFVVP 627
Cdd:cd17646 392 DDQVKIR-GFRVEPGEIEAALAAHPAVTHAVVVAraaPAGAARLVGYVVP 440
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
280-611 |
1.22e-19 |
|
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: 92.16 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAeRIPELGEEDVYIGYLPLAHVLELSAelvclshgcrigysspqtlad 359
Cdd:cd05935 85 DLALIPYTSGTTGLPKGCMHTHFSAAANALQSA-VWTGLTPSDVILACLPLFHVTGFVG--------------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 360 qsskikkgskgdtsmlkpTLMAAVpeimdriykNVMNKVSEMSSFQRNLfiLAYNYKMEQISKGRNTP-----LCDSFVF 434
Cdd:cd05935 143 ------------------SLNTAV---------YVGGTYVLMARWDRET--ALELIEKYKVTFWTNIPtmlvdLLATPEF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 435 RKvRSLlgGNIRLLLCGGAPL-SATTQRFMNIcFCCPVGQGYGLTEsagagTISEVWDYNTGR-----VGAPLVCCEIKL 508
Cdd:cd05935 194 KT-RDL--SSLKVLTGGGAPMpPAVAEKLLKL-TGLRFVEGYGLTE-----TMSQTHTNPPLRpklqcLGIP*FGVDARV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 509 KNWEEGGYFNtdkPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDeNGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLqA 588
Cdd:cd05935 265 IDIETGRELP---PNEVGEIVVRGPQIFKGYWNRPEETEESFIEI-KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINV-S 339
|
330 340
....*....|....*....|...
gi 115502350 589 GEYVSLGKVEAALKNLPLVDNIC 611
Cdd:cd05935 340 GFKVWPAEVEAKLYKHPAI*EVC 362
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
261-612 |
2.40e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 92.25 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 261 ALGAKASMenqPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGE----EDVYIGYLPLAHVLEL 336
Cdd:PRK08751 193 ALGRKHSM---PTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKleegCEVVITALPLYHIFAL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 337 SAE-LVCLS-HGCRIGYSSPQTLadqsskikkgsKGDTSMLKPTLMAAVPEImdriyknvmnkvsemssfqRNLFilayn 414
Cdd:PRK08751 270 TANgLVFMKiGGCNHLISNPRDM-----------PGFVKELKKTRFTAFTGV-------------------NTLF----- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 415 ykmeqiSKGRNTPLCDSFVFRKVRSLLGGnirlllcGGAPLSATTQRFMNICFCcPVGQGYGLTESAGAGTIS--EVWDY 492
Cdd:PRK08751 315 ------NGLLNTPGFDQIDFSSLKMTLGG-------GMAVQRSVAERWKQVTGL-TLVEAYGLTETSPAACINplTLKEY 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 493 NtGRVGAPLVCCEIKLKNweeggyfNTDKPHPRGEI---LIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFE 569
Cdd:PRK08751 381 N-GSIGLPIPSTDACIKD-------DAGTVLAIGEIgelCIKGPQVMKGYWKRPEETAKVM--DADG--WLHTGDIARMD 448
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 115502350 570 PDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLVDNICA 612
Cdd:PRK08751 449 EQGFVYIVDRKKDMI-LVSGFNVYPNEIEDVIAMMPGVLEVAA 490
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
229-607 |
2.41e-19 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 92.04 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 229 PRLRHIITVDGKPPTwsefpkgiivhtmaAVEALGAKASMENQPH-------SKPLPSDIAVIMYTSGSTGLPKGVMISH 301
Cdd:PRK13295 154 PALRHVVVVGGDGAD--------------SFEALLITPAWEQEPDapailarLRPGPDDVTQLIYTSGTTGEPKGVMHTA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 302 SNIIAGITGMAERIpELGEEDVYIGYLPLAHvlelsaeLVCLSHGCRIGYSSPQT--LADQSSKIKKGSKGDTSMLKPTl 379
Cdd:PRK13295 220 NTLMANIVPYAERL-GLGADDVILMASPMAH-------QTGFMYGLMMPVMLGATavLQDIWDPARAAELIRTEGVTFT- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 380 MAAVPEIMDriyknvMNKVSEMSsfqrnlfilaynykmeqiskGRNTPlcdsfvfrkvrSLlggniRLLLCGGAPLSATT 459
Cdd:PRK13295 291 MASTPFLTD------LTRAVKES--------------------GRPVS-----------SL-----RTFLCAGAPIPGAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 460 QRFMNICFCCPVGQGYGLTESAGAGTI--SEVWDYNTGRVGAPLVCCEIKLKNweeggyfNTDKPHPRGEI---LIGGQS 534
Cdd:PRK13295 329 VERARAALGAKIVSAWGMTENGAVTLTklDDPDERASTTDGCPLPGVEVRVVD-------ADGAPLPAGQIgrlQVRGCS 401
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115502350 535 VTMGYYKNEAKTKADFfedengQRWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLV 607
Cdd:PRK13295 402 NFGGYLKRPQLNGTDA------DGWFDTGDLARIDADGYIRISGRSKDVI-IRGGENIPVVEIEALLYRHPAI 467
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
124-604 |
6.23e-19 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 91.95 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 124 FKKVIL--GQYNWLSYEDVFVRAFNFGNGLQMlGQKPKTNIAIFCETRAewmiAAQACF-----------MYNFqlvtly 190
Cdd:PRK06814 646 FKKLAVedPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNAN----GAAVTFfalqsagrvpaMINF------ 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 191 aTLGGPAIVHALNETEVTNIITSKELL-QTKLKDIVSLVPRLRHIITVDgkpptwsEFPKGIivHTMAAVEALgAKASME 269
Cdd:PRK06814 715 -SAGIANILSACKAAQVKTVLTSRAFIeKARLGPLIEALEFGIRIIYLE-------DVRAQI--GLADKIKGL-LAGRFP 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 270 NQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPLAHVLELSAELVC-LSHGCR 348
Cdd:PRK06814 784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARID-FSPEDKVFNALPVFHSFGLTGGLVLpLLSGVK 862
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 IG-YSSPQTladqsskikkgskgdtsmlkptlMAAVPEIMDRIYKNVMnkvsemssFQRNLFILAY-NYkmeqiskgrnt 426
Cdd:PRK06814 863 VFlYPSPLH-----------------------YRIIPELIYDTNATIL--------FGTDTFLNGYaRY----------- 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 427 plCDSFVFRkvrsllggNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAgagtisEVWDYNT------GRVGAP 500
Cdd:PRK06814 901 --AHPYDFR--------SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETA------PVIALNTpmhnkaGTVGRL 964
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 LVCCEIKLK---NWEEGgyfntdkphprGEILIGGQSVTMGYYKNEAKTKADffEDENGqrWLCTGDIGEFEPDGCLKII 577
Cdd:PRK06814 965 LPGIEYRLEpvpGIDEG-----------GRLFVRGPNVMLGYLRAENPGVLE--PPADG--WYDTGDIVTIDEEGFITIK 1029
|
490 500
....*....|....*....|....*..
gi 115502350 578 DRKKDLVKLqAGEYVSLGKVEAALKNL 604
Cdd:PRK06814 1030 GRAKRFAKI-AGEMISLAAVEELAAEL 1055
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
286-607 |
7.06e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 90.85 E-value: 7.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 286 YTSGSTGLPKGVMISHS----NIIAGITGMaeripELGEEDVYIGYLPLAHvlelsaelvclshgCRiGYSSPQTLAdqs 361
Cdd:PLN03102 193 YTSGTTADPKGVVISHRgaylSTLSAIIGW-----EMGTCPVYLWTLPMFH--------------CN-GWTFTWGTA--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 362 skikkgSKGDTSMLKPTLMAavPEImdriYKNV-MNKVSEMSSFQRNLFILAYNYKMEQISKGrntplcdsfvfrkvrsl 440
Cdd:PLN03102 250 ------ARGGTSVCMRHVTA--PEI----YKNIeMHNVTHMCCVPTVFNILLKGNSLDLSPRS----------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 441 lgGNIRLLLCGGAPLSATTQRFMNICFccPVGQGYGLTESAGAGTISEVWD-YN----------TGRVGAP-LVCCEIKL 508
Cdd:PLN03102 301 --GPVHVLTGGSPPPAALVKKVQRLGF--QVMHAYGLTEATGPVLFCEWQDeWNrlpenqqmelKARQGVSiLGLADVDV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 509 KNWEeggyfnTDKPHPR-----GEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDL 583
Cdd:PLN03102 377 KNKE------TQESVPRdgktmGEIVIKGSSIMKGYLKNPKATSEAF---KHG--WLNTGDVGVIHPDGHVEIKDRSKDI 445
|
330 340
....*....|....*....|....
gi 115502350 584 VkLQAGEYVSLGKVEAALKNLPLV 607
Cdd:PLN03102 446 I-ISGGENISSVEVENVLYKYPKV 468
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
280-607 |
9.60e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 90.29 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGM----AERIPELGEEDVYIGYLPLAHVLELSAELV-CLSHGCRIGYSSP 354
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeASQYEYPGSDNVYLAALPMFHIYGLSLFVVgLLSLGSTIVVMRR 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 355 QTLADQSSKIKKgskgdtsmLKPTLMAAVPEIMdriyknvmnkvsemssfqrnlfilaynykMEQISKGRntPLC-DSFv 433
Cdd:PLN02574 279 FDASDMVKVIDR--------FKVTHFPVVPPIL-----------------------------MALTKKAK--GVCgEVL- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 434 frkvrsllgGNIRLLLCGGAPLSA-TTQRFMNICFCCPVGQGYGLTESAGAGT----ISEVWDYNTGRVGAPLVccEIKL 508
Cdd:PLN02574 319 ---------KSLKQVSCGAAPLSGkFIQDFVQTLPHVDFIQGYGMTESTAVGTrgfnTEKLSKYSSVGLLAPNM--QAKV 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 509 KNWEEGGYFntdKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLQa 588
Cdd:PLN02574 388 VDWSTGCLL---PPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDG----WLRTGDIAYFDEDGYLYIVDRLKEIIKYK- 459
|
330
....*....|....*....
gi 115502350 589 GEYVSLGKVEAALKNLPLV 607
Cdd:PLN02574 460 GFQIAPADLEAVLISHPEI 478
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
278-634 |
1.52e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 89.73 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGI---TGMAERIPELGEEDVYIGyLPLAHVLELSAElvCLSHgcrigyssp 354
Cdd:PRK08974 205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLANLeqaKAAYGPLLHPGKELVVTA-LPLYHIFALTVN--CLLF--------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 355 qtladqsskIKKGSKGdtsmlkptLMAAVPeimdriyKNVMNKVSEMSsfqrnlfilayNYKMEQISkGRNT---PLCDS 431
Cdd:PRK08974 273 ---------IELGGQN--------LLITNP-------RDIPGFVKELK-----------KYPFTAIT-GVNTlfnALLNN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 432 FVFRKVRSllgGNIRLLLCGGAPL-SATTQRFMNICfCCPVGQGYGLTESAG--AGTISEVWDYNtGRVGAPLVCCEIKL 508
Cdd:PRK08974 317 EEFQELDF---SSLKLSVGGGMAVqQAVAERWVKLT-GQYLLEGYGLTECSPlvSVNPYDLDYYS-GSIGLPVPSTEIKL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 509 KNwEEGgyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTkADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQA 588
Cdd:PRK08974 392 VD-DDG---NEVPPGEPGELWVKGPQVMLGYWQRPEAT-DEVIKDG----WLATGDIAVMDEEGFLRIVDRKKDMI-LVS 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 115502350 589 GEYVSLGKVEAALKNLPLVDNICAYANSYHS---YVIGFVVPNQKELTE 634
Cdd:PRK08974 462 GFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVsgeAVKIFVVKKDPSLTE 510
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
200-584 |
1.56e-18 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 89.69 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 200 HALNETEVTNIITSK--ELLQTKlKDIVSLVPRlrhiiTVDGKPPTWSefpkgiIVHTMAAVEALGAKASMENQPhSKPL 277
Cdd:PRK07059 136 QVLAKTAVKHVVVASmgDLLGFK-GHIVNFVVR-----RVKKMVPAWS------LPGHVRFNDALAEGARQTFKP-VKLG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGM------AERIPELGEEDVYIGYLPLAHVLELSaelVCLSHGCRigy 351
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMeawlqpAFEKKPRPDQLNFVCALPLYHIFALT---VCGLLGMR--- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 352 sspqtladqsskikkgsKGDTSMLKPTlmaavPeimdriyKNVMNKVSEMSSFQRNLFI---LAYNYKMeqiskgrNTPL 428
Cdd:PRK07059 277 -----------------TGGRNILIPN-----P-------RDIPGFIKELKKYQVHIFPavnTLYNALL-------NNPD 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 429 CDSFVFRKVRSLLGGnirlllcGGAPLSATTQRFMNICfCCPVGQGYGLTESAGAGTISEV-WDYNTGRVGAPLVCCEIK 507
Cdd:PRK07059 321 FDKLDFSKLIVANGG-------GMAVQRPVAERWLEMT-GCPITEGYGLSETSPVATCNPVdATEFSGTIGLPLPSTEVS 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNwEEGGYFNTDKPhprGEILIGGQSVTMGYYKNEAKTK----AD-FFEdengqrwlcTGDIGEFEPDGCLKIIDRKKD 582
Cdd:PRK07059 393 IRD-DDGNDLPLGEP---GEICIRGPQVMAGYWNRPDETAkvmtADgFFR---------TGDVGVMDERGYTKIVDRKKD 459
|
..
gi 115502350 583 LV 584
Cdd:PRK07059 460 MI 461
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
155-647 |
2.30e-18 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 89.04 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 155 GQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKD-IVSL---VPR 230
Cdd:PRK06087 70 GIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDlILPLqnqLPQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 231 LRHIITVDGKPPTWSEFpkgiivhTMAAVEAlgakasmENQPHSKPLPS---DIAVIMYTSGSTGLPKGVMISHSNIIAG 307
Cdd:PRK06087 150 LQQIVGVDKLAPATSSL-------SLSQIIA-------DYEPLTTAITThgdELAAVLFTSGTEGLPKGVMLTHNNILAS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 308 ITGMAERIpELGEEDVYIGYLPLAHvlelsaelvclSHGCRIGYSSPqTLADQSSKIKKGSKGDTSML-----KPT-LMA 381
Cdd:PRK06087 216 ERAYCARL-NLTWQDVFMMPAPLGH-----------ATGFLHGVTAP-FLIGARSVLLDIFTPDACLAlleqqRCTcMLG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 382 AVPEIMDrIYKNVMNKVSEMSSfqrnlfilaynykmeqiskgrntplcdsfvfrkvrsllggnIRLLLCGGAPLSATT-- 459
Cdd:PRK06087 283 ATPFIYD-LLNLLEKQPADLSA-----------------------------------------LRFFLCGGTTIPKKVar 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 460 ---QRFMNICFCcpvgqgYGLTESAGAGTISEvwDYNTGRVGA----PLVCCEIKLKNweegGYFNTDKPHPRGEILIGG 532
Cdd:PRK06087 321 ecqQRGIKLLSV------YGSTESSPHAVVNL--DDPLSRFMHtdgyAAAGVEIKVVD----EARKTLPPGCEGEEASRG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 533 QSVTMGYYKN-EAKTKAdffEDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLV---- 607
Cdd:PRK06087 389 PNVFMGYLDEpELTARA---LDEEG--WYYSGDLCRMDEAGYIKITGRKKDII-VRGGENISSREVEDILLQHPKIhdac 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 115502350 608 ----------DNICAYA---NSYHSyvigfvvPNQKELTE-LARKKGLKGTWEE 647
Cdd:PRK06087 463 vvampderlgERSCAYVvlkAPHHS-------LTLEEVVAfFSRKRVAKYKYPE 509
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
135-607 |
3.96e-18 |
|
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: 88.19 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQTKLKDIVSLVPRLRHIITVDGKPPtwsEFPKGIIVHTMAAVEALGAKASMEnqphskplPSDIAVIMYTSGSTGLP 294
Cdd:cd05959 110 ELAPVLAAALTKSEHTLVVLIVSGGAGP---EAGALLLAELVAAEAEQLKPAATH--------ADDPAFWLYSSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 295 KGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVC-LSHGCRI----GYSSPQTLADqssKIKKGsk 369
Cdd:cd05959 179 KGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFpLSVGATTvlmpERPTPAAVFK---RIRRY-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 370 gdtsmlKPTLMAAVPEimdrIYkNVMNKVSEMSSfqrnlfilaynykmeqiskgrntplcDSFVfrkvrsllggNIRLLL 449
Cdd:cd05959 254 ------RPTVFFGVPT----LY-AAMLAAPNLPS--------------------------RDLS----------SLRLCV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 450 CGGAPLSATT-QRFMNIcFCCPVGQGYGLTE------SAGAGTIsevwDYNTgrVGAPLVCCEIKLKNwEEGGYFNTDKP 522
Cdd:cd05959 287 SAGEALPAEVgERWKAR-FGLDILDGIGSTEmlhiflSNRPGRV----RYGT--TGKPVPGYEVELRD-EDGGDVADGEP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 523 hprGEILIGGQSVTMGYYKNEAKTKADfFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALK 602
Cdd:cd05959 359 ---GELYVRGPSSATMYWNNRDKTRDT-FQGE----WTRTGDKYVRDDDGFYTYAGRADDMLKV-SGIWVSPFEVESALV 429
|
....*
gi 115502350 603 NLPLV 607
Cdd:cd05959 430 QHPAV 434
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
279-584 |
4.87e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 88.17 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 279 SDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGE-EDVYIGYLPLAHVLELSAELvclshgcrigysspqtl 357
Cdd:PRK06710 206 NDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMTAVM----------------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 adqsskikkgskgDTSMLKPTLMAAVPEI-MDRIYKNVMNKVSEMSSFQRNLFILAYNykmeqiskgrnTPLCDSFVFRK 436
Cdd:PRK06710 269 -------------NLSIMQGYKMVLIPKFdMKMVFEAIKKHKVTLFPGAPTIYIALLN-----------SPLLKEYDISS 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 437 VRSLLGGNirlllcggAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNT-GRVGAPLVCCEIKLKNWEEGG 515
Cdd:PRK06710 325 IRACISGS--------APLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEKRVpGSIGVPWPDTEAMIMSLETGE 396
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115502350 516 YFntdKPHPRGEILIGGQSVTMGYYkNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLV 584
Cdd:PRK06710 397 AL---PPGEIGEIVVKGPQIMKGYW-NKPEETAAVLQDG----WLHTGDVGYMDEDGFFYVKDRKKDMI 457
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
254-607 |
5.69e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 87.63 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 254 HTMAAVEALGAkASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSN--------IIA-GITGmAERIPELGeedvy 324
Cdd:PRK06145 125 AAQADSRRLAQ-GGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNlhwksidhVIAlGLTA-SERLLVVG----- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 325 igylPLAHV--LELSAeLVCLSHG---CRIGYSSPQTLADQSSKikkgSKGDTSMLKPTLMAAVPEIMDRiyknvmnkvs 399
Cdd:PRK06145 198 ----PLYHVgaFDLPG-IAVLWVGgtlRIHREFDPEAVLAAIER----HRLTCAWMAPVMLSRVLTVPDR---------- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 400 emssFQRNLFILAYnykmeQISKGRNTPlcdSFVFRKVRSLLggnirlllcggaplsaTTQRFMNicfccpvgqGYGLTE 479
Cdd:PRK06145 259 ----DRFDLDSLAW-----CIGGGEKTP---ESRIRDFTRVF----------------TRARYID---------AYGLTE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 480 SAGAGTISEVWDY--NTGRVGAPLVCCEIKLKNwEEGGYFntdKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDengq 557
Cdd:PRK06145 302 TCSGDTLMEAGREieKIGSTGRALAHVEIRIAD-GAGRWL---PPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD---- 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 115502350 558 rWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLV 607
Cdd:PRK06145 374 -WFRSGDVGYLDEEGFLYLTDRKKDMI-ISGGENIASSEVERVIYELPEV 421
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
278-627 |
1.12e-17 |
|
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: 86.21 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIagitgmaeRIPELGEEDVYIGylP---LAHVLELS-----AE-LVCLSHGCR 348
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVL--------NYVSQPPARLDVG--PgsrVAQVLSIAfdaciGEiFSTLCNGGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 IGYSSP-QTLADQSSKIkkgskgDTSMLKPTLMAAVPEimdriyknvmnkvsemSSFQrnlfilaynykmeqiskgrntp 427
Cdd:cd17653 174 LVLADPsDPFAHVARTV------DALMSTPSILSTLSP----------------QDFP---------------------- 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 428 lcdsfvfrkvrsllggNIRLLLCGGAPLSAT-------TQRFMNicfccpvgqGYGLTESAGAGTISEVWDYNTGRVGAP 500
Cdd:cd17653 210 ----------------NLKTIFLGGEAVPPSlldrwspGRRLYN---------AYGPTECTISSTMTELLPGQPVTIGKP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 L--VCCEIKLKNWEEggyfntdKPHPR-GEILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGCLK 575
Cdd:cd17653 265 IpnSTCYILDADLQP-------VPEGVvGEICISGVQVARGYLGNPALTASKFVPDpfWPGSRMYRTGDYGRWTEDGGLE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 115502350 576 IIDRKKDLVKLQaGEYVSLGKVEA-ALKNLPLVDNicAYANSYHSYVIGFVVP 627
Cdd:cd17653 338 FLGREDNQVKVR-GFRINLEEIEEvVLQSQPEVTQ--AAAIVVNGRLVAFVTP 387
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
273-610 |
1.25e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 86.96 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 273 HSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERI-PELGEEDVYIGYLPLAHVLELSAelVCLShgcrigy 351
Cdd:PLN02330 178 NEEILQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSLFSVgPEMIGQVVTLGLIPFFHIYGITG--ICCA------- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 352 sspqTLADQSsKIKKGSKGDTSMLKPTLMAA-------VPEIMDRIYKNvmnkvsemssfqrnlfilaynykmeqiskgr 424
Cdd:PLN02330 249 ----TLRNKG-KVVVMSRFELRTFLNALITQevsfapiVPPIILNLVKN------------------------------- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 425 ntPLCDSFVFRKVRsllggnIRLLLCGGAPL-----SATTQRFMNIcfccPVGQGYGLTE-----------SAGAGTISE 488
Cdd:PLN02330 293 --PIVEEFDLSKLK------LQAIMTAAAPLapellTAFEAKFPGV----QVQEAYGLTEhscitlthgdpEKGHGIAKK 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 489 vwdyntGRVGAPLVCCEIKLKNWEEGGYFNTDKPhprGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEF 568
Cdd:PLN02330 361 ------NSVGFILPNLEVKFIDPDTGRSLPKNTP---GELCVRSQCVMQGYYNNKEETDRTI--DEDG--WLHTGDIGYI 427
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 115502350 569 EPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDNI 610
Cdd:PLN02330 428 DDDGDIFIVDRIKELIKYK-GFQVAPAELEAILLTHPSVEDA 468
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
135-639 |
1.40e-17 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 86.70 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFmynfQL----VTLYATLGGPAIVHALNETEVTNI 210
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACA----RIgavhSPVFPGFGAEALADRIEDAEAKVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 211 ITSKEL--------LQTKLKDIVSLVPRLRHIITVDG-----KPPTWSEFpkgiivhtmaavEALGAKASMENQPHskPL 277
Cdd:COG0365 116 ITADGGlrggkvidLKEKVDEALEELPSLEHVIVVGRtgadvPMEGDLDW------------DELLAAASAEFEPE--PT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PS-DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELV-CLSHGC-------R 348
Cdd:COG0365 182 DAdDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSYIVYgPLLNGAtvvlyegR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 IGYSSPQTLADQSSKikkgskgdtsmLKPTLMAAVPeimdRIYKNVMNKVSEmssfqrnlFILAYNykmeqiskgrntpl 428
Cdd:COG0365 262 PDFPDPGRLWELIEK-----------YGVTVFFTAP----TAIRALMKAGDE--------PLKKYD-------------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 429 cdsfvfrkVRSLlggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGA-GTISEVWDYNTGRVGAPLVCCEIK 507
Cdd:COG0365 305 --------LSSL-----RLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIfISNLPGLPVKPGSMGKPVPGYDVA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNwEEGgyfNTDKPHPRGEILIGGQSVTM--GYYKNEAKTKADFFEDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVK 585
Cdd:COG0365 372 VVD-EDG---NPVPPGEEGELVIKGPWPGMfrGYWNDPERYRETYFGRFPG--WYRTGDGARRDEDGYFWILGRSDDVIN 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115502350 586 LqAGEYVSLGKVEAALKNLPLVDNiCAyansyhsyVIG------------FVVPNQ---------KELTELARKK 639
Cdd:COG0365 446 V-SGHRIGTAEIESALVSHPAVAE-AA--------VVGvpdeirgqvvkaFVVLKPgvepsdelaKELQAHVREE 510
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
134-614 |
3.10e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 85.58 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 134 WLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITS 213
Cdd:PRK06155 46 RWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 214 KELLQtKLKDIVSLVPRLRHIITVDGKPPtwsefpkgiiVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGL 293
Cdd:PRK06155 126 AALLA-ALEAADPGDLPLPAVWLLDAPAS----------VSVPAGWSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 294 PKGVMISHSNI-IAGITgMAERIpELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYsspqtladqsskikkGSKGDT 372
Cdd:PRK06155 195 SKGVCCPHAQFyWWGRN-SAEDL-EIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL---------------EPRFSA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 373 SMLKPTLMAAvpeimdriYKNVMNKVSEMSSfqrnlfILAYNYKMEQISKGRntplcdsfvfrkVRSLLGGnirlllcGG 452
Cdd:PRK06155 258 SGFWPAVRRH--------GATVTYLLGAMVS------ILLSQPARESDRAHR------------VRVALGP-------GV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 453 AP--LSATTQRfmnicFCCPVGQGYGLTES--AGAGTISEVWDYNTGRVgAPLVccEIKLKNwEEGGYFNTDKPhprGEI 528
Cdd:PRK06155 305 PAalHAAFRER-----FGVDLLDGYGSTETnfVIAVTHGSQRPGSMGRL-APGF--EARVVD-EHDQELPDGEP---GEL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 529 LIGGQ---SVTMGYYKNEAKTKADFfedenGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLP 605
Cdd:PRK06155 373 LLRADepfAFATGYFGMPEKTVEAW-----RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRR-GENISSFEVEQVLLSHP 446
|
....*....
gi 115502350 606 LVDNICAYA 614
Cdd:PRK06155 447 AVAAAAVFP 455
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
226-614 |
5.03e-17 |
|
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: 84.41 E-value: 5.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 226 SLVPRLRHIITVDGKPPTWsefpkgiivhtmAAVEAL-GAKASMENQPHSKPlpsDIAVIMYTSGSTGLPKGVMISHSNI 304
Cdd:cd05922 78 GAADRLRDALPASPDPGTV------------LDADGIrAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQNL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 305 IAGITGMAERIpELGEEDVYIGYLPLAHVLELSaelVCLSHgcrigysspqTLADQSSKIKKGSKGDTSMLKP------T 378
Cdd:cd05922 143 LANARSIAEYL-GITADDRALTVLPLSYDYGLS---VLNTH----------LLRGATLVLTNDGVLDDAFWEDlrehgaT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 379 LMAAVP---EIMDRIyknvmnkvsemssfqrnlfilaynykmeqiskgrntplcdSFVFRKVRSLlggniRLLLCGGAPL 455
Cdd:cd05922 209 GLAGVPstyAMLTRL----------------------------------------GFDPAKLPSL-----RYLTQAGGRL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 456 SATT-QRFmnicfcCPVGQG------YGLTESAGAGTI--SEVWDYNTGRVGAPLVCCEIKLKNwEEGGYFNTDKPhprG 526
Cdd:cd05922 244 PQETiARL------RELLPGaqvyvmYGQTEATRRMTYlpPERILEKPGSIGLAIPGGEFEILD-DDGTPTPPGEP---G 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 527 EILIGGQSVTMGYYKNEA-KTKADFFEDEngqrwLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLP 605
Cdd:cd05922 314 EIVHRGPNVMKGYWNDPPyRRKEGRGGGV-----LHTGDLARRDEDGFLFIVGRRDRMIKL-FGNRISPTEIEAAARSIG 387
|
....*....
gi 115502350 606 LVDNICAYA 614
Cdd:cd05922 388 LIIEAAAVG 396
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
150-584 |
6.73e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 84.48 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 150 GLQMLGQKPKTNIAIFCETRAEWmiaaqacfmynfqLVTLYAT--LG------GPA-----IVHALNETEVTNIITSK-- 214
Cdd:PRK08315 59 GLLALGIEKGDRVGIWAPNVPEW-------------VLTQFATakIGailvtiNPAyrlseLEYALNQSGCKALIAADgf 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ------ELLQT---KLKDIV------SLVPRLRHIITVDG-KPPTWSEFPKGIIVHTMAAVEALGAKASmENQPHskplp 278
Cdd:PRK08315 126 kdsdyvAMLYElapELATCEpgqlqsARLPELRRVIFLGDeKHPGMLNFDELLALGRAVDDAELAARQA-TLDPD----- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 279 sDIAVIMYTSGSTGLPKGVMISHSNII--AGITGMAERipeLGEED-----VyigylPLAH----VLelsAELVCLSHGC 347
Cdd:PRK08315 200 -DPINIQYTSGTTGFPKGATLTHRNILnnGYFIGEAMK---LTEEDrlcipV-----PLYHcfgmVL---GNLACVTHGA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 348 RIGYSSP--------QTLADQSSKIKKG--------------SKGDTSMLKPTLMAAVP---EIMDRIyknvmnkVSEMS 402
Cdd:PRK08315 268 TMVYPGEgfdplatlAAVEEERCTALYGvptmfiaeldhpdfARFDLSSLRTGIMAGSPcpiEVMKRV-------IDKMH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 403 sfqrnlfilaynykMEQISkgrntplcdsfvfrkvrsllggnirlllcggaplsattqrfmnICfccpvgqgYGLTESAG 482
Cdd:PRK08315 341 --------------MSEVT-------------------------------------------IA--------YGMTETSP 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 483 AGTISEVWD---YNTGRVGAPLVCCEIKLKNWEEGgyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrW 559
Cdd:PRK08315 356 VSTQTRTDDpleKRVTTVGRALPHLEVKIVDPETG---ETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI--DADG--W 428
|
490 500
....*....|....*....|....*
gi 115502350 560 LCTGDIGEFEPDGCLKIIDRKKDLV 584
Cdd:PRK08315 429 MHTGDLAVMDEEGYVNIVGRIKDMI 453
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
280-607 |
1.04e-16 |
|
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: 81.78 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAErIPELGEEDVYIGYLPLAHVLELSAE-LVCLSHGCRIgysSPQTLA 358
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWAD-CADLTEDDRYLIINPFFHTFGYKAGiVACLLTGATV---VPVAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 359 DQSSKIKKGSKGDTSML--KPTLMAAVPEIMDRiyknvmnKVSEMSSFQrnlfilaynykmEQISKGRNTPLCdsfVFRK 436
Cdd:cd17638 77 DVDAILEAIERERITVLpgPPTLFQSLLDHPGR-------KKFDLSSLR------------AAVTGAATVPVE---LVRR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 437 VRSLLGgnirlllcggaplsattqrFMNicfccpVGQGYGLTEsAGAGTISEVWDYNT---GRVGAPLVCCEIKLKNwee 513
Cdd:cd17638 135 MRSELG-------------------FET------VLTAYGLTE-AGVATMCRPGDDAEtvaTTCGRACPGFEVRIAD--- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 ggyfntdkphpRGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVS 593
Cdd:cd17638 186 -----------DGEVLVRGYNVMQGYLDDPEATAEAI--DADG--WLHTGDVGELDERGYLRITDRLKDMY-IVGGFNVY 249
|
330
....*....|....
gi 115502350 594 LGKVEAALKNLPLV 607
Cdd:cd17638 250 PAEVEGALAEHPGV 263
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
278-639 |
1.06e-16 |
|
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: 83.13 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGmAERIPELGEEDVYIGY-------------LPLAHvlelSAELVCLS 344
Cdd:cd17643 92 PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA-TQRWFGFNEDDVWTLFhsyafdfsvweiwGALLH----GGRLVVVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 345 HGCRigySSPQTLADQsskIKKGskgdtsmlKPTLMAAVPeimdriyknvmnkvsemSSFQRNLfilaynykMEQISKGR 424
Cdd:cd17643 167 YEVA---RSPEDFARL---LRDE--------GVTVLNQTP-----------------SAFYQLV--------EAADRDGR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 425 NTPlcdsfvfrkvrsllggNIRLLLCGGAPLSATTQRFMNICFCCPVGQ---GYGLTESAGAGTI-----SEVWDYNTGR 496
Cdd:cd17643 208 DPL----------------ALRYVIFGGEALEAAMLRPWAGRFGLDRPQlvnMYGITETTVHVTFrpldaADLPAAAASP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 497 VGAPLVCCEIKLKNweeggyfNTDKPHPR---GEILIGGQSVTMGYYKNEAKTKADFFEDEN---GQRWLCTGDIGEFEP 570
Cdd:cd17643 272 IGRPLPGLRVYVLD-------ADGRPVPPgvvGELYVSGAGVARGYLGRPELTAERFVANPFggpGSRMYRTGDLARRLP 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115502350 571 DGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDNICAYANSYH---SYVIGFVVPNQK------ELTELARKK 639
Cdd:cd17643 345 DGELEYLGRADEQVKIR-GFRIELGEIEAALATHPSVRDAAVIVREDEpgdTRLVAYVVADDGaaadiaELRALLKEL 421
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
278-706 |
1.28e-16 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 83.69 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIagITGMAE-RIPELGEEDVYIGYLPLAHVLELSAELVCLSHG-CRIGYSSPQ 355
Cdd:PLN02860 171 PDDAVLICFTSGTTGRPKGVTISHSALI--VQSLAKiAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGaCHVLLPKFD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 356 T-LADQSSKikkgSKGDTSMLkptlmaAVPEIM-DriyknvmnkvsemssfqrnlfILAYNyKMEQISKGrntplcdsfv 433
Cdd:PLN02860 249 AkAALQAIK----QHNVTSMI------TVPAMMaD---------------------LISLT-RKSMTWKV---------- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 434 FRKVRSLL--GGNIRLLLcggapLSATTQRFMnicfCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPL-VCCEIKLKN 510
Cdd:PLN02860 287 FPSVRKILngGGSLSSRL-----LPDAKKLFP----NAKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLqTVNQTKSSS 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 511 WEEGGYFNTDKPHPRGEILIG-------GQSVT-----MGYYKNEAKTKAdffEDENGQRWLCTGDIGEFEPDGCLKIID 578
Cdd:PLN02860 358 VHQPQGVCVGKPAPHVELKIGldessrvGRILTrgphvMLGYWGQNSETA---SVLSNDGWLDTGDIGWIDKAGNLWLIG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 579 RKKDLVKlQAGEYVSLGKVEAALKNLPLVDNicayansyhSYVIGfvVPNQKeLTELA-------------------RKK 639
Cdd:PLN02860 435 RSNDRIK-TGGENVYPEEVEAVLSQHPGVAS---------VVVVG--VPDSR-LTEMVvacvrlrdgwiwsdnekenAKK 501
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115502350 640 GLKGTWEELCNSCEMENevlkvlseaaisasLEKFEIPVKIRLSPEPWTpetglVTDAFKLKRKELK 706
Cdd:PLN02860 502 NLTLSSETLRHHCREKN--------------LSRFKIPKLFVQWRKPFP-----LTTTGKIRRDEVR 549
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
272-607 |
1.62e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 82.73 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 272 PHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVlelsaelvclsHG----- 346
Cdd:PRK07787 121 RYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW-QWTADDVLVHGLPLFHV-----------HGlvlgv 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 347 ---CRIGYS-------SPQTLADQSSkikkgskgdtsmLKPTLMAAVPEIMDRIyknvmnkVSEMSSfqrnlfilaynyk 416
Cdd:PRK07787 189 lgpLRIGNRfvhtgrpTPEAYAQALS------------EGGTLYFGVPTVWSRI-------AADPEA------------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 417 meqiskgrntplcdsfvfrkVRSLLGGniRLLLCGGAPLSATT-QRFMNICFCCPVgQGYGLTESagAGTISEVWD--YN 493
Cdd:PRK07787 237 --------------------ARALRGA--RLLVSGSAALPVPVfDRLAALTGHRPV-ERYGMTET--LITLSTRADgeRR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 494 TGRVGAPLVCCEIKLKnwEEGGyfnTDKPHPR---GEILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGEFEP 570
Cdd:PRK07787 292 PGWVGLPLAGVETRLV--DEDG---GPVPHDGetvGELQVRGPTLFDGYLNRPDATAAAFTADG----WFRTGDVAVVDP 362
|
330 340 350
....*....|....*....|....*....|....*....
gi 115502350 571 DGCLKIIDRKK-DLVKlqAGEY-VSLGKVEAALKNLPLV 607
Cdd:PRK07787 363 DGMHRIVGREStDLIK--SGGYrIGAGEIETALLGHPGV 399
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
152-611 |
1.86e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 83.09 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 152 QMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLvpRL 231
Cdd:PRK08314 54 QECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNL--RL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 232 RHII--------TVDG--KPPTWSEFPKGIIVHTMAAV----EALGAKASMEnqPHSkPLPSDIAVIMYTSGSTGLPKGV 297
Cdd:PRK08314 132 RHVIvaqysdylPAEPeiAVPAWLRAEPPLQALAPGGVvawkEALAAGLAPP--PHT-AGPDDLAVLPYTSGTTGVPKGC 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 298 MISHSNIIAGITGmAERIPELGEEDVYIGYLPLAHVLELsaelvclshgcrigysspqtladQSskikkgskgdtSMLKP 377
Cdd:PRK08314 209 MHTHRTVMANAVG-SVLWSNSTPESVVLAVLPLFHVTGM-----------------------VH-----------SMNAP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 378 TLMAAVPEIMDRiyknvmnkvsemssFQRNLfilaynyKMEQISKGRNT---------------PLCDSFVFRKVRSLLG 442
Cdd:PRK08314 254 IYAGATVVLMPR--------------WDREA-------AARLIERYRVThwtniptmvvdflasPGLAERDLSSLRYIGG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 443 gnirlllcGGAPL-SATTQRFM---NICFCcpvgQGYGLTESAgAGTISEVWDyntgrvgAP-LVCCEIKLknweeggyF 517
Cdd:PRK08314 313 --------GGAAMpEAVAERLKeltGLDYV----EGYGLTETM-AQTHSNPPD-------RPkLQCLGIPT--------F 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 518 NTD---------KPHPR---GEILIGGQSVTMGYYKNEAKTKADFFEDEnGQRWLCTGDIGEFEPDGCLKIIDRKKDLVK 585
Cdd:PRK08314 365 GVDarvidpetlEELPPgevGEIVVHGPQVFKGYWNRPEATAEAFIEID-GKRFFRTGDLGRMDEEGYFFITDRLKRMIN 443
|
490 500
....*....|....*....|....*.
gi 115502350 586 lQAGEYVSLGKVEAALKNLPLVDNIC 611
Cdd:PRK08314 444 -ASGFKVWPAEVENLLYKHPAIQEAC 468
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
269-705 |
3.35e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 83.47 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 269 ENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERiPELGEEDVYIGYLPLA---HVLELSAELVClsh 345
Cdd:PRK12316 4684 AHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER-YELTPDDRVLQFMSFSfdgSHEGLYHPLIN--- 4759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 346 GCRI-----GYSSPQTLADQsskikkgskgdtsmlkptlmaavpeiMDRIYKNVMNkvsemssfqrnlFILAYNYKMEQI 420
Cdd:PRK12316 4760 GASVvirddSLWDPERLYAE--------------------------IHEHRVTVLV------------FPPVYLQQLAEH 4801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 421 SKGRNTPlcdsfvfrkvrsllgGNIRLLLCGGAPLSATTQRFMnICFCCPVG--QGYGLTESAGAGTISEVWDYNT-GRV 497
Cdd:PRK12316 4802 AERDGEP---------------PSLRVYCFGGEAVAQASYDLA-WRALKPVYlfNGYGPTETTVTVLLWKARDGDAcGAA 4865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 498 GAPLvccEIKLKNweEGGYFNTDKPHPR-----GEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEFE 569
Cdd:PRK12316 4866 YMPI---GTPLGN--RSGYVLDGQLNPLpvgvaGELYLGGEGVARGYLERPALTAERFVPDpfgAPGGRLYRTGDLARYR 4940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 570 PDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDN--ICAYANSYHSYVIGFVVPNQKELTElarkkglkgtwee 647
Cdd:PRK12316 4941 ADGVIDYLGRVDHQVKIR-GFRIELGEIEARLREHPAVREavVIAQEGAVGKQLVGYVVPQDPALAD------------- 5006
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 115502350 648 lcnSCEMENEVLKVLsEAAISASLEKFEIPVK-IRLSPEPWTPETglvtdafKLKRKEL 705
Cdd:PRK12316 5007 ---ADEAQAELRDEL-KAALRERLPEYMVPAHlVFLARMPLTPNG-------KLDRKAL 5054
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
278-718 |
3.89e-16 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 82.23 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEED-VYIGYLPLAHVLELSAEL-VCLSHGcriGysspq 355
Cdd:PRK08180 208 PDTIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPpVLVDWLPWNHTFGGNHNLgIVLYNG---G----- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 356 TLAdqsskIKKGskgdtsmlKPT--LMAA----VPEIMDRIYKNVmNKVSEMssfqrnlfILAYnykMEqiskgRNTPLC 429
Cdd:PRK08180 280 TLY-----IDDG--------KPTpgGFDEtlrnLREISPTVYFNV-PKGWEM--------LVPA---LE-----RDAALR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 430 DSFvFRKVRsllggnirLLLCGGAPLSATT----QRF-MNIC-----FCCpvgqGYGLTESAGAGTISEVWDYNTGRVGA 499
Cdd:PRK08180 330 RRF-FSRLK--------LLFYAGAALSQDVwdrlDRVaEATCgerirMMT----GLGMTETAPSATFTTGPLSRAGNIGL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PLVCCEIKLKnwEEGGYFntdkphprgEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEF-EPDgclkiiD 578
Cdd:PRK08180 397 PAPGCEVKLV--PVGGKL---------EVRVKGPNVTPGYWRAPELTAEAF--DEEG--YYRSGDAVRFvDPA------D 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 579 RKKDLV---------KLQAGEYVSLGKVEAALKNL--PLVDNICAyANSYHSYVIGFVVPNQKELTELARkKGLKGTWEE 647
Cdd:PRK08180 456 PERGLMfdgriaedfKLSSGTWVSVGPLRARAVSAgaPLVQDVVI-TGHDRDEIGLLVFPNLDACRRLAG-LLADASLAE 533
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115502350 648 LCNSCEMEN---EVLKVLSEAAISASLEkfeiPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYG 718
Cdd:PRK08180 534 VLAHPAVRAafrERLARLNAQATGSSTR----VARALLLDEPPSLDAGEITDKGYINQRAVLARRAALVEALYA 603
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
278-627 |
3.91e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 81.59 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPelGEEdvyigylpLAHVL-------ELSA-ELVC-LSHGCR 348
Cdd:cd12115 104 PDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFS--AEE--------LAGVLastsicfDLSVfELFGpLATGGK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 IgysspqTLADQS-SKIKKGSKGDTSMLK--PTLMAAVPEiMDRIYKNV--MNKVSEmsSFQRNLfiLAYNYKMEQIskg 423
Cdd:cd12115 174 V------VLADNVlALPDLPAAAEVTLINtvPSAAAELLR-HDALPASVrvVNLAGE--PLPRDL--VQRLYARLQV--- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 424 rntplcdsfvfRKVRSLLGgnirlllcggaPLSATTQRFMnicfcCPVGQGYGLTESAG---AGTISEVWDyntgRVGAP 500
Cdd:cd12115 240 -----------ERVVNLYG-----------PSEDTTYSTV-----APVPPGASGEVSIGrplANTQAYVLD----RALQP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 LvcceiklknweeggyfntdKPHPRGEILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGCLKIID 578
Cdd:cd12115 289 V-------------------PLGVPGELYIGGAGVARGYLGRPGLTAERFLPDpfGPGARLYRTGDLVRWRPDGLLEFLG 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 115502350 579 RKKDLVKLQaGEYVSLGKVEAALKNLPLVDNICAYA---NSYHSYVIGFVVP 627
Cdd:cd12115 350 RADNQVKVR-GFRIELGEIEAALRSIPGVREAVVVAigdAAGERRLVAYIVA 400
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
248-629 |
5.01e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.90 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 248 PKGIIVHTMAAVEALGAKASMENqPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERiPELGEEDVYIGY 327
Cdd:PRK12467 626 PAGLRSLCLDEPADLLCGYSGHN-PEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAER-LQLAADDSMLMV 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 328 LPLAHVLELSAELVCLSHGCRIGYSSPQTLADQsskikkgskgdtsmlkptlmAAVPEIMDRIYKNVMNKVSEMssfqrn 407
Cdd:PRK12467 704 STFAFDLGVTELFGALASGATLHLLPPDCARDA--------------------EAFAALMADQGVTVLKIVPSH------ 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 408 lfilaynYKMeqiskgrntpLCDSFVFRKVRSLlggniRLLLCGGAPLS-ATTQRFMNICFCCPVGQGYGLTESAGAGTI 486
Cdd:PRK12467 758 -------LQA----------LLQASRVALPRPQ-----RALVCGGEALQvDLLARVRALGPGARLINHYGPTETTVGVST 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 487 SEV----WDYNTGRVGAPLVCCEIKLKNweegGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRW 559
Cdd:PRK12467 816 YELsdeeRDFGNVPIGQPLANLGLYILD----HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDpfgADGGRL 891
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115502350 560 LCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDN--ICAYANSYHSYVIGFVVPNQ 629
Cdd:PRK12467 892 YRTGDLARYRADGVIEYLGRMDHQVKIR-GFRIELGEIEARLLAQPGVREavVLAQPGDAGLQLVAYLVPAA 962
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
256-605 |
9.16e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 80.62 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 256 MAAVEALGAKASMENQPHSKPLPSD-IAVIMYTSGSTGLPKGVMISHSNIIA-----GITGmaeripELGEEDVYIGYLP 329
Cdd:PRK09088 111 VEDLAAFIASADALEPADTPSIPPErVSLILFTSGTSGQPKGVMLSERNLQQtahnfGVLG------RVDAHSSFLCDAP 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 330 LAHVLELSAEL-VCLSHGCRI----GYSSPQTLadqsskikkGSKGDTSmLKPTLMAAVPEIMDRIyknvmnkvsemssf 404
Cdd:PRK09088 185 MFHIIGLITSVrPVLAVGGSIlvsnGFEPKRTL---------GRLGDPA-LGITHYFCVPQMAQAF-------------- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 405 qrnlfilaynykmeqiskgRNTPLCDSFVFRKVRSLLggnirlllCGGAPLSATTQRFMnICFCCPVGQGYGLTEsagAG 484
Cdd:PRK09088 241 -------------------RAQPGFDAAALRHLTALF--------TGGAPHAAEDILGW-LDDGIPMVDGFGMSE---AG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 485 TI------SEVWDYNTGRVGAPLVCCEIKLKNWEEggyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFfeDENGqr 558
Cdd:PRK09088 290 TVfgmsvdCDVIRAKAGAAGIPTPTVQTRVVDDQG----NDCPAGVPGELLLRGPNLSPGYWRRPQATARAF--TGDG-- 361
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 115502350 559 WLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLP 605
Cdd:PRK09088 362 WFRTGDIARRDADGFFWVVDRKKDMF-ISGGENVYPAEIEAVLADHP 407
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
275-584 |
1.16e-15 |
|
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: 80.22 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 275 KPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVLELSA-ELVCLSHGCRigyss 353
Cdd:cd05908 102 CELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNST-EWKTKDRILSWMPLTHDMGLIAfHLAPLIAGMN----- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 354 pQTLADQSSKIKkgskgdtsmlKPTLMaavpeimdrIYKNVMNKVSEMSS--FQRNLFI------LAYNYKMEQISKGRN 425
Cdd:cd05908 176 -QYLMPTRLFIR----------RPILW---------LKKASEHKATIVSSpnFGYKYFLktlkpeKANDWDLSSIRMILN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 426 ------TPLCDSFVFRKVRSLLGGNIRLLLCG------GAPLSATTQRFMNICFccpVGQGYGLTESAGAGTISEVWDYN 493
Cdd:cd05908 236 gaepidYELCHEFLDHMSKYGLKRNAILPVYGlaeasvGASLPKAQSPFKTITL---GRRHVTHGEPEPEVDKKDSECLT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 494 TGRVGAPLVCCEIKLKNWE----EGGYFntdkphprGEILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGeFE 569
Cdd:cd05908 313 FVEVGKPIDETDIRICDEDnkilPDGYI--------GHIQIRGKNVTPGYYNNPEATAKVFTDDG----WLKTGDLG-FI 379
|
330
....*....|....*
gi 115502350 570 PDGCLKIIDRKKDLV 584
Cdd:cd05908 380 RNGRLVITGREKDII 394
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
125-607 |
1.69e-15 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 79.90 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 125 KKVILGQYNWLSYEDVFVRAFNFGNGLQM-LGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALN 203
Cdd:PRK06839 18 RIAIITEEEEMTYKQLHEYVSKVAAYLIYeLNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 204 ETEVTNIITSKELLQTKLKdivslvprLRHIITVdgKPPTWSEFPKGIIVHtmaavEALGAKASMENQPHskplpsdiaV 283
Cdd:PRK06839 98 DSGTTVLFVEKTFQNMALS--------MQKVSYV--QRVISITSLKEIEDR-----KIDNFVEKNESASF---------I 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 284 IMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHV--LELSAeLVCLSHGCRIgysspqTLADQS 361
Cdd:PRK06839 154 ICYTSGTTGKPKGAVLTQENMFWNALNNTFAI-DLTMHDRSIVLLPLFHIggIGLFA-FPTLFAGGVI------IVPRKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 362 SKIKKGSKGDTSmlKPTLMAAVPEIMDRIYKNVMNKVSEMSSfqrnlfilaynykmeqiskgrntplcdsfvfrkvrsll 441
Cdd:PRK06839 226 EPTKALSMIEKH--KVTVVMGVPTIHQALINCSKFETTNLQS-------------------------------------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 442 ggnIRLLLCGGAPLSAT-TQRFMNICFccPVGQGYGLTESAGAGTISEVWDY--NTGRVGAPLVCCEIKL-----KNWEE 513
Cdd:PRK06839 266 ---VRWFYNGGAPCPEElMREFIDRGF--LFGQGFGMTETSPTVFMLSEEDArrKVGSIGKPVLFCDYELidenkNKVEV 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 GGYfntdkphprGEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVS 593
Cdd:PRK06839 341 GEV---------GELLIRGPNVMKEYWNRPDATEETI---QDG--WLCTGDLARVDEDGFVYIVGRKKEMI-ISGGENIY 405
|
490
....*....|....
gi 115502350 594 LGKVEAALKNLPLV 607
Cdd:PRK06839 406 PLEVEQVINKLSDV 419
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
278-607 |
2.12e-15 |
|
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: 78.29 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAeRIPELGEEDVYIGYLPLAHVLELSAELVC-LSHGCRIGYSSPQt 356
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLA-LNSLFDPDDVLLCGLPLFHVNGSVVTLLTpLASGAHVVLAGPA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 357 ladqsskikkGSKGdtsmlkptlmaavPEIMDRIYKNVMN-KVSEMSSFQRNLFILAynykmeQISKGRNTplcdsfvfr 435
Cdd:cd05944 79 ----------GYRN-------------PGLFDNFWKLVERyRITSLSTVPTVYAALL------QVPVNADI--------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 436 kvrsllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTIS-EVWDYNTGRVGAPLVCCEIKLKNWE-E 513
Cdd:cd05944 121 -------SSLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLVAVNpPDGPKRPGSVGLRLPYARVRIKVLDgV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 GGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFfedenGQRWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVS 593
Cdd:cd05944 194 GRLLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNAFV-----ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGGHNID 267
|
330
....*....|....
gi 115502350 594 LGKVEAALKNLPLV 607
Cdd:cd05944 268 PALIEEALLRHPAV 281
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
278-633 |
2.62e-15 |
|
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: 79.29 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPL---AHVLELSAELVClSHGCRIgyssp 354
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIY-QGEHLRVALFASIsfdASVTEIFASLLS-GNTLYI----- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 355 qtladqsskIKKGSKGDtsmlkptlmaaVPEIMDRIYKNVMNkvsemssfqrnlfilaynykmeqISKGRNTPLCdsfVF 434
Cdd:cd17655 209 ---------VRKETVLD-----------GQALTQYIRQNRIT-----------------------IIDLTPAHLK---LL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 435 RKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFC--CPVGQGYGLTES---AGAGTISEVWDyNTGRV--GAPLVCCEIK 507
Cdd:cd17655 243 DAADDSEGLSLKHLIVGGEALSTELAKKIIELFGtnPTITNAYGPTETtvdASIYQYEPETD-QQVSVpiGKPLGNTRIY 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNwEEGgyfntdKPHP---RGEILIGGQSVTMGYYKNEAKTKADFFEDE--NGQRWLCTGDIGEFEPDGCLKIIDRKKD 582
Cdd:cd17655 322 ILD-QYG------RPQPvgvAGELYIGGEGVARGYLNRPELTAEKFVDDPfvPGERMYRTGDLARWLPDGNIEFLGRIDH 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 115502350 583 LVKLQaGEYVSLGKVEAALKNLPLVDNICAYANSYHS---YVIGFVVPNqKELT 633
Cdd:cd17655 395 QVKIR-GYRIELGEIEARLLQHPDIKEAVVIARKDEQgqnYLCAYIVSE-KELP 446
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
269-705 |
3.52e-15 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 80.39 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 269 ENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVLELSAELVCLSHGCR 348
Cdd:PRK12316 645 EENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAY-GLGVGDTVLQKTPFSFDVSVWEFFWPLMSGAR 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 IGYSSPQTLADqsskikkgskgdtsmlkptlMAAVPEIMDRIYKNVMNKV-SEMSSFQRNlfilaynykmeqiskgRNTP 427
Cdd:PRK12316 724 LVVAAPGDHRD--------------------PAKLVELINREGVDTLHFVpSMLQAFLQD----------------EDVA 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 428 LCDSfvfrkvrsllggnIRLLLCGGAPLSATTQ-RFMNICFCCPVGQGYGLTESAGAGT----ISEVWDynTGRVGAPL- 501
Cdd:PRK12316 768 SCTS-------------LRRIVCSGEALPADAQeQVFAKLPQAGLYNLYGPTEAAIDVThwtcVEEGGD--SVPIGRPIa 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 502 -VCCEIKLKNWEeggyfntdkPHP---RGEILIGGQSVTMGYYKNEAKTKADFFEDE--NGQRWLCTGDIGEFEPDGCLK 575
Cdd:PRK12316 833 nLACYILDANLE---------PVPvgvLGELYLAGRGLARGYHGRPGLTAERFVPSPfvAGERMYRTGDLARYRADGVIE 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 576 IIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDNICAYANSYHSYViGFVVPnqkeltelarkkglkgtweelcnscEME 655
Cdd:PRK12316 904 YAGRIDHQVKLR-GLRIELGEIEARLLEHPWVREAAVLAVDGKQLV-GYVVL-------------------------ESE 956
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 115502350 656 NEVLKVLSEAAISASLEKFEIPVKI-RLSPEPWTPETglvtdafKLKRKEL 705
Cdd:PRK12316 957 GGDWREALKAHLAASLPEYMVPAQWlALERLPLTPNG-------KLDRKAL 1000
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
135-607 |
4.69e-15 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 78.34 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQTkLKDIVSLVPRLRHIITVDGKPPTWSEFpkgiivhtmaaVEALGAKASMENQPHSKPlpSDIAVIMYTSGSTGLP 294
Cdd:TIGR02262 111 ALLPV-IKAALGKSPHLEHRVVVGRPEAGEVQL-----------AELLATESEQFKPAATQA--DDPAFWLYSSGSTGMP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 295 KGVMISHSNIIAGITGMAERIPELGEEDVYigylplahvleLSAELVCLSHGCRIGYSSPQTLadqsskikkgskGDTSM 374
Cdd:TIGR02262 177 KGVVHTHSNPYWTAELYARNTLGIREDDVC-----------FSAAKLFFAYGLGNALTFPMSV------------GATTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 375 L---KPTlMAAVPEIMDRIYKNVMNKVSEMssFQRNLfilaynykmeqiskgrNTPLCdsfvfrkvRSLLGGNIRLLLCG 451
Cdd:TIGR02262 234 LmgeRPT-PDAVFDRLRRHQPTIFYGVPTL--YAAML----------------ADPNL--------PSEDQVRLRLCTSA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 452 GAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNwEEGGYFNTDKPhprGEILIG 531
Cdd:TIGR02262 287 GEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVG-DGGQDVADGEP---GELLIS 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115502350 532 GQSVTMGYYKNEAKTkADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLV 607
Cdd:TIGR02262 363 GPSSATMYWNNRAKS-RDTFQGE----WTRSGDKYVRNDDGSYTYAGRTDDMLKV-SGIYVSPFEIESALIQHPAV 432
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
280-607 |
5.17e-15 |
|
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: 77.89 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDV-------YIGY-------LPLAhvleLSAELVCLSh 345
Cdd:cd05919 92 DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRvfssakmFFGYglgnslwFPLA----VGASAVLNP- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 346 gcriGYSSPQTLADQSSKikkgskgdtsmLKPTLMAAVPEImdriYKNVMnkvsemssfqrnlfilaynykmeqiskgrn 425
Cdd:cd05919 167 ----GWPTAERVLATLAR-----------FRPTVLYGVPTF----YANLL------------------------------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 426 tPLCDsFVFRKVRSllggnIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCE 505
Cdd:cd05919 198 -DSCA-GSPDALRS-----LRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 506 IKLKNwEEGgyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDengqrWLCTGDIGEFEPDGCLKIIDRKKDLVK 585
Cdd:cd05919 271 IRLVD-EEG---HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-----WYRTGDKFCRDADGWYTHAGRADDMLK 341
|
330 340
....*....|....*....|..
gi 115502350 586 LqAGEYVSLGKVEAALKNLPLV 607
Cdd:cd05919 342 V-GGQWVSPVEVESLIIQHPAV 362
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
278-584 |
9.65e-15 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 77.61 E-value: 9.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAErIPELGEEDVYIGYLPLAHVlelsaelvclsHGCRIgySSPQTL 357
Cdd:PRK07514 155 ADDLAAILYTSGTTGRSKGAMLSHGNLLSNALTLVD-YWRFTPDDVLIHALPIFHT-----------HGLFV--ATNVAL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 ADQSSKIKKgSKGDTS-----MLKPTLMAAVPEIMDRIYKNvmnkvsemSSFQRNLfilaynykmeqiskgrntplcdsf 432
Cdd:PRK07514 221 LAGASMIFL-PKFDPDavlalMPRATVMMGVPTFYTRLLQE--------PRLTREA------------------------ 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 433 vfrkvrsllGGNIRLLLCGGAPLSATTQRfmniCFCCPVGQG----YGLTESAgagtisevwdYNT----------GRVG 498
Cdd:PRK07514 268 ---------AAHMRLFISGSAPLLAETHR----EFQERTGHAilerYGMTETN----------MNTsnpydgerraGTVG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 499 APLVCCEIKLKNWEEGgyfntdKPHPRGE---ILIGGQSVTMGYYKNEAKTKADFFEDenGqrWLCTGDIGEFEPDGCLK 575
Cdd:PRK07514 325 FPLPGVSLRVTDPETG------AELPPGEigmIEVKGPNVFKGYWRMPEKTAEEFRAD--G--FFITGDLGKIDERGYVH 394
|
....*....
gi 115502350 576 IIDRKKDLV 584
Cdd:PRK07514 395 IVGRGKDLI 403
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
277-639 |
9.73e-15 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 77.62 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 277 LPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVLELSAELVC-LSHGCRI-----G 350
Cdd:PRK05852 174 LRPDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGY-RLSPRDATVAVMPLYHGHGLIAALLAtLASGGAVllparG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 351 YSSPQTLADqsskikkgskgDTSMLKPTLMAAVPEImdriYKNVMNKVSEMSSfqrnlfilaynykmeqiskGRNTPlcd 430
Cdd:PRK05852 253 RFSAHTFWD-----------DIKAVGATWYTAVPTI----HQILLERAATEPS-------------------GRKPA--- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 431 sfVFRKVRSllggnirlllCGgAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEV-WDYNT----------GRVGA 499
Cdd:PRK05852 296 --ALRFIRS----------CS-APLTAETAQALQTEFAAPVVCAFGMTEATHQVTTTQIeGIGQTenpvvstglvGRSTG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PlvccEIKLKNwEEGGYFntdKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDengqrWLCTGDIGEFEPDGCLKIIDR 579
Cdd:PRK05852 363 A----QIRIVG-SDGLPL---PAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG-----WLRTGDLGSLSAAGDLSIRGR 429
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115502350 580 KKDLVKlQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSY---VIGFVVPNQ------KELTELARKK 639
Cdd:PRK05852 430 IKELIN-RGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYgeaVAAVIVPREsapptaEELVQFCRER 497
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
219-718 |
1.46e-14 |
|
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: 77.09 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 219 TKLKDIVSLV-PRLrhIITVDGKP---PTWSEFPKGI-IVHTMAAVEALGAK--ASMENQP--------HSKPLPSDIAV 283
Cdd:cd05921 92 AKLKHLFELLkPGL--VFAQDAAPfarALAAIFPLGTpLVVSRNAVAGRGAIsfAELAATPptaavdaaFAAVGPDTVAK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 284 IMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEED-VYIGYLPLAHVLELSA--ELVCLSHGcrigysspqTLADQ 360
Cdd:cd05921 170 FLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpVLVDWLPWNHTFGGNHnfNLVLYNGG---------TLYID 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 361 SSKIKKGSKGDTsmlkptlMAAVPEIMDRIYKNVmNKVSEMssfqrnlFILAynykMEqiskgRNTPLCDSFvFRKVrsl 440
Cdd:cd05921 241 DGKPMPGGFEET-------LRNLREISPTVYFNV-PAGWEM-------LVAA----LE-----KDEALRRRF-FKRL--- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 441 lggniRLLLCGGAPLS------------ATTQRFMnicfccPVGQGYGLTESAGAGTISeVWDYN-TGRVGAPLVCCEIK 507
Cdd:cd05921 293 -----KLMFYAGAGLSqdvwdrlqalavATVGERI------PMMAGLGATETAPTATFT-HWPTErSGLIGLPAPGTELK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKnwEEGGYFntdkphprgEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEF-EPDgclkiiDRKKDLV-- 584
Cdd:cd05921 361 LV--PSGGKY---------EVRVKGPNVTPGYWRQPELTAQAF--DEEG--FYCLGDAAKLaDPD------DPAKGLVfd 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 585 -------KLQAGEYVSLGKVEAALKNL--PLVDN--ICAYANSYhsyvIGF-VVPNQKELTELARKKGLKgtweelcnsc 652
Cdd:cd05921 420 grvaedfKLASGTWVSVGPLRARAVAAcaPLVHDavVAGEDRAE----VGAlVFPDLLACRRLVGLQEAS---------- 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115502350 653 emENEVLKVLS-EAAISASLEKFE--------IPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYG 718
Cdd:cd05921 486 --DAEVLRHAKvRAAFRDRLAALNgeatgsssRIARALLLDEPPSIDKGEITDKGYINQRAVLERRAALVERLYA 558
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
277-630 |
2.83e-14 |
|
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: 75.58 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 277 LPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMaERIPELGEE------------DVYIGylPLAHVLELSAELVCLS 344
Cdd:cd17650 91 QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW-RREYELDSFpvrllqmasfsfDVFAG--DFARSLLNGGTLVICP 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 345 HGCRIgysSPQTLADqsskIKKGSKGDTSMLKPTLMAAVpeiMDRIYKNVMnKVSEMssfqrNLFILaynykmeqiskGR 424
Cdd:cd17650 168 DEVKL---DPAALYD----LILKSRITLMESTPALIRPV---MAYVYRNGL-DLSAM-----RLLIV-----------GS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 425 NTPLCDSFVFRKVRslLGGNIRLLlcggaplsattqrfmnicfccpvgQGYGLTESAGAGTISEVWDYNTGR-----VGA 499
Cdd:cd17650 221 DGCKAQDFKTLAAR--FGQGMRII------------------------NSYGVTEATIDSTYYEEGRDPLGDsanvpIGR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PLVCCEIKLKNweeggyfNTDKPHP---RGEILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGCL 574
Cdd:cd17650 275 PLPNTAMYVLD-------ERLQPQPvgvAGELYIGGAGVARGYLNRPELTAERFVENpfAPGERMYRTGDLARWRADGNV 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 115502350 575 KIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDNICAYA---NSYHSYVIGFVVPNQK 630
Cdd:cd17650 348 ELLGRVDHQVKIR-GFRIELGEIESQLARHPAIDEAVVAVredKGGEARLCAYVVAAAT 405
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
278-607 |
2.95e-14 |
|
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: 75.48 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPeLGEEDVYIGYLPL---AHVLELSAELVClshGCRIGYSSP 354
Cdd:cd17649 93 PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYG-LTPGDRELQFASFnfdGAHEQLLPPLIC---GACVVLRPD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 355 QTLADQsskikkgskgdtsmlkptlmAAVPEIMDRIYKNVMNkvsemssfqrnlFILAYNYK----MEQISKGRNTPLcd 430
Cdd:cd17649 169 ELWASA--------------------DELAEMVRELGVTVLD------------LPPAYLQQlaeeADRTGDGRPPSL-- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 431 sfvfrkvrsllggniRLLLCGGAPLSATTQR--FMNICFCCpvgQGYGLTEsagaGTISE-VWDYNTGR--------VGA 499
Cdd:cd17649 215 ---------------RLYIFGGEALSPELLRrwLKAPVRLF---NAYGPTE----ATVTPlVWKCEAGAaragasmpIGR 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PLvcceiklknweeGGY----FNTD-KPHPR---GEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEF 568
Cdd:cd17649 273 PL------------GGRsayiLDADlNPVPVgvtGELYIGGEGLARGYLGRPELTAERFVPDpfgAPGSRLYRTGDLARW 340
|
330 340 350
....*....|....*....|....*....|....*....
gi 115502350 569 EPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLV 607
Cdd:cd17649 341 RDDGVIEYLGRVDHQVKIR-GFRIELGEIEAALLEHPGV 378
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
135-627 |
4.26e-14 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 76.53 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQtklkdivslvpRLrhiitvdgkPPtwsefPKGIivhtmaAVEALGAKASMENQPHSKPL----PSDIAVIMYTSGS 290
Cdd:PRK12316 2109 HLLE-----------RL---------PL-----PAGV------ARLPLDRDAEWADYPDTAPAvqlaGENLAYVIYTSGS 2157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 291 TGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAhvLELSAE--LVCLSHGCRI-----GYSSPQTLADQSSK 363
Cdd:PRK12316 2158 TGLPKGVAVSHGALVAHCQAAGERY-ELSPADCELQFMSFS--FDGAHEqwFHPLLNGARVlirddELWDPEQLYDEMER 2234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 364 ikkgsKGDTsmlkptlMAAVPEIMdriyknvmnkvsemssfqrnLFILAynykmEQISKGRNTPlcdsfvfrkvrsllgg 443
Cdd:PRK12316 2235 -----HGVT-------ILDFPPVY--------------------LQQLA-----EHAERDGRPP---------------- 2261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 444 NIRLLLCGGAPLSAT----------TQRFMNicfccpvgqGYGLTESAGAGTISEV-WDYNTGRVGAPLVCCEIKLKNWE 512
Cdd:PRK12316 2262 AVRVYCFGGEAVPAAslrlawealrPVYLFN---------GYGPTEAVVTPLLWKCrPQDPCGAAYVPIGRALGNRRAYI 2332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 513 EGGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaG 589
Cdd:PRK12316 2333 LDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDpfsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIR-G 2411
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 115502350 590 EYVSLGKVEAALKNLPLVDN--ICAYANSYHSYVIGFVVP 627
Cdd:PRK12316 2412 FRIELGEIEARLQAHPAVREavVVAQDGASGKQLVAYVVP 2451
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
279-626 |
4.85e-14 |
|
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: 73.83 E-value: 4.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 279 SDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLA 358
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 359 DQSSKIKKGSKGDTSMLKPTLMAAVPEimdrIYKNVMNKVSEMssfqrnlfilaynykmeqiskgrntplcdsfvfrkvr 438
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVS----ELKSANATVPSL------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 439 sllggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDY-NTGRVGAPLVCCEIKLKNWEEGGYF 517
Cdd:cd17635 120 -------RLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGTALCLPTDDDSiEINAVGRPYPGVDVYLAATDGIAGP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 518 NTDKphprGEILIGGQSVTMGYYKNEAKTkADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKV 597
Cdd:cd17635 193 SASF----GTIWIKSPANMLGYWNNPERT-AEVLIDG----WVNTGDLGERREDGFLFITGRSSESI-NCGGVKIAPDEV 262
|
330 340 350
....*....|....*....|....*....|..
gi 115502350 598 EAALKNLPLVDNICAYA---NSYHSYVIGFVV 626
Cdd:cd17635 263 ERIAEGVSGVQECACYEisdEEFGELVGLAVV 294
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
278-607 |
6.63e-14 |
|
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: 74.54 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGmaERIPELGEEDVYIGYLPL---AHVLELsaeLVCLSHGCRIGYSSP 354
Cdd:cd12117 135 PDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKN--TNYVTLGPDDRVLQTSPLafdASTFEI---WGALLNGARLVLAPK 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 355 QTLADQSSkikkgskgdtsmlkptLMAAVPEimdriyknvmNKVSEM---SSfqrnLFilaynykmeqiskgrntplcdS 431
Cdd:cd12117 210 GTLLDPDA----------------LGALIAE----------EGVTVLwltAA----LF---------------------N 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 432 FVFRKVRSLLGGnIRLLLCGGAPLS-ATTQRFMNICFCCPVGQGYGLTESAGAGTISEV--WDYNTGRV--GAPLVccei 506
Cdd:cd12117 239 QLADEDPECFAG-LRELLTGGEVVSpPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVteLDEVAGSIpiGRPIA---- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 507 klknweeggyfNTD--------KPHPR---GEILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGC 573
Cdd:cd12117 314 -----------NTRvyvldedgRPVPPgvpGELYVGGDGLALGYLNRPALTAERFVADpfGPGERLYRTGDLARWLPDGR 382
|
330 340 350
....*....|....*....|....*....|....
gi 115502350 574 LKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLV 607
Cdd:cd12117 383 LEFLGRIDDQVKIR-GFRIELGEIEAALRAHPGV 415
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
230-648 |
7.65e-14 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 74.55 E-value: 7.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 230 RLRHIITVdGKPP---TWSEFP---KGIIVHTMAAVEALGAKASMENQPHS-KPlpSDIAVIMYTSGSTGLPKGVMISHS 302
Cdd:PRK04813 90 RIEMIIEV-AKPSliiATEELPleiLGIPVITLDELKDIFATGNPYDFDHAvKG--DDNYYIIFTSGTTGKPKGVQISHD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 303 NIIAgITGMAERIPELGEEDVYIGYLP---------LAHVLELSAELVCLSHgcrigysspqtlaDQSSKIKkgskgdts 373
Cdd:PRK04813 167 NLVS-FTNWMLEDFALPEGPQFLNQAPysfdlsvmdLYPTLASGGTLVALPK-------------DMTANFK-------- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 374 mlkpTLMAAVPEImdRIykNVMnkVSeMSSFqrnlfilaynykMEqiskgrntpLC---DSFVFRKVRSLlggnIRLLLC 450
Cdd:PRK04813 225 ----QLFETLPQL--PI--NVW--VS-TPSF------------AD---------MClldPSFNEEHLPNL----THFLFC 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 451 GGApLSATT-----QRF-----MNIcfccpvgqgYGLTESAGAGTISEVWD-----YNTGRVGAPLVCCEIKLKNWEEGG 515
Cdd:PRK04813 269 GEE-LPHKTakkllERFpsatiYNT---------YGPTEATVAVTSIEITDemldqYKRLPIGYAKPDSPLLIIDEEGTK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 516 YFNTDKphprGEILIGGQSVTMGYYKNEAKTKADFFEdENGQRWLCTGDIGEFEpDGCLKIIDRKKDLVKLqAGEYVSLG 595
Cdd:PRK04813 339 LPDGEQ----GEIVISGPSVSKGYLNNPEKTAEAFFT-FDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKL-NGYRIELE 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 115502350 596 KVEAALKNLPLVDNICA---YANSYHSYVIGFVVPNQKELT-ELARKKGLKgtwEEL 648
Cdd:PRK04813 412 EIEQNLRQSSYVESAVVvpyNKDHKVQYLIAYVVPKEEDFErEFELTKAIK---KEL 465
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
278-634 |
1.04e-13 |
|
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: 73.97 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPlAHVLELSAELVCLShgcrigYSSPQTL 357
Cdd:cd17648 93 STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFFS-NYVFDFFVEQMTLA------LLNGQKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 A--DQSSKIKKGskgdtsmlkptlmaAVPEIMDRiyknvmNKVSEMSSfqrnlfilaynykmeqiskgrnTP-LCDSFVF 434
Cdd:cd17648 166 VvpPDEMRFDPD--------------RFYAYINR------EKVTYLSG----------------------TPsVLQQYDL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 435 RKVRSLlggniRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEvwdYNTGR-----VGAPL--VCCEIk 507
Cdd:cd17648 204 ARLPHL-----KRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRF---FPGDQrfdksLGRPVrnTKCYV- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 lknweeggyFNTD-KPHP---RGEILIGGQSVTMGYYKNEAKTKADF----FEDE------NGQRWLCTGDIGEFEPDGC 573
Cdd:cd17648 275 ---------LNDAmKRVPvgaVGELYLGGDGVARGYLNRPELTAERFlpnpFQTEqerargRNARLYKTGDLVRWLPSGE 345
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 574 LKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLV---------DNICAYANSyHSYVIGFVVPNQKELTE 634
Cdd:cd17648 346 LEYLGRNDFQVKIR-GQRIEPGEVEAALASYPGVrecavvakeDASQAQSRI-QKYLVGYYLPEPGHVPE 413
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
263-717 |
1.30e-13 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 74.99 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 263 GAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVLELSAELVC 342
Cdd:PRK12316 3180 GDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAY-GLGVGDRVLQFTTFSFDVFVEELFWP 3258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 343 LSHGCRIGYSSPQTLADQsskikkgskgdtsmlkptlmAAVPEIMDRIYKNVMNKVSEMSSFqrnlfilaynykmeqisk 422
Cdd:PRK12316 3259 LMSGARVVLAGPEDWRDP--------------------ALLVELINSEGVDVLHAYPSMLQA------------------ 3300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 423 grntplcdsfVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFccPVGQGYGLTESAGAGTISEVWDYNTGR--VGAP 500
Cdd:PRK12316 3301 ----------FLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGL--PLYNLYGPTEATITVTHWQCVEEGKDAvpIGRP 3368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 LVCCEIKLKNweegGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGCLKIID 578
Cdd:PRK12316 3369 IANRACYILD----GSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDpfVPGERLYRTGDLARYRADGVIEYIG 3444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 579 RKKDLVKLQaGEYVSLGKVEAALKNLPLVDNICAYANSYHSyVIGFVVPNQKEltelarkkglkGTWEelcnscemenEV 658
Cdd:PRK12316 3445 RVDHQVKIR-GFRIELGEIEARLLEHPWVREAVVLAVDGRQ-LVAYVVPEDEA-----------GDLR----------EA 3501
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 659 LKvlseAAISASLEKFEIPVK-IRLSPEPWTPETglvtdafKLKRKELKTHYQADIERMY 717
Cdd:PRK12316 3502 LK----AHLKASLPEYMVPAHlLFLERMPLTPNG-------KLDRKALPRPDAALLQQDY 3550
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
220-599 |
2.00e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.54 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 220 KLKDIVSLV-PRL----------RHIITVDGKPPTW---SEFPKGIIVHTMAAVEALGAKASMEnQPHSKPLPSDIAVIM 285
Cdd:PRK12582 148 KLKHLFDLVkPRVvfaqsgapfaRALAALDLLDVTVvhvTGPGEGIASIAFADLAATPPTAAVA-AAIAAITPDTVAKYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 286 YTSGSTGLPKGVMISHSNIIAGITGMAERIPEL--GEEDVYIGYLPLAHVLELSAELvclsHGCRIGYSspqTLadqssK 363
Cdd:PRK12582 227 FTSGSTGMPKAVINTQRMMCANIAMQEQLRPREpdPPPPVSLDWMPWNHTMGGNANF----NGLLWGGG---TL-----Y 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 364 IKKGsKGDTSMLKPTLmAAVPEIMDRIYKNVMnkvsemssfqrnlfiLAYNYKMEQISKgrNTPLCDSFvFRkvrsllgg 443
Cdd:PRK12582 295 IDDG-KPLPGMFEETI-RNLREISPTVYGNVP---------------AGYAMLAEAMEK--DDALRRSF-FK-------- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 444 NIRLLLCGGAPLS-------------ATTQRFmnicfccPVGQGYGLTESAGagTISEV-WDYN-TGRVGAPLVCCEIKL 508
Cdd:PRK12582 347 NLRLMAYGGATLSddlyermqalavrTTGHRI-------PFYTGYGATETAP--TTTGThWDTErVGLIGLPLPGVELKL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 509 KnweeggyfntdkphPRG---EILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEF-EPDGCLK--IID-RKK 581
Cdd:PRK12582 418 A--------------PVGdkyEVRVKGPNVTPGYHKDPELTAAAF--DEEG--FYRLGDAARFvDPDDPEKglIFDgRVA 479
|
410
....*....|....*...
gi 115502350 582 DLVKLQAGEYVSLGKVEA 599
Cdd:PRK12582 480 EDFKLSTGTWVSVGTLRP 497
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
141-718 |
2.19e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 73.10 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 141 FVRAFnfgnglQMLGQKPKTNIAIFCETRAE-WMIAAQACFMyNFQLVTLYAtLGGPAIvHA--LNETEVTNIITSKELL 217
Cdd:PRK06188 50 YIQAF------EALGLGTGDAVALLSLNRPEvLMAIGAAQLA-GLRRTALHP-LGSLDD-HAyvLEDAGISTLIVDPAPF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 218 QTKLKDIVSLVPRLRHIITVDGKPptwsefpkgiivhtmAAVEALGAKASMENQP-HSKPLPSDIAVIMYTSGSTGLPKG 296
Cdd:PRK06188 121 VERALALLARVPSLKHVLTLGPVP---------------DGVDLLAAAAKFGPAPlVAAALPPDIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 297 VMISHSNIIAGITG-MAERipELGEEDVYIGYLPLAH--------VLELSAELVCLShgcriGYSSPQTLAdqssKIKKg 367
Cdd:PRK06188 186 VMGTHRSIATMAQIqLAEW--EWPADPRFLMCTPLSHaggafflpTLLRGGTVIVLA-----KFDPAEVLR----AIEE- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 368 SKGDTSMLKPTLMAAV---PEIMDRiyknvmnkvsEMSSFQrnlfilaynykmeqiskgrntplcdsfvfrkvrsllggn 444
Cdd:PRK06188 254 QRITATFLVPTMIYALldhPDLRTR----------DLSSLE--------------------------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 445 irLLLCGGAPLSAT-----TQRFMNIcfccpVGQGYGLTESAGAGTISEVWDYNTGRV------GAPLVCCEIKLKNwEE 513
Cdd:PRK06188 285 --TVYYGASPMSPVrlaeaIERFGPI-----FAQYYGQTEAPMVITYLRKRDHDPDDPkrltscGRPTPGLRVALLD-ED 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 GGYFNTDKPhprGEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVklqageyVS 593
Cdd:PRK06188 357 GREVAQGEV---GEICVRGPLVMDGYWNRPEETAEAF---RDG--WLHTGDVAREDEDGFYYIVDRKKDMI-------VT 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 594 LG------KVEAALKNLPLVDNICayansyhsyVIGfvVPNQKeltelarkkglkgtWEELCNSCemenEVLKvlSEAAI 667
Cdd:PRK06188 422 GGfnvfprEVEDVLAEHPAVAQVA---------VIG--VPDEK--------------WGEAVTAV----VVLR--PGAAV 470
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 115502350 668 SAslEKFEIPVKIRLSPePWTPETGLVTDAF------KLKRKELKTHYQADIERMYG 718
Cdd:PRK06188 471 DA--AELQAHVKERKGS-VHAPKQVDFVDSLpltalgKPDKKALRARYWEGRGRAVG 524
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
260-607 |
7.94e-13 |
|
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: 71.21 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 260 EALGAKASMENQphskplpSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIgylplahvlelsae 339
Cdd:cd05972 69 EAAGAKAIVTDA-------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWL-GLRPDDIHW-------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 340 lvclshgcrigysspqTLADQSskikkGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSE-MSSFQRNLFILAYN-YKM 417
Cdd:cd05972 127 ----------------NIADPG-----WAKGAWSSFFGPWLLGATVFVYEGPRFDAERILElLERYGVTSFCGPPTaYRM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 418 EQiskgrnTPLCDSFVFrkvrsllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRV 497
Cdd:cd05972 186 LI------KQDLSSYKF--------SHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSM 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 498 GAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQSVTM--GYYKNEAKTKADFFEDengqrWLCTGDIGEFEPDGCLK 575
Cdd:cd05972 252 GRPTPGYDVAIID-DDG---RELPPGEEGDIAIKLPPPGLflGYVGDPEKTEASIRGD-----YYLTGDRAYRDEDGYFW 322
|
330 340 350
....*....|....*....|....*....|..
gi 115502350 576 IIDRKKDLVKlQAGEYVSLGKVEAALKNLPLV 607
Cdd:cd05972 323 FVGRADDIIK-SSGYRIGPFEVESALLEHPAV 353
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
278-644 |
1.15e-12 |
|
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: 70.66 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAgitgmaeripelgeedvyigylplahvlelsaelVCLSHGCRIGYsspqTL 357
Cdd:cd17645 103 PDDLAYVIYTSGSTGLPKGVMIEHHNLVN----------------------------------LCEWHRPYFGV----TP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 ADQSSKIKkGSKGDTSMLK--PTLMA-AVPEIMDRIYKNVMNKVSEMssFQRNLFILAYnykmeqiskgRNTPLCDSFVF 434
Cdd:cd17645 145 ADKSLVYA-SFSFDASAWEifPHLTAgAALHVVPSERRLDLDALNDY--FNQEGITISF----------LPTGAAEQFMQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 435 RKVRSLlggniRLLLCGGAPLSATTQRFMNICfccpvgQGYGLTESAGAGTISEV-WDYNTGRVGAPLVCCEIKLKNweE 513
Cdd:cd17645 212 LDNQSL-----RVLLTGGDKLKKIERKGYKLV------NNYGPTENTVVATSFEIdKPYANIPIGKPIDNTRVYILD--E 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 GgyfNTDKPH-PRGEILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGE 590
Cdd:cd17645 279 A---LQLQPIgVAGELCIAGEGLARGYLNRPELTAEKFIVHpfVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIR-GY 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 115502350 591 YVSLGKVEAALKNLPLVDNICAYA---NSYHSYVIGFVVPnQKELTELARKKGLKGT 644
Cdd:cd17645 355 RIEPGEIEPFLMNHPLIELAAVLAkedADGRKYLVAYVTA-PEEIPHEELREWLKND 410
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
186-607 |
1.30e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 70.75 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 186 LVTLYATLGGPAIVHALNETEVTNIITSKELLQTkLKDIVSLVPRLrHIITVDGKPPtwsEFPKGIIVHTMAaVEALGAK 265
Cdd:PRK08162 95 LNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEV-AREALALLPGP-KPLVIDVDDP---EYPGGRFIGALD-YEAFLAS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 266 ASMENQPHskpLPSD----IAvIMYTSGSTGLPKGVMISH--------SNIIAGitgmaeripELGEEDVYIGYLPLAHv 333
Cdd:PRK08162 169 GDPDFAWT---LPADewdaIA-LNYTSGTTGNPKGVVYHHrgaylnalSNILAW---------GMPKHPVYLWTLPMFH- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 334 lelsaelvclshgCRiGYSSPQTLAdqsskikkgskgdtsmlkptLMAAVpeimdriykNV-MNKVSEMSSFqrnlfila 412
Cdd:PRK08162 235 -------------CN-GWCFPWTVA--------------------ARAGT---------NVcLRKVDPKLIF-------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 413 ynykmEQISKGRNTPLCDSFVfrkVRSLL-----------GGNIRLLLCGGAPLSATTQRFMNICFCcpVGQGYGLTESA 481
Cdd:PRK08162 264 -----DLIREHGVTHYCGAPI---VLSALinapaewragiDHPVHAMVAGAAPPAAVIAKMEEIGFD--LTHVYGLTETY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 482 GAGTI---SEVWD--------YNTGRVGAPLVCCE-IKLKNWEeggyfnTDKPHPR-----GEILIGGQSVTMGYYKNEA 544
Cdd:PRK08162 334 GPATVcawQPEWDalplderaQLKARQGVRYPLQEgVTVLDPD------TMQPVPAdgetiGEIMFRGNIVMKGYLKNPK 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115502350 545 KTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLV 607
Cdd:PRK08162 408 ATEEAF---AGG--WFHTGDLAVLHPDGYIKIKDRSKDII-ISGGENISSIEVEDVLYRHPAV 464
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
198-607 |
2.11e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 70.07 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 198 IVHALNETEVTNIITSKELLqtKLKDIVSLVPRLRHIITV---DGKPPTWS-EFPKGIIVHTMAAVEALGAKASMENQPH 273
Cdd:PRK06178 122 LSYELNDAGAEVLLALDQLA--PVVEQVRAETSLRHVIVTslaDVLPAEPTlPLPDSLRAPRLAAAGAIDLLPALRACTA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 274 SKPLPS----DIAVIMYTSGSTGLPKGVMISHSNII---AGITGMAEripELGEEDVYIGYLP----------LAHVLEL 336
Cdd:PRK06178 200 PVPLPPpaldALAALNYTGGTTGMPKGCEHTQRDMVytaAAAYAVAV---VGGEDSVFLSFLPefwiagenfgLLFPLFS 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 337 SAELVCLshgcrigysspqtladqsskikkgSKGDTSmlkpTLMAAVPEImdRIYKNVM---NKVSEM---SSFQRNLFI 410
Cdd:PRK06178 277 GATLVLL------------------------ARWDAV----AFMAAVERY--RVTRTVMlvdNAVELMdhpRFAEYDLSS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 411 LaynykmeqiskgRNTPlCDSFVfRKvrslLGGNIRlllcggaplsattQRFMNICFCCPVGQGYGLTESAGAGTIS--- 487
Cdd:PRK06178 327 L------------RQVR-VVSFV-KK----LNPDYR-------------QRWRALTGSVLAEAAWGMTETHTCDTFTagf 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 488 EVWDYN-TGR---VGAPLVCCEIKLKNweeggyFNTDKPHP---RGEILIGGQSVTMGYYKNEAKTkADFFEDEngqrWL 560
Cdd:PRK06178 376 QDDDFDlLSQpvfVGLPVPGTEFKICD------FETGELLPlgaEGEIVVRTPSLLKGYWNKPEAT-AEALRDG----WL 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 115502350 561 CTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLV 607
Cdd:PRK06178 445 HTGDIGKIDEQGFLHYLGRRKEMLKVN-GMSVFPSEVEALLGQHPAV 490
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
135-607 |
2.74e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 69.96 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:PRK07788 75 LTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDD 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLqTKLKDIVSLVPRLRHIIT-VDGKPPTWSEFPkgiivhTMAAVEALGAKASMenqphskPLPSDIA--VIMyTSGST 291
Cdd:PRK07788 155 EFT-DLLSALPPDLGRLRAWGGnPDDDEPSGSTDE------TLDDLIAGSSTAPL-------PKPPKPGgiVIL-TSGTT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 292 GLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGyLPLAHVLELSAELVCLSHGCRI----GYSSPQTLADqsskIKKg 367
Cdd:PRK07788 220 GTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLP-APMFHATGWAHLTLAMALGSTVvlrrRFDPEATLED----IAK- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 368 skgdtsmLKPTLMAAVPeimdriyknVMnkvsemssFQRNLfilaynykmEQISKGRNTPLCDSfvfrkvrsllggnIRL 447
Cdd:PRK07788 294 -------HKATALVVVP---------VM--------LSRIL---------DLGPEVLAKYDTSS-------------LKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 448 LLCGGAPLSATT-QRFMN-----ICfccpvgQGYGLTESAGAgTIS--EVWDYNTGRVGAPLVCCEIKLknweeggYFNT 519
Cdd:PRK07788 328 IFVSGSALSPELaTRALEafgpvLY------NLYGSTEVAFA-TIAtpEDLAEAPGTVGRPPKGVTVKI-------LDEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 520 DKPHPRGE---ILIGGQSVTMGYYKNEAKTKADFFedengqrwLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGK 596
Cdd:PRK07788 394 GNEVPRGVvgrIFVGNGFPFEGYTDGRDKQIIDGL--------LSSGDVGYFDEDGLLFVDGRDDDMI-VSGGENVFPAE 464
|
490
....*....|.
gi 115502350 597 VEAALKNLPLV 607
Cdd:PRK07788 465 VEDLLAGHPDV 475
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
231-681 |
3.04e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 69.54 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 231 LRHIITVDGkPPTWSefpkgiivhtMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITG 310
Cdd:PRK09274 137 VRRLVTVGG-RLLWG----------GTTLATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEA 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 311 MAERIP-ELGEEDvyigyLPLAHVLELSAelVCLshgcrigysspqtladqsskikkgskGDTSMLkPTLMAAVPEIMD- 388
Cdd:PRK09274 206 LREDYGiEPGEID-----LPTFPLFALFG--PAL--------------------------GMTSVI-PDMDPTRPATVDp 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 389 -RIyknvmnkVSEMSSFQ-RNLFIL-AYNYKMEQISKGRNTPLcdsfvfrkvrsllgGNIRLLLCGGAPLSATT-QRF-- 462
Cdd:PRK09274 252 aKL-------FAAIERYGvTNLFGSpALLERLGRYGEANGIKL--------------PSLRRVISAGAPVPIAViERFra 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 463 -MNicfccPVGQ---GYGLTESAGAGTIS---------EVWDYNTGR-VGAPLVCCEIKL--------KNWEEggyfntD 520
Cdd:PRK09274 311 mLP-----PDAEiltPYGATEALPISSIEsreilfatrAATDNGAGIcVGRPVDGVEVRIiaisdapiPEWDD------A 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 521 KPHPR---GEILIGGQSVTMGYYKNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLgKV 597
Cdd:PRK09274 380 LRLATgeiGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTI-PC 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 598 EAALKNLPLVdnicayansYHSYVIGFVVPN-QKELTELARKKGLKgtweelCNSCEMENEVLKVLSEAAISASLEKF-- 674
Cdd:PRK09274 459 ERIFNTHPGV---------KRSALVGVGVPGaQRPVLCVELEPGVA------CSKSALYQELRALAAAHPHTAGIERFli 523
|
....*....
gi 115502350 675 --EIPVKIR 681
Cdd:PRK09274 524 hpSFPVDIR 532
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
148-607 |
3.42e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 69.58 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 148 GNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKEL---LQTKLKDI 224
Cdd:PRK08316 50 AAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPALaptAEAALALL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 225 VSLVPRLRHIITVDGKPPTWSEFpkgiivhtmaavealgaKASMENQPHSKPLP----SDIAVIMYTSGSTGLPKGVMIS 300
Cdd:PRK08316 130 PVDTLILSLVLGGREAPGGWLDF-----------------ADWAEAGSVAEPDVeladDDLAQILYTSGTESLPKGAMLT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 301 H--------SNIIAGitgmaeripELGEEDVYIGYLPLAHvlelSAEL-VCLshgcrigysSPQTLAdqsskikkgskGD 371
Cdd:PRK08316 193 HraliaeyvSCIVAG---------DMSADDIPLHALPLYH----CAQLdVFL---------GPYLYV-----------GA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 372 TSMLkptLMAAVPEIMdriyknvmnkvsemssfqrnlfilaynykMEQISKGRNTPL------------CDSFVFRKVRS 439
Cdd:PRK08316 240 TNVI---LDAPDPELI-----------------------------LRTIEAERITSFfapptvwisllrHPDFDTRDLSS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 440 LLGGnirlllCGGA------PLSATTQRFMNICF--CcpvgqgYGLTESAGAGTI--SEVWDYNTGRVGAPLVCCEIKLK 509
Cdd:PRK08316 288 LRKG------YYGAsimpveVLKELRERLPGLRFynC------YGQTEIAPLATVlgPEEHLRRPGSAGRPVLNVETRVV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 510 NwEEGgyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKlQAG 589
Cdd:PRK08316 356 D-DDG---NDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF---RGG--WFHSGDLGVMDEEGYITVVDRKKDMIK-TGG 425
|
490
....*....|....*...
gi 115502350 590 EYVSLGKVEAALKNLPLV 607
Cdd:PRK08316 426 ENVASREVEEALYTHPAV 443
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
135-344 |
3.75e-12 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 69.52 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQA-------CFMYNFQLVtlyatlgGPAIVHALNETEV 207
Cdd:PRK08279 63 ISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGlaklgavVALLNTQQR-------GAVLAHSLNLVDA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 208 TNIITSKELLQTklkdIVSLVPrlrhiiTVDGKPPTWSEFPK-GIIVHTMAAVEALGAKASMENQPHSKPLPS-DIAVIM 285
Cdd:PRK08279 136 KHLIVGEELVEA----FEEARA------DLARPPRLWVAGGDtLDDPEGYEDLAAAAAGAPTTNPASRSGVTAkDTAFYI 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115502350 286 YTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVlelSAELVCLS 344
Cdd:PRK08279 206 YTSGTTGLPKAAVMSHMRWLKAMGGFGGLL-RLTPDDVLYCCLPLYHN---TGGTVAWS 260
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
267-705 |
5.45e-12 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 69.80 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 267 SMENqPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLA---HVLELSAELVcl 343
Cdd:PRK12467 1707 SDSN-PAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY-QLSAADVVLQFTSFAfdvSVWELFWPLI-- 1782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 344 sHGCRIGYSSPQTLADQSSKIkkgskgdtsmlkptlmaavpEIMDRIYKNVMNKVSEMssFQrnlfilAYNYKMEQISKg 423
Cdd:PRK12467 1783 -NGARLVIAPPGAHRDPEQLI--------------------QLIERQQVTTLHFVPSM--LQ------QLLQMDEQVEH- 1832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 424 rntplCDSfvfrkvrsllggnIRLLLCGGAPLSATTQRFMNICFcCPVG--QGYGLTESA---GAGTISEVWDynTGRVG 498
Cdd:PRK12467 1833 -----PLS-------------LRRVVCGGEALEVEALRPWLERL-PDTGlfNLYGPTETAvdvTHWTCRRKDL--EGRDS 1891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 499 APLvccEIKLKNWeeGGYF--NTDKPHPR---GEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEFEP 570
Cdd:PRK12467 1892 VPI---GQPIANL--STYIldASLNPVPIgvaGELYLGGVGLARGYLNRPALTAERFVADpfgTVGSRLYRTGDLARYRA 1966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 571 DGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDN--ICAYANSYHSYVIGFVVPNQKELTELA-RKKGLKGTwee 647
Cdd:PRK12467 1967 DGVIEYLGRIDHQVKIR-GFRIELGEIEARLREQGGVREavVIAQDGANGKQLVAYVVPTDPGLVDDDeAQVALRAI--- 2042
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 115502350 648 lcnscemenevLKvlseAAISASLEKFEIPVK-IRLSPEPWTPETglvtdafKLKRKEL 705
Cdd:PRK12467 2043 -----------LK----NHLKASLPEYMVPAHlVFLARMPLTPNG-------KLDRKAL 2079
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
192-598 |
7.04e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 68.97 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 192 TLGGPAIVHALNETEVTNIITSKELLQT-KLKDIVSLVPRLRHIITVDGKPPTWSEFPKGIIVHTMAAvealgAKASMEN 270
Cdd:PRK08043 288 TAGVKGLTSAITAAEIKTIFTSRQFLDKgKLWHLPEQLTQVRWVYLEDLKDDVTTADKLWIFAHLLMP-----RLAQVKQ 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 271 QPhskplpSDIAVIMYTSGSTGLPKGVMISHSNIIAGItgmaERIPELGE---EDVYIGYLPLAHVLELSAELVC-LSHG 346
Cdd:PRK08043 363 QP------EDAALILFTSGSEGHPKGVVHSHKSLLANV----EQIKTIADftpNDRFMSALPLFHSFGLTVGLFTpLLTG 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 347 CRIG-YSSPQTladqsskikkgskgdtsmlkptlMAAVPEImdrIYKNVMNKVSEMSSFQRNLFILAYNYKMeqiskgrn 425
Cdd:PRK08043 433 AEVFlYPSPLH-----------------------YRIVPEL---VYDRNCTVLFGTSTFLGNYARFANPYDF-------- 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 426 tplcdsfvfrkvrsllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCE 505
Cdd:PRK08043 479 -----------------ARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 506 ---IKLKNWEEGgyfntdkphprGEILIGGQSVTMGYYKNEA--KTKADFFEDENGQR---WLCTGDIGEFEPDGCLKII 577
Cdd:PRK08043 542 arlLSVPGIEQG-----------GRLQLKGPNIMNGYLRVEKpgVLEVPTAENARGEMergWYDTGDIVRFDEQGFVQIQ 610
|
410 420
....*....|....*....|.
gi 115502350 578 DRKKDLVKLqAGEYVSLGKVE 598
Cdd:PRK08043 611 GRAKRFAKI-AGEMVSLEMVE 630
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
253-609 |
8.98e-12 |
|
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: 68.14 E-value: 8.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 253 VHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIiAGITGMAERIPELGEEDVYIGYLPL-- 330
Cdd:cd17651 110 LVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSL-ANLVAWQARASSLGPGARTLQFAGLgf 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 331 -AHVLELsaeLVCLSHGCRIGYSSPQTLADqsskikkgskgdtsmlKPTLMAAVPEimdriyknvmNKVSEmsSFQRNLF 409
Cdd:cd17651 189 dVSVQEI---FSTLCAGATLVLPPEEVRTD----------------PPALAAWLDE----------QRISR--VFLPTVA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 410 ILAynykmeqiskgrntpLCDSFVFRKVRSLLggnIRLLLCGGAPLSAT--------TQRFMNICFccpvgqGYGLTES- 480
Cdd:cd17651 238 LRA---------------LAEHGRPLGVRLAA---LRYLLTGGEQLVLTedlrefcaGLPGLRLHN------HYGPTETh 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 481 -AGAGTISEVWDYNTGR--VGAPLVCCEIK-LKNWeeggyfntDKPHPR---GEILIGGQSVTMGYYKNEAKTKADFFED 553
Cdd:cd17651 294 vVTALSLPGDPAAWPAPppIGRPIDNTRVYvLDAA--------LRPVPPgvpGELYIGGAGLARGYLNRPELTAERFVPD 365
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 115502350 554 E--NGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDN 609
Cdd:cd17651 366 PfvPGARMYRTGDLARWLPDGELEFLGRADDQVKIR-GFRIELGEIEAALARHPGVRE 422
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
249-584 |
1.03e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 68.10 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 249 KGIIVHTMAavEALGAkasmenqPHSKPLP---SDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYI 325
Cdd:PRK07768 128 KGIRVLTVA--DLLAA-------DPIDPVEtgeDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 326 GYLPLAHVLELsaelvclshgcrIGY-SSPQTLADQSSKIkkgskgdTSM--LKPTLMAavPEIMDRiYKNVMnkvsems 402
Cdd:PRK07768 199 SWLPLFHDMGM------------VGFlTVPMYFGAELVKV-------TPMdfLRDPLLW--AELISK-YRGTM------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 403 sfqrnlfILAYNYKMeqiskgrntplcdSFVFRKVRSLLG------GNIRLLLCGGAPLS-ATTQRFmnicfcCPVGQG- 474
Cdd:PRK07768 250 -------TAAPNFAY-------------ALLARRLRRQAKpgafdlSSLRFALNGAEPIDpADVEDL------LDAGARf 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 475 ----------YGLTESAGAGTISEvwdyntgrVGAPLVCCEIKLKNWEEGGYF-NTDKPHPR------------------ 525
Cdd:PRK07768 304 glrpeailpaYGMAEATLAVSFSP--------CGAGLVVDEVDADLLAALRRAvPATKGNTRrlatlgpplpglevrvvd 375
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115502350 526 -----------GEILIGGQSVTMGYykneakTKADFFE---DENGqrWLCTGDIGEFEPDGCLKIIDRKKDLV 584
Cdd:PRK07768 376 edgqvlpprgvGVIELRGESVTPGY------LTMDGFIpaqDADG--WLDTGDLGYLTEEGEVVVCGRVKDVI 440
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
135-607 |
4.22e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 66.06 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFM---------YNF---QLVTLYATLGGPAIVHal 202
Cdd:PRK07798 29 LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKaravpvnvnYRYvedELRYLLDDSDAVALVY-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 203 nETEvtniitskelLQTKLKDIVSLVPRLRHIITVDGkpPTWSEFPKGIIvhtmaAVEALGAKASMEnQPHSKPLPSDIa 282
Cdd:PRK07798 107 -ERE----------FAPRVAEVLPRLPKLRTLVVVED--GSGNDLLPGAV-----DYEDALAAGSPE-RDFGERSPDDL- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 283 VIMYTSGSTGLPKGVMISHSNIIAgiTGMAERIPELGE--EDVYigylplAHVLELSAEL------VC-LSHGcrigyss 353
Cdd:PRK07798 167 YLLYTGGTTGMPKGVMWRQEDIFR--VLLGGRDFATGEpiEDEE------ELAKRAAAGPgmrrfpAPpLMHG------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 354 pqtlADQSSKIKKGSKGDTSMLKPTLM---AAVPEIMDRiyknvmNKVSEMS----SFQRnlfilaynykmeqiskgrnt 426
Cdd:PRK07798 232 ----AGQWAAFAALFSGQTVVLLPDVRfdaDEVWRTIER------EKVNVITivgdAMAR-------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 427 PLCDSFVFRKVRSLlgGNIRLLLCGGAPLSATT-QRFM----NICfccpVGQGYGLTESaGAGTISEVWDYNTGRvGAPL 501
Cdd:PRK07798 282 PLLDALEARGPYDL--SSLFAIASGGALFSPSVkEALLellpNVV----LTDSIGSSET-GFGGSGTVAKGAVHT-GGPR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 502 V-----CCEIklknwEEGGYFNTDKPHPRGEILIGGqSVTMGYYKNEAKTKADFFEdENGQRWLCTGDIGEFEPDGCLKI 576
Cdd:PRK07798 354 FtigprTVVL-----DEDGNPVEPGSGEIGWIARRG-HIPLGYYKDPEKTAETFPT-IDGVRYAIPGDRARVEADGTITL 426
|
490 500 510
....*....|....*....|....*....|.
gi 115502350 577 IDRkKDLVKLQAGEYVSLGKVEAALKNLPLV 607
Cdd:PRK07798 427 LGR-GSVCINTGGEKVFPEEVEEALKAHPDV 456
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
278-627 |
5.97e-11 |
|
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: 65.15 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDvyigylplaHVLELSAelvclshgcrIGYsspqtl 357
Cdd:cd17644 105 PENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEY-GITSSD---------RVLQFAS----------IAF------ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 358 aDQSSK--IKKGSKGDTSMLKPTLMAAVPEIMdriyknvmnkVSEMSSFQRNLFILAYNYKMEQISKGRNTpLCDsfvfr 435
Cdd:cd17644 159 -DVAAEeiYVTLLSGATLVLRPEEMRSSLEDF----------VQYIQQWQLTVLSLPPAYWHLLVLELLLS-TID----- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 436 kvrslLGGNIRLLLCGG-APLSATTQRFMNIcfccpVGQ------GYGLTESAGAGTISEVWDYNTGRVGAPLVCCEI-K 507
Cdd:cd17644 222 -----LPSSLRLVIVGGeAVQPELVRQWQKN-----VGNfiqlinVYGPTEATIAATVCRLTQLTERNITSVPIGRPIaN 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADF----FEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDL 583
Cdd:cd17644 292 TQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFishpFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQ 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 115502350 584 VKLQaGEYVSLGKVEAALKNLPLVDNICAYA---NSYHSYVIGFVVP 627
Cdd:cd17644 372 VKIR-GFRIELGEIEAVLSQHNDVKTAVVIVredQPGNKRLVAYIVP 417
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
280-643 |
6.79e-11 |
|
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: 65.04 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAErIPELGEEDVYIGYLPLAHVLELSAE--LVCLSHGCRIGYS---SP 354
Cdd:cd05920 140 EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAE-VCGLDQDTVYLAVLPAAHNFPLACPgvLGTLLAGGRVVLApdpSP 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 355 QT---LADQSskikkgskgdtsmlKPTLMAAVPEImdriyknVMNKVSEMSSFQRNLfilaynykmeqiskgrntplcds 431
Cdd:cd05920 219 DAafpLIERE--------------GVTVTALVPAL-------VSLWLDAAASRRADL----------------------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 432 fvfrkvrsllgGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTEsagaGTIS--------EVWDYNTGRVGAPLVc 503
Cdd:cd05920 255 -----------SSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE----GLLNytrlddpdEVIIHTQGRPMSPDD- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 504 cEIKLknWEEGGyfNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDL 583
Cdd:cd05920 319 -EIRV--VDEEG--NPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVEGRIKDQ 389
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115502350 584 VKlQAGEYVSLGKVEAALKNLPLVDNiCAYANSYHSY----VIGFVVPNQKELTELARKKGLKG 643
Cdd:cd05920 390 IN-RGGEKIAAEEVENLLLRHPAVHD-AAVVAMPDELlgerSCAFVVLRDPPPSAAQLRRFLRE 451
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
277-706 |
8.88e-11 |
|
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: 64.76 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 277 LPSDIAVIMYTSGSTGLPKGVMISHSniiagitgmaeripelgeedVYIGYLPlahvlelsaelvclshgcriGYSSPQT 356
Cdd:cd05971 86 GSDDPALIIYTSGTTGPPKGALHAHR--------------------VLLGHLP--------------------GVQFPFN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 357 LADQSSKIKKGSK------GDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQ--RNLFILAYNYKMeqiskgrntpl 428
Cdd:cd05971 126 LFPRDGDLYWTPAdwawigGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYgvTTAFLPPTALKM----------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 429 cdsfvFRKV---RSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTE-SAGAGTISEVWDYNTGRVGAPLVCC 504
Cdd:cd05971 195 -----MRQQgeqLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTEcNLVIGNCSALFPIKPGSMGKPIPGH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 505 EIKLKNwEEGgyfNTDKPHPRGEILIG-GQSVTM-GYYKNEAKTKADFFEDengqrWLCTGDIGEFEPDGCLKIIDRKKD 582
Cdd:cd05971 270 RVAIVD-DNG---TPLPPGEVGEIAVElPDPVAFlGYWNNPSATEKKMAGD-----WLLTGDLGRKDSDGYFWYVGRDDD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 583 LVKlQAGEYVSLGKVEAALKNLPLVDNICayansyhsyVIG------------FVVPNQKELT--ELARkkglkgtweel 648
Cdd:cd05971 341 VIT-SSGYRIGPAEIEECLLKHPAVLMAA---------VVGipdpirgeivkaFVVLNPGETPsdALAR----------- 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 115502350 649 cnscEMENEVlkvlseaaiSASLEKFEIPVKIRLSPEPWTPETGlvtdafKLKRKELK 706
Cdd:cd05971 400 ----EIQELV---------KTRLAAHEYPREIEFVNELPRTATG------KIRRRELR 438
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
248-589 |
1.62e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.02 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 248 PKGIIVHTMAAVEALGAKASMENQPHSKPlpsdiAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGY 327
Cdd:PRK05851 126 DSSVTVHDLATAAHTNRSASLTPPDSGGP-----AVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGCSW 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 328 LPLAHVLELSAELVCLSHGcrigysSPQTLADQSSkikkgskgdtsmlkptlMAAVPeimdriyknvMNKVSEMSSfQRN 407
Cdd:PRK05851 201 LPLYHDMGLAFLLTAALAG------APLWLAPTTA-----------------FSASP----------FRWLSWLSD-SRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 408 LFILAYNYKMEQISKgrntplcdsfVFRKVRSLLGGNIRLLLCGGAPLS-ATTQRFMNIcfCCPVG-------QGYGLTE 479
Cdd:PRK05851 247 TLTAAPNFAYNLIGK----------YARRVSDVDLGALRVALNGGEPVDcDGFERFATA--MAPFGfdagaaaPSYGLAE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 480 SAGAGTIS---------EVWDYNTG------RVGAPLVCCEIKLKNWEEGGYFNTdkpHPRGEILIGGQSvTMGYYKNEA 544
Cdd:PRK05851 315 STCAVTVPvpgiglrvdEVTTDDGSgarrhaVLGNPIPGMEVRISPGDGAAGVAG---REIGEIEIRGAS-MMSGYLGQA 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 115502350 545 KTKADffedengqRWLCTGDIGEFEpDGCLKIIDRKKDLVKLqAG 589
Cdd:PRK05851 391 PIDPD--------DWFPTGDLGYLV-DGGLVVCGRAKELITV-AG 425
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
202-671 |
1.80e-10 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 63.93 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 202 LNETEVTNIITSKELLqtklkdivslvPRLRHIITVDGKPPtwsefpKGIIVHTMAAVEALGAKASMEN---QP----HS 274
Cdd:PRK08008 105 LQNSQASLLVTSAQFY-----------PMYRQIQQEDATPL------RHICLTRVALPADDGVSSFTQLkaqQPatlcYA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 275 KPLPS-DIAVIMYTSGSTGLPKGVMISHSNII-AGITGMAEriPELGEEDVYIGYLPLAHV-LELSAELVCLSHGCRI-- 349
Cdd:PRK08008 168 PPLSTdDTAEILFTSGTTSRPKGVVITHYNLRfAGYYSAWQ--CALRDDDVYLTVMPAFHIdCQCTAAMAAFSAGATFvl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 350 --GYSSpQTLADQSSKIKKGSKGDTSMLKPTLMAAVPEIMDRiyknvMNKVSEMssfqrnLFILAynykmeqISKGRNTP 427
Cdd:PRK08008 246 leKYSA-RAFWGQVCKYRATITECIPMMIRTLMVQPPSANDR-----QHCLREV------MFYLN-------LSDQEKDA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 428 LCDSFvfrkvrsllggNIRLLlcggaplsattqrfmnicfccpvgQGYGLTESAGaGTISevwDYNTGR-----VGAPLV 502
Cdd:PRK08008 307 FEERF-----------GVRLL------------------------TSYGMTETIV-GIIG---DRPGDKrrwpsIGRPGF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 503 CCEIKLKNwEEGgyfNTDKPHPRGEILIG---GQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDR 579
Cdd:PRK08008 348 CYEAEIRD-DHN---RPLPAGEIGEICIKgvpGKTIFKEYYLDPKATAKVLEADG----WLHTGDTGYVDEEGFFYFVDR 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 580 KKDLVKlQAGEYVSLGKVEAALKNLPLVDNICayansyhsyVIG------------FVVPNQKE-LTElarkkglkgtwE 646
Cdd:PRK08008 420 RCNMIK-RGGENVSCVELENIIATHPKIQDIV---------VVGikdsirdeaikaFVVLNEGEtLSE-----------E 478
|
490 500
....*....|....*....|....*
gi 115502350 647 ELCNSCEMENEVLKVLSEAAISASL 671
Cdd:PRK08008 479 EFFAFCEQNMAKFKVPSYLEIRKDL 503
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
280-612 |
1.88e-10 |
|
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: 63.65 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLAD 359
Cdd:cd05958 98 DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEATPD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 360 QSSKIkkgskgdTSMLKPTLMAAVPEIMDRiyknvmnkvsemssfqrnlfILAYNYKMEQiskgrntplcdsfvfrkvrs 439
Cdd:cd05958 178 LLLSA-------IARYKPTVLFTAPTAYRA--------------------MLAHPDAAGP-------------------- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 440 lLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTE------SAGAGtisevwDYNTGRVGAPLVCCEIKLKNwEE 513
Cdd:cd05958 211 -DLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEmfhifiSARPG------DARPGATGKPVPGYEAKVVD-DE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 GgyfntdKPHPRGEilIGGQSVT--MGYYKNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEY 591
Cdd:cd05958 283 G------NPVPDGT--IGRLAVRgpTGCRYLADKRQRTYVQGG----WNITGDTYSRDPDGYFRHQGRSDDMIVS-GGYN 349
|
330 340
....*....|....*....|.
gi 115502350 592 VSLGKVEAALKNLPLVDNiCA 612
Cdd:cd05958 350 IAPPEVEDVLLQHPAVAE-CA 369
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
229-614 |
2.35e-10 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 64.30 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 229 PRLrhIITVDGKPPTWSEFPKGiivhTMAAVEALGAKAsmENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGI 308
Cdd:PRK10252 556 PSL--LITTADQLPRFADVPDL----TSLCYNAPLAPQ--GAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 309 TGMAERIPeLGEEDVYIGYLPLA---HVLEL------SAELVCLSHGcriGYSSPQTLADQSSKikkgsKGDT------S 373
Cdd:PRK10252 628 LWMQNHYP-LTADDVVLQKTPCSfdvSVWEFfwpfiaGAKLVMAEPE---AHRDPLAMQQFFAE-----YGVTtthfvpS 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 374 MLKPTLMAAVPEimdriyknvmNKVSEMSSFQRnlfilaynykmeqiskgrntplcdsfVFrkvrsllggnirlllCGGA 453
Cdd:PRK10252 699 MLAAFVASLTPE----------GARQSCASLRQ--------------------------VF---------------CSGE 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 454 PLSATTQRFMNICFCCPVGQGYGLTESA--------GAGTISEVwdynTGR---VGAPLvcceiklknWEEGGYFNTDKP 522
Cdd:PRK10252 728 ALPADLCREWQQLTGAPLHNLYGPTEAAvdvswypaFGEELAAV----RGSsvpIGYPV---------WNTGLRILDARM 794
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 523 HP-----RGEILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLG 595
Cdd:PRK10252 795 RPvppgvAGDLYLTGIQLAQGYLGRPDLTASRFIADpfAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIR-GQRIELG 873
|
410
....*....|....*....
gi 115502350 596 KVEAALKNLPLVDNICAYA 614
Cdd:PRK10252 874 EIDRAMQALPDVEQAVTHA 892
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
277-607 |
1.33e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 61.33 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 277 LPSDI-AVIMYTSGSTGLPKGVMISHSNIIA-GITGMAERIPELGEEDVYIGyLPLAHVLELSAELVCLSHGCRI----- 349
Cdd:PRK07786 171 IPNDSpALIMYTSGTTGRPKGAVLTHANLTGqAMTCLRTNGADINSDVGFVG-VPLFHIAGIGSMLPGLLLGAPTviypl 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 350 GYSSPQTLADqsskIKKGSKGDTSMLKPTLMAAVPEimdriyknvmnkvsemssfqrnlfilaynykmEQISKGRNTPLc 429
Cdd:PRK07786 250 GAFDPGQLLD----VLEAEKVTGIFLVPAQWQAVCA--------------------------------EQQARPRDLAL- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 430 dsfvfrkvrsllggniRLLLCGGAPLSATTQRFMNICFccPVGQ---GYGLTESA-------GAGTISEVwdyntGRVGA 499
Cdd:PRK07786 293 ----------------RVLSWGAAPASDTLLRQMAATF--PEAQilaAFGQTEMSpvtcmllGEDAIRKL-----GSVGK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PLVCCEIKLKNWEeggyFNTDKPHPRGEILIGGQSVTMGYYKNEAKTkADFFEDEngqrWLCTGDIGEFEPDGCLKIIDR 579
Cdd:PRK07786 350 VIPTVAARVVDEN----MNDVPVGEVGEIVYRAPTLMSGYWNNPEAT-AEAFAGG----WFHSGDLVRQDEEGYVWVVDR 420
|
330 340
....*....|....*....|....*...
gi 115502350 580 KKDLVkLQAGEYVSLGKVEAALKNLPLV 607
Cdd:PRK07786 421 KKDMI-ISGGENIYCAEVENVLASHPDI 447
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
278-607 |
1.78e-09 |
|
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: 60.34 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNiIAGITGMAERIPELGEEDVYIGYLPL---AHVLELSAELvcLSHGC-----RI 349
Cdd:cd17652 92 PDNLAYVIYTSGSTGRPKGVVVTHRG-LANLAAAQIAAFDVGPGSRVLQFASPsfdASVWELLMAL--LAGATlvlapAE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 350 GYSSPQTLAD--QSSKIkkgskgDTSMLKPTLMAAVPEimdriyknvmnkvsemssfqrnlfilaynykmeqiskgrntp 427
Cdd:cd17652 169 ELLPGEPLADllREHRI------THVTLPPAALAALPP------------------------------------------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 428 lcdsfvfrkvRSLLGGniRLLLCGGAPLS-------ATTQRFMNicfccpvgqGYGLTESAGAGTISEVW-DYNTGRVGA 499
Cdd:cd17652 201 ----------DDLPDL--RTLVVAGEACPaelvdrwAPGRRMIN---------AYGPTETTVCATMAGPLpGGGVPPIGR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PLVCCEIklknweeggYFNTDKPHP-----RGEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEFEPD 571
Cdd:cd17652 260 PVPGTRV---------YVLDARLRPvppgvPGELYIAGAGLARGYLNRPGLTAERFVADpfgAPGSRMYRTGDLARWRAD 330
|
330 340 350
....*....|....*....|....*....|....*.
gi 115502350 572 GCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLV 607
Cdd:cd17652 331 GQLEFLGRADDQVKIR-GFRIELGEVEAALTEHPGV 365
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
278-584 |
2.01e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 61.34 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIA---------GItgmaeripELGEEDVYIGYLPLAHVLELsaelvclshgcr 348
Cdd:PRK05691 165 PDDIAFLQYTSGSTALPKGVQVSHGNLVAneqlirhgfGI--------DLNPDDVIVSWLPLYHDMGL------------ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 349 IGysspqtladqsskikkgskgdtSMLKPtLMAAVPEIMdriyknvmnkvseMSSfqrNLFILAYNYKMEQISKGRNT-- 426
Cdd:PRK05691 225 IG----------------------GLLQP-IFSGVPCVL-------------MSP---AYFLERPLRWLEAISEYGGTis 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 427 --P-----LCDSfvfRKVRSLLGG----NIRLLLCGGAP-----LSATTQRFMNiC-------FCCpvgqgYGLTESA-- 481
Cdd:PRK05691 266 ggPdfayrLCSE---RVSESALERldlsRWRVAYSGSEPirqdsLERFAEKFAA-CgfdpdsfFAS-----YGLAEATlf 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 482 ------GAGTISEVWD---YNTGRV----GAPLVCC-------EIKLKNWEEGGYFNTDKPhprGEILIGGQSVTMGYYK 541
Cdd:PRK05691 337 vsggrrGQGIPALELDaeaLARNRAepgtGSVLMSCgrsqpghAVLIVDPQSLEVLGDNRV---GEIWASGPSIAHGYWR 413
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 115502350 542 N-EAKTKAdfFEDENGQRWLCTGDIGeFEPDGCLKIIDRKKDLV 584
Cdd:PRK05691 414 NpEASAKT--FVEHDGRTWLRTGDLG-FLRDGELFVTGRLKDML 454
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
280-639 |
2.23e-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: 60.18 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAgitgmaeripELGEEDVYIGYLPLAHVLELSAelvclshgcrigYSSPQTLAD 359
Cdd:cd17656 129 DLLYIIYTSGTTGKPKGVQLEHKNMVN----------LLHFEREKTNINFSDKVLQFAT------------CSFDVCYQE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 360 QSSKIKKGskGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILaynykmeqiskgrntplcdsfvfRKVRS 439
Cdd:cd17656 187 IFSTLLSG--GTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE-----------------------REFIN 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 440 LLGGNIRLLLCGGAPLSAT-TQRFMNICFCCPVGQGYGLTES--AGAGTIS---EVWDYNTgrVGAPLVCCEIKLKNWEE 513
Cdd:cd17656 242 RFPTCVKHIITAGEQLVITnEFKEMLHEHNVHLHNHYGPSEThvVTTYTINpeaEIPELPP--IGKPISNTWIYILDQEQ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 ggyfntdKPHPRG---EILIGGQSVTMGYYKNEAKTKADFFED--ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQa 588
Cdd:cd17656 320 -------QLQPQGivgELYISGASVARGYLNRQELTAEKFFPDpfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR- 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 115502350 589 GEYVSLGKVEAALKNLPLVDN--ICAYANSY-HSYVIGFVVPNQKELTELARKK 639
Cdd:cd17656 392 GYRIELGEIEAQLLNHPGVSEavVLDKADDKgEKYLCAYFVMEQELNISQLREY 445
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
280-584 |
2.92e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.13 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLAD 359
Cdd:PRK07769 181 TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDAL-EGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 360 QSSK-IKKgskgdtsmlkptlMAAVPEIMDRIyknvmnkvsemssfqrnlFILAYNYKMEQiSKGRNTPLCDSfvfrkvR 438
Cdd:PRK07769 260 RPGRwIRE-------------LARKPGGTGGT------------------FSAAPNFAFEH-AAARGLPKDGE------P 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 439 SLLGGNIRLLLCGGAPLSATTQRFMNICFcCPVG-------QGYGLTESA----------------------GAGTISEV 489
Cdd:PRK07769 302 PLDLSNVKGLLNGSEPVSPASMRKFNEAF-APYGlpptaikPSYGMAEATlfvsttpmdeeptviyvdrdelNAGRFVEV 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 490 WDYNTGRVgAPLVCCEIKLKNWEEGGYFNTDKPHPR---GEILIGGQSVTMGYYKNEAKTKADFFE-------------D 553
Cdd:PRK07769 381 PADAPNAV-AQVSAGKVGVSEWAVIVDPETASELPDgqiGEIWLHGNNIGTGYWGKPEETAATFQNilksrlseshaegA 459
|
330 340 350
....*....|....*....|....*....|.
gi 115502350 554 ENGQRWLCTGDIGEFEpDGCLKIIDRKKDLV 584
Cdd:PRK07769 460 PDDALWVRTGDYGVYF-DGELYITGRVKDLV 489
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
401-642 |
3.01e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 60.01 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 401 MSSF--QRNLFILAYN-YKMEQISKGRNTPLCDSFVFRKVRSLLGGNI------RLLLCGGAP----LsATTQRFMNIcf 467
Cdd:PRK07445 179 MRSFltGGKLVILPYKrLKSGQELPPNPSDFFLSLVPTQLQRLLQLRPqwlaqfRTILLGGAPawpsL-LEQARQLQL-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 468 ccPVGQGYGLTESAG-----------AGTISevwdyntgrVGAPLVCCEIKLKNweeggyfntdkpHPRGEILIGGQSVT 536
Cdd:PRK07445 256 --RLAPTYGMTETASqiatlkpddflAGNNS---------SGQVLPHAQITIPA------------NQTGNITIQAQSLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 537 MGYYKNEaktkadffedENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNLPLVDNICAY--A 614
Cdd:PRK07445 313 LGYYPQI----------LDSQGIFETDDLGYLDAQGYLHILGRNSQKI-ITGGENVYPAEVEAAILATGLVQDVCVLglP 381
|
250 260
....*....|....*....|....*....
gi 115502350 615 NSY-HSYVIGFVVPNQKELTELARKKGLK 642
Cdd:PRK07445 382 DPHwGEVVTAIYVPKDPSISLEELKTAIK 410
|
|
| PTZ00297 |
PTZ00297 |
pantothenate kinase; Provisional |
129-717 |
4.34e-09 |
|
pantothenate kinase; Provisional
Pssm-ID: 140318 [Multi-domain] Cd Length: 1452 Bit Score: 60.25 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 129 LGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATlgGPAIVHALNETEVT 208
Cdd:PTZ00297 452 SGESEWLTYGTVDARARELGSGLLALGVRPGDVIGVDCEASRNIVILEVACALYGFTTLPLVGK--GSTMRTLIDEHKIK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 209 NIITSKellqtklKDIVSLVP-RLRHIITVdgkpptwsefpkgiiVHTMAAVEALGAKAS------------MENQPHSK 275
Cdd:PTZ00297 530 VVFADR-------NSVAAILTcRSRKLETV---------------VYTHSFYDEDDHAVArdlnitlipyefVEQKGRLC 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 276 PLP-----SDIAVIMY-----TSGSTGLPKGVMISHSNIIAGITG--MAERIPELGEEDVYIGYLPLAHVLELSAELVCL 343
Cdd:PTZ00297 588 PVPlkehvTTDTVFTYvvdntTSASGDGLAVVRVTHADVLRDISTlvMTGVLPSSFKKHLMVHFTPFAMLFNRVFVLGLF 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 344 SHGCRIGYSSPQTLADQSSKIkkgskgdtsmlKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQIS-K 422
Cdd:PTZ00297 668 AHGSAVATVDAAHLQRAFVKF-----------QPTILVAAPSLFSTSRLQLSRANERYSAVYSWLFERAFQLRSRLINiH 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 423 GRNTPLCDSFVFRKVRSLLGGNIR-LLLC-GGAPLSATTQRFMNICFcCPVGQGYGLTESAGAGTISevwdyntgrvGAP 500
Cdd:PTZ00297 737 RRDSSLLRFIFFRATQELLGGCVEkIVLCvSEESTSFSLLEHISVCY-VPCLREVFFLPSEGVFCVD----------GTP 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 LVCCEIKLKNWEEggyfntdkphPRGEILIGGQSVTMgyyKNEAKTKADFFEDENGQRWLCTgdIGefEPDGCLKIIdrk 580
Cdd:PTZ00297 806 APSLQVDLEPFDE----------PSDGAGIGQLVLAK---KGEPRRTLPIAAQWKRDRTLRL--LG--PPLGILLPV--- 865
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 581 kdlvklqAGEYVSLGKVEAALKNLPLVDNICAYANSYHSyVIGFVVPN---------QKELTELARKKGLKGTWEELcnS 651
Cdd:PTZ00297 866 -------AYEYVIAAELERIFSQSRYVNDIFLYADPSRP-IIAIVSPNrdtvefewrQSHCMGEGGGPARQLGWTEL--V 935
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115502350 652 CEMENEVLKVLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMY 717
Cdd:PTZ00297 936 AYASSLLTADFACIAKENGLHPSNVPEYVHLHPHAFKDHSTFLTPYGKIRRDAVHSYFSSVIERFY 1001
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
284-607 |
6.14e-09 |
|
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: 58.55 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 284 IMYTSGSTGLPKGVMISHSNI---IAGITGMAERIPELGEED----------VYIGYLPLAHVLELSAELVCLSHGCRIG 350
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQEDIfrmLMGGADFGTGEFTPSEDAhkaaaaaagtVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 351 YSSPQTLADQsskikkgskgdtsmlkptlmaaVPEIMDRIYKNVMNKVSEmsSFQRNLfilaynykMEQISKGRNTPLcd 430
Cdd:cd05924 88 LPDDRFDPEE----------------------VWRTIEKHKVTSMTIVGD--AMARPL--------IDALRDAGPYDL-- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 431 sfvfrkvrsllgGNIRLLLCGGAPLSATT-QRFMNICFCCPVGQGYGLTESAGAGTIsevwdYNTGRV--GAPLVCCEIK 507
Cdd:cd05924 134 ------------SSLFAISSGGALLSPEVkQGLLELVPNITLVDAFGSSETGFTGSG-----HSAGSGpeTGPFTRANPD 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNWEEGGYFNTDKPHPRGEILIGGQsVTMGYYKNEAKTKADFFEdENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKlQ 587
Cdd:cd05924 197 TVVLDDDGRVVPPGSGGVGWIARRGH-IPLGYYGDEAKTAETFPE-VDGVRYAVPGDRATVEADGTVTLLGRGSVCIN-T 273
|
330 340
....*....|....*....|
gi 115502350 588 AGEYVSLGKVEAALKNLPLV 607
Cdd:cd05924 274 GGEKVFPEEVEEALKSHPAV 293
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
278-601 |
1.05e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 58.29 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERI-PElgEEDVYIGYLPLAHVLEL-SAELVCLSHGCRIGYSS-- 353
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFsPK--EDDVMMSFLPPFHAYGFnSCTLFPLLSGVPVVFAYnp 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 354 --PQTLADQSSKIKKgskgdtsmlkpTLMAAVPEIMDRIYKNVMNKVSEMSSfqrnlfilaynykmeqiskgrntplcds 431
Cdd:PRK06334 260 lyPKKIVEMIDEAKV-----------TFLGSTPVFFDYILKTAKKQESCLPS---------------------------- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 432 fvfrkvrsllggnIRLLLCGGAPL-----SATTQRFMNICfccpVGQGYGLTESAGAGTISEVwdyNTGR----VGAPLV 502
Cdd:PRK06334 301 -------------LRFVVIGGDAFkdslyQEALKTFPHIQ----LRQGYGTTECSPVITINTV---NSPKhescVGMPIR 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 503 CCEIKLKNWEeggyfnTDKPHPRGE---ILIGGQSVTMGYYKNEAKTKadfFEDENGQRWLCTGDIGEFEPDGCLKIIDR 579
Cdd:PRK06334 361 GMDVLIVSEE------TKVPVSSGEtglVLTRGTSLFSGYLGEDFGQG---FVELGGETWYVTGDLGYVDRHGELFLKGR 431
|
330 340
....*....|....*....|..
gi 115502350 580 KKDLVKLqAGEYVSLGKVEAAL 601
Cdd:PRK06334 432 LSRFVKI-GAEMVSLEALESIL 452
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
282-593 |
1.24e-08 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 58.22 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 282 AVIMYTSGSTGLPKGVMISH-SNIIAGITGMAERIPELGEEDVYIGYLPLAHvlelsaelvclSHGCRIGYSSPQTLADQ 360
Cdd:PRK06018 180 AGMCYTSGTTGDPKGVLYSHrSNVLHALMANNGDALGTSAADTMLPVVPLFH-----------ANSWGIAFSAPSMGTKL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 361 sskIKKGSKGDTSML-------KPTLMAAVPEIMdriyknvmnkvsemssfqrnLFILAYnykMEQisKGRNTPlcdsfv 433
Cdd:PRK06018 249 ---VMPGAKLDGASVyelldteKVTFTAGVPTVW--------------------LMLLQY---MEK--EGLKLP------ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 434 frkvrsllggNIRLLLCGGAPL-SATTQRFMNicFCCPVGQGYGLTESAGAGTISEV---WDYNTG--------RVGAPL 501
Cdd:PRK06018 295 ----------HLKMVVCGGSAMpRSMIKAFED--MGVEVRHAWGMTEMSPLGTLAALkppFSKLPGdarldvlqKQGYPP 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 502 VCCEIKLKNweeggyfNTDKPHPR-----GEILIGGQSVTMGYYKNEAKTKadffeDENGqrWLCTGDIGEFEPDGCLKI 576
Cdd:PRK06018 363 FGVEMKITD-------DAGKELPWdgktfGRLKVRGPAVAAAYYRVDGEIL-----DDDG--FFDTGDVATIDAYGYMRI 428
|
330
....*....|....*..
gi 115502350 577 IDRKKDLVKlQAGEYVS 593
Cdd:PRK06018 429 TDRSKDVIK-SGGEWIS 444
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
135-607 |
2.00e-08 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 57.13 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQtklkdivslvprlrhiitvdgkpptwsefpkgiivhtmaavealgakasmenqphsKPLPSDIAVIMYTSGSTGLP 294
Cdd:cd05969 81 ELYE--------------------------------------------------------RTDPEDPTLLHYTSGTTGTP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 295 KGVMISHSNIIA-GITGmaERIPELGEEDVYIGYLPLAHVLELSAELVC-LSHGCrigysspQTLADQSSKIKKGSKGDT 372
Cdd:cd05969 105 KGVLHVHDAMIFyYFTG--KYVLDLHPDDIYWCTADPGWVTGTVYGIWApWLNGV-------TNVVYEGRFDAESWYGII 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 373 SMLKPTLMAAVPEIMDRIyknvMNKVSEmssfqrnlfiLAYNYKMEqiskgrntplcdsfvfrkvrsllggNIRLLLCGG 452
Cdd:cd05969 176 ERVKVTVWYTAPTAIRML----MKEGDE----------LARKYDLS-------------------------SLRFIHSVG 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 453 APLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEV-WDYNTGRVGAPLVCCEIKLKNwEEGgyfNTDKPHPRGEILI- 530
Cdd:cd05969 217 EPLNPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPcMPIKPGSMGKPLPGVKAAVVD-ENG---NELPPGTKGILALk 292
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115502350 531 -GGQSVTMGYYKNEAKTKADFFedeNGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLV 607
Cdd:cd05969 293 pGWPSMFRGIWNDEERYKNSFI---DG--WYLTGDLAYRDEDGYFWFVGRADDIIKT-SGHRVGPFEVESALMEHPAV 364
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
198-630 |
2.56e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 57.10 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 198 IVHALNETEVTNIITSKELLQtKLKDIVSLVPRLRHIITVDGKPPTWSEfpkgiiVHTMAAVEALGAKASMENQPHSKPL 277
Cdd:PRK05620 103 IVHIINHAEDEVIVADPRLAE-QLGEILKECPCVRAVVFIGPSDADSAA------AHMPEGIKVYSYEALLDGRSTVYDW 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 P----SDIAVIMYTSGSTGLPKGVMISHSNIIagITGMAERIPE---LGEEDVYIGYLPLAHVLELSAELVCLSHGCRIG 350
Cdd:PRK05620 176 PeldeTTAAAICYSTGTTGAPKGVVYSHRSLY--LQSLSLRTTDslaVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPLV 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 351 YSSPQTLADQSSKIKKgskgdTSMlkPTLMAAVPEIMdriyknvmnkVSEMSSFQRNlfilaynyKMEQISkgrntplcd 430
Cdd:PRK05620 254 FPGPDLSAPTLAKIIA-----TAM--PRVAHGVPTLW----------IQLMVHYLKN--------PPERMS--------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 431 sfvfrkvrsllggnIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEV---------WDY--NTGRVGA 499
Cdd:PRK05620 300 --------------LQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVARPpsgvsgearWAYrvSQGRFPA 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 500 PLvccEIKLKNweEGGYFNTdkpHPR--GEILIGGQSVTMGYYKNEAKTK---ADFFEDENGQR---------WLCTGDI 565
Cdd:PRK05620 366 SL---EYRIVN--DGQVMES---TDRneGEIQVRGNWVTASYYHSPTEEGggaASTFRGEDVEDandrftadgWLRTGDV 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115502350 566 GEFEPDGCLKIIDRKKDLVKlQAGEYVslgkVEAALKNLplvdnICAYANSYHSYVIGFvvPNQK 630
Cdd:PRK05620 438 GSVTRDGFLTIHDRARDVIR-SGGEWI----YSAQLENY-----IMAAPEVVECAVIGY--PDDK 490
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
286-607 |
5.95e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.01 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 286 YTSGSTGLPKGVMISHSniiaGITGMAERIP---ELGEEDVYIGYLPLAH---------VLELSAELVCLSHgcrigyss 353
Cdd:PLN02479 202 YTSGTTASPKGVVLHHR----GAYLMALSNAliwGMNEGAVYLWTLPMFHcngwcftwtLAALCGTNICLRQ-------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 354 PQTLADQSSKIKKGSkgdtsmlkpTLMAAVPEIMDRIYknvmnkvsemssfqrnlfilaynykmeqiskgrNTPLCDSFV 433
Cdd:PLN02479 270 VTAKAIYSAIANYGV---------THFCAAPVVLNTIV---------------------------------NAPKSETIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 434 frkvrsLLGGNIRLLLCGGAP----LSATTQRFMNicfccpVGQGYGLTESAGAGTI---SEVWDYNTGRVGAPLVCCE- 505
Cdd:PLN02479 308 ------PLPRVVHVMTAGAAPppsvLFAMSEKGFR------VTHTYGLSETYGPSTVcawKPEWDSLPPEEQARLNARQg 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 506 IKLKNWEEGGYFN--TDKPHPR-----GEILIGGQSVTMGYYKNEAKTKADFfedENGqrWLCTGDIGEFEPDGCLKIID 578
Cdd:PLN02479 376 VRYIGLEGLDVVDtkTMKPVPAdgktmGEIVMRGNMVMKGYLKNPKANEEAF---ANG--WFHSGDLGVKHPDGYIEIKD 450
|
330 340
....*....|....*....|....*....
gi 115502350 579 RKKDLVkLQAGEYVSLGKVEAALKNLPLV 607
Cdd:PLN02479 451 RSKDII-ISGGENISSLEVENVVYTHPAV 478
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
229-595 |
9.87e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 55.05 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 229 PRLRHIITVDGKPptwsefpKGIIVHTMAAvEALGAKASMENQPHSKPLpsdiaVIMYTSGSTGLPKGVMISHSNIIAGI 308
Cdd:PRK07470 126 PDLTHVVAIGGAR-------AGLDYEALVA-RHLGARVANAAVDHDDPC-----WFFFTSGTTGRPKAAVLTHGQMAFVI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 309 TG-MAERIPELGEEDVYIGYLPLahvlelsaelvclSHGCRIgysspQTLAdQSSKikkgskGDTSMLKPTLMAAVPEIM 387
Cdd:PRK07470 193 TNhLADLMPGTTEQDASLVVAPL-------------SHGAGI-----HQLC-QVAR------GAATVLLPSERFDPAEVW 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 388 DRIYKNvmnKVSemssfqrNLFILAYNYKM--EQiskgrntPLCDSFvfrKVRSLlggniRLLLCGGAPLSATTQRFMNI 465
Cdd:PRK07470 248 ALVERH---RVT-------NLFTVPTILKMlvEH-------PAVDRY---DHSSL-----RYVIYAGAPMYRADQKRALA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 466 CFCCPVGQGYGLTESAGAGTI-----SEVWDYNTGRVGaplvCC-------EIKLKNwEEGgyfNTDKPHPRGEILIGGQ 533
Cdd:PRK07470 303 KLGKVLVQYFGLGEVTGNITVlppalHDAEDGPDARIG----TCgfertgmEVQIQD-DEG---RELPPGETGEICVIGP 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115502350 534 SVTMGYYKN-EAKTKAdfFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLvklqageYVSLG 595
Cdd:PRK07470 375 AVFAGYYNNpEANAKA--FRDG----WFRTGDLGHLDARGFLYITGRASDM-------YISGG 424
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
135-707 |
1.13e-07 |
|
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: 54.67 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWmiaaqacfmynfqLVTLYAT--LGGPAivhalnetevtniit 212
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEY-------------VLLWLGLvkIGAVA--------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 213 skELLQTKLKDIVslvprLRHIITVDGkpptwsefPKGIIVhtmaavealgakasmenqphskplpsDIAVIMYTSGSTG 292
Cdd:cd05940 56 --ALINYNLRGES-----LAHCLNVSS--------AKHLVV--------------------------DAALYIYTSGTTG 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 293 LPKGVMISHSNIIAGITGMAERIPELGEEDVYIgYLPLAHVlelSAELVCLSHGCRIGysspQTLAdqsskIKKgskgdt 372
Cdd:cd05940 95 LPKAAIISHRRAWRGGAFFAGSGGALPSDVLYT-CLPLYHS---TALIVGWSACLASG----ATLV-----IRK------ 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 373 smlkptlmaavpeimdriyknvmnKVSEmSSFQRNlfILAYN-----YKMEQISKGRNTPLCDSFVFRKVRSLLGGNIRl 447
Cdd:cd05940 156 ------------------------KFSA-SNFWDD--IRKYQatifqYIGELCRYLLNQPPKPTERKHKVRMIFGNGLR- 207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 448 llcgGAPLSATTQRFMNICFCcpvgQGYGLTEsagaGTISEV-WDYNTGRVG---------APLVCCEIKLKNWE----E 513
Cdd:cd05940 208 ----PDIWEEFKERFGVPRIA----EFYAATE----GNSGFInFFGKPGAIGrnpsllrkvAPLALVKYDLESGEpirdA 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 514 GGYFntdKPHPRGEI-----LIGGQSVTMGYYKNEAKTKA---DFFEDenGQRWLCTGDIGEFEPDGCLKIIDRKKDLVK 585
Cdd:cd05940 276 EGRC---IKVPRGEPgllisRINPLEPFDGYTDPAATEKKilrDVFKK--GDAWFNTGDLMRLDGEGFWYFVDRLGDTFR 350
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 586 LQaGEYVSLGKVEAALKNLPLVDNicayANSYhsyviGFVVPNqkelTElaRKKGLKGTweelcNSCEMENEVLKVLSeA 665
Cdd:cd05940 351 WK-GENVSTTEVAAVLGAFPGVEE----ANVY-----GVQVPG----TD--GRAGMAAI-----VLQPNEEFDLSALA-A 408
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 115502350 666 AISASLEKFEIPVKIRLSPEPWTPETglvtdaFKLKRKELKT 707
Cdd:cd05940 409 HLEKNLPGYARPLFLRLQPEMEITGT------FKQQKVDLRN 444
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
223-637 |
2.04e-07 |
|
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: 54.38 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 223 DIVSLVPRLRHIItVDGKPPTWSEFpkgiivhtmaavEALGAKASMENQPHskPLPSDIAVIMYTSGSTGLPKGVMISHS 302
Cdd:COG1021 143 ELQAEVPSLRHVL-VVGDAGEFTSL------------DALLAAPADLSEPR--PDPDDVAFFQLSGGTTGLPKLIPRTHD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 303 NIIAGITGMAErIPELGEEDVYIGYLPLAHVLELSAE--LVCLSHGCRI---GYSSPQT---LADQSskikkgskgdtsm 374
Cdd:COG1021 208 DYLYSVRASAE-ICGLDADTVYLAALPAAHNFPLSSPgvLGVLYAGGTVvlaPDPSPDTafpLIERE------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 375 lKPTLMAAVPEIMDRIyknvmnkvsemssfqrnlfilaynykMEQISKGRNTPlcdsfvfrkvRSLlggniRLLLCGGAP 454
Cdd:COG1021 274 -RVTVTALVPPLALLW--------------------------LDAAERSRYDL----------SSL-----RVLQVGGAK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 455 LSATTQRFMNICFCCPVGQGYGLTEsagaGTIsevwdyNTGRVGAP--LVC-------C---EIKLKNwEEGgyfntdKP 522
Cdd:COG1021 312 LSPELARRVRPALGCTLQQVFGMAE----GLV------NYTRLDDPeeVILttqgrpiSpddEVRIVD-EDG------NP 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 523 HPRGEIligGQSVT------MGYYKNEAKTKADFfeDENGqrWLCTGDIGEFEPDGCLKIIDRKKDLVKlQAGEYVSLGK 596
Cdd:COG1021 375 VPPGEV---GELLTrgpytiRGYYRAPEHNARAF--TPDG--FYRTGDLVRRTPDGYLVVEGRAKDQIN-RGGEKIAAEE 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 115502350 597 VEAALKNLPLVDN--------------ICAyansyhsyvigFVVPNQKELT--ELAR 637
Cdd:COG1021 447 VENLLLAHPAVHDaavvampdeylgerSCA-----------FVVPRGEPLTlaELRR 492
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
135-584 |
2.51e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 53.75 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACfmynfQLVTLYAT-----LGGPAIVHALNETEVTN 209
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAA-----RRSGLYYTpinwhLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 210 IITSKELLQTkLKDIVSLVPR-LRHIITVDGKPPTWSEFPkgiivhtmaavEALGAKAsmenqPHSKPLPSDIAVIMYTS 288
Cdd:PRK08276 87 LIVSAALADT-AAELAAELPAgVPLLLVVAGPVPGFRSYE-----------EALAAQP-----DTPIADETAGADMLYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 289 GSTGLPKGVM--ISHSNIIAGITGMAERI---PELGEEDVYIGYLPLAH---------VLELSAELVCLSHgcrigYSSP 354
Cdd:PRK08276 150 GTTGRPKGIKrpLPGLDPDEAPGMMLALLgfgMYGGPDSVYLSPAPLYHtaplrfgmsALALGGTVVVMEK-----FDAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 355 QTLAdqssKIKKgSKGDTSMLKPTL---MAAVPEimdriyknvmnKVsemssfqRNlfilAYNykmeqiskgrntplcds 431
Cdd:PRK08276 225 EALA----LIER-YRVTHSQLVPTMfvrMLKLPE-----------EV-------RA----RYD----------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 432 fvfrkVRSLlggniRLLLCGGAPLSATTQRFMnICFCCPV-GQGYGLTESAGAGTI-SEVWDYNTGRVGAPLVCceiKLK 509
Cdd:PRK08276 261 -----VSSL-----RVAIHAAAPCPVEVKRAM-IDWWGPIiHEYYASSEGGGVTVItSEDWLAHPGSVGKAVLG---EVR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 510 NWEEGGyfntdKPHPRGEI-LI----GGQSVTmgYYKNEAKTKADffedENGQRWLCTGDIGEFEPDGCLKIIDRKKDLV 584
Cdd:PRK08276 327 ILDEDG-----NELPPGEIgTVyfemDGYPFE--YHNDPEKTAAA----RNPHGWVTVGDVGYLDEDGYLYLTDRKSDMI 395
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
247-584 |
2.63e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.86 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 247 FPKGIIVHTMAAVEALGAKASMENQ----------PHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIP 316
Cdd:PRK09192 134 TPDELLPWVNEATHGNPLLHVLSHAwfkalpeadvALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 317 ELGEEDVYIGYLPLAHVLELSaelvclshGCRIgysSPqtLADQSSkikkgskgdTSMLKPTLMAAVPEI-MDRIYKNvM 395
Cdd:PRK09192 214 KVRPGDRCVSWLPFYHDMGLV--------GFLL---TP--VATQLS---------VDYLPTRDFARRPLQwLDLISRN-R 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 396 NKVSEMSSFqrnlfilayNYKmeqiskgrntpLCDsfvfRKVRSLLGGNI-----RLLLCGGAPLSA-TTQRFMNiCFcC 469
Cdd:PRK09192 271 GTISYSPPF---------GYE-----------LCA----RRVNSKDLAELdlscwRVAGIGADMIRPdVLHQFAE-AF-A 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 470 PVG-------QGYGLTESA--------GAGTISEVWD--------------YNTGRV------GAPLVCCEIKLKNweEG 514
Cdd:PRK09192 325 PAGfddkafmPSYGLAEATlavsfsplGSGIVVEEVDrdrleyqgkavapgAETRRVrtfvncGKALPGHEIEIRN--EA 402
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115502350 515 GyfnTDKPHPR-GEILIGGQSVTMGYYKNEAKTKAdffEDENGqrWLCTGDIGeFEPDGCLKIIDRKKDLV 584
Cdd:PRK09192 403 G---MPLPERVvGHICVRGPSLMSGYFRDEESQDV---LAADG--WLDTGDLG-YLLDGYLYITGRAKDLI 464
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
283-628 |
2.72e-07 |
|
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: 53.07 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 283 VIMYTSGSTGLPKGVMISHSNIIAGITGMAeRIPELGEEDVYIGYLPLAHVLEL-------------------SAELVC- 342
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQALLAQALVLA-VLQAIDEGTVFLNSGPLFHIGTLmftlatfhaggtnvfvrrvDAEEVLe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 343 --LSHGCRIGYSSPQTLaDQSSKIKKGSKGDTSMLKPTlmAAVPEIMDRIyknvmnkvsemssfqrnlfilaynykmeqi 420
Cdd:cd17636 83 liEAERCTHAFLLPPTI-DQIVELNADGLYDLSSLRSS--PAAPEWNDMA------------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 421 skgrntPLCDSFVFRKVRsllggnirlllcggaplsattqrfmnicfccpvgqGYGLTESAGAGTISEVWDYNTGRVGAP 500
Cdd:cd17636 130 ------TVDTSPWGRKPG-----------------------------------GYGQTEVMGLATFAALGGGAIGGAGRP 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 LVCCEIKLKNwEEGgyfNTDKPHPRGEILIGGQSVTMGYYKNEaktkadffeDENGQR----WLCTGDIGEFEPDGCLKI 576
Cdd:cd17636 169 SPLVQVRILD-EDG---REVPDGEVGEIVARGPTVMAGYWNRP---------EVNARRtrggWHHTNDLGRREPDGSLSF 235
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 115502350 577 IDRKKDLVKlQAGEYVSLGKVEAALKNLPLVDNICayansyhsyVIGfvVPN 628
Cdd:cd17636 236 VGPKTRMIK-SGAENIYPAEVERCLRQHPAVADAA---------VIG--VPD 275
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
216-634 |
2.77e-07 |
|
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: 53.67 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 216 LLQTKLK--DIVSLVPR--LRHIITVDGKPPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPL-PSDIAVIMYTSGS 290
Cdd:cd05923 82 LINPRLKaaELAELIERgeMTAAVIAVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPRePEQPAFVFYTSGT 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 291 TGLPKGVMISHSNIIAGITGMAERIPEL-GEEDVYIGYLPLAHVLELSAELV-CLSHG---CRIGYSSPQTLADQSSKik 365
Cdd:cd05923 162 TGLPKGAVIPQRAAESRVLFMSTQAGLRhGRHNVVLGLMPLYHVIGFFAVLVaALALDgtyVVVEEFDPADALKLIEQ-- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 366 kgskgdtsmLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFilaynykmeqisKGRNTPlcDSfVFRKVRSLLGGNI 445
Cdd:cd05923 240 ---------ERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTF------------AGATMP--DA-VLERVNQHLPGEK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 446 rlllcggAPLSATTQrFMNICFCCPVGQGYGLTesagAGTISEVwdyNTGRVGAPLVcceIKLKNWEEggyfntdkphpr 525
Cdd:cd05923 296 -------VNIYGTTE-AMNSLYMRDARTGTEMR----PGFFSEV---RIVRIGGSPD---EALANGEE------------ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 526 GEILI--GGQSVTMGYYKNEAKTKADFFEdengqRWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKN 603
Cdd:cd05923 346 GELIVaaAADAAFTGYLNQPEATAKKLQD-----GWYRTGDVGYVDPSGDVRILGRVDDMI-ISGGENIHPSEIERVLSR 419
|
410 420 430
....*....|....*....|....*....|....
gi 115502350 604 LPLVDNICAYA---NSYHSYVIGFVVPNQKELTE 634
Cdd:cd05923 420 HPGVTEVVVIGvadERWGQSVTACVVPREGTLSA 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
268-607 |
3.07e-07 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 54.40 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 268 MENQPHSKP---LPSD-IAVIMYTSGSTGLPKGVMISHSniiagitGMAERIP------ELGEEDVYIGYLPLA---HVL 334
Cdd:PRK05691 1258 LDSWPSQAPglhLHGDnLAYVIYTSGSTGQPKGVGNTHA-------ALAERLQwmqatyALDDSDVLMQKAPISfdvSVW 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 335 ELSAELVClshGCRIGYSSPqtladqsskikkGSKGDTSMLKP-------TLMAAVPEIMdriyknvmnkvsemssfqrN 407
Cdd:PRK05691 1331 ECFWPLIT---GCRLVLAGP------------GEHRDPQRIAElvqqygvTTLHFVPPLL-------------------Q 1376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 408 LFIlaynykmeqiskgrNTPL---CDSfvfrkvrsllggnIRLLLCGGAPLSATTQ-RFMNICFCCPVGQGYGLTESAGA 483
Cdd:PRK05691 1377 LFI--------------DEPLaaaCTS-------------LRRLFSGGEALPAELRnRVLQRLPQVQLHNRYGPTETAIN 1429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 484 GTISEVWDYNTGR--VGAPL--VCCEIKlknweeGGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFED---ENG 556
Cdd:PRK05691 1430 VTHWQCQAEDGERspIGRPLgnVLCRVL------DAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDplgEDG 1503
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 115502350 557 QRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLV 607
Cdd:PRK05691 1504 ARLYRTGDRARWNADGALEYLGRLDQQVKLR-GFRVEPEEIQARLLAQPGV 1553
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
449-627 |
3.88e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 53.34 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 449 LCGGA--PLSATTQ-RFMNI-CFCcpvgqGYGLTESAGAGTISEVwDYNTGrVGAPLVCCEIKLKNweeggyfntdkphp 524
Cdd:PRK09029 246 LLGGAaiPVELTEQaEQQGIrCWC-----GYGLTEMASTVCAKRA-DGLAG-VGSPLPGREVKLVD-------------- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 525 rGEILIGGQSVTMGYYKNEAKTKadfFEDENGqrWLCTGDIGEFEpDGCLKIIDRKKDLVkLQAGEYVSLGKVEAALKNL 604
Cdd:PRK09029 305 -GEIWLRGASLALGYWRQGQLVP---LVNDEG--WFATRDRGEWQ-NGELTILGRLDNLF-FSGGEGIQPEEIERVINQH 376
|
170 180
....*....|....*....|...
gi 115502350 605 PLVDNIcayansyhsyvigFVVP 627
Cdd:PRK09029 377 PLVQQV-------------FVVP 386
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
237-611 |
4.41e-07 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 52.74 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 237 VDGKPPTWSEFPKGIIVHTMAAVEALGAkasmenqphSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERip 316
Cdd:PRK07824 2 LAGRAPALLPVPAQDERRAALLRDALRV---------GEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDR-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 317 eLGEEDVYIGYLPLAHVLELSAELVCLSHGcrigySSPQTLaDQSskikkgskgdTSMLKPTLMAAvpeimdriyknvmn 396
Cdd:PRK07824 71 -LGGPGQWLLALPAHHIAGLQVLVRSVIAG-----SEPVEL-DVS----------AGFDPTALPRA-------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 397 kVSEMSSFQRNLFILAYnykmeQISKGRNTPlcdsfvfRKVRSLlggniRLL---LCGGAPLSATTQRF---MNIcfccP 470
Cdd:PRK07824 120 -VAELGGGRRYTSLVPM-----QLAKALDDP-------AATAAL-----AELdavLVGGGPAPAPVLDAaaaAGI----N 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 471 VGQGYGLTESAGAGtiseVWDyntgrvGAPLVCCEIKLKNweeggyfntdkphprGEILIGGQSVTMGYYKNEaktKADF 550
Cdd:PRK07824 178 VVRTYGMSETSGGC----VYD------GVPLDGVRVRVED---------------GRIALGGPTLAKGYRNPV---DPDP 229
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115502350 551 FEDENgqrWLCTGDIGEFEpDGCLKIIDRKKDLVKlQAGEYVSLGKVEAALKNLPLVDNIC 611
Cdd:PRK07824 230 FAEPG---WFRTDDLGALD-DGVLTVLGRADDAIS-TGGLTVLPQVVEAALATHPAVADCA 285
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
269-628 |
5.47e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 53.63 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 269 ENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAErIPELGEEDVYIGYLPLAH---VLELSAELVClsH 345
Cdd:PRK12467 3227 ENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAE-AYELDANDRVLLFMSFSFdgaQERFLWTLIC--G 3303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 346 GCRIgysspqtladqsskIKKGSKGDTSMLKPTLMAAVPEIMDriyknvmnkvsemssfqrnlFILAYNYKMEQISKGRN 425
Cdd:PRK12467 3304 GCLV--------------VRDNDLWDPEELWQAIHAHRISIAC--------------------FPPAYLQQFAEDAGGAD 3349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 426 tplcdsfvfrkvrsllGGNIRLLLCGG--APLSATTQRFMNICfccPVG--QGYGLTESAgagTISEVWDY-NTGRVGAP 500
Cdd:PRK12467 3350 ----------------CASLDIYVFGGeaVPPAAFEQVKRKLK---PRGltNGYGPTEAV---VTVTLWKCgGDAVCEAP 3407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 501 LVCCEIKLKNweEGGYF--NTDKPHPRG---EILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEFEPDG 572
Cdd:PRK12467 3408 YAPIGRPVAG--RSIYVldGQLNPVPVGvagELYIGGVGLARGYHQRPSLTAERFVADpfsGSGGRLYRTGDLARYRADG 3485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 115502350 573 CLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDN--ICAYANSYHSYVIGFVVPN 628
Cdd:PRK12467 3486 VIEYLGRIDHQVKIR-GFRIELGEIEARLLQHPSVREavVLARDGAGGKQLVAYVVPA 3542
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
259-628 |
5.84e-07 |
|
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: 52.68 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 259 VEALGAK---ASMENQP---HSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGiTGMAeRIPELGEEDVYIGYLPLAH 332
Cdd:cd05938 118 VISLLDKvdaASDEPVPaslRAHVTIKSPALYIYTSGTTGLPKAARISHLRVLQC-SGFL-SLCGVTADDVIYITLPLYH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 333 VlelSAELVCLsHGCrigysspqtladqsskIKKGSkgdTSMLKPTLMAAvpEIMDRIYK---NVMNKVSEmssfqrnlf 409
Cdd:cd05938 196 S---SGFLLGI-GGC----------------IELGA---TCVLKPKFSAS--QFWDDCRKhnvTVIQYIGE--------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 410 ILAYNYkmeqiskgrNTPLCDSFVFRKVRSLLGGNIRlllcggaplsATT-----QRFMNICFCcpvgQGYGLTEsagaG 484
Cdd:cd05938 242 LLRYLC---------NQPQSPNDRDHKVRLAIGNGLR----------ADVwreflRRFGPIRIR----EFYGSTE----G 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 485 TISEVwDYnTGRVGA-PLVCCEIKLKNWEEGGYFNTDKPHP------------RGE--ILIG---GQSVTMGYYKNEAKT 546
Cdd:cd05938 295 NIGFF-NY-TGKIGAvGRVSYLYKLLFPFELIKFDVEKEEPvrdaqgfcipvaKGEpgLLVAkitQQSPFLGYAGDKEQT 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 547 K----ADFFedENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALKNLPLVDNicayANSYhsyvi 622
Cdd:cd05938 373 EkkllRDVF--KKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWK-GENVATTEVADVLGLLDFLQE----VNVY----- 440
|
....*.
gi 115502350 623 GFVVPN 628
Cdd:cd05938 441 GVTVPG 446
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
135-324 |
7.26e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 52.59 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACfMYNFQLVT-LYATLGGPAIVHALNETEVTNIITS 213
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGA-LKNGAIVGpLFEAFMEEAVRDRLEDSEAKVLITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 214 KELLQTKLKDivsLVPRLRHIITVDG----KPPTWSeFPKgiivhtmaAVEALGAKASMEnqphskPL-PSDIAVIMYTS 288
Cdd:PRK04319 153 PALLERKPAD---DLPSLKHVLLVGEdveeGPGTLD-FNA--------LMEQASDEFDIE------WTdREDGAILHYTS 214
|
170 180 190
....*....|....*....|....*....|....*..
gi 115502350 289 GSTGLPKGVMISHSNIIAG-ITGmaERIPELGEEDVY 324
Cdd:PRK04319 215 GSTGKPKGVLHVHNAMLQHyQTG--KYVLDLHEDDVY 249
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
445-715 |
7.84e-07 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 52.39 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 445 IRLLLCGGAPLSATTQRFMnICFCCPV-GQGYGLTES-AGAGTISEVWDYNTGRVGAPLVCCEIKLKNwEEGgyfntdKP 522
Cdd:PRK12406 273 LRHVIHAAAPCPADVKRAM-IEWWGPViYEYYGSTESgAVTFATSEDALSHPGTVGKAAPGAELRFVD-EDG------RP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 523 HPRGEI------LIGGQSVTmgyYKNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGK 596
Cdd:PRK12406 345 LPQGEIgeiysrIAGNPDFT---YHNKPEKRAEIDRGG----FITSGDVGYLDADGYLFLCDRKRDMV-ISGGVNIYPAE 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 597 VEAALKNLPLVDNiCAYansyhsyvigFVVPNQkeltELArkkglkgtwEELCNSCEMENEVlkVLSEAAISASLE---- 672
Cdd:PRK12406 417 IEAVLHAVPGVHD-CAV----------FGIPDA----EFG---------EALMAVVEPQPGA--TLDEADIRAQLKarla 470
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 115502350 673 KFEIPVKIRLSPEpwTPEtglvTDAFKLKRKELKTHYQADIER 715
Cdd:PRK12406 471 GYKVPKHIEIMAE--LPR----EDSGKIFKRRLRDPYWANAGR 507
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
278-707 |
8.31e-07 |
|
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: 52.05 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 278 PSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPLAH-VLELSAELVCLSHGCRIGYSS--- 353
Cdd:cd05937 86 PDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDL-NLKNGDRTYTCMPLYHgTAAFLGACNCLMSGGTLALSRkfs 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 354 -----PQTLADQSSKIKKgskgdTSMLKPTLMAAVPEIMDRIYKnvmnkvsemssfqrnlfilaynykmeqiskgrntpl 428
Cdd:cd05937 165 asqfwKDVRDSGATIIQY-----VGELCRYLLSTPPSPYDRDHK------------------------------------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 429 cdsfvfrkVRSLLGGNIRlllcgGAPLSATTQRFmNIcfccP-VGQGYGLTESAGAgtiseVWDYNTGRVGAPLVCCEIK 507
Cdd:cd05937 204 --------VRVAWGNGLR-----PDIWERFRERF-NV----PeIGEFYAATEGVFA-----LTNHNVGDFGAGAIGHHGL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNWE-EGGYF------NTDKPHPR--------------GEIL--IGGQSVTM--GYYKNEAKTKADFFED--ENGQRWL 560
Cdd:cd05937 261 IRRWKfENQVVlvkmdpETDDPIRDpktgfcvrapvgepGEMLgrVPFKNREAfqGYLHNEDATESKLVRDvfRKGDIYF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 561 CTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEaalknlplvDNICAYANSYHSYVIGFVVPNQKeltELARKKG 640
Cdd:cd05937 341 RTGDLLRQDADGRWYFLDRLGDTFRWK-SENVSTTEVA---------DVLGAHPDIAEANVYGVKVPGHD---GRAGCAA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115502350 641 LKGTweelcNSCEMENEVLKVLSEAAISASLEKFEIPVKIRLSPEpwtpetGLVTDAFKLKRKELKT 707
Cdd:cd05937 408 ITLE-----ESSAVPTEFTKSLLASLARKNLPSYAVPLFLRLTEE------VATTDNHKQQKGVLRD 463
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
135-630 |
9.01e-07 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 52.07 E-value: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSK 214
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 215 ELLQTklkdivslVPRlrhiiTVDGKPPT-----WSEFPkgiivhTMAAVEALGAkASMENQPHSKPLPSDiaVIMYTSG 289
Cdd:PRK13382 149 EFSAT--------VDR-----ALADCPQAtrivaWTDED------HDLTVEVLIA-AHAGQRPEPTGRKGR--VILLTSG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 290 STGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGyLPLAHVLELSAELVCLSHGCrigysspqTLADQsskiKKGSK 369
Cdd:PRK13382 207 TTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVIV-APMFHAWGFSQLVLAASLAC--------TIVTR----RRFDP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 370 GDTSML----KPTLMAAVPEIMDRIyknvmnkvsemssfqrnlfilaynykMEQISKGRNTPLCdsfvfrkvRSLlggni 445
Cdd:PRK13382 274 EATLDLidrhRATGLAVVPVMFDRI--------------------------MDLPAEVRNRYSG--------RSL----- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 446 RLLLCGGAPL-----SATTQRFMNICFccpvgQGYGLTEsAGAGTISEVWDY----NTGrvGAPLVCCEIKLKNWEeggy 516
Cdd:PRK13382 315 RFAAASGSRMrpdvvIAFMDQFGDVIY-----NNYNATE-AGMIATATPADLraapDTA--GRPAEGTEIRILDQD---- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 517 FNTDKPHPRGEILIGGQSVTMGYYKNEAKtkaDFFEDengqrWLCTGDIGEFEPDGCLKIIDRKKDLVkLQAGEYVSLGK 596
Cdd:PRK13382 383 FREVPTGEVGTIFVRNDTQFDGYTSGSTK---DFHDG-----FMASGDVGYLDENGRLFVVGRDDEMI-VSGGENVYPIE 453
|
490 500 510
....*....|....*....|....*....|....*..
gi 115502350 597 VEAALKNLPLVDNICAYA---NSYHSYVIGFVVPNQK 630
Cdd:PRK13382 454 VEKTLATHPDVAEAAVIGvddEQYGQRLAAFVVLKPG 490
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
276-608 |
1.92e-06 |
|
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: 50.92 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 276 PLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERI-PELGEEDVyIGYLPLA---HVLELSAELVCLSHgCRIGY 351
Cdd:cd05910 82 PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYgIRPGEVDL-ATFPLFAlfgPALGLTSVIPDMDP-TRPAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 352 SSPQTLADQSSKikkgskgdtsmLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRnlfilaynykmeQISKGRNTPLcds 431
Cdd:cd05910 160 ADPQKLVGAIRQ-----------YGVSIVFGSPALLERVARYCAQHGITLPSLRR------------VLSAGAPVPI--- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 432 FVFRKVRSLLGGNIRLLLCGGA----PLSATTQRfmnicfccPVGQGYGLTESAGAGTIsevwdyntgrVGAPLVCCEIK 507
Cdd:cd05910 214 ALAARLRKMLSDEAEILTPYGAtealPVSSIGSR--------ELLATTTAATSGGAGTC----------VGRPIPGVRVR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 508 LKNWEEGGYFNTDKPH--PR---GEILIGGQSVTMGYYKNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKD 582
Cdd:cd05910 276 IIEIDDEPIAEWDDTLelPRgeiGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAH 355
|
330 340
....*....|....*....|....*.
gi 115502350 583 LVKLQAGEYVSLgKVEAALKNLPLVD 608
Cdd:cd05910 356 RVITTGGTLYTE-PVERVFNTHPGVR 380
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
250-354 |
3.19e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 50.33 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 250 GIIVHTMAAVEALGAKASMENQPHSKPLPSdIAVIMYTSGSTGLPKGVMISHSNIIAGIT-------GMAERIPELGEED 322
Cdd:PRK05850 132 GQSAPPVIEVDLLDLDSPRGSDARPRDLPS-TAYLQYTSGSTRTPAGVMVSHRNVIANFEqlmsdyfGDTGGVPPPDTTV 210
|
90 100 110
....*....|....*....|....*....|....*.
gi 115502350 323 VyiGYLPLAH----VLELSAELVClshGCRIGYSSP 354
Cdd:PRK05850 211 V--SWLPFYHdmglVLGVCAPILG---GCPAVLTSP 241
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
526-598 |
1.51e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 48.16 E-value: 1.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115502350 526 GEILIGGQSVTMGYYKNEAKTKADffedengqRWLCTGDIGEFEPDGCLKIIDRKKDLVKlQAGEYVSLGKVE 598
Cdd:PRK07008 385 GDLQVRGPWVIDRYFRGDASPLVD--------GWFPTGDVATIDADGFMQITDRSKDVIK-SGGEWISSIDIE 448
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
135-584 |
2.52e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 47.38 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRA---EWMIAAQACFMYnFQLVTLYATLGGPAivHALNETEVTNII 211
Cdd:PRK13391 25 VTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLrylEVCWAAERSGLY-YTCVNSHLTPAEAA--YIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 212 TSKELLqtklkDIVSL----VPRLRHIITVD--GKPPTWSEFPkgiivhtmaavEALgakasmENQPhSKPLPSDI--AV 283
Cdd:PRK13391 102 TSAAKL-----DVARAllkqCPGVRHRLVLDgdGELEGFVGYA-----------EAV------AGLP-ATPIADESlgTD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 284 IMYTSGSTGLPKGVM--ISHSNIIA--GITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRI----GYSSPQ 355
Cdd:PRK13391 159 MLYSSGTTGRPKGIKrpLPEQPPDTplPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVivmeHFDAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 356 TLA-DQSSKIKKgskgdtSMLKPTL---MAAVPEIMDRIYknvmnkvsEMSSFQRNLFilaynykmeqiskgrntplcds 431
Cdd:PRK13391 239 YLAlIEEYGVTH------TQLVPTMfsrMLKLPEEVRDKY--------DLSSLEVAIH---------------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 432 fvfrkvrsllggnirlllcGGAPLSATTQRFMnICFCCPV-GQGYGLTESAGAGTI-SEVWDYNTGRVGAPLVCceiKLK 509
Cdd:PRK13391 283 -------------------AAAPCPPQVKEQM-IDWWGPIiHEYYAATEGLGFTACdSEEWLAHPGTVGRAMFG---DLH 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115502350 510 NWEEGGyfntdKPHPRGEI----LIGGQSVTmgYYKNEAKTKADFFEDENgqrWLCTGDIGEFEPDGCLKIIDRKKDLV 584
Cdd:PRK13391 340 ILDDDG-----AELPPGEPgtiwFEGGRPFE--YLNDPAKTAEARHPDGT---WSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
178-332 |
4.41e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 46.60 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 178 ACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTkLKDIVSLVPrlrhIITVDGkpPTWSEfpkgiivhTMA 257
Cdd:PRK07867 73 AAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAEL-LDGLDPGVR----VINVDS--PAWAD--------ELA 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115502350 258 AveALGAKAsmenqPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNI-IAGITgMAERIpELGEEDVYIGYLPLAH 332
Cdd:PRK07867 138 A--HRDAEP-----PFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVaSAGVM-LAQRF-GLGPDDVCYVSMPLFH 204
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
135-607 |
4.57e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 46.66 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACfmynfqlvtlyATLGgpAIVHALN----ETEVTNI 210
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC-----------ARLG--ATVIAVNtryrSHEVAHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 211 ITSKE----LLQTKLKDI----------VSLVPRLRHIITVDGKPPT--------WSEFPKGiivHTMAAVEALGAKASM 268
Cdd:PRK06164 103 LGRGRarwlVVWPGFKGIdfaailaavpPDALPPLRAIAVVDDAADAtpapapgaRVQLFAL---PDPAPPAAAGERAAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 269 ENQPhskplpsdiAVIMYTSGSTGLPKGVM------ISHSNIIAGITGMaeripelGEEDVYIGYLPLAHVLELSAELVC 342
Cdd:PRK06164 180 PDAG---------ALLFTTSGTTSGPKLVLhrqatlLRHARAIARAYGY-------DPGAVLLAALPFCGVFGFSTLLGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 343 LSHG----CRIGYSSPQTLAD-QSSKIKKGSKGDtsmlkptlmaavpEIMDRIYKNVMN-------KVSEMSSFQRNLFI 410
Cdd:PRK06164 244 LAGGaplvCEPVFDAARTARAlRRHRVTHTFGND-------------EMLRRILDTAGEradfpsaRLFGFASFAPALGE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 411 LAynykmeQISKGRNTPLcdsfvfrkvRSLLGGN--IRLLLCGGAPLSATTQRfmnicfccpvgQGYGLTESAGAGTisE 488
Cdd:PRK06164 311 LA------ALARARGVPL---------TGLYGSSevQALVALQPATDPVSVRI-----------EGGGRPASPEARV--R 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 489 VWDYNTGRVGAPLVcceiklknweeggyfntdkphpRGEILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGEF 568
Cdd:PRK06164 363 ARDPQDGALLPDGE----------------------SGEIEIRAPSLMRGYLDNPDATARALTDDG----YFRTGDLGYT 416
|
490 500 510
....*....|....*....|....*....|....*....
gi 115502350 569 EPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLV 607
Cdd:PRK06164 417 RGDGQFVYQTRMGDSLRL-GGFLVNPAEIEHALEALPGV 454
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
136-324 |
1.55e-04 |
|
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: 44.88 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 136 SYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKE 215
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 216 LLQ----TKLKDIVS-----LVPRLRHIITVD--GKPPTWSEfPKGIIVHtmaaveALGAKASMENQPHSKPlPSDIAVI 284
Cdd:cd17634 166 GVRagrsVPLKKNVDdalnpNVTSVEHVIVLKrtGSDIDWQE-GRDLWWR------DLIAKASPEHQPEAMN-AEDPLFI 237
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 115502350 285 MYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVY 324
Cdd:cd17634 238 LYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIY 277
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
260-299 |
2.61e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.77 E-value: 2.61e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 115502350 260 EALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMI 299
Cdd:PRK05691 3850 EEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVMV 3889
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
251-332 |
2.69e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 44.25 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 251 IIVHTMAAVEALGAKASMEnqPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIpELGEEDVYIGYLPL 330
Cdd:PRK13388 124 LDVDTPAYAELVAAAGALT--PHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERF-GLTRDDVCYVSMPL 200
|
..
gi 115502350 331 AH 332
Cdd:PRK13388 201 FH 202
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
528-607 |
2.94e-04 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 43.96 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 528 ILIGGQSVTMGYYKNEAKTKADFFEDEngqrWLCTGDIGEFEPDGCLKIIDRKKDLVKLqAGEYVSLGKVEAALKNLPLV 607
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATRSALTPDG----FFRTGDIAVWDEEGYVEIKDRLKDLIKS-GGEWISSVDLENALMGHPKV 437
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
130-302 |
3.84e-04 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 43.70 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 130 GQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACfmynfqlvtlyATLGGP-AIVHA------- 201
Cdd:cd05966 80 DQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAC-----------ARIGAVhSVVFAgfsaesl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 202 ---LNETEVTNIITSKELLQTK----LKDIV----SLVPRLRHIITVD--GKPPTWSEfPKGIIVHTmaaveaLGAKASM 268
Cdd:cd05966 149 adrINDAQCKLVITADGGYRGGkvipLKEIVdealEKCPSVEKVLVVKrtGGEVPMTE-GRDLWWHD------LMAKQSP 221
|
170 180 190
....*....|....*....|....*....|....*
gi 115502350 269 ENQPhsKPLPS-DIAVIMYTSGSTGLPKGVMisHS 302
Cdd:cd05966 222 ECEP--EWMDSeDPLFILYTSGSTGKPKGVV--HT 252
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
266-304 |
3.98e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 3.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 115502350 266 ASMENQPHSKP----LPSDIAVIMYTSGSTGLPKGVMISHSNI 304
Cdd:PRK05691 2316 AALAAYSDAPLpflsLPQHQAYLIYTSGSTGKPKGVVVSHGEI 2358
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
526-637 |
4.15e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 44.00 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 526 GEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALK 602
Cdd:PRK05691 2533 GELYVGGAGLAQGYHDRPGLTAERFVADpfaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIR-GFRIELGEIESRLL 2611
|
90 100 110
....*....|....*....|....*....|....*..
gi 115502350 603 NLPLVDN--ICAYANSYHSYVIGFVVPNQKELTELAR 637
Cdd:PRK05691 2612 EHPAVREavVLALDTPSGKQLAGYLVSAVAGQDDEAQ 2648
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
135-332 |
1.10e-03 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 42.03 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 135 LSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAE----WM----IAAQACFMyNFQLvtlyatlGGPAIVHALNETE 206
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEfvalWLglakIGVETALI-NSNL-------RLESLLHCITVSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 207 VTNIITSkelLQTKLKDIVSLVPrlrhiitvdgkpptwsefPKGIIVhtmaavealGAKasmenqphskplpsDIAVIMY 286
Cdd:cd05939 76 AKALIFN---LLDPLLTQSSTEP------------------PSQDDV---------NFR--------------DKLFYIY 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 115502350 287 TSGSTGLPKGVMISHSNI--IAGITGMAERIpelGEEDVYIGYLPLAH 332
Cdd:cd05939 112 TSGTTGLPKAAVIVHSRYyrIAAGAYYAFGM---RPEDVVYDCLPLYH 156
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
526-642 |
2.09e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 526 GEILIGGQSVTMGYYKNEAKTKADFFED---ENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQaGEYVSLGKVEAALK 602
Cdd:PRK05691 4067 GELCVAGTGVGRGYVGDPLRTALAFVPHpfgAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIR-GYRIELGEIEARLH 4145
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 115502350 603 NLPLVDN--ICAYANSYHSYVIGFVVPNQKELTELARKKGLK 642
Cdd:PRK05691 4146 EQAEVREaaVAVQEGVNGKHLVGYLVPHQTVLAQGALLERIK 4187
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
220-301 |
2.49e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 41.32 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 220 KLKDIVSLVPRLRHIITVD--GKPPTWSEFPKgiiVHTMAAVEALGAKASMENQPhskpLPSDIAV-IMYTSGSTGLPKG 296
Cdd:PRK03584 208 KVAELRAALPSLEHVVVVPylGPAAAAAALPG---ALLWEDFLAPAEAAELEFEP----VPFDHPLwILYSSGTTGLPKC 280
|
....*
gi 115502350 297 VMISH 301
Cdd:PRK03584 281 IVHGH 285
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
280-337 |
3.65e-03 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 40.49 E-value: 3.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 115502350 280 DIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELS 337
Cdd:PRK12476 194 DVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLS 251
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
171-323 |
3.96e-03 |
|
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: 40.53 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115502350 171 EWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQtKLKDIVSLVPRLRHIITVDGKP-PTWSEFPK 249
Cdd:cd05928 79 EWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAP-EVDSVASECPSLKTKLLVSEKSrDGWLNFKE 157
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115502350 250 giivhtmaaveaLGAKASMEnqpHS--KPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDV 323
Cdd:cd05928 158 ------------LLNEASTE---HHcvETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDI 218
|
|
| |
