|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
42-518 |
0e+00 |
|
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: 566.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRaivTYELYI---AALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVI 118
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPR---VPELWAvilAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 119 sfssltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAH 198
Cdd:cd05972 78 ------------------------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 199 LQMApKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATAFVYNG-RFHPETYLELLQNYQINVLCCTPTEYRMMAK 277
Cdd:cd05972 110 IPTA-AYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGpRFDAERILELLERYGVTSFCGPPTAYRMLIK 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 278 LShLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDG 357
Cdd:cd05972 189 QD-LSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 358 KEVGPNVKGNIAVPLDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDAL 437
Cdd:cd05972 268 RELPPGEEGDIAIKLPPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 438 TNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05972 348 LEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVELR 427
|
.
gi 1801842045 518 D 518
Cdd:cd05972 428 D 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
8-520 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 565.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 8 APENYNIVSE-IEKYASED-HKKAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIA 85
Cdd:COG0365 4 VGGRLNIAYNcLDRHAEGRgDKVALIWEGEDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 86 ALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSSLT---KEFENVKEYDQ-------LKKFIVAGHK------EDWV 149
Cdd:COG0365 84 CARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGGLrggKVIDLKEKVDEaleelpsLEHVIVVGRTgadvpmEGDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 150 SIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWS 229
Cdd:COG0365 164 DWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 230 PFLSVLGMGATAFVYNGRF---HPETYLELLQNYQINVLCCTPTEYRMMAK--LSHLEQYNLEYLHSAVSAGEPLNREVV 304
Cdd:COG0365 244 IVYGPLLNGATVVLYEGRPdfpDPGRLWELIEKYGVTVFFTAPTAIRALMKagDEPLKKYDLSSLRLLGSAGEPLNPEVW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 305 EQFKRHFNITVRDGYGQTEST-LLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPALFKGYFK 383
Cdd:COG0365 324 EWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGMFRGYWN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 384 DEARTKAA---STGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIV 460
Cdd:COG0365 404 DPERYRETyfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 461 KAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAE 520
Cdd:COG0365 484 KAFVVLKPGVEPSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
6-518 |
6.24e-150 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 440.39 E-value: 6.24e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 6 LLAPENYNIVSEI-EKYASED-HKKAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELY 83
Cdd:cd05970 10 INVPENFNFAYDVvDAMAKEYpDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 84 IAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFS--SLTKEFENVKE--YDQLKKFIVAGH-KEDWVSIEDEKEKV 158
Cdd:cd05970 90 LALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAedNIPEEIEKAAPecPSKPKLVWVGDPvPEGWIDFRKLIKNA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 159 NDDLK----GADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMApKHWLCIQENDLVWATAAPGWQKWVWSPFLSV 234
Cdd:cd05970 170 SPDFErptaNSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTA-KYWQNVREGGLHLTVADTGWGKAVWGKIYGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 235 LGMGATAFVYN-GRFHPETYLELLQNYQINVLCCTPTEYRMMAKlSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNI 313
Cdd:cd05970 249 WIAGAAVFVYDyDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 314 TVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLD--LP-ALFKGYFKDEARTKA 390
Cdd:cd05970 328 KLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgKPvGLFGGYYKDAEKTAE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 391 ASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDY 470
Cdd:cd05970 408 VWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGY 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1801842045 471 EASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd05970 488 EPSEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
9-520 |
5.53e-138 |
|
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: 409.55 E-value: 5.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 9 PENYNIVSEIEKYASEDHKK-------AIIYKDNEHENISVSYKELISNANKVGNVFLNH-GLKKGDKVLIMMPRAIVTY 80
Cdd:cd05928 2 PEYFNFASDVLDQWADKEKAgkrppnpALWWVNGKGDEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 81 ELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSSLTKEFENV-KEYDQLK-KFIVAGHKED-WVSIEDEKEK 157
Cdd:cd05928 82 LVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVaSECPSLKtKLLVSEKSRDgWLNFKELLNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 158 VNDDLKGADT-TRDDLAILsYTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLG 236
Cdd:cd05928 162 ASTEHHCVETgSQEPMAIY-FTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 237 MGATAFVYN-GRFHPETYLELLQNYQINVLCCTPTEYRMMAKlSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITV 315
Cdd:cd05928 241 QGACVFVHHlPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 316 RDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAV---PLDLPALFKGYFKDEARTKAAS 392
Cdd:cd05928 320 YEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkPIRPFGLFSGYVDNPEKTAATI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 393 TGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEA 472
Cdd:cd05928 400 RGDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLS 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1801842045 473 SD--ELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAE 520
Cdd:cd05928 480 HDpeQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
13-514 |
6.71e-130 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 390.02 E-value: 6.71e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 13 NIVSE-IEKYASEDH--KKAIIYKDnEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRaivTYELYIA---A 86
Cdd:PRK04319 43 NIAYEaIDRHADGGRkdKVALRYLD-ASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPR---IPELYFAllgA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 87 LKLGiAIV-PSSEMLRTKDLQYRITHGEIDAVISFSSLTKEfENVKEYDQLKK-FIVAGHKE---DWVSIEDEKEKVNDD 161
Cdd:PRK04319 119 LKNG-AIVgPLFEAFMEEAVRDRLEDSEAKVLITTPALLER-KPADDLPSLKHvLLVGEDVEegpGTLDFNALMEQASDE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 162 LKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMApKHWLCIQENDLVWATAAPGW----QKWVWSPFLsvlgM 237
Cdd:PRK04319 197 FDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCTADPGWvtgtSYGIFAPWL----N 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 238 GATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLS--HLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITV 315
Cdd:PRK04319 272 GATNVIDGGRFSPERWYRILEDYKVTVWYTAPTAIRMLMGAGddLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLPI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 316 RDGYGQTES-TLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPALFKGYFKDEARTKAASTG 394
Cdd:PRK04319 352 HDNWWMTETgGIMIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWPSMMRGIWNNPEKYESYFAG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 395 DYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASD 474
Cdd:PRK04319 432 DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE 511
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1801842045 475 ELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKI-RRV 514
Cdd:PRK04319 512 ELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKImRRV 552
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
43-521 |
4.64e-123 |
|
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: 367.98 E-value: 4.64e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSS 122
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 LtkefenvkeydqlkkfivaghkedwvsiedeKEKvnddlkgadTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMA 202
Cdd:cd05969 82 L-------------------------------YER---------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 203 PKHwLCIQENDLVWATAAPGWQK----WVWSPFLSvlgmGATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKL 278
Cdd:cd05969 122 KYV-LDLHPDDIYWCTADPGWVTgtvyGIWAPWLN----GVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKE 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 279 SH--LEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTES-TLLIGFLKDTEPRMGSMGKGIPGSFVTVIDD 355
Cdd:cd05969 197 GDelARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETgSIMIANYPCMPIKPGSMGKPLPGVKAAVVDE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 356 DGKEVGPNVKGNIAVPLDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVED 435
Cdd:cd05969 277 NGNELPPGTKGILALKPGWPSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 436 ALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVE 515
Cdd:cd05969 357 ALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRV 436
|
....*.
gi 1801842045 516 LRDAEI 521
Cdd:cd05969 437 LKAKEL 442
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
26-519 |
2.16e-121 |
|
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: 364.13 E-value: 2.16e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYkdnehENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDL 105
Cdd:COG0318 14 DRPALVF-----GGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 106 QYRITHGEIDAVISfssltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadttrddlAILSYTSGTTGNP 185
Cdd:COG0318 89 AYILEDSGARALVT-----------------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 186 KAVTHSHGWGYAHLQMAPkHWLCIQENDlVWATAAP-----GWqkwvWSPFLSVLGMGATAfVYNGRFHPETYLELLQNY 260
Cdd:COG0318 116 KGVMLTHRNLLANAAAIA-AALGLTPGD-VVLVALPlfhvfGL----TVGLLAPLLAGATL-VLLPRFDPERVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 261 QINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLI--GFLKDTEPRM 338
Cdd:COG0318 189 RVTVLFGVPTMLARLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVtvNPEDPGERRP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 339 GSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRD 418
Cdd:COG0318 269 GSVGRPLPGVEVRIVDEDGRELPPGEVGEIVV--RGPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 419 DIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPRAIE 498
Cdd:COG0318 347 DMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAE---ELRAFLRERLARYKVPRRVE 423
|
490 500
....*....|....*....|.
gi 1801842045 499 FVENLPKTNSGKIRRVELRDA 519
Cdd:COG0318 424 FVDELPRTASGKIDRRALRER 444
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
42-520 |
2.44e-110 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 335.31 E-value: 2.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEidAVISfs 121
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGG--AVYA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 122 sltkefenvkeydqlkkfivaghkedwvsIEDEKEKVNDDLkgadttrddlaILSYTSGTTGNPKAVTHSHGwGYAHLQM 201
Cdd:cd05974 77 -----------------------------AVDENTHADDPM-----------LLYFTSGTTSKPKLVEHTHR-SYPVGHL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 202 APKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATAFVYN-GRFHPETYLELLQNYQINVLCCTPTEYRMmaklsh 280
Cdd:cd05974 116 STMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNyARFDAKRVLAALVRYGVTTLCAPPTVWRM------ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 281 LEQYNLEY----LHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDD 356
Cdd:cd05974 190 LIQQDLASfdvkLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPD 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 357 GkevGPNVKGNIAVPL--DLPA-LFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEV 433
Cdd:cd05974 270 G---APATEGEVALDLgdTRPVgLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 434 EDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVEnLPKTNSGKIRR 513
Cdd:cd05974 347 ESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETALEIFRFSRERLAPYKRIRRLEFAE-LPKTISGKIRR 425
|
....*..
gi 1801842045 514 VELRDAE 520
Cdd:cd05974 426 VELRRRE 432
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
42-518 |
2.96e-110 |
|
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: 335.17 E-value: 2.96e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFS 121
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 122 SltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadttrDDLAILSYTSGTTGNPKAVTHSHGWGYAHL-- 199
Cdd:cd05971 87 S-----------------------------------------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLpg 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 200 -QMApkHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATAFVYNG-RFHPETYLELLQNYQINVLCCTPTEYRMMAK 277
Cdd:cd05971 120 vQFP--FNLFPRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMtKFDPKAALDLMSRYGVTTAFLPPTALKMMRQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 278 L-SHLEQYNLEyLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEP-RMGSMGKGIPGSFVTVIDD 355
Cdd:cd05971 198 QgEQLKHAQVK-LRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFPiKPGSMGKPIPGHRVAIVDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 356 DGKEVGPNVKGNIAVPLDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVED 435
Cdd:cd05971 277 NGTPLPPGEVGEIAVELPDPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 436 ALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVE 515
Cdd:cd05971 357 CLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRE 436
|
...
gi 1801842045 516 LRD 518
Cdd:cd05971 437 LRA 439
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
43-517 |
2.10e-97 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 302.13 E-value: 2.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISfss 122
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 ltkefenvkEYDQLkkfivagHKEDwvsiedekekvnddlkgadttrDDLAILSYTSGTTGNPKAVTHS----HGWGyAH 198
Cdd:cd05973 79 ---------DAANR-------HKLD----------------------SDPFVMMFTSGTTGLPKGVPVPlralAAFG-AY 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 199 LQMApkhwLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYRM-MAK 277
Cdd:cd05973 120 LRDA----VDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLlMAA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 278 LSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIG-FLKDTEP-RMGSMGKGIPGSFVTVIDD 355
Cdd:cd05973 196 GAEVPARPKGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLAnHHALEHPvHAGSAGRAMPGWRVAVLDD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 356 DGKEVGPNVKGNIAVPLDLPAL--FKGYFKDEarTKAAStGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEV 433
Cdd:cd05973 276 DGDELGPGEPGRLAIDIANSPLmwFRGYQLPD--TPAID-GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 434 EDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:cd05973 353 ESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
....
gi 1801842045 514 VELR 517
Cdd:cd05973 433 FLLR 436
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
41-517 |
6.85e-95 |
|
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: 296.40 E-value: 6.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISF 120
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 SSLTkefenvkeydqlkKFIVAGHKEDwvsiedekekvnddlKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQ 200
Cdd:cd05936 104 VSFT-------------DLLAAGAPLG---------------ERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 201 MApKHWL--CIQENDLVWATAapgwqkwvwsPFLSVLGMGA--TAFVYNG-------RFHPETYLELLQNYQINVLCCTP 269
Cdd:cd05936 156 QI-KAWLedLLEGDDVVLAAL----------PLFHVFGLTValLLPLALGativlipRFRPIGVLKEIRKHRVTIFPGVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 270 TEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGF-LKDTEPRMGSMGKGIPGS 348
Cdd:cd05936 225 TMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVnPLDGPRKPGSIGIPLPGT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 349 FVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTI 428
Cdd:cd05936 305 EVKIVDDDGEELPPGEVGELWV--RGPQVMKGYWNRPEETAEAFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 429 GPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNS 508
Cdd:cd05936 383 YPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEE---EIIAFCREQLAGYKVPRQVEFRDELPKSAV 459
|
....*....
gi 1801842045 509 GKIRRVELR 517
Cdd:cd05936 460 GKILRRELR 468
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
171-512 |
3.26e-94 |
|
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: 290.34 E-value: 3.26e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 171 DLAILSYTSGTTGNPKAVTHSHGwGYAHLQMAPKHWLCIQENDLVWATAAPGWQkWVWSPFLSVLGMGATAFVYnGRFHP 250
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHR-NLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVVLL-PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 251 ETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTE--STLLI 328
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTEtgGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 329 GFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDND 408
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVV--RGPSVMKGYWNNPEATAAVDEDGWYRTGDLGRLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 409 GYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQddyEASDELIQELQVFCKNEV 488
Cdd:cd04433 236 GYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLR---PGADLDAEELRAHVRERL 312
|
330 340
....*....|....*....|....
gi 1801842045 489 APYKYPRAIEFVENLPKTNSGKIR 512
Cdd:cd04433 313 APYKVPRRVVFVDALPRTASGKID 336
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
10-517 |
1.07e-93 |
|
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: 294.66 E-value: 1.07e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 10 ENYNIVSEI--EKYASEDHKKAIIYKDNeheniSVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAAL 87
Cdd:cd05959 1 EKYNAATLVdlNLNEGRGDKTAFIDDAG-----SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 88 KLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSSLTKEFENVKEYDQ--LKKFIVAGHKEDW---VSIEDEKEKVNDDL 162
Cdd:cd05959 76 RAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEhtLVVLIVSGGAGPEagaLLLAELVAAEAEQL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 163 KGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATA----APGWQKWVWSPFlsvlGMG 238
Cdd:cd05959 156 KPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAklffAYGLGNSLTFPL----SVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 239 ATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDG 318
Cdd:cd05959 232 ATTVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 319 YGQTEstLLIGFLKDT--EPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDY 396
Cdd:cd05959 312 IGSTE--MLHIFLSNRpgRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYV--RGPSSATMYWNNRDKTRDTFQGEW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 397 YVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEL 476
Cdd:cd05959 388 TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEAL 467
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1801842045 477 IQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05959 468 EEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
12-518 |
7.65e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 290.16 E-value: 7.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 12 YNIVSEIEKYASEDHKKAIIYKDNEHEnisVSYKELISNANKVGNVFLNHGLKKGDKVLIMM---PRAIvtyELYIAALK 88
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFDGRR---TTYAELDERVNRLANALRALGVKKGDRVAVFDwnsHEYL---EAYFAVPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 89 LGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSSLTKEFENVKEY-DQLKKFIV------AGHKEDWVSIEDEKEKVNDD 161
Cdd:PRK06187 79 IGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQlPTVRTVIVegdgpaAPLAPEVGEYEELLAAASDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 162 LKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLqMAPKHWLCIQEND--LVWA----TAAPGWqkwvwsPFLSVL 235
Cdd:PRK06187 159 FDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHS-LAVCAWLKLSRDDvyLVIVpmfhVHAWGL------PYLALM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 236 gMGATAfVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITV 315
Cdd:PRK06187 232 -AGAKQ-VIPRRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFGIDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 316 RDGYGQTESTLLIGFL------KDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVK--GNIAVplDLPALFKGYFKDEAR 387
Cdd:PRK06187 310 VQGYGMTETSPVVSVLppedqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDGGevGEIIV--RGPWLMQGYWNRPEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 388 TKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQ 467
Cdd:PRK06187 388 TAETIDGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1801842045 468 DDYEASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK06187 468 PGATLDAK---ELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
41-517 |
7.37e-91 |
|
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: 285.14 E-value: 7.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNH-GLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVIs 119
Cdd:cd05958 10 EWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVAL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 120 fssltkefenvkeydqlkkfivaghkedwvsiedekekvnddLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHL 199
Cdd:cd05958 89 ------------------------------------------CAHALTASDDICILAFTSGTTGAPKATMHFHRDPLASA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 200 QMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATAFVYNGRfHPETYLELLQNYQINVLCCTPTEYRMMAKLS 279
Cdd:cd05958 127 DRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVLLEEA-TPDLLLSAIARYKPTVLFTAPTAYRAMLAHP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 280 HLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTEstLLIGFLKDTE--PRMGSMGKGIPGSFVTVIDDDG 357
Cdd:cd05958 206 DAAGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTE--MFHIFISARPgdARPGATGKPVPGYEAKVVDDEG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 358 KEVGPNVKGNIAVplDLPALFKGYFKDEARTKAAstGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDAL 437
Cdd:cd05958 284 NPVPDGTIGRLAV--RGPTGCRYLADKRQRTYVQ--GGWNITGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 438 TNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05958 360 LQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
37-517 |
1.77e-90 |
|
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: 283.97 E-value: 1.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 37 HENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDA 116
Cdd:cd05919 6 AADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 117 VIsfssltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadTTRDDLAILSYTSGTTGNPKAVTHSHGWGY 196
Cdd:cd05919 86 VV------------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 197 AHLQMAPKHWLCIQENDLVWATA----APGWQKWVWSPflsvLGMGATAFVYNGRFHPETYLELLQNYQINVLCCTPTEY 272
Cdd:cd05919 118 LFADAMAREALGLTPGDRVFSSAkmffGYGLGNSLWFP----LAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 273 RMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLigFLKDT--EPRMGSMGKGIPGSFV 350
Cdd:cd05919 194 ANLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHI--FLSNRpgAWRLGSTGRPVPGYEI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 351 TVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGP 430
Cdd:cd05919 272 RLVDEEGHTIPPGEEGDLLV--RGPSAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 431 FEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGK 510
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGK 429
|
....*..
gi 1801842045 511 IRRVELR 517
Cdd:cd05919 430 LQRFKLR 436
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
26-518 |
1.22e-84 |
|
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: 274.05 E-value: 1.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYKDNEHENI-SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPraiVTYELYIAAL---KLGI--AIVP---S 96
Cdd:cd05966 68 DKVAIIWEGDEPDQSrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMP---MIPELVIAMLacaRIGAvhSVVFagfS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 97 SEMLRTkdlqyRITHGEIDAVISFSSL--------TKEF--ENVKEYDQLKKFIVAGHKEDWVSIEDEKEKVNDDLKGAD 166
Cdd:cd05966 145 AESLAD-----RINDAQCKLVITADGGyrggkvipLKEIvdEALEKCPSVEKVLVVKRTGGEVPMTEGRDLWWHDLMAKQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 167 TTR---------DDLAILsYTSGTTGNPKAVTHSHGwGYA-HLQMAPKHWLCIQENDLVWATAAPGW----QKWVWSPfl 232
Cdd:cd05966 220 SPEcepewmdseDPLFIL-YTSGSTGKPKGVVHTTG-GYLlYAATTFKYVFDYHPDDIYWCTADIGWitghSYIVYGP-- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 233 svLGMGATAFVYNGRF---HPETYLELLQNYQINVLCCTPTEYRMMAKL--SHLEQYNLEYLHSAVSAGEPLNREVVEQF 307
Cdd:cd05966 296 --LANGATTVMFEGTPtypDPGRYWDIVEKHKVTIFYTAPTAIRALMKFgdEWVKKHDLSSLRVLGSVGEPINPEAWMWY 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 308 KRH---FNITVRDGYGQTES-TLLI---GFLKDTEPrmGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPALFKG 380
Cdd:cd05966 374 YEVigkERCPIVDTWWQTETgGIMItplPGATPLKP--GSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPWPGMART 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 381 YFKDEAR---TKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRG 457
Cdd:cd05966 452 IYGDHERyedTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKG 531
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1801842045 458 NIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKI-RRVeLRD 518
Cdd:cd05966 532 EAIYAFVTLKDGEEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKImRRI-LRK 592
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
26-513 |
2.83e-78 |
|
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: 252.53 E-value: 2.83e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYkdnehENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPssemlrtkdL 105
Cdd:cd17631 10 DRTALVF-----GGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP---------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 106 QYRITHGEIDAVISFSsltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkGADTTRDDLAILSYTSGTTGNP 185
Cdd:cd17631 76 NFRLTPPEVAYILADS------------------------------------------GAKVLFDDLALLMYTSGTTGRP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 186 KAVTHSHG---WGYAHLQMApkhwLCIQENDlVWATAAP-----GWQKWVwspfLSVLGMGATAfVYNGRFHPETYLELL 257
Cdd:cd17631 114 KGAMLTHRnllWNAVNALAA----LDLGPDD-VLLVVAPlfhigGLGVFT----LPTLLRGGTV-VILRKFDPETVLDLI 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 258 QNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRhFNITVRDGYGQTESTLLIGFL--KDTE 335
Cdd:cd17631 184 ERHRVTSFFLVPTMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTFLspEDHR 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 336 PRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEG 415
Cdd:cd17631 263 RKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVV--RGPHVMAGYWNRPEATAAAFRDGWFHTGDLGRLDEDGYLYIVD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 416 RRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPR 495
Cdd:cd17631 341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDED---ELIAHCRERLARYKIPK 417
|
490
....*....|....*...
gi 1801842045 496 AIEFVENLPKTNSGKIRR 513
Cdd:cd17631 418 SVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
38-424 |
7.64e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 248.00 E-value: 7.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 38 ENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAV 117
Cdd:pfam00501 18 EGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 I--SFSSLTKEFENVKEYDQLKKFIV---AGHKEDWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSH 192
Cdd:pfam00501 98 ItdDALKLEELLEALGKLEVVKLVLVldrDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTGKPKGVMLTH 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 193 G---WGYAHLQMAPKHWLCIQENDLVWATA----APGWQKWVWSPFLSvlgmGATAFVYNG--RFHPETYLELLQNYQIN 263
Cdd:pfam00501 178 RnlvANVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLSLGLLGPLLA----GATVVLPPGfpALDPAALLELIERYKVT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 264 VLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTEST---LLIGFLKDTEPRMGS 340
Cdd:pfam00501 254 VLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTgvvTTPLPLDEDLRSLGS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 341 MGKGIPGSFVTVIDDD-GKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAA-STGDYYVTGDQAHIDNDGYFWFEGRRD 418
Cdd:pfam00501 334 VGRPLPGTEVKIVDDEtGEPVPPGEPGELCV--RGPGVMKGYLNDPELTAEAfDEDGWYRTGDLGRRDEDGYLEIVGRKK 411
|
....*.
gi 1801842045 419 DIIISS 424
Cdd:pfam00501 412 DQIKLG 417
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
41-519 |
1.77e-76 |
|
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: 249.76 E-value: 1.77e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISF 120
Cdd:TIGR02262 30 SLSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 SSLTKEFEN-VKEYDQLKKFIVAGHKED-WVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAH 198
Cdd:TIGR02262 110 GALLPVIKAaLGKSPHLEHRVVVGRPEAgEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 199 LQMAPKHWLCIQENDLVWATA----APGWQKWVWSPflsvLGMGATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYRM 274
Cdd:TIGR02262 190 AELYARNTLGIREDDVCFSAAklffAYGLGNALTFP----MSVGATTVLMGERPTPDAVFDRLRRHQPTIFYGVPTLYAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 275 MAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTEstLLIGFLKDTEPRM--GSMGKGIPGSFVTV 352
Cdd:TIGR02262 266 MLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTE--MLHIFLSNLPGDVryGTSGKPVPGYRLRL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 353 IDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFE 432
Cdd:TIGR02262 344 VGDGGQDVADGEPGELLI--SGPSSATMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 433 VEDALTNHAAVKECAVVASpHDIRGNIV-KAFIILQDDYEASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKI 511
Cdd:TIGR02262 422 IESALIQHPAVLEAAVVGV-ADEDGLIKpKAFVVLRPGQTALET---ELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKI 497
|
....*...
gi 1801842045 512 RRVELRDA 519
Cdd:TIGR02262 498 QRFKLREG 505
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
29-511 |
4.54e-75 |
|
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: 245.59 E-value: 4.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKDNEHEnisVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVP------SSEMLRt 102
Cdd:cd05911 1 AQIDADTGKE---LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAanpiytADELAH- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 103 kdlQYRITHgeidAVISFSSLtKEFENVKE----YDQLKKFIVAGHKEDWV-SIED--------EKEKVNDDLKgadTTR 169
Cdd:cd05911 77 ---QLKISK----PKVIFTDP-DGLEKVKEaakeLGPKDKIIVLDDKPDGVlSIEDllsptlgeEDEDLPPPLK---DGK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHgwgyahlqmapKHwlCIQENDLVWATaapgWQKWVWSP--FLSVL----GMGATAFV 243
Cdd:cd05911 146 DDTAAILYSSGTTGLPKGVCLSH-----------RN--LIANLSQVQTF----LYGNDGSNdvILGFLplyhIYGLFTTL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 244 ---YNG-------RFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF-N 312
Cdd:cd05911 209 aslLNGatviimpKFDSELFLDLIEKYKITFLYLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFpN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 313 ITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKE-VGPNVKGNIAVplDLPALFKGYFKDEARTKAA 391
Cdd:cd05911 289 ATIKQGYGMTETGGILTVNPDGDDKPGSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICV--RGPQVMKGYYNNPEATKET 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 392 STGDYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDY 470
Cdd:cd05911 367 FDEDGWLhTGDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1801842045 471 EASDeliQELQVFCKNEVAPYKYPRA-IEFVENLPKTNSGKI 511
Cdd:cd05911 447 KLTE---KEVKDYVAKKVASYKQLRGgVVFVDEIPKSASGKI 485
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
29-518 |
1.05e-72 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 242.99 E-value: 1.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKDNEHENI-SVSYKELISNANKVGNVFLNHGLKKGDKVLI---MMPRAIVTYelyIAALKLGiAIvpSSEML---R 101
Cdd:cd05967 69 ALIYDSPVTGTErTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIympMIPEAAIAM---LACARIG-AI--HSVVFggfA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 102 TKDLQYRITHGEIDAVISfSSLTKEFENVKEYDQL--KKFIVAGHKEDWVSIedekekVNDDLKGADTTR---------- 169
Cdd:cd05967 143 AKELASRIDDAKPKLIVT-ASCGIEPGKVVPYKPLldKALELSGHKPHHVLV------LNRPQVPADLTKpgrdldwsel 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 ---------------DDLAILsYTSGTTGNPKAVTHSHGwGYA-HLQMAPKHWLCIQENDLVWATAAPGW----QKWVWS 229
Cdd:cd05967 216 lakaepvdcvpvaatDPLYIL-YTSGTTGKPKGVVRDNG-GHAvALNWSMRNIYGIKPGDVWWAASDVGWvvghSYIVYG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 230 PFLSvlgmGATAFVYNGR--FHPE--TYLELLQNYQINVLCCTPTEYRMMAKL----SHLEQYNLEYLHSAVSAGEPLNR 301
Cdd:cd05967 294 PLLH----GATTVLYEGKpvGTPDpgAFWRVIEKYQVNALFTAPTAIRAIRKEdpdgKYIKKYDLSSLRTLFLAGERLDP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 302 EVVEQFKRHFNITVRDGYGQTES-----TLLIGfLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDL-P 375
Cdd:cd05967 370 PTLEWAENTLGVPVIDHWWQTETgwpitANPVG-LEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPLpP 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 376 ALFKGYFKDEARTKAASTGD---YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASP 452
Cdd:cd05967 449 GCLLTLWKNDERFKKLYLSKfpgYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVR 528
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801842045 453 HDIRGNIVKAFIILQDDYEAS-DELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd05967 529 DELKGQVPLGLVVLKEGVKITaEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
27-518 |
2.98e-72 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 241.97 E-value: 2.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYK-DNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIvtyELYIAAL---KLGIA--IVP---SS 97
Cdd:PRK00174 83 KVAIIWEgDDPGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIP---EAAVAMLacaRIGAVhsVVFggfSA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 98 EMLRTkdlqyRITHGEIDAVISfsslTKEF----------ENV----KEYDQLKKFIV---AGHKEDWVS-----IEDEK 155
Cdd:PRK00174 160 EALAD-----RIIDAGAKLVIT----ADEGvrggkpiplkANVdealANCPSVEKVIVvrrTGGDVDWVEgrdlwWHELV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 156 EKVNDDLK----GADttrDDLAILsYTSGTTGNPKAVTHSHGwGYA-HLQMAPKHWLCIQENDLVWATAAPGW----QKW 226
Cdd:PRK00174 231 AGASDECEpepmDAE---DPLFIL-YTSGSTGKPKGVLHTTG-GYLvYAAMTMKYVFDYKDGDVYWCTADVGWvtghSYI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 227 VWSPflsvLGMGATAFVY--------NGRFhpetyLELLQNYQINVLCCTPTEYRMMAKL--SHLEQYNLEYLHSAVSAG 296
Cdd:PRK00174 306 VYGP----LANGATTLMFegvpnypdPGRF-----WEVIDKHKVTIFYTAPTAIRALMKEgdEHPKKYDLSSLRLLGSVG 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 297 EPLNREVVEQFKRHF---NITVRDGYGQTES-----TLLIGfLKDTEPrmGSMGKGIPGSFVTVIDDDGKEVGPNVKGNI 368
Cdd:PRK00174 377 EPINPEAWEWYYKVVggeRCPIVDTWWQTETggimiTPLPG-ATPLKP--GSATRPLPGIQPAVVDEEGNPLEGGEGGNL 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 369 AVPLDLPALFKGYFKDEARTKAA--ST-GDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKE 445
Cdd:PRK00174 454 VIKDPWPGMMRTIYGDHERFVKTyfSTfKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAE 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801842045 446 CAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKI-RRVeLRD 518
Cdd:PRK00174 534 AAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGKImRRI-LRK 606
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
27-520 |
7.20e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 238.71 E-value: 7.20e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYKDNEhenisVSYKELISNANKVGNvFLNH--GLKKGDKVLIMM---PRAIVTYelyIAALKLGIAIVPSSEMLR 101
Cdd:PRK08314 26 KTAIVFYGRA-----ISYRELLEEAERLAG-YLQQecGVRKGDRVLLYMqnsPQFVIAY---YAILRANAVVVPVNPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 102 TKDLQYRITHGEIDAVISFSSLTKEFENVKEYDQLKKFIVAGHKE-----------DWVSIEDEKEKV--------NDDL 162
Cdd:PRK08314 97 EEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSDylpaepeiavpAWLRAEPPLQALapggvvawKEAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 163 KGADT------TRDDLAILSYTSGTTGNPKAVTHSHGwgyahlqmapkhwlciqendLVWATAApGWQKWVWS------- 229
Cdd:PRK08314 177 AAGLAppphtaGPDDLAVLPYTSGTTGVPKGCMHTHR--------------------TVMANAV-GSVLWSNStpesvvl 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 230 ---PFLSVLGM--GATAFVYNG-------RFHPETYLELLQNYQINVLCCTPTeyrMMAKL---SHLEQYNLEYLHSAVS 294
Cdd:PRK08314 236 avlPLFHVTGMvhSMNAPIYAGatvvlmpRWDREAAARLIERYRVTHWTNIPT---MVVDFlasPGLAERDLSSLRYIGG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 295 AGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMgkGIPgSFVT---VID-DDGKEVGPNVKGNIAV 370
Cdd:PRK08314 313 GGAAMPEAVAERLKELTGLDYVEGYGLTETMAQTHSNPPDRPKLQCL--GIP-TFGVdarVIDpETLEELPPGEVGEIVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 371 plDLPALFKGYFKDEARTKAA----STGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKEC 446
Cdd:PRK08314 390 --HGPQVFKGYWNRPEATAEAfieiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801842045 447 AVVASPHDIRGNIVKAFIILQDDYEA---SDELIQelqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAE 520
Cdd:PRK08314 468 CVIATPDPRRGETVKAVVVLRPEARGkttEEEIIA----WAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQE 540
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-517 |
1.64e-69 |
|
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: 229.10 E-value: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISfss 122
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 ltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadttrdDLAILSYTSGTTGNPKAV--THSHgwgYAHLQ 200
Cdd:cd05934 82 ------------------------------------------------DPASILYTSGTTGPPKGVviTHAN---LTFAG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 201 MAPKHWLCIQENDlVWATAAP----GWQKWVWSPFLSVlgmGATaFVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMA 276
Cdd:cd05934 111 YYSARRFGLGEDD-VYLTVLPlfhiNAQAVSVLAALSV---GAT-LVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLL 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 277 KLSHLEQYNLEYLHSAVSAGEPlnREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDD 356
Cdd:cd05934 186 AQPPSPDDRAHRLRAAYGAPNP--PELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 357 GKEVGPNVKGNIAV-PLDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVED 435
Cdd:cd05934 264 GQELPAGEPGELVIrGLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 436 ALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVE 515
Cdd:cd05934 344 AILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPE---ELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQ 420
|
..
gi 1801842045 516 LR 517
Cdd:cd05934 421 LR 422
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
26-511 |
2.03e-68 |
|
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: 230.54 E-value: 2.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYKDNEHENI-SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKD 104
Cdd:cd17634 68 DRTAIIYEGDDTSQSrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 105 LQYRITHGEIDAVISFSSLTKEFENVkeydQLKKFI-----------------------VAGHKEDWVSIEDEKEKVNDD 161
Cdd:cd17634 148 VAGRIIDSSSRLLITADGGVRAGRSV----PLKKNVddalnpnvtsvehvivlkrtgsdIDWQEGRDLWWRDLIAKASPE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 162 LKGADTTRDDLAILSYTSGTTGNPKAVTHSHGwGYA-HLQMAPKHWLCIQENDLVWATAAPGWQkwVWSPFL--SVLGMG 238
Cdd:cd17634 224 HQPEAMNAEDPLFILYTSGTTGKPKGVLHTTG-GYLvYAATTMKYVFDYGPGDIYWCTADVGWV--TGHSYLlyGPLACG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 239 ATAFVYNGRFH---PETYLELLQNYQINVLCCTPTEYRMMAKLSH--LEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNI 313
Cdd:cd17634 301 ATTLLYEGVPNwptPARMWQVVDKHGVNILYTAPTAIRALMAAGDdaIEGTDRSSLRILGSVGEPINPEAYEWYWKKIGK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 314 T---VRDGYGQTE-STLLIGFLKDTEP-RMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPALFKGYFKDEAR- 387
Cdd:cd17634 381 EkcpVVDTWWQTEtGGFMITPLPGAIElKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWPGQTRTLFGDHERf 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 388 --TKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFII 465
Cdd:cd17634 461 eqTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVV 540
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1801842045 466 LQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKI 511
Cdd:cd17634 541 LNHGVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
41-513 |
2.08e-68 |
|
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: 226.59 E-value: 2.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISF 120
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 SSLtkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadttrDDLAILSYTSGTTGNPKAVTHSHGWGYAHLq 200
Cdd:cd05935 81 SEL----------------------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANA- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 201 MAPKHWLCIQENDLVWATAapgwqkwvwsPFLSVLGM----------GATaFVYNGRFHPETYLELLQNYQINVLCCTPT 270
Cdd:cd05935 114 LQSAVWTGLTPSDVILACL----------PLFHVTGFvgslntavyvGGT-YVLMARWDRETALELIEKYKVTFWTNIPT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 271 EYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIgflkDTEP--RMGSMGKGIPGS 348
Cdd:cd05935 183 MLVDLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQT----HTNPplRPKLQCLGIP*F 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 349 FVT--VID-DDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGD----YYVTGDQAHIDNDGYFWFEGRRDDII 421
Cdd:cd05935 259 GVDarVIDiETGRELPPNEVGEIVV--RGPQIFKGYWNRPEETEESFIEIkgrrFFRTGDLGYMDEEGYFFFVDRVKRMI 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 422 ISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDY--EASDELIQElqvFCKNEVAPYKYPRAIEF 499
Cdd:cd05935 337 NVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIE---WAREQMAAYKYPREVEF 413
|
490
....*....|....
gi 1801842045 500 VENLPKTNSGKIRR 513
Cdd:cd05935 414 VDELPRSASGKILW 427
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
9-518 |
3.77e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 217.46 E-value: 3.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 9 PENYNIVSEIEKYASE-DHKKAIIYKDNeheniSVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRA---IVTYelyI 84
Cdd:PRK07656 2 NEWMTLPELLARAARRfGDKEAYVFGDQ-----RLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSphwVIAA---L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 85 AALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSSLTKEFENVKEYD-QLKKFIV------AGHKEDWVSIEDEKEK 157
Cdd:PRK07656 74 GALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLpALEHVVIceteedDPHTEKMKTFTDFLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 158 VNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAhlqmAPKHW---LCIQENDLVWATaapgwqkwvwSPFLSV 234
Cdd:PRK07656 154 GDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQLLS----NAADWaeyLGLTEGDRYLAA----------NPFFHV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 235 LGM----------GATAFVYNgRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVV 304
Cdd:PRK07656 220 FGYkagvnaplmrGATILPLP-VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 305 EQFKRHFNI-TVRDGYGQTESTLLIGFLKDTEPRM---GSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKG 380
Cdd:PRK07656 299 ERFESELGVdIVLTGYGLSEASGVTTFNRLDDDRKtvaGTIGTAIAGVENKIVNELGEEVPVGEVGELLV--RGPNVMKG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 381 YFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNI 459
Cdd:PRK07656 377 YYDDPEATAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 460 VKAFIILQDDYEAS-DELIQelqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK07656 457 GKAYVVLKPGAELTeEELIA----YCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
13-519 |
6.64e-61 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 211.19 E-value: 6.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 13 NIVSEIEKY--ASEDHKKAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLG 90
Cdd:cd05968 61 NIVEQLLDKwlADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 91 IAIVP-----SSEMLRTkdlqyRITHGEIDAVIS---FS------SLTKEFENVKEYD-QLKKFIV--------AGHKED 147
Cdd:cd05968 141 GIVVPifsgfGKEAAAT-----RLQDAEAKALITadgFTrrgrevNLKEEADKACAQCpTVEKVVVvrhlgndfTPAKGR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 148 WVSIEDEKEKVNDDLkgADTTRDDLAILSYTSGTTGNPKAVTHSHGwGY---AHLQMApkHWLCIQENDLV-WATAApGW 223
Cdd:cd05968 216 DLSYDEEKETAGDGA--ERTESEDPLMIIYTSGTTGKPKGTVHVHA-GFplkAAQDMY--FQFDLKPGDLLtWFTDL-GW 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 224 QKWVWSPFLSVLgMGATAFVYNGR-FHPET--YLELLQNYQINVLCCTPTEYR--MMAKLSHLEQYNLEYLHSAVSAGEP 298
Cdd:cd05968 290 MMGPWLIFGGLI-LGATMVLYDGApDHPKAdrLWRMVEDHEITHLGLSPTLIRalKPRGDAPVNAHDLSSLRVLGSTGEP 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 299 LNREVVEQFKRHF---NITVRDGYGQTE-STLLIG--FLKDTEPrmGSMGKGIPGSFVTVIDDDGKEVGPNVkGNIAVPL 372
Cdd:cd05968 369 WNPEPWNWLFETVgkgRNPIINYSGGTEiSGGILGnvLIKPIKP--SSFNGPVPGMKADVLDESGKPARPEV-GELVLLA 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 373 DLPALFKGYFKDEAR---TKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVV 449
Cdd:cd05968 446 PWPGMTRGFWRDEDRyleTYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 450 ASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:cd05968 526 GVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAA 595
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
41-518 |
1.77e-60 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 207.62 E-value: 1.77e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVIS- 119
Cdd:PRK13391 24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 120 ------FSSLTKEFENVKEYDQLKKFivaGHKEDWVSIEDEKEKVNDDlKGADTTRDDLaiLSYTSGTTGNPKAVthshg 193
Cdd:PRK13391 104 aakldvARALLKQCPGVRHRLVLDGD---GELEGFVGYAEAVAGLPAT-PIADESLGTD--MLYSSGTTGRPKGI----- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 194 wgYAHL-QMAPKHWLCIQE---------NDLVWATAAP----GWQKWVwspfLSVLGMGATAFVYNgRFHPETYLELLQN 259
Cdd:PRK13391 173 --KRPLpEQPPDTPLPLTAflqrlwgfrSDMVYLSPAPlyhsAPQRAV----MLVIRLGGTVIVME-HFDAEQYLALIEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 260 YQINVLCCTPTEYRMMAKLSHlEQ---YNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTEStLLIGFLKDTE- 335
Cdd:PRK13391 246 YGVTHTQLVPTMFSRMLKLPE-EVrdkYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEG-LGFTACDSEEw 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 336 -PRMGSMGKGIPGSfVTVIDDDGKEVGPNVKGNIavpldlpaLFKG-----YFKDEARTKAAST--GDYYVTGDQAHIDN 407
Cdd:PRK13391 324 lAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTI--------WFEGgrpfeYLNDPAKTAEARHpdGTWSTVGDIGYVDE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 408 DGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNE 487
Cdd:PRK13391 395 DGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPALAAELIAFCRQR 474
|
490 500 510
....*....|....*....|....*....|.
gi 1801842045 488 VAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK13391 475 LSRQKCPRSIDFEDELPRLPTGKLYKRLLRD 505
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
26-518 |
1.45e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 205.55 E-value: 1.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYKDnehenISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDL 105
Cdd:PRK08316 26 DKTALVFGD-----RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 106 QYRITHGEIDAVISFSSLTKEFENVKEYDQLKKFIVA------GHKEDWVSIEDEKEKVNDDLKGADTTRDDLAILSYTS 179
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSlvlggrEAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 180 GTTGNPKAVTHSHG---WGYAHLQMApkhwLCIQENDLVWAtAAPGW---QKWVW-SPFLSVlgmGATAFVYNGRfHPET 252
Cdd:PRK08316 181 GTESLPKGAMLTHRaliAEYVSCIVA----GDMSADDIPLH-ALPLYhcaQLDVFlGPYLYV---GATNVILDAP-DPEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 253 YLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQTEstllIGFL 331
Cdd:PRK08316 252 ILRTIEAERITSFFAPPTVWISLLRHPDFDTRDLSSLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTE----IAPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 332 ------KDTEPRMGSMGKgiPGSFV--TVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKAASTGDYYVTGDQA 403
Cdd:PRK08316 328 atvlgpEEHLRRPGSAGR--PVLNVetRVVDDDGNDVAPGEVGEIV--HRSPQLMLGYWDDPEKTAEAFRGGWFHSGDLG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 404 HIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVF 483
Cdd:PRK08316 404 VMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTED---ELIAH 480
|
490 500 510
....*....|....*....|....*....|....*
gi 1801842045 484 CKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK08316 481 CRARLAGFKVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
29-519 |
1.71e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 204.75 E-value: 1.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKDNEHenisVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYR 108
Cdd:PRK08276 3 VIMAPSGEV----VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 109 ITHGEIDAVIS---FSSLTKEFENVKEYDQLKKFIVAGHKEDWVSIEDEKEKVNDDLKGADTTRDDLAilsYTSGTTGNP 185
Cdd:PRK08276 79 VDDSGAKVLIVsaaLADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGADML---YSSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 186 KAV----THSHGWGYAHLQMA-PKHWLCIQENDLVWATA-----APGwqkwVWSpfLSVLGMGATAfVYNGRFHPETYLE 255
Cdd:PRK08276 156 KGIkrplPGLDPDEAPGMMLAlLGFGMYGGPDSVYLSPAplyhtAPL----RFG--MSALALGGTV-VVMEKFDAEEALA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 256 LLQNYQINVLCCTPTEYRMMAKLSH--LEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTEStllIGF-LK 332
Cdd:PRK08276 229 LIERYRVTHSQLVPTMFVRMLKLPEevRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEG---GGVtVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 333 DTE---PRMGSMGKGIPGSfVTVIDDDGKEVGPNVKGNIAVPLDLPAlFKgYFKDEARTKAASTGDYYVT-GDQAHIDND 408
Cdd:PRK08276 306 TSEdwlAHPGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYP-FE-YHNDPEKTAAARNPHGWVTvGDVGYLDED 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 409 GYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEV 488
Cdd:PRK08276 383 GYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDALAAELIAWLRGRL 462
|
490 500 510
....*....|....*....|....*....|.
gi 1801842045 489 APYKYPRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:PRK08276 463 AHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
41-518 |
6.93e-59 |
|
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: 200.65 E-value: 6.93e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPssemlrtkdLQYRITHGEIdavisf 120
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVL---------LNTRLTPNEL------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 ssltkefenvkeydqlkkfivaghkedwvsiedekekvNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHlQ 200
Cdd:cd05912 66 --------------------------------------AFQLKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWS-A 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 201 MAPKHWLCIQENDlVWATAAPGWQKWVWSPFLSVLGMGATAFVYNgRFHPETYLELLQNYQINVLCCTPTEY-RMMAKLS 279
Cdd:cd05912 107 IGSALNLGLTEDD-NWLCALPLFHISGLSILMRSVIYGMTVYLVD-KFDAEQVLHLINSGKVTIISVVPTMLqRLLEILG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 280 HLEQYNLEYLhsaVSAGEPLNREVVEQFKRHfNITVRDGYGQTESTLLIGFLK--DTEPRMGSMGKGIPGSFVTVIDDDG 357
Cdd:cd05912 185 EGYPNNLRCI---LLGGGPAPKPLLEQCKEK-GIPVYQSYGMTETCSQIVTLSpeDALNKIGSAGKPLFPVELKIEDDGQ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 358 KEVGPN---VKGniavpldlPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVE 434
Cdd:cd05912 261 PPYEVGeilLKG--------PNVTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 435 DALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAsdeliQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRV 514
Cdd:cd05912 333 EVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISE-----EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRH 407
|
....
gi 1801842045 515 ELRD 518
Cdd:cd05912 408 ELKQ 411
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
39-518 |
1.61e-58 |
|
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: 201.77 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 39 NISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVI 118
Cdd:cd05926 12 TPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 119 -SFSSLTKEFENVKEYD--------QLKKFIVAGHKEDwVSIEDEKEKVNDDLKGADttRDDLAILSYTSGTTGNPKAVT 189
Cdd:cd05926 92 tPKGELGPASRAASKLGlailelalDVGVLIRAPSAES-LSNLLADKKNAKSEGVPL--PDDLALILHTSGTTGRPKGVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 190 HSHGwgyaHLQMAPKHW---LCIQENDLVWATAapgwqkwvwsPF----------LSVLGMGATAfVYNGRFHPETYLEL 256
Cdd:cd05926 169 LTHR----NLAASATNItntYKLTPDDRTLVVM----------PLfhvhglvaslLSTLAAGGSV-VLPPRFSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 257 LQNYQINVLCCTPTEYRMMAKlSHLEQYNLEY--LHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGF--LK 332
Cdd:cd05926 234 VRDYNATWYTAVPTIHQILLN-RPEPNPESPPpkLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMTSnpLP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 333 DTEPRMGSMGKGIpGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDGYF 411
Cdd:cd05926 313 PGPRKPGSVGKPV-GVEVRILDEDGEILPPGVVGEIC--LRGPNVTRGYLNNPEANAEAAFKDgWFRTGDLGYLDADGYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 412 WFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPY 491
Cdd:cd05926 390 FLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEE---ELRAFCRKHLAAF 466
|
490 500
....*....|....*....|....*..
gi 1801842045 492 KYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd05926 467 KVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
18-518 |
5.20e-56 |
|
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: 196.21 E-value: 5.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 18 IEKYASEDHKKAIIykdNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSS 97
Cdd:cd17642 24 MKRYASVPGTIAFT---DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 98 EMLRTKDLQYRIthGEIDAVISFSS---LTKEFENVKEYDQLKKFIVAGHKEDWVSI-EDEKEKVNDDLKGADTTR---- 169
Cdd:cd17642 101 DIYNERELDHSL--NISKPTIVFCSkkgLQKVLNVQKKLKIIKTIIILDSKEDYKGYqCLYTFITQNLPPGFNEYDfkpp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 -----DDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMapkhwlciQENDLVWATAAPGWQKWVWSPFLSVLGMGATA--- 241
Cdd:cd17642 179 sfdrdEQVALIMNSSGSTGLPKGVQLTHKNIVARFSH--------ARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLgyl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 242 -----FVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNIT-V 315
Cdd:cd17642 251 icgfrVVLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgI 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 316 RDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVID-DDGKEVGPNVKGNIAVPLDLpaLFKGYFKDEARTKAASTG 394
Cdd:cd17642 331 RQGYGLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPM--IMKGYVNNPEATKALIDK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 395 DYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAS 473
Cdd:cd17642 409 DGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKTMT 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1801842045 474 DeliQELQVFCKNEVAPYKYPR-AIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd17642 489 E---KEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
26-518 |
7.67e-56 |
|
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: 193.28 E-value: 7.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYKDNEHenisvSYKELISNANKVGNVFLNHG-LKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKD 104
Cdd:cd05941 1 DRIAIVDDGDSI-----TYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 105 LQYRITHGEIDAVIsfssltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadttrdDLAILSYTSGTTGN 184
Cdd:cd05941 76 LEYVITDSEPSLVL----------------------------------------------------DPALILYTSGTTGR 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 185 PKAVTHSHGWGYAHLQMapkhwlciqendLVwataapgwQKWVWSP---FLSVL------GM----------GATaFVYN 245
Cdd:cd05941 104 PKGVVLTHANLAANVRA------------LV--------DAWRWTEddvLLHVLplhhvhGLvnallcplfaGAS-VEFL 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 246 GRFHPETYLELLQNYQINVLCCTPTEYrmmAKLshLEQYNLEYLHSA-------------VSAGEPLNREVVEQFKRHFN 312
Cdd:cd05941 163 PKFDPKEVAISRLMPSITVFMGVPTIY---TRL--LQYYEAHFTDPQfaraaaaerlrlmVSGSAALPVPTLEEWEAITG 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 313 ITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPN-------VKGniavpldlPALFKGYFKDE 385
Cdd:cd05941 238 HTLLERYGMTEIGMALSNPLDGERRPGTVGMPLPGVQARIVDEETGEPLPRgevgeiqVRG--------PSVFKEYWNKP 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 386 ARTKAASTGD-YYVTGDQAHIDNDGYFWFEGR-RDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAF 463
Cdd:cd05941 310 EATKEEFTDDgWFKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAV 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1801842045 464 IILQDDYEASDEliQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd05941 390 VVLRAGAAALSL--EELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
36-516 |
1.07e-55 |
|
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: 193.13 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 36 EHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRaivTYELYIAAL---KLGIAIVPssemLrtkDLQY---RI 109
Cdd:cd05930 7 VDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLER---SLEMVVAILavlKAGAAYVP----L---DPSYpaeRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 110 TH--GEIDAvisfssltkefenvkeydqlkKFIVaghkedwvsiedekekvnddlkgadTTRDDLAILSYTSGTTGNPKA 187
Cdd:cd05930 77 AYilEDSGA---------------------KLVL-------------------------TDPDDLAYVIYTSGSTGKPKG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 188 VTHSHGwGYAHLQMAPKHWLCIQENDLVWATAAPG-----WQkwVWSPFLSvlgmGATAFV--YNGRFHPETYLELLQNY 260
Cdd:cd05930 111 VMVEHR-GLVNLLLWMQEAYPLTPGDRVLQFTSFSfdvsvWE--IFGALLA----GATLVVlpEEVRKDPEALADLLAEE 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 261 QINVLCCTPTEYRMMakLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQTESTLLIGFLKDTEPRMG 339
Cdd:cd05930 184 GITVLHLTPSLLRLL--LQELELAALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYYRVPPDDEE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 340 SM----GKGIPGSFVTVIDDDGKEVGPNVKGNIAV--PldlpALFKGYFKDEARTKA-------ASTGDYYVTGDQAHID 406
Cdd:cd05930 262 DGrvpiGRPIPNTRVYVLDENLRPVPPGVPGELYIggA----GLARGYLNRPELTAErfvpnpfGPGERMYRTGDLVRWL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 407 NDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQElqvFCKN 486
Cdd:cd05930 338 PDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRA---HLAE 414
|
490 500 510
....*....|....*....|....*....|
gi 1801842045 487 EVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd05930 415 RLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
170-517 |
4.21e-55 |
|
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: 189.03 E-value: 4.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSH----GWGYA---HLQMAPKHWLCIQeNDLVWAtaapgwqkwvwspFLSVLGM----- 237
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHhnivNNGYFigeRLGLTEQDRLCIP-VPLFHC-------------FGSVLGVlaclt 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 238 -GATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYrmMAKLSHLE--QYNLEYLHSAVSAGEPLNREVVEQFKRHFNIT 314
Cdd:cd05917 68 hGATMVFPSPSFDPLAVLEAIEKEKCTALHGVPTMF--IAELEHPDfdKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 315 -VRDGYGQTESTLLI--GFLKDT-EPRMGSMGKGIPGSFVTVIDDDGKEV-GPNVKGNIAVPLDLpaLFKGYFKDEARTK 389
Cdd:cd05917 146 dVTIAYGMTETSPVStqTRTDDSiEKRVNTVGRIMPHTEAKIVDPEGGIVpPVGVPGELCIRGYS--VMKGYWNDPEKTA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 390 AASTGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQD 468
Cdd:cd05917 224 EAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKE 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1801842045 469 DYEASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05917 304 GAELTEE---DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
27-520 |
7.23e-55 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 191.71 E-value: 7.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYKDNeheniSVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQ 106
Cdd:PRK03640 18 RTAIEFEEK-----KVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 107 YRITHGEIDAVISFSSLTKEFEnvkeydqlkkfivaGHKEDWVSIEDEKEKVNDDLKgADTTRDDLAILSYTSGTTGNPK 186
Cdd:PRK03640 93 WQLDDAEVKCLITDDDFEAKLI--------------PGISVKFAELMNGPKEEAEIQ-EEFDLDEVATIMYTSGTTGKPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 187 AVTHSHGwgyahlqmapKHW---------LCIQENDlVWATAAP-----GwqkwvwspfLSVL------GMgaTAFVYNg 246
Cdd:PRK03640 158 GVIQTYG----------NHWwsavgsalnLGLTEDD-CWLAAVPifhisG---------LSILmrsviyGM--RVVLVE- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 247 RFHPETYLELLQNYQINVLCCTPTeyrMMAKLshLEQYNLEYLHSAVSA----GEPLNREVVEQFKRHfNITVRDGYGQT 322
Cdd:PRK03640 215 KFDAEKINKLLQTGGVTIISVVST---MLQRL--LERLGEGTYPSSFRCmllgGGPAPKPLLEQCKEK-GIPVYQSYGMT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 323 ESTLLIGFL--KDTEPRMGSMGKGIPGSFVTvIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTG 400
Cdd:PRK03640 289 ETASQIVTLspEDALTKLGSAGKPLFPCELK-IEKDGVVVPPFEEGEIVV--KGPNVTKGYLNREDATRETFQDGWFKTG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 401 DQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILqdDYEASDEliqEL 480
Cdd:PRK03640 366 DIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEE---EL 440
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1801842045 481 QVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAE 520
Cdd:PRK03640 441 RHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLV 480
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
41-516 |
1.67e-54 |
|
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: 191.29 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGiAIV----PSSemlrtkdlqyriTHGEI-- 114
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG-AVVttanPLS------------TPAEIak 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 115 -----DAVISFSSlTKEFENVKEYDQlkKFIVAGHKED--WVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKA 187
Cdd:cd05904 99 qvkdsGAKLAFTT-AELAEKLASLAL--PVVLLDSAEFdsLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 188 VTHSHGWGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPF-LSVLGMGATAFVYnGRFHPETYLELLQNYQINVLC 266
Cdd:cd05904 176 VMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFaLGLLRLGATVVVM-PRFDLEELLAAIERYKVTHLP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 267 CTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQTEST--LLIGFLKDTEP-RMGSMG 342
Cdd:cd05904 255 VVPPIVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYGMTESTgvVAMCFAPEKDRaKYGSVG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 343 KGIPGSFVTVID-DDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDI 420
Cdd:cd05904 335 RLVPNVEAKIVDpETGESLPPNQTGELWI--RGPSIMKGYLNNPEATAATIDKEGWLhTGDLCYIDEDGYLFIVDRLKEL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 421 IISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQElqvFCKNEVAPYKYPRAIEFV 500
Cdd:cd05904 413 IKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMD---FVAKQVAPYKKVRKVAFV 489
|
490
....*....|....*.
gi 1801842045 501 ENLPKTNSGKIRRVEL 516
Cdd:cd05904 490 DAIPKSPSGKILRKEL 505
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
27-518 |
1.74e-54 |
|
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: 190.97 E-value: 1.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYKDnehenISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQ 106
Cdd:cd12118 20 RTSIVYGD-----RRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 107 YRITHGEIDAVIsfssLTKEFEnvkeYDQlkkFIVAGHKE-DWVSIEDEkekvnddlkgadttrDDLAILSYTSGTTGNP 185
Cdd:cd12118 95 FILRHSEAKVLF----VDREFE----YED---LLAEGDPDfEWIPPADE---------------WDPIALNYTSGTTGRP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 186 KAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATA---APGWQkWVWSPFlsvlGMGATAfVYNGRFHPETYLELLQNYQI 262
Cdd:cd12118 149 KGVVYHHRGAYLNALANILEWEMKQHPVYLWTLPmfhCNGWC-FPWTVA----AVGGTN-VCLRKVDAKAIYDLIEKHKV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 263 NVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRhFNITVRDGYGQTEST--LLIGFLK---DTEPR 337
Cdd:cd12118 223 THFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKMEE-LGFDVTHVYGLTETYgpATVCAWKpewDELPT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 338 ------MGSMGKGIPGSF-VTVIDD--------DGKEVGPNV-KGNIavpldlpaLFKGYFKDEARTKAASTGDYYVTGD 401
Cdd:cd12118 302 eerarlKARQGVRYVGLEeVDVLDPetmkpvprDGKTIGEIVfRGNI--------VMKGYLKNPEATAEAFRGGWFHSGD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 402 QAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQ 481
Cdd:cd12118 374 LAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEE---EII 450
|
490 500 510
....*....|....*....|....*....|....*..
gi 1801842045 482 VFCKNEVAPYKYPRAIEFVEnLPKTNSGKIRRVELRD 518
Cdd:cd12118 451 AFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVLRD 486
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
41-517 |
1.85e-54 |
|
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: 189.51 E-value: 1.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVIsf 120
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 ssLTKEFenvkeydqlKKFivaghkedwvSIEDEKekvnddlkgadttrDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQ 200
Cdd:cd05903 79 --VPERF---------RQF----------DPAAMP--------------DAVALLLFTSGTTGEPKGVMHSHNTLSASIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 201 MAPKHWLcIQENDLVWaTAAP-----GWQKWVWSPFLsvlgMGATAfVYNGRFHPETYLELLQNYQIN-VLCCTP----- 269
Cdd:cd05903 124 QYAERLG-LGPGDVFL-VASPmahqtGFVYGFTLPLL----LGAPV-VLQDIWDPDKALALMREHGVTfMMGATPfltdl 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 270 --TEYRMMAKLSHLEQYNLeylhsavsAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEP--RMGSMGKGI 345
Cdd:cd05903 197 lnAVEEAGEPLSRLRTFVC--------GGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEdrRLYTDGRPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 346 PGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSG 425
Cdd:cd05903 269 PGVEIKVVDDTGATLAPGVEGELLS--RGPSVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 426 YTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQElqVFCKNEVAPYKYPRAIEFVENLPK 505
Cdd:cd05903 347 ENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVA--YLDRQGVAKQYWPERLVHVDDLPR 424
|
490
....*....|..
gi 1801842045 506 TNSGKIRRVELR 517
Cdd:cd05903 425 TPSGKVQKFRLR 436
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
42-529 |
2.91e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 192.17 E-value: 2.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFS 121
Cdd:PRK06710 50 ITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 122 SLTKEFENVKEYDQLKKFIVA-----------------GHKED--------------WVSIEDEKEKVNDDLKGADttrD 170
Cdd:PRK06710 130 LVFPRVTNVQSATKIEHVIVTriadflpfpknllypfvQKKQSnlvvkvsesetihlWNSVEKEVNTGVEVPCDPE---N 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 171 DLAILSYTSGTTGNPKAVTHSHGWGYAHLQMApKHWL--CIQENDLVWATAapgwqkwvwsPFLSVLGMGAT-------- 240
Cdd:PRK06710 207 DLALLQYTGGTTGFPKGVMLTHKNLVSNTLMG-VQWLynCKEGEEVVLGVL----------PFFHVYGMTAVmnlsimqg 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 241 -AFVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGY 319
Cdd:PRK06710 276 yKMVLIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 320 GQTESTLLI--GFLkdTEPRM-GSMGKGIPGSFVTVID-DDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGD 395
Cdd:PRK06710 356 GLTESSPVThsNFL--WEKRVpGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVV--KGPQIMKGYWNKPEETAAVLQDG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 396 YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDE 475
Cdd:PRK06710 432 WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEE 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1801842045 476 liqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEIKKYQQQNS 529
Cdd:PRK06710 512 ---ELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEKRKNEDEQT 562
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
20-518 |
4.03e-52 |
|
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: 185.14 E-value: 4.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 20 KYASEDH-KKAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSE 98
Cdd:cd12119 3 EHAARLHgDREIVSRTHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 99 MLRTKDLQYRITHGEIDAVISFSSLTKEFENVK-EYDQLKKFIVAGHKED--------WVSIEDEKEKVNDDLKGADTTR 169
Cdd:cd12119 83 RLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIApRLPTVEHVVVMTDDAAmpepagvgVLAYEELLAAESPEYDWPDFDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHGWGYAH-LQMAPKHWLCIQENDLVWAtAAPGWQKWVW-SPFLSVlgMGATAFVYNGR 247
Cdd:cd12119 163 NTAAAICYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVVLP-VVPMFHVNAWgLPYAAA--MVGAKLVLPGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 248 F-HPETYLELLQNYQINVLCCTPTEYRMMakLSHLE--QYNLEYLHSAVSAGEPLNREVVEQFKRHFnITVRDGYGQTE- 323
Cdd:cd12119 240 YlDPASLAELIEREGVTFAAGVPTVWQGL--LDHLEanGRDLSSLRRVVIGGSAVPRSLIEAFEERG-VRVIHAWGMTEt 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 324 STLL-IGFLKDTEPRMG---------SMGKGIPGSFVTVIDDDGKEV--GPNVKGNIAVplDLPALFKGYFKDEARTKAA 391
Cdd:cd12119 317 SPLGtVARPPSEHSNLSedeqlalraKQGRPVPGVELRIVDDDGRELpwDGKAVGELQV--RGPWVTKSYYKNDEESEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 392 STGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYE 471
Cdd:cd12119 395 TEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGAT 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1801842045 472 ASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd12119 475 VTAE---ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
12-523 |
6.49e-52 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 184.29 E-value: 6.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 12 YNIVSEIEKYASEDHKKAIIYKDNEheniSVSYKELISNANKVGNVFLNH-GLKKGDKVLIMMPRAIVTYELYIAALKLG 90
Cdd:PRK06839 2 QGIAYWIEKRAYLHPDRIAIITEEE----EMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 91 IAIVPssemlrtkdLQYRITHGEIDAVISFSSLT-----KEFENVKEYDQLKKFIvaghkEDWVSIEDEKEKVNDDLKGA 165
Cdd:PRK06839 78 CIAVP---------LNIRLTENELIFQLKDSGTTvlfveKTFQNMALSMQKVSYV-----QRVISITSLKEIEDRKIDNF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 166 DT-TRDDLAILSYTSGTTGNPK-AVTHSHG--WGYAHLQMA---PKHWLCIqendlvwataapgwqkwVWSPFLSVLGMG 238
Cdd:PRK06839 144 VEkNESASFIICYTSGTTGKPKgAVLTQENmfWNALNNTFAidlTMHDRSI-----------------VLLPLFHIGGIG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 239 ATAF---------VYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKR 309
Cdd:PRK06839 207 LFAFptlfaggviIVPRKFEPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFID 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 310 HfNITVRDGYGQTES--TLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEAR 387
Cdd:PRK06839 287 R-GFLFGQGFGMTETspTVFMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLI--RGPNVMKEYWNRPDA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 388 TKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQ 467
Cdd:PRK06839 364 TEETIQDGWLCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKK 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1801842045 468 DDYEASDELIQElqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELrdAEIKK 523
Cdd:PRK06839 444 SSSVLIEKDVIE---HCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQL--VNQLK 494
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
50-517 |
1.15e-51 |
|
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: 182.64 E-value: 1.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 50 NANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYI----AALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSSLTk 125
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFavayAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 126 efenvkeyDQLKKFIVAGHKEDWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQmAPKH 205
Cdd:cd05922 81 --------DRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANAR-SIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 206 WLCIQENDLVwATAAPGWQKWVWSPFLSVLGMGATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLShLEQYN 285
Cdd:cd05922 152 YLGITADDRA-LTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTRLG-FDPAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 286 LEYLHSAVSAGEPLNREVVEQFKRHFNIT-VRDGYGQTESTLLIGFLKDTE--PRMGSMGKGIPGSFVTVIDDDGKEVGP 362
Cdd:cd05922 230 LPSLRYLTQAGGRLPQETIARLRELLPGAqVYVMYGQTEATRRMTYLPPERilEKPGSIGLAIPGGEFEILDDDGTPTPP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 363 NVKGNIAVplDLPALFKGYFKDEA-RTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHA 441
Cdd:cd05922 310 GEPGEIVH--RGPNVMKGYWNDPPyRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801842045 442 AVKECAVVASPhDIRGNIVKAFIILQDDYEASDeliqeLQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05922 388 LIIEAAAVGLP-DPLGEKLALFVTAPDKIDPKD-----VLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
29-510 |
6.68e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 182.39 E-value: 6.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKDNEhenisVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVpssemlrtkDLQYR 108
Cdd:PRK07798 21 ALVCGDRR-----LTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPV---------NVNYR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 109 ITHGEID---------AVISFSSLTKEFENVKeyDQLKKFIVaghkedWVSIEDEK--------EKVNDDLKGADTTR-- 169
Cdd:PRK07798 87 YVEDELRyllddsdavALVYEREFAPRVAEVL--PRLPKLRT------LVVVEDGSgndllpgaVDYEDALAAGSPERdf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 -----DDLAILsYTSGTTGNPKAVTHSHG--W-----GYAHLQMAPKHwlciQENDLVWATAAPGWQKWV---------- 227
Cdd:PRK07798 159 gerspDDLYLL-YTGGTTGMPKGVMWRQEdiFrvllgGRDFATGEPIE----DEEELAKRAAAGPGMRRFpapplmhgag 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 228 -WSPFLSVLGMGATAFVYNGRFHPETYLELLQNYQINVLCCT------PteyrMMAKLSHLEQYNLEYLHSAVSAGEPLN 300
Cdd:PRK07798 234 qWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP----LLDALEARGPYDLSSLFAIASGGALFS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 301 REVVEQFKRHF-NITVRDGYGQTEStlliGFLKDTEPRMGSMGKGIP----GSFVTVIDDDGKEVGP--NVKGNIA---- 369
Cdd:PRK07798 310 PSVKEALLELLpNVVLTDSIGSSET----GFGGSGTVAKGAVHTGGPrftiGPRTVVLDEDGNPVEPgsGEIGWIArrgh 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 370 VPLdlpalfkGYFKDEARTkaAST-----GD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAV 443
Cdd:PRK07798 386 IPL-------GYYKDPEKT--AETfptidGVrYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801842045 444 KECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGK 510
Cdd:PRK07798 457 ADALVVGVPDERWGQEVVAVVQLREGARPDLA---ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
14-517 |
1.66e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 180.95 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 14 IVSEIEKYASedhKKAIIYKDnehenISVSYKELISNANKVGNVFLNHGLKKGDKV-LIMMPRAIVTYELyIAALKLGIA 92
Cdd:PRK06188 18 LVSALKRYPD---RPALVLGD-----TRLTYGQLADRISRYIQAFEALGLGTGDAVaLLSLNRPEVLMAI-GAAQLAGLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 93 IVPSSEMLRTKDLQYRITHGEIDAVISFSS--LTKEFENVKEYDQLKKFIVAGHKEDWVSIEDEKEKVNDDLKGADTTRD 170
Cdd:PRK06188 89 RTALHPLGSLDDHAYVLEDAGISTLIVDPApfVERALALLARVPSLKHVLTLGPVPDGVDLLAAAAKFGPAPLVAAALPP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 171 DLAILSYTSGTTGNPKAVTHSH--GWGYAHLQMAPKHWlciqENDLVWATAAP-----GwqkwvwSPFLSVLGMGATAFV 243
Cdd:PRK06188 169 DIAGLAYTGGTTGKPKGVMGTHrsIATMAQIQLAEWEW----PADPRFLMCTPlshagG------AFFLPTLLRGGTVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 244 YNGrFHPETYLELLQNYQINVLCCTPTE-YRMM-------AKLSHLEQynLEYLHSAVSAGEPlnREVVEQFKRHFNITv 315
Cdd:PRK06188 239 LAK-FDPAEVLRAIEEQRITATFLVPTMiYALLdhpdlrtRDLSSLET--VYYGASPMSPVRL--AEAIERFGPIFAQY- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 316 rdgYGQTESTLLIGFL--KDTEP----RMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAV--PLdlpaLFKGYFKDEAR 387
Cdd:PRK06188 313 ---YGQTEAPMVITYLrkRDHDPddpkRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVrgPL----VMDGYWNRPEE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 388 TKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQ 467
Cdd:PRK06188 386 TAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLR 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1801842045 468 DDyEASDEliQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK06188 466 PG-AAVDA--AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
43-519 |
1.71e-49 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 178.80 E-value: 1.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSS 122
Cdd:PRK06155 48 TYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 LTKEFENVKEYDQLKKFI------VAGHKE---DWVSIEDEKEKVN-DDLKGADTtrddLAILsYTSGTTGNPKAVTHSH 192
Cdd:PRK06155 128 LLAALEAADPGDLPLPAVwlldapASVSVPagwSTAPLPPLDAPAPaAAVQPGDT----AAIL-YTSGTTGPSKGVCCPH 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 193 G----WGYahlQMApkHWLCIQENDlVWATAAPGWQKWVWSPFLSVLGMGATaFVYNGRFHPETYLELLQNYQinvlcCT 268
Cdd:PRK06155 203 AqfywWGR---NSA--EDLEIGADD-VLYTTLPLFHTNALNAFFQALLAGAT-YVLEPRFSASGFWPAVRRHG-----AT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 269 PTeYRMMAKLSHL------EQYNLEYLHSAVSAGEPLnrEVVEQFKRHFNITVRDGYGQTESTLLIGFLKDtEPRMGSMG 342
Cdd:PRK06155 271 VT-YLLGAMVSILlsqparESDRAHRVRVALGPGVPA--ALHAAFRERFGVDLLDGYGSTETNFVIAVTHG-SQRPGSMG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 343 KGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLP-ALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDII 421
Cdd:PRK06155 347 RLAPGFEARVVDEHDQELPDGEPGELLLRADEPfAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 422 ISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDyEASDEliQELQVFCKNEVAPYKYPRAIEFVE 501
Cdd:PRK06155 427 RRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEP--VALVRHCEPRLAYFAVPRYVEFVA 503
|
490
....*....|....*...
gi 1801842045 502 NLPKTNSGKIRRVELRDA 519
Cdd:PRK06155 504 ALPKTENGKVQKFVLREQ 521
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
62-523 |
5.45e-49 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 177.55 E-value: 5.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 62 GLKKGDKVLIMMPRaIVTYElyIA---ALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSSLTKEFENVKEY----- 133
Cdd:PRK08974 70 GLKKGDRVALMMPN-LLQYP--IAlfgILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKtpvkh 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 134 -------DQL---------------KKFIVAGHKEDWVSIED--EKEKVNDDLKgADTTRDDLAILSYTSGTTGNPKAVT 189
Cdd:PRK08974 147 viltrmgDQLstakgtlvnfvvkyiKRLVPKYHLPDAISFRSalHKGRRMQYVK-PELVPEDLAFLQYTGGTTGVAKGAM 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 190 HSHGWGYAHLQMApkhwlciqendlvwataapgwqKWVWSPFLSV------------------------LGMGATA-FVY 244
Cdd:PRK08974 226 LTHRNMLANLEQA----------------------KAAYGPLLHPgkelvvtalplyhifaltvncllfIELGGQNlLIT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 245 NGRFHPETYLELlQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTE- 323
Cdd:PRK08974 284 NPRDIPGFVKEL-KKYPFTAITGVNTLFNALLNNEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEc 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 324 STLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQA 403
Cdd:PRK08974 363 SPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWV--KGPQVMLGYWQRPEATDEVIKDGWLATGDIA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 404 HIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQelqvF 483
Cdd:PRK08974 441 VMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELIT----H 516
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1801842045 484 CKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEIKK 523
Cdd:PRK08974 517 CRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
26-531 |
7.81e-49 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 176.86 E-value: 7.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIiyKDNEheNISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPR----AIVtyelYIAALKLGIAIVPSSEMLR 101
Cdd:PRK06087 38 DKIAV--VDNH--GASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGwcefTII----YLACLKVGAVSVPLLPSWR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 102 TKDLQYRIT------------HGEIDAVISFSSLTKEFENVKE---YDQLKKfivaGHKEDWVS-IEDEKEKVNDDLkga 165
Cdd:PRK06087 110 EAELVWVLNkcqakmffaptlFKQTRPVDLILPLQNQLPQLQQivgVDKLAP----ATSSLSLSqIIADYEPLTTAI--- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 166 DTTRDDLAILSYTSGTTGNPKAVTHSHGwgyaHLQMAPKHW---LCIQENDLVWATA----APGWQKWVWSPFLsvlgMG 238
Cdd:PRK06087 183 TTHGDELAAVLFTSGTEGLPKGVMLTHN----NILASERAYcarLNLTWQDVFMMPAplghATGFLHGVTAPFL----IG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 239 ATAfVYNGRFHPETYLELLQNYQIN-VLCCTPTEYRMmakLSHLEQ--YNLEYLHSAVSAGEPLNREVVEQFKRHfNITV 315
Cdd:PRK06087 255 ARS-VLLDIFTPDACLALLEQQRCTcMLGATPFIYDL---LNLLEKqpADLSALRFFLCGGTTIPKKVARECQQR-GIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 316 RDGYGQTEST--LLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAAST 393
Cdd:PRK06087 330 LSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEAS--RGPNVFMGYLDEPELTARALD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 394 GD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDyEA 472
Cdd:PRK06087 408 EEgWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP-HH 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1801842045 473 SDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEIKKYQQQNSSH 531
Cdd:PRK06087 487 SLTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRLTQDVCEE 545
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
175-518 |
9.17e-49 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 175.26 E-value: 9.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 175 LSYTSGTTGNPKAV--THSHGWGYAHLQMAPKhWLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATAFVYNgRFHPET 252
Cdd:cd05929 130 MLYSGGTTGRPKGIkrGLPGGPPDNDTLMAAA-LGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME-KFDPEE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 253 YLELLQNYQINVLCCTPTEYRMMAKLSHLEQ--YNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTE---STLL 327
Cdd:cd05929 208 FLRLIERYRVTFAQFVPTMFVRLLKLPEAVRnaYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEgqgLTII 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 328 IGFLKDTEPrmGSMGKGIPGSfVTVIDDDGKEVGPNVKGNIAVpldLPALFKGYFKDEARTKAASTGDYYVT-GDQAHID 406
Cdd:cd05929 288 NGEEWLTHP--GSVGRAVLGK-VHILDEDGNEVPPGEIGEVYF---ANGPGFEYTNDPEKTAAARNEGGWSTlGDVGYLD 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 407 NDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKN 486
Cdd:cd05929 362 EDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALAEELIAFLRD 441
|
330 340 350
....*....|....*....|....*....|..
gi 1801842045 487 EVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd05929 442 RLSRYKCPRSIEFVAELPRDDTGKLYRRLLRD 473
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
27-521 |
1.07e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 176.89 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYKdneHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQ 106
Cdd:PRK12583 34 REALVVR---HQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 107 YRITHGEIDAVI---SFSS---------LTKEFENVK-------EYDQLKKFIV-----AGHKEDWVSIEDEKEKVND-- 160
Cdd:PRK12583 111 YALGQSGVRWVIcadAFKTsdyhamlqeLLPGLAEGQpgalaceRLPELRGVVSlapapPPGFLAWHELQARGETVSRea 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 161 -DLKGADTTRDDLAILSYTSGTTGNPKAVTHSH------GWGYAH-LQMAPKHWLCIQendlvwataapgwqkwvwSPFL 232
Cdd:PRK12583 191 lAERQASLDRDDPINIQYTSGTTGFPKGATLSHhnilnnGYFVAEsLGLTEHDRLCVP------------------VPLY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 233 SVLGM----------GATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYrmMAKLSHLE--QYNLEYLHSAVSAGEPLN 300
Cdd:PRK12583 253 HCFGMvlanlgcmtvGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMF--IAELDHPQrgNFDLSSLRTGIMAGAPCP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 301 REVVEQFKRHFNIT-VRDGYGQTES---TLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLpa 376
Cdd:PRK12583 331 IEVMRRVMDEMHMAeVQIAYGMTETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYS-- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 377 LFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDI 455
Cdd:PRK12583 409 VMKGYWNNPEATAESIDEDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1801842045 456 RGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEI 521
Cdd:PRK12583 489 YGEEIVAWVRLHPGHAASEE---ELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISI 551
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
25-517 |
5.02e-48 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 174.10 E-value: 5.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 25 DHKKAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMM---PRAIVTYelyIAALKLGIAIVPSSEMLR 101
Cdd:PRK08008 21 GHKTALIFESSGGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLdncPEFIFCW---FGLAKIGAIMVPINARLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 102 TKDLQYRITHGEIDAVI---SFSSLTKEFENVKEYdQLKKFIVAGHKEDW----VSIEDEKEKVNDDLKGADT-TRDDLA 173
Cdd:PRK08008 98 REESAWILQNSQASLLVtsaQFYPMYRQIQQEDAT-PLRHICLTRVALPAddgvSSFTQLKAQQPATLCYAPPlSTDDTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 174 ILSYTSGTTGNPKAVTHSHgwgyAHLQMAPKH--WLCIQENDLVWATAAPGW----QKWVWSPFLSVlgmGATaFVYNGR 247
Cdd:PRK08008 177 EILFTSGTTSRPKGVVITH----YNLRFAGYYsaWQCALRDDDVYLTVMPAFhidcQCTAAMAAFSA---GAT-FVLLEK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 248 FHPETYLELLQNYQINVLCCTPTEYR--MMAKLSHLEQYN-----LEYLHsaVSAGEPlnrevvEQFKRHFNITVRDGYG 320
Cdd:PRK08008 249 YSARAFWGQVCKYRATITECIPMMIRtlMVQPPSANDRQHclrevMFYLN--LSDQEK------DAFEERFGVRLLTSYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 321 QTEStlLIGFLKDT---EPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPlDLPA--LFKGYFKDEARTKAASTGD 395
Cdd:PRK08008 321 MTET--IVGIIGDRpgdKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIK-GVPGktIFKEYYLDPKATAKVLEAD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 396 YYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASD 474
Cdd:PRK08008 398 GWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSE 477
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1801842045 475 EliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK08008 478 E---EFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
41-517 |
8.43e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 174.20 E-value: 8.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPssemlrtkdLQYRITHGEI------ 114
Cdd:PRK07786 42 TTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVP---------VNFRLTPPEIaflvsd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 115 ---DAVISFSSLTKEFENVKEYD-QLKKFIVAG--HKEDWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAV 188
Cdd:PRK07786 113 cgaHVVVTEAALAPVATAVRDIVpLLSTVVVAGgsSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGRPKGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 THSHgwgyahLQMAPKHWLCIQENDLVWATAApgwqKWVWSPFLSVLG---------MGATAFVYN-GRFHPETYLELLQ 258
Cdd:PRK07786 193 VLTH------ANLTGQAMTCLRTNGADINSDV----GFVGVPLFHIAGigsmlpgllLGAPTVIYPlGAFDPGQLLDVLE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 259 NYQINVLCCTPTEYRMM-----AKLSHLEQYNLEYlhSAVSAGEPLNREVVEQFKRHFNITVrdgYGQTE----STLLIG 329
Cdd:PRK07786 263 AEKVTGIFLVPAQWQAVcaeqqARPRDLALRVLSW--GAAPASDTLLRQMAATFPEAQILAA---FGQTEmspvTCMLLG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 330 flKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDG 409
Cdd:PRK07786 338 --EDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIV--YRAPTLMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 410 YFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDyeaSDEL-IQELQVFCKNEV 488
Cdd:PRK07786 414 YVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRND---DAALtLEDLAEFLTDRL 490
|
490 500
....*....|....*....|....*....
gi 1801842045 489 APYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK07786 491 ARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
27-517 |
7.37e-47 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 173.55 E-value: 7.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYKDNE-HENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIvtyELYIAALKLG-IAIVPSSEM--LRT 102
Cdd:PLN02654 105 KIAIYWEGNEpGFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLM---ELPIAMLACArIGAVHSVVFagFSA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 103 KDLQYRITHGEIDAVISFSSLTKEFENVKEYDQLKKFIVAGHKEDwVSI--------------EDEKEKVNDDLKGAD-- 166
Cdd:PLN02654 182 ESLAQRIVDCKPKVVITCNAVKRGPKTINLKDIVDAALDESAKNG-VSVgicltyenqlamkrEDTKWQEGRDVWWQDvv 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 167 ----TTRD-------DLAILSYTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATAAPGW---QKWV-WSPF 231
Cdd:PLN02654 261 pnypTKCEvewvdaeDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWitgHSYVtYGPM 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 232 LSvlgmGATAFVYNGR-FHPET--YLELLQNYQINVLCCTPTEYR--MMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQ 306
Cdd:PLN02654 341 LN----GATVLVFEGApNYPDSgrCWDIVDKYKVTIFYTAPTLVRslMRDGDEYVTRHSRKSLRVLGSVGEPINPSAWRW 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 307 FkrhFNIT------VRDGYGQTESTlliGFLKDTEP-----RMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLP 375
Cdd:PLN02654 417 F---FNVVgdsrcpISDTWWQTETG---GFMITPLPgawpqKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSWP 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 376 ALFKGYFKDEAR---TKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASP 452
Cdd:PLN02654 491 GAFRTLYGDHERyetTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIE 570
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801842045 453 HDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PLN02654 571 HEVKGQGIYAFVTLVEGVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
42-516 |
9.40e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 171.76 E-value: 9.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFS 121
Cdd:PRK06178 59 ITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 122 SLTKEFENVKEYDQLKKFIVAGHKE----------------------DWVSIEDEKEKVNDDLKGADTTRDDLAILSYTS 179
Cdd:PRK06178 139 QLAPVVEQVRAETSLRHVIVTSLADvlpaeptlplpdslraprlaaaGAIDLLPALRACTAPVPLPPPALDALAALNYTG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 180 GTTGNPKAVTHSHGwgyahlqmapkhwlciqenDLVWATAA------PGWQKWVWSPFLSV-------LGM------GAT 240
Cdd:PRK06178 219 GTTGMPKGCEHTQR-------------------DMVYTAAAayavavVGGEDSVFLSFLPEfwiagenFGLlfplfsGAT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 241 aFVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHS--AVSAGEPLNREVVEQFKRHFNITVRDG 318
Cdd:PRK06178 280 -LVLLARWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 319 -YGQTES----TLLIGFLKD-----TEPRMgsMGKGIPGSFVTVIDDDGKEVGP-NVKGNIAVplDLPALFKGYFKDEAR 387
Cdd:PRK06178 359 aWGMTEThtcdTFTAGFQDDdfdllSQPVF--VGLPVPGTEFKICDFETGELLPlGAEGEIVV--RTPSLLKGYWNKPEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 388 TKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQ 467
Cdd:PRK06178 435 TAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLK 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1801842045 468 DDYEASDEliqELQVFCKNEVAPYKYPRaIEFVENLPKTNSGKIRRVEL 516
Cdd:PRK06178 515 PGADLTAA---ALQAWCRENMAVYKVPE-IRIVDALPMTATGKVRKQDL 559
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
41-520 |
1.73e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 167.80 E-value: 1.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMM--PRAIVtYELYiAALKLGIAIVpsseMLRT-------KDLQYRitH 111
Cdd:PRK07788 74 TLTYAELDEQSNALARGLLALGVRAGDGVAVLArnHRGFV-LALY-AAGKVGARII----LLNTgfsgpqlAEVAAR--E 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 112 GeIDAVISFSSLTKEFENVK-EYDQLKKFIVAGHKEDWVSIEDEkekVNDDLKGADTT--------RDDLAILsyTSGTT 182
Cdd:PRK07788 146 G-VKALVYDDEFTDLLSALPpDLGRLRAWGGNPDDDEPSGSTDE---TLDDLIAGSSTaplpkppkPGGIVIL--TSGTT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 183 GNPKAVTHSHGWGYAHL-QMAPKHWLCIQENDLVwatAAPGWQKWVWSPFLSVLGMGATaFVYNGRFHPETYLELLQNYQ 261
Cdd:PRK07788 220 GTPKGAPRPEPSPLAPLaGLLSRVPFRAGETTLL---PAPMFHATGWAHLTLAMALGST-VVLRRRFDPEATLEDIAKHK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 262 INVLCCTPTEYRMMAKL--SHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTE-STLLIGFLKDTEPRM 338
Cdd:PRK07788 296 ATALVVVPVMLSRILDLgpEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvAFATIATPEDLAEAP 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 339 GSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPalFKGYFKDeaRTKAASTGdYYVTGDQAHIDNDGYFWFEGRRD 418
Cdd:PRK07788 376 GTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP--FEGYTDG--RDKQIIDG-LLSSGDVGYFDEDGLLFVDGRDD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 419 DIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDyEASDEliQELQVFCKNEVAPYKYPRAIE 498
Cdd:PRK07788 451 DMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG-AALDE--DAIKDYVRDNLARYKVPRDVV 527
|
490 500
....*....|....*....|..
gi 1801842045 499 FVENLPKTNSGKIRRVELRDAE 520
Cdd:PRK07788 528 FLDELPRNPTGKVLKRELREMD 549
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
41-513 |
4.95e-45 |
|
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: 164.34 E-value: 4.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPssemlrtkdlqyrithgeidavISF 120
Cdd:cd05945 16 TLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP----------------------LDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 SSLTKEFENVKEYDQLKKFIVAGhkedwvsiedekekvnddlkgadttrDDLAILSYTSGTTGNPKAVTHSHG------- 193
Cdd:cd05945 74 SSPAERIREILDAAKPALLIADG--------------------------DDNAYIIFTSGSTGRPKGVQISHDnlvsftn 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 194 WGYAHLQMAPkhwlciqenDLVWATAAPgwqkwvWSPFLSV------LGMGATAFVyNGRFHPETYLEL---LQNYQINV 264
Cdd:cd05945 128 WMLSDFPLGP---------GDVFLNQAP------FSFDLSVmdlypaLASGATLVP-VPRDATADPKQLfrfLAEHGITV 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 265 LCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQTESTLLIGFLKDTEPRMGSM-- 341
Cdd:cd05945 192 WVSTPSFAAMCLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTPEVLDGYdr 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 342 ---GKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDY----YVTGDQAHIDNDGYFWFE 414
Cdd:cd05945 272 lpiGYAKPGAKLVILDEDGRPVPPGEKGELVI--SGPSVSKGYLNNPEKTAAAFFPDEgqraYRTGDLVRLEADGLLFYR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 415 GRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAsdELIQELQVFCKNEVAPYKYP 494
Cdd:cd05945 350 GRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEA--GLTKAIKAELAERLPPYMIP 427
|
490
....*....|....*....
gi 1801842045 495 RAIEFVENLPKTNSGKIRR 513
Cdd:cd05945 428 RRFVYLDELPLNANGKIDR 446
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
41-518 |
9.01e-45 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 165.96 E-value: 9.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRaIVTYELYIAA-LKLGIAIVPSSEMLRTKDLQYRITHGEIDAVIS 119
Cdd:PRK07059 48 AITYGELDELSRALAAWLQSRGLAKGARVAIMMPN-VLQYPVAIAAvLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 120 FSSLTKEFENVKEYDQLKKFIVA---------GHKEDWVsIEDEKEKV-----------ND--------DLKGADTTRDD 171
Cdd:PRK07059 127 LENFATTVQQVLAKTAVKHVVVAsmgdllgfkGHIVNFV-VRRVKKMVpawslpghvrfNDalaegarqTFKPVKLGPDD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 172 LAILSYTSGTTGNPKAVTHSHGWGYA-----HLQMAPKHWLCIQENDLVWATAAPgwqkwVWSPF-LSV---LGM---GA 239
Cdd:PRK07059 206 VAFLQYTGGTTGVSKGATLLHRNIVAnvlqmEAWLQPAFEKKPRPDQLNFVCALP-----LYHIFaLTVcglLGMrtgGR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 240 TAFVYNGRFHPeTYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGY 319
Cdd:PRK07059 281 NILIPNPRDIP-GFIKELKKYQVHIFPAVNTLYNALLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTGCPITEGY 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 320 GQTE-STLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGD-YY 397
Cdd:PRK07059 360 GLSEtSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICI--RGPQVMAGYWNRPDETAKVMTADgFF 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 398 VTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELI 477
Cdd:PRK07059 438 RTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVK 517
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1801842045 478 QelqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK07059 518 A----FCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
42-518 |
2.23e-44 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 164.84 E-value: 2.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVIsfs 121
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLV--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 122 sLTKEFENvkeYD-------------QLKKFIVAGhKEDWVSIED-----EKEKVNDDLKGADTTR---DDLAILSYTSG 180
Cdd:PRK13295 133 -VPKTFRG---FDhaamarrlrpelpALRHVVVVG-GDGADSFEAllitpAWEQEPDAPAILARLRpgpDDVTQLIYTSG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 181 TTGNPKAVTHSHGWGYAHLQMAPKHwLCIQENDLVWATAAPGWQkwvwSPFLSVLGM----GATAfVYNGRFHPETYLEL 256
Cdd:PRK13295 208 TTGEPKGVMHTANTLMANIVPYAER-LGLGADDVILMASPMAHQ----TGFMYGLMMpvmlGATA-VLQDIWDPARAAEL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 257 LQNYQIN-VLCCTP--TEyrmMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLL-IGFLK 332
Cdd:PRK13295 282 IRTEGVTfTMASTPflTD---LTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVtLTKLD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 333 DTEPRMG-SMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGdYYVTGDQAHIDNDGYF 411
Cdd:PRK13295 359 DPDERAStTDGCPLPGVEVRVVDADGAPLPAGQIGRLQV--RGCSNFGGYLKRPQLNGTDADG-WFDTGDLARIDADGYI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 412 WFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQD----DYEASDELIQELQVfckne 487
Cdd:PRK13295 436 RISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPgqslDFEEMVEFLKAQKV----- 510
|
490 500 510
....*....|....*....|....*....|.
gi 1801842045 488 VAPYkYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK13295 511 AKQY-IPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
177-513 |
3.16e-44 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 165.51 E-value: 3.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 177 YTSGTTGNPKAVTHSHGwGYA-HLQMAPKHWLCIQENDLVWATAAPGW----QKWVWSPFLSvlgmGATAFVYNG---RF 248
Cdd:PRK10524 240 YTSGTTGKPKGVQRDTG-GYAvALATSMDTIFGGKAGETFFCASDIGWvvghSYIVYAPLLA----GMATIMYEGlptRP 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 249 HPETYLELLQNYQINVLCCTPTEYRMMAK--LSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTES-- 324
Cdd:PRK10524 315 DAGIWWRIVEKYKVNRMFSAPTAIRVLKKqdPALLRKHDLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTETgw 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 325 ---TLLIGfLKDTEPRMGSMGKGIPGSFVTVIDD-DGKEVGPNVKGNIAV--PLDlPALFKGYFKDEAR---TKAASTGD 395
Cdd:PRK10524 395 pilAIARG-VEDRPTRLGSPGVPMYGYNVKLLNEvTGEPCGPNEKGVLVIegPLP-PGCMQTVWGDDDRfvkTYWSLFGR 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 396 -YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQD-----D 469
Cdd:PRK10524 473 qVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDsdslaD 552
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1801842045 470 YEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:PRK10524 553 REARLALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
27-518 |
4.75e-44 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 162.75 E-value: 4.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYKDNEhenisVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPssemlrtkdLQ 106
Cdd:PRK06145 18 RAALVYRDQE-----ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLP---------IN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 107 YRITHGEIDAVISFSSltkefenvkeydqlKKFIVAGHKEDWVSIEDEKEKVNDDLKGADTTR----------------D 170
Cdd:PRK06145 84 YRLAADEVAYILGDAG--------------AKLLLVDEEFDAIVALETPKIVIDAAAQADSRRlaqggleippqaavapT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 171 DLAILSYTSGTTGNPKAVTHSHG---WGYAHLQMApkhwLCIQENDL---------VWATAAPGwqkwvwspfLSVLGMG 238
Cdd:PRK06145 150 DLVRLMYTSGTTDRPKGVMHSYGnlhWKSIDHVIA----LGLTASERllvvgplyhVGAFDLPG---------IAVLWVG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 239 ATAFVYNgRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRD 317
Cdd:PRK06145 217 GTLRIHR-EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFtRARYID 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 318 GYGQTESTLLIGFLKDTEP--RMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKAASTGD 395
Cdd:PRK06145 296 AYGLTETCSGDTLMEAGREieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEIC--MRGPKVTKGYWKDPEKTAEAFYGD 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 396 YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQddyEASDE 475
Cdd:PRK06145 374 WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLN---PGATL 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1801842045 476 LIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK06145 451 TLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
41-519 |
1.72e-42 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 159.66 E-value: 1.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNH-GLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVIS 119
Cdd:PRK08751 50 TITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 120 FSSLTKEFENVKEYDQLKKFIVAGHKE----------DWVSIEDEKEKVNDDLKGA------------------DTTRDD 171
Cdd:PRK08751 130 IDNFGTTVQQVIADTPVKQVITTGLGDmlgfpkaalvNFVVKYVKKLVPEYRINGAirfrealalgrkhsmptlQIEPDD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 172 LAILSYTSGTTGNPKAVTHSHGWGYAHLQMApKHWLC----IQENDLVWATAAPGWQKWVWSP----FLSVlgMGATAFV 243
Cdd:PRK08751 210 IAFLQYTGGTTGVAKGAMLTHRNLVANMQQA-HQWLAgtgkLEEGCEVVITALPLYHIFALTAnglvFMKI--GGCNHLI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 244 YNGRFHPeTYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTE 323
Cdd:PRK08751 287 SNPRDMP-GFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 324 ST--LLIGFLkDTEPRMGSMGKGIPGSFVTVIDDDGK-----EVGP-NVKGniavpldlPALFKGYFKDEARTKAASTGD 395
Cdd:PRK08751 366 TSpaACINPL-TLKEYNGSIGLPIPSTDACIKDDAGTvlaigEIGElCIKG--------PQVMKGYWKRPEETAKVMDAD 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 396 YYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASD 474
Cdd:PRK08751 437 GWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAE 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1801842045 475 eliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:PRK08751 517 ----DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDA 557
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
29-527 |
2.19e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 159.21 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKdneHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMP-RA---IVTYelyiAALKLGIAIVPSSEMLRTKD 104
Cdd:PRK08315 34 ALVYR---DQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPnVPewvLTQF----ATAKIGAILVTINPAYRLSE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 105 LQYRITHGEIDAVISFSSL---------------TKEFE----NVKEYDQLKKFIVAGHKE-----DWVSIEDEKEKVND 160
Cdd:PRK08315 107 LEYALNQSGCKALIAADGFkdsdyvamlyelapeLATCEpgqlQSARLPELRRVIFLGDEKhpgmlNFDELLALGRAVDD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 161 D-LK--GADTTRDDLAILSYTSGTTGNPKAVTHSH----GWGY---AHLQMAPKHWLCIQendlvwataapgwqkwVwsP 230
Cdd:PRK08315 187 AeLAarQATLDPDDPINIQYTSGTTGFPKGATLTHrnilNNGYfigEAMKLTEEDRLCIP----------------V--P 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 231 F-------LSVLGM---GATAfVYNG-RFHPETYLELLQNYQinvlcCT-----PTeyrM-MAKLSHLE--QYNLEYLHS 291
Cdd:PRK08315 249 LyhcfgmvLGNLACvthGATM-VYPGeGFDPLATLAAVEEER-----CTalygvPT---MfIAELDHPDfaRFDLSSLRT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 292 AVSAGEPLNREVVEQFKRHFNIT-VRDGYGQTESTLLIgFLKDT----EPRMGSMGKGIPGSFVTVID-DDGKEVGPNVK 365
Cdd:PRK08315 320 GIMAGSPCPIEVMKRVIDKMHMSeVTIAYGMTETSPVS-TQTRTddplEKRVTTVGRALPHLEVKIVDpETGETVPRGEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 366 GNI-----AVpldlpalFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTN 439
Cdd:PRK08315 399 GELctrgySV-------MKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYT 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 440 HAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQElqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:PRK08315 472 HPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRD---FCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
....*...
gi 1801842045 520 EIKKYQQQ 527
Cdd:PRK08315 549 MIEELGLQ 556
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
37-519 |
2.96e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 158.57 E-value: 2.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 37 HENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDA 116
Cdd:PRK08162 39 HGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 117 VI---SFSSLTKE----FENVK--------------------EYDQlkkFIVAGHKE-DWVSIEDEKEkvnddlkgadtt 168
Cdd:PRK08162 119 LIvdtEFAEVAREalalLPGPKplvidvddpeypggrfigalDYEA---FLASGDPDfAWTLPADEWD------------ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 169 rddlAI-LSYTSGTTGNPKAVTHSHGWGYahlqmapkhwLCIQENDLVWATAapgwQKWVwspFLSVLGMgataFVYNG- 246
Cdd:PRK08162 184 ----AIaLNYTSGTTGNPKGVVYHHRGAY----------LNALSNILAWGMP----KHPV---YLWTLPM----FHCNGw 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 247 -----------------RFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKR 309
Cdd:PRK08162 239 cfpwtvaaragtnvclrKVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 310 -HFNIT-VrdgYGQTE--------------STLLIgflkDTEPRMGSMgKGIP---GSFVTVID--------DDGKEVGP 362
Cdd:PRK08162 319 iGFDLThV---YGLTEtygpatvcawqpewDALPL----DERAQLKAR-QGVRyplQEGVTVLDpdtmqpvpADGETIGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 363 -NVKGNIAVpldlpalfKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHA 441
Cdd:PRK08162 391 iMFRGNIVM--------KGYLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHP 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801842045 442 AVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPRAIEFVEnLPKTNSGKIRRVELRDA 519
Cdd:PRK08162 463 AVLVAAVVAKPDPKWGEVPCAFVELKDGASATEE---EIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQKFVLREQ 536
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
170-521 |
6.79e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 158.97 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHGwgyahlQMAPKHW-----LCIQENDLVWAtAAP-----GWQKWVWSPFLS----VL 235
Cdd:PRK07529 213 DDVAAYFHTGGTTGMPKLAQHTHG------NEVANAWlgallLGLGPGDTVFC-GLPlfhvnALLVTGLAPLARgahvVL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 236 GMGAtafvynGRFHPETY---LELLQNYQINVLCCTPTEYRMMAKLShLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFN 312
Cdd:PRK07529 286 ATPQ------GYRGPGVIanfWKIVERYRINFLSGVPTVYAALLQVP-VDGHDISSLRYALCGAAPLPVEVFRRFEAATG 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 313 ITVRDGYGQTESTLL--IGFLkDTEPRMGSMGKGIPGSFVTVI--DDDG---KEVGPNVKGNIAVplDLPALFKGYFkDE 385
Cdd:PRK07529 359 VRIVEGYGLTEATCVssVNPP-DGERRIGSVGLRLPYQRVRVVilDDAGrylRDCAVDEVGVLCI--AGPNVFSGYL-EA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 386 ARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFI 464
Cdd:PRK07529 435 AHNKGLWLEDGWLnTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYV 514
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801842045 465 ILQDDYEASDEliqELQVFCKNEVA-PYKYPRAIEFVENLPKTNSGKIRRVELRDAEI 521
Cdd:PRK07529 515 QLKPGASATEA---ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALRRDAI 569
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
41-519 |
1.01e-41 |
|
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: 156.84 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIV---PSsemLRTKDLQYRITHGEIDAV 117
Cdd:COG1021 50 RLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVfalPA---HRRAEISHFAEQSEAVAY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 I--------SFSSLTKEFenVKEYDQLKKFIVAGHKEDWVSIED-EKEKVndDLKGADTTRDDLAILSYTSGTTGNPKAV 188
Cdd:COG1021 127 IipdrhrgfDYRALAREL--QAEVPSLRHVLVVGDAGEFTSLDAlLAAPA--DLSEPRPDPDDVAFFQLSGGTTGLPKLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 --THsHGWGYAHLQMAPkhwLC-IQEND--LVWATAA-------PGwqkwvwspFLSVLGMGATAfVYNGRFHPETYLEL 256
Cdd:COG1021 203 prTH-DDYLYSVRASAE---ICgLDADTvyLAALPAAhnfplssPG--------VLGVLYAGGTV-VLAPDPSPDTAFPL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 257 LQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKD-TE 335
Cdd:COG1021 270 IERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLVNYTRLDDpEE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 336 PRMGSMGKGI-PGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDGYFWF 413
Cdd:COG1021 350 VILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLT--RGPYTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 414 EGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQvfcKNEVAPYKY 493
Cdd:COG1021 428 EGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLR---ERGLAAFKL 504
|
490 500
....*....|....*....|....*.
gi 1801842045 494 PRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:COG1021 505 PDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
43-519 |
1.52e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 155.74 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPssemlrtkdLQYRITHGEIDAVIsfss 122
Cdd:PRK09088 24 TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVP---------LNWRLSASELDALL---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 ltkefENVKEYDQLKKFIVAGHKEDWVSIEDEKEKVnDDLKGADTT---RDDLAILSYTSGTTGNPKAVTHSHgwgyAHL 199
Cdd:PRK09088 91 -----QDAEPRLLLGDDAVAAGRTDVEDLAAFIASA-DALEPADTPsipPERVSLILFTSGTSGQPKGVMLSE----RNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 200 QMAPKHW--LCIQENDLVWATAAPGWQK-WVWSPFLSVLGMGATAFVYNGrFHPETYLELLQNYQINV--LCCTPteyRM 274
Cdd:PRK09088 161 QQTAHNFgvLGRVDAHSSFLCDAPMFHIiGLITSVRPVLAVGGSILVSNG-FEPKRTLGRLGDPALGIthYFCVP---QM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 275 MAKLSHLEQYN---LEYLHSAVSAGEPLNREVVEQFKRHfNITVRDGYGQTESTLLIGFLKDTE---PRMGSMGKGIPGS 348
Cdd:PRK09088 237 AQAFRAQPGFDaaaLRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGTVFGMSVDCDvirAKAGAAGIPTPTV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 349 FVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYT 427
Cdd:PRK09088 316 QTRVVDDQGNDCPAGVPGELL--LRGPNLSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFWVVDRKKDMFISGGEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 428 IGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDdyeASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTN 507
Cdd:PRK09088 394 VYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPAD---GAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTA 470
|
490
....*....|..
gi 1801842045 508 SGKIRRVELRDA 519
Cdd:PRK09088 471 SGKLQKARLRDA 482
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
162-527 |
1.54e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 156.85 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 162 LKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAH-LQMAPKHWLCIQENDLVWATAAPGWQkwvwspflsvlgmgat 240
Cdd:PRK05677 199 VTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANmLQCRALMGSNLNEGCEILIAPLPLYH---------------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 241 afVYNGRFHPETYLeLLQNYqiNVLCCTPTEYRMMAK-------------------LSHLEQY-NLEY--LHSAVSAGEP 298
Cdd:PRK05677 263 --IYAFTFHCMAMM-LIGNH--NILISNPRDLPAMVKelgkwkfsgfvglntlfvaLCNNEAFrKLDFsaLKLTLSGGMA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 299 LNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALF 378
Cdd:PRK05677 338 LQLATAERWKEVTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCV--KGPQVM 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 379 KGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRG 457
Cdd:PRK05677 416 KGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSG 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 458 NIVKAFIILQDDYEASDELIQElqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEIKKYQQQ 527
Cdd:PRK05677 496 EAIKVFVVVKPGETLTKEQVME---HMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGLK 562
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
14-517 |
2.54e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 154.94 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 14 IVSEIEKYAS-EDHKKAIIYKDNEhenisVSYKELISNANKVGNvFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIA 92
Cdd:PRK07638 3 ITKEYKKHASlQPNKIAIKENDRV-----LTYKDWFESVCKVAN-WLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 93 IVPSSEMLRTKDLQYRITHGEIDAVISFSSLTKEFENVK----EYDQLKKFIvaghkedwvsiedekEKVNDDLKGADTT 168
Cdd:PRK07638 77 CVPLDIKWKQDELKERLAISNADMIVTERYKLNDLPDEEgrviEIDEWKRMI---------------EKYLPTYAPIENV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 169 RDDLAILSYTSGTTGNPKAVTHSH-GWgyAHLQMAPKHWLCIQENDLVwatAAPGwqKWVWSPFL----SVLGMGATAFV 243
Cdd:PRK07638 142 QNAPFYMGFTSGSTGKPKAFLRAQqSW--LHSFDCNVHDFHMKREDSV---LIAG--TLVHSLFLygaiSTLYVGQTVHL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 244 YNgRFHPETYLELLQNYQINVLCCTPTeyrMMAKLSHLEQYnLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQT 322
Cdd:PRK07638 215 MR-KFIPNQVLDKLETENISVMYTVPT---MLESLYKENRV-IENKMKIISSGAKWEAEAKEKIKNIFpYAKLYEFYGAS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 323 ESTLlIGFL--KDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTG 400
Cdd:PRK07638 290 ELSF-VTALvdEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYV--KSPQFFMGYIIGGVLARELNADGWMTVR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 401 DQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDyeasdelIQEL 480
Cdd:PRK07638 367 DVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSAT-------KQQL 439
|
490 500 510
....*....|....*....|....*....|....*..
gi 1801842045 481 QVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK07638 440 KSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
62-519 |
4.66e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 155.20 E-value: 4.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 62 GLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSemlrtkdlqYRITHGEID---------AVISFSSLTKEFENVKE 132
Cdd:PRK07470 53 GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTN---------FRQTPDEVAylaeasgarAMICHADFPEHAAAVRA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 133 Y-DQLKKFIVAGHKEDWVSIEDE-KEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGwgyahlQMA---PKHwL 207
Cdd:PRK07470 124 AsPDLTHVVAIGGARAGLDYEALvARHLGARVANAAVDHDDPCWFFFTSGTTGRPKAAVLTHG------QMAfviTNH-L 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 208 CiqenDLVwataaPGWQKWVWSPFLSVLGMGA-------------TAFVYNGRFHPETYLELLQNYQINVLCCTPTEYRM 274
Cdd:PRK07470 197 A----DLM-----PGTTEQDASLVVAPLSHGAgihqlcqvargaaTVLLPSERFDPAEVWALVERHRVTNLFTVPTILKM 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 275 MAKLSHLEQYNLEYLHSAVSAGEPLNRE-----------VVEQFkrhfnitvrdgYGQTESTLLIGFL--------KDTE 335
Cdd:PRK07470 268 LVEHPAVDRYDHSSLRYVIYAGAPMYRAdqkralaklgkVLVQY-----------FGLGEVTGNITVLppalhdaeDGPD 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 336 PRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLdlPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEG 415
Cdd:PRK07470 337 ARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIG--PAVFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 416 RRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPR 495
Cdd:PRK07470 415 RASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA---ELLAWLDGKVARYKLPK 491
|
490 500
....*....|....*....|....
gi 1801842045 496 AIEFVENLPKTNSGKIRRVELRDA 519
Cdd:PRK07470 492 RFFFWDALPKSGYGKITKKMVREE 515
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
170-510 |
1.07e-40 |
|
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: 150.61 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILsYTSGTTGNPKAVTHSHGWGYAHLQMAPKH--------WLCIQEN----DLVWATAAP---GWQKWVWspfLSV 234
Cdd:cd05924 4 DDLYIL-YTGGTTGMPKGVMWRQEDIFRMLMGGADFgtgeftpsEDAHKAAaaaaGTVMFPAPPlmhGTGSWTA---FGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 235 LGMGATAFVYNGRFHPETYLELLQNYQINVLCCTPTeyrMMAK-----LSHLEQYNLEYLHSAVSAGEPLNREVVEQFKR 309
Cdd:cd05924 80 LLGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGD---AMARplidaLRDAGPYDLSSLFAISSGGALLSPEVKQGLLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 310 HF-NITVRDGYGQTEStlliGFLKDTEPRMGSMGKG---IPGSFVTVIDDDGKEV--GPNVKGNIA----VPLdlpalfk 379
Cdd:cd05924 157 LVpNITLVDAFGSSET----GFTGSGHSAGSGPETGpftRANPDTVVLDDDGRVVppGSGGVGWIArrghIPL------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 380 GYFKDEARTKAA-STGD---YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDI 455
Cdd:cd05924 226 GYYGDEAKTAETfPEVDgvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDER 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1801842045 456 RGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGK 510
Cdd:cd05924 306 WGQEVVAVVQLREGAGVDLE---ELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
40-518 |
1.62e-40 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 154.21 E-value: 1.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 40 ISVSYKELISNANKVGNVFLNH-GLKKGDKVLIMMPRaIVTYELYI-AALKLGIAIVPSSEMLRTKDLQYRITHGEIDAV 117
Cdd:PRK12492 48 VTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPN-VLQYPIAVfGALRAGLIVVNTNPLYTAREMRHQFKDSGARAL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 ISFSSLTKEFENVK-----EY----------------------DQLKKFIVAGHKEDWVSIEDE-KEKVNDDLKGADTTR 169
Cdd:PRK12492 127 VYLNMFGKLVQEVLpdtgiEYlieakmgdllpaakgwlvntvvDKVKKMVPAYHLPQAVPFKQAlRQGRGLSLKPVPVGL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHGWGYAHL--------QMAPKHWLCIQENDLVWATAAPGWQKWVWSPflSVLGMGATA 241
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANMlqvraclsQLGPDGQPLMKEGQEVMIAPLPLYHIYAFTA--NCMCMMVSG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 242 ----FVYNGRFHPeTYLELLQNYQINVLCCTPTEYrmMAKLSHLEQYNLEY--LHSAVSAGEPLNREVVEQFKRHFNITV 315
Cdd:PRK12492 285 nhnvLITNPRDIP-GFIKELGKWRFSALLGLNTLF--VALMDHPGFKDLDFsaLKLTNSGGTALVKATAERWEQLTGCTI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 316 RDGYGQTESTLLIGflkdTEP-----RMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYF-KDEARTK 389
Cdd:PRK12492 362 VEGYGLTETSPVAS----TNPygelaRLGTVGIPVPGTALKVIDDDGNELPLGERGELCI--KGPQVMKGYWqQPEATAE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 390 AASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDD 469
Cdd:PRK12492 436 ALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARDP 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1801842045 470 YEAsdelIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK12492 516 GLS----VEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
26-449 |
2.05e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 154.49 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYKDNEHEnISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMP-RaivtYELYI---AALKLGIAIVPSSEMLR 101
Cdd:COG1022 26 DRVALREKEDGIW-QSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDnR----PEWVIadlAILAAGAVTVPIYPTSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 102 TKDLQYRITHGEIDAVIsfssltkeFENVKEYDQLK---------KFIV-----AGHKEDWVS-----IEDEKEKVNDDL 162
Cdd:COG1022 101 AEEVAYILNDSGAKVLF--------VEDQEQLDKLLevrdelpslRHIVvldprGLRDDPRLLsldelLALGREVADPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 163 ---KGADTTRDDLAILSYTSGTTGNPKAVTHSHG-W---GYAHLQMAPkhwlcIQENDLvwataapgwqkwvwspFLSVL 235
Cdd:COG1022 173 leaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRnLlsnARALLERLP-----LGPGDR----------------TLSFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 236 -------GMGATAFVYNGrFH------PETYLELLQNYQINVLCCTP--------TEYRMMAKLSHLEQ----------- 283
Cdd:COG1022 232 plahvfeRTVSYYALAAG-ATvafaesPDTLAEDLREVKPTFMLAVPrvwekvyaGIQAKAEEAGGLKRklfrwalavgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 284 ---------------YNLEY------------------LHSAVSAGEPLNREVVEqFKRHFNITVRDGYGQTESTLLIGF 330
Cdd:COG1022 311 ryararlagkspsllLRLKHaladklvfsklrealggrLRFAVSGGAALGPELAR-FFRALGIPVLEGYGLTETSPVITV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 331 LKDTEPRMGSMGKGIPGsfVTV-IDDDGkEV---GPNVkgniavpldlpalFKGYFKDEARTKAASTGD-YYVTGDQAHI 405
Cdd:COG1022 390 NRPGDNRIGTVGPPLPG--VEVkIAEDG-EIlvrGPNV-------------MKGYYKNPEATAEAFDADgWLHTGDIGEL 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1801842045 406 DNDGYFWFEGRRDDIII-SSGYTIGPFEVEDALTNHAAVKECAVV 449
Cdd:COG1022 454 DEDGFLRITGRKKDLIVtSGGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
40-518 |
4.76e-40 |
|
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: 151.72 E-value: 4.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 40 ISVSYKELISNANKVGNVfLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVpsseMLR----TKDLQYRITHGEID 115
Cdd:cd05909 6 TSLTYRKLLTGAIALARK-LAKMTKEGENVGVMLPPSAGGALANFALALSGKVPV----MLNytagLRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 116 AVISfsslTKEFenvKEYDQLKKFIVAGHKEDWVSIEDEKEKVN--DDLKG-----------------ADTTRDDLAILS 176
Cdd:cd05909 81 TVLT----SKQF---IEKLKLHHLFDVEYDARIVYLEDLRAKISkaDKCKAflagkfppkwllrifgvAPVQPDDPAVIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 177 YTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIqENDLVwATAAP-----GWQKWVWSPFLsvlgMGATAFVYNGRFHPE 251
Cdd:cd05909 154 FTSGSEGLPKGVVLSHKNLLANVEQITAIFDPN-PEDVV-FGALPffhsfGLTGCLWLPLL----SGIKVVFHPNPLDYK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 252 TYLELLQNYQINVLCCTPTEYRMMAKLSHLEQynLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGF- 330
Cdd:cd05909 228 KIPELIYDKKATILLGTPTFLRGYARAAHPED--FSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVISVn 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 331 LKDTEPRMGSMGKGIPGSFVTVIDDDGK-EVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDG 409
Cdd:cd05909 306 TPQSPNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLV--RGPNVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 410 YFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVK-ECAVVASPHDIRGNIVKAFiilqddYEASDELIQELQVFCKNEV 488
Cdd:cd05909 384 FLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLL------TTTTDTDPSSLNDILKNAG 457
|
490 500 510
....*....|....*....|....*....|.
gi 1801842045 489 APYKY-PRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd05909 458 ISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
26-516 |
1.60e-39 |
|
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: 150.35 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYKDNEHEnisVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDL 105
Cdd:cd05923 16 DACAIADPARGLR---LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 106 QYRITHGEIDAVIsfssLTKEFENVKEydqlkkFIVAGHKEDWVSIED---EKEKVNDDLKGADTTRDDLAILSYTSGTT 182
Cdd:cd05923 93 AELIERGEMTAAV----IAVDAQVMDA------IFQSGVRVLALSDLVglgEPESAGPLIEDPPREPEQPAFVFYTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 183 GNPKAVTHSHgwgyahlqmapKHwlcIQENDLVWATAAP---GWQKWVWS--PFLSVLGMGAT---AFVYNGR------F 248
Cdd:cd05923 163 GLPKGAVIPQ-----------RA---AESRVLFMSTQAGlrhGRHNVVLGlmPLYHVIGFFAVlvaALALDGTyvvveeF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 249 HPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTEStllI 328
Cdd:cd05923 229 DPADALKLIEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA---M 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 329 GFLKDTEPRMGSMGKgiPG-----SFVTVIDDDGKEVGPNVKGNIAVPLDLPALFKGYFKDEARTKAASTGDYYVTGDQA 403
Cdd:cd05923 306 NSLYMRDARTGTEMR--PGffsevRIVRIGGSPDEALANGEEGELIVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 404 HIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQelqvF 483
Cdd:cd05923 384 YVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQ----F 459
|
490 500 510
....*....|....*....|....*....|....
gi 1801842045 484 CK-NEVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd05923 460 CRaSELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
41-472 |
3.14e-39 |
|
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: 148.51 E-value: 3.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRaivTYELYI---AALKLGIAIVPSSEMLRTKDLQYRITHGEIDAV 117
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRN---RPEWTIadlAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 IsfssltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgADTTrDDLAILSYTSGTTGNPKAVTHSHGwgya 197
Cdd:cd05907 82 F----------------------------------------------VEDP-DDLATIIYTSGTTGRPKGVMLSHR---- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 198 HLqmapkHWLCIQENDLVwaTAAPGWQKWVWSPFLSVLG--MGATAFVYNG---RFHP--ETYLELLQNYQINVLCCTPT 270
Cdd:cd05907 111 NI-----LSNALALAERL--PATEGDRHLSFLPLAHVFErrAGLYVPLLAGariYFASsaETLLDDLSEVRPTVFLAVPR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 271 EYRMMAKLSH-----------LEQYNLEYLHSAVSAGEPLNREVVEQFkRHFNITVRDGYGQTESTLLIGFLKDTEPRMG 339
Cdd:cd05907 184 VWEKVYAAIKvkavpglkrklFDLAVGGRLRFAASGGAPLPAELLHFF-RALGIPVYEGYGLTETSAVVTLNPPGDNRIG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 340 SMGKGIPGsfVTV-IDDDGKEVgpnVKGniavpldlPALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDGYFWFEGRR 417
Cdd:cd05907 263 TVGKPLPG--VEVrIADDGEIL---VRG--------PNVMLGYYKNPEATAEALDADgWLHTGDLGEIDEDGFLHITGRK 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1801842045 418 DDIII-SSGYTIGPFEVEDALTNHAAVKECAVVAsphDIRGNIVkAFIILqdDYEA 472
Cdd:cd05907 330 KDLIItSGGKNISPEPIENALKASPLISQAVVIG---DGRPFLV-ALIVP--DPEA 379
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
167-525 |
1.38e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 148.61 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 167 TTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMApKHWLciqendlvwataaPGWQKwvwSP--FLSVLGM------- 237
Cdd:PRK05605 216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAQG-KAWV-------------PGLGD---GPerVLAALPMfhayglt 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 238 -GATAFVYNG-------RFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKR 309
Cdd:PRK05605 279 lCLTLAVSIGgelvllpAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFSGAMALPVSTVELWEK 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 310 HFNITVRDGYGQTE-STLLIGFLKDTEPRMGSMGKGIPGSFVTVID-DDGKEVGPN-------VKGniavpldlPALFKG 380
Cdd:PRK05605 359 LTGGLLVEGYGLTEtSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpEDPDETMPDgeegellVRG--------PQVFKG 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 381 YFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIV 460
Cdd:PRK05605 431 YWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEV 510
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801842045 461 KAFIILQDDyEASDEliQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEIKKYQ 525
Cdd:PRK05605 511 VAAVVLEPG-AALDP--EGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVREELLEKLG 572
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
170-517 |
1.70e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 146.67 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDLVwaTAAPGWQkwVWSPFLSVLG---MGATaFVYNG 246
Cdd:PRK07787 128 DAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLV--HGLPLFH--VHGLVLGVLGplrIGNR-FVHTG 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 247 RFHPETYLELLqNYQINVLCCTPTEY-RMMAKLSHLEQynleyLHSA---VSAGEPLNREVVEQFKRHFNITVRDGYGQT 322
Cdd:PRK07787 203 RPTPEAYAQAL-SEGGTLYFGVPTVWsRIAADPEAARA-----LRGArllVSGSAALPVPVFDRLAALTGHRPVERYGMT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 323 ESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDD-------DGKEVGP-NVKGniavpldlPALFKGYFKDEARTKAASTG 394
Cdd:PRK07787 277 ETLITLSTRADGERRPGWVGLPLAGVETRLVDEdggpvphDGETVGElQVRG--------PTLFDGYLNRPDATAAAFTA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 395 D-YYVTGDQAHIDNDGYFWFEGRRD-DIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDyEA 472
Cdd:PRK07787 349 DgWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADD-VA 427
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1801842045 473 SDELIQelqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK07787 428 ADELID----FVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
41-517 |
2.33e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 147.08 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIM---MPRAIVtyeLYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAV 117
Cdd:PRK13390 24 QVSYRQLDDDSAALARVLYDAGLRTGDVVALLsdnSPEALV---VLWAALRSGLYITAINHHLTAPEADYIVGDSGARVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 ISFSSLTKEFENVKEYDQLKkFIVAGHKEDWVSIEDEkekvnddLKGAD---TTRDDLAILSYTSGTTGNPKAVTHS--- 191
Cdd:PRK13390 101 VASAALDGLAAKVGADLPLR-LSFGGEIDGFGSFEAA-------LAGAGprlTEQPCGAVMLYSSGTTGFPKGIQPDlpg 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 192 ---HGWGYAHLQMApKHWLCIQENDlVWATAAPGWQK--WVWSPFLSVLGmgaTAFVYNGRFHPETYLELLQNYQINVLC 266
Cdd:PRK13390 173 rdvDAPGDPIVAIA-RAFYDISESD-IYYSSAPIYHAapLRWCSMVHALG---GTVVLAKRFDAQATLGHVERYRITVTQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 267 CTPTEYRMMAKLSH--LEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIgFLKDTE--PRMGSMG 342
Cdd:PRK13390 248 MVPTMFVRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMT-FIDSPDwlAHPGSVG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 343 KGIPGSfVTVIDDDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTKAAS--TGDYYVT-GDQAHIDNDGYFWFEGRRDD 419
Cdd:PRK13390 327 RSVLGD-LHICDDDGNELPAGRIGTVYFERD--RLPFRYLNDPEKTAAAQhpAHPFWTTvGDLGSVDEDGYLYLADRKSF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 420 IIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEF 499
Cdd:PRK13390 404 MIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIAHYKAPRSVEF 483
|
490
....*....|....*...
gi 1801842045 500 VENLPKTNSGKIRRVELR 517
Cdd:PRK13390 484 VDELPRTPTGKLVKGLLR 501
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
177-519 |
6.86e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 146.00 E-value: 6.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 177 YTSGTTGNPKAVTHShgwgyahlqmAPKhwlciQENDLVWATAA-------PGWQKWVWSPFL----SVLGMGATAF--- 242
Cdd:PRK12406 159 YTSGTTGHPKGVRRA----------APT-----PEQAAAAEQMRaliyglkPGIRALLTGPLYhsapNAYGLRAGRLggv 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 243 -VYNGRFHPETYLELLQNYQINVLCCTPTeyrMMAKLSHL-----EQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVR 316
Cdd:PRK12406 224 lVLQPRFDPEELLQLIERHRITHMHMVPT---MFIRLLKLpeevrAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIY 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 317 DGYGQTESTLLIGFL-KDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPALFKGYFKDEARTkAASTGD 395
Cdd:PRK12406 301 EYYGSTESGAVTFATsEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFTYHNKPEKRA-EIDRGG 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 396 YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDE 475
Cdd:PRK12406 380 FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEA 459
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1801842045 476 LIQElqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:PRK12406 460 DIRA---QLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
43-448 |
1.54e-37 |
|
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: 142.79 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFL-NHGLKKGDKVLIMMPRaivTYELYI---AALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVI 118
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLER---SAELVVailAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 119 SFSSLTKEFenvkeyDQLKKFIVAGHKEDWVSIEDEkekVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGwGYAH 198
Cdd:TIGR01733 78 TDSALASRL------AGLVLPVILLDPLELAALDDA---PAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHR-SLVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 199 LQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGmGATAFVYNG---RFHPETYLELLQNYQINVLCCTPTEYRMM 275
Cdd:TIGR01733 148 LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLA-GATLVVPPEdeeRDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 276 AKLSHLEQYNLEYLhsaVSAGEPLNREVVEQFKRHF-NITVRDGYGQTESTL-----LIGFLKDTEPRMGSMGKGIPGSF 349
Cdd:TIGR01733 227 AAALPPALASLRLV---ILGGEALTPALVDRWRARGpGARLINLYGPTETTVwstatLVDPDDAPRESPVPIGRPLANTR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 350 VTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAA---------STGDYYVTGDQAHIDNDGYFWFEGRRDDI 420
Cdd:TIGR01733 304 LYVLDDDLRPVPVGVVGELYI--GGPGVARGYLNRPELTAERfvpdpfaggDGARLYRTGDLVRYLPDGNLEFLGRIDDQ 381
|
410 420
....*....|....*....|....*...
gi 1801842045 421 IISSGYTIGPFEVEDALTNHAAVKECAV 448
Cdd:TIGR01733 382 VKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
41-518 |
1.74e-37 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 145.29 E-value: 1.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMP--RAIVtyELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVI 118
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRnhRGFV--EALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 119 sfssLTKEFENVKEYDqLKKFIVAGHKEDWVSIEDEK--EKVNDDLKGAD---TTRDDLAILsYTSGTTGNPKAVTHSHG 193
Cdd:PRK13382 146 ----YDEEFSATVDRA-LADCPQATRIVAWTDEDHDLtvEVLIAAHAGQRpepTGRKGRVIL-LTSGTTGTPKGARRSGP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 194 WGYAHLQ--MAPKHWLCIQENDLVwataAPGWQKWVWSPFLSVLGMGATaFVYNGRFHPETYLELLQNYQINVLCCTPTE 271
Cdd:PRK13382 220 GGIGTLKaiLDRTPWRAEEPTVIV----APMFHAWGFSQLVLAASLACT-IVTRRRFDPEATLDLIDRHRATGLAVVPVM 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 272 YRMMAKL--SHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLL-IGFLKDTEPRMGSMGKGIPGS 348
Cdd:PRK13382 295 FDRIMDLpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIaTATPADLRAAPDTAGRPAEGT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 349 FVTVIDDDGKEVGPNVKGNIAVPLDLpaLFKGYfkDEARTKAASTGdYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTI 428
Cdd:PRK13382 375 EIRILDQDFREVPTGEVGTIFVRNDT--QFDGY--TSGSTKDFHDG-FMASGDVGYLDENGRLFVVGRDDEMIVSGGENV 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 429 GPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDyeaSDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNS 508
Cdd:PRK13382 450 YPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPG---ASATPETLKQHVRDNLANYKVPRDIVVLDELPRGAT 526
|
490
....*....|
gi 1801842045 509 GKIRRVELRD 518
Cdd:PRK13382 527 GKILRRELQA 536
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
42-517 |
2.98e-37 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 146.33 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGI-AIVPSSEMLRT-KDLQYRITHGEIdaVIS 119
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVmAFLANPELHRDdHALAARNTEPAL--VVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 120 FSSLTKEFENVKEYDqlkkfivaghKEDWVSIEDEKEKVNDDLKGADTTrddlAILSYTSGTTGNPKAVTHSHGWGYAHL 199
Cdd:PRK06060 109 SDALRDRFQPSRVAE----------AAELMSEAARVAPGGYEPMGGDAL----AYATYTSGTTGPPKAAIHRHADPLTFV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 200 QMAPKHWLCIQENDLVWATA----APGWQKWVWSPF-------LSVLGMGA-TAFVYNGRFHPETYLELLQNYQINVLCC 267
Cdd:PRK06060 175 DAMCRKALRLTPEDTGLCSArmyfAYGLGNSVWFPLatggsavINSAPVTPeAAAILSARFGPSVLYGVPNFFARVIDSC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 268 TPTEYRMmaklshleqynleyLHSAVSAGEPLNREVVEQFKRHFN-ITVRDGYGQTEstllIG--FLKDT--EPRMGSMG 342
Cdd:PRK06060 255 SPDSFRS--------------LRCVVSAGEALELGLAERLMEFFGgIPILDGIGSTE----VGqtFVSNRvdEWRLGTLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 343 KGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEarTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIII 422
Cdd:PRK06060 317 RVLPPYEIRVVAPDGTTAGPGVEGDLWV--RGPAIAKGYWNRP--DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 423 SSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVEN 502
Cdd:PRK06060 393 IGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDR 472
|
490
....*....|....*
gi 1801842045 503 LPKTNSGKIRRVELR 517
Cdd:PRK06060 473 LPRTPNGKLVRGALR 487
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
43-516 |
3.02e-37 |
|
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: 143.62 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIV---PSsemlrtkdlqYRitHGEIDAVIS 119
Cdd:cd05920 42 TYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVlalPS----------HR--RSELSAFCA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 120 FSsltkefenvkeydQLKKFIVAGHKEDWVSIEDEKEKVNDdlkgadttRDDLAILSYTSGTTGNPKAVTHSHGwGYAHL 199
Cdd:cd05920 110 HA-------------EAVAYIVPDRHAGFDHRALARELAES--------IPEVALFLLSGGTTGTPKLIPRTHN-DYAYN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 200 QMAPKHWlCIQENDLVWATAAPGWQKWVWS-P-FLSVLGMGATAfVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAK 277
Cdd:cd05920 168 VRASAEV-CGLDQDTVYLAVLPAAHNFPLAcPgVLGTLLAGGRV-VLAPDPSPDAAFPLIEREGVTVTALVPALVSLWLD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 278 LSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPR-MGSMGKGI-PGSFVTVIDD 355
Cdd:cd05920 246 AAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPDEViIHTQGRPMsPDDEIRVVDE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 356 DGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVE 434
Cdd:cd05920 326 EGNPVPPGEEGELLT--RGPYTIRGYYRAPEHNARAFTPDgFYRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 435 DALTNHAAVKECAVVASPHDIRGNIVKAFIILQDdyeASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRV 514
Cdd:cd05920 404 NLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD---PPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKK 480
|
..
gi 1801842045 515 EL 516
Cdd:cd05920 481 AL 482
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
36-516 |
3.57e-37 |
|
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: 142.83 E-value: 3.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 36 EHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPR---AIVTYelyIAALKLGIAIVPSsemlrtkDLQY---RI 109
Cdd:cd17643 7 VDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRsaeLIVAL---LAILKAGGAYVPI-------DPAYpveRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 110 THGEIDAvisfssltkefenvkeydQLKKFIvaghkedwvsiedekekvnddlkgadTTRDDLAILSYTSGTTGNPKAVT 189
Cdd:cd17643 77 AFILADS------------------GPSLLL--------------------------TDPDDLAYVIYTSGSTGRPKGVV 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 190 HSHGwGYAHLQMAPKHWLCIQENDLVWA--TAAPGWQKW-VWSPFLSvlgmGATAFV--YNGRFHPETYLELLQNYQINV 264
Cdd:cd17643 113 VSHA-NVLALFAATQRWFGFNEDDVWTLfhSYAFDFSVWeIWGALLH----GGRLVVvpYEVARSPEDFARLLRDEGVTV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 265 LCCTPTEYR--MMAKLS-HLEQYNLEYLhsaVSAGEPLNREVVEQFKRHFNI---TVRDGYGQTESTLLIGFLK----DT 334
Cdd:cd17643 188 LNQTPSAFYqlVEAADRdGRDPLALRYV---IFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVHVTFRPldaaDL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 335 EPRMGS-MGKGIPGSFVTVIDDDGKEVGPNVKGNIAVP--------LDLPALFKGYFKDEARTKAASTgdYYVTGDQAHI 405
Cdd:cd17643 265 PAAAASpIGRPLPGLRVYVLDADGRPVPPGVVGELYVSgagvargyLGRPELTAERFVANPFGGPGSR--MYRTGDLARR 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 406 DNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDdyeASDELIQELQVFCK 485
Cdd:cd17643 343 LPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADD---GAAADIAELRALLK 419
|
490 500 510
....*....|....*....|....*....|.
gi 1801842045 486 NEVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd17643 420 ELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
36-520 |
1.29e-36 |
|
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: 145.38 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 36 EHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIvtyELYIA---ALKLGIAIVPssemLrtkDLQY---RI 109
Cdd:COG1020 496 VFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSL---EMVVAllaVLKAGAAYVP----L---DPAYpaeRL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 110 TH----GEIDAVISFSSLTKEFenvkeydqlkkfivAGHKEDWVSIEDEK-EKVNDDLKGADTTRDDLAILSYTSGTTGN 184
Cdd:COG1020 566 AYmledAGARLVLTQSALAARL--------------PELGVPVLALDALAlAAEPATNPPVPVTPDDLAYVIYTSGSTGR 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 185 PKAVTHSHGwGYAHLQMAPKHWLCIQENDLVWATAAPG-----WQkwVWSPFLSvlgmGATAFVYN--GRFHPETYLELL 257
Cdd:COG1020 632 PKGVMVEHR-ALVNLLAWMQRRYGLGPGDRVLQFASLSfdasvWE--IFGALLS----GATLVLAPpeARRDPAALAELL 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 258 QNYQINVLCCTPTeyrMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQF-KRHFNITVRDGYGQTESTL--LIGFLKDT 334
Cdd:COG1020 705 ARHRVTVLNLTPS---LLRALLDAAPEALPSLRLVLVGGEALPPELVRRWrARLPGARLVNLYGPTETTVdsTYYEVTPP 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 335 EPRMGSM--GKGIPGSFVTVIDDDGKEVGPNVKGniavplDL----PALFKGYFKDEARTKAA-------STGD-YYVTG 400
Cdd:COG1020 782 DADGGSVpiGRPIANTRVYVLDAHLQPVPVGVPG------ELyiggAGLARGYLNRPELTAERfvadpfgFPGArLYRTG 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 401 DQAHIDNDGYFWFEGRRDD---IiisSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELI 477
Cdd:COG1020 856 DLARWLPDGNLEFLGRADDqvkI---RGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALL 932
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1801842045 478 QELQvfcKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAE 520
Cdd:COG1020 933 RLAL---ALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPA 972
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
177-513 |
1.35e-36 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 138.31 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 177 YTSGTTGNPKAVTHSHgwgyahlqmapKHWLC---IQENDLVW----ATAAPGwqKWVWSPFL----SVLGMGATaFVYN 245
Cdd:cd17633 7 FTSGTTGLPKAYYRSE-----------RSWIEsfvCNEDLFNIsgedAILAPG--PLSHSLFLygaiSALYLGGT-FIGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 246 GRFHPETYLELLQNYQINVLCCTPTeyrmMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVR-DGYGQTES 324
Cdd:cd17633 73 RKFNPKSWIRKINQYNATVIYLVPT----MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLiEFYGTSEL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 325 TLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGP-NVKGNIAvpldlpalFKGYFkdeaRTKAASTGDYYVTGDQA 403
Cdd:cd17633 149 SFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEIGKiFVKSEMV--------FSGYV----RGGFSNPDGWMSVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 404 HIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVkAFIILQDDYEAsdeliQELQVF 483
Cdd:cd17633 217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIA-VALYSGDKLTY-----KQLKRF 290
|
330 340 350
....*....|....*....|....*....|
gi 1801842045 484 CKNEVAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:cd17633 291 LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
170-517 |
1.38e-36 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 139.15 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHG------WGYAHLQMapkhwlcIQENDLVWAtAAPGWQkwVWSPFLSVLGM---GAT 240
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSnevynaWMLALNSL-------FDPDDVLLC-GLPLFH--VNGSVVTLLTPlasGAH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 241 AFV-----YNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLShlEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITV 315
Cdd:cd05944 72 VVLagpagYRNPGLFDNFWKLVERYRITSLSTVPTVYAALLQVP--VNADISSLRFAMSGAAPLPVELRARFEDATGLPV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 316 RDGYGQTESTLLIGF-LKDTEPRMGSMGKGIPGSFVTVIDDDG-----KEVGPNVKGNIAVPLdlPALFKGYFKDEARTK 389
Cdd:cd05944 150 VEGYGLTEATCLVAVnPPDGPKRPGSVGLRLPYARVRIKVLDGvgrllRDCAPDEVGEICVAG--PGVFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 390 AASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDD 469
Cdd:cd05944 228 AFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1801842045 470 YEASDEliqELQVFCKNEVAPY-KYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05944 308 AVVEEE---ELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
43-519 |
5.08e-35 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 137.70 E-value: 5.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMM---PRAIVtyeLYIAALKLGIAIVPSSEMLRTKDLQYRITHGEiDAVis 119
Cdd:PRK07514 30 TYGDLDAASARLANLLVALGVKPGDRVAVQVeksPEALA---LYLATLRAGAVFLPLNTAYTLAELDYFIGDAE-PAL-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 120 fssltkefenvkeydqlkkFIVAGHKEDWVSIEDEK------EKVNDDLKGADTTR---------------DDLAILSYT 178
Cdd:PRK07514 104 -------------------VVCDPANFAWLSKIAAAagaphvETLDADGTGSLLEAaaaapddfetvprgaDDLAAILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 179 SGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATaapgwqkwvwsPFLSVLGMgataFV------YNG------ 246
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHAL-----------PIFHTHGL----FVatnvalLAGasmifl 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 247 -RFHPETYLELLQnyQINVLCCTPTEY-RMmaklshLEQYNLEYLHSA-----VSAGEPLNREVVEQFKRHFNITVRDGY 319
Cdd:PRK07514 230 pKFDPDAVLALMP--RATVMMGVPTFYtRL------LQEPRLTREAAAhmrlfISGSAPLLAETHREFQERTGHAILERY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 320 GQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVID-DDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGD-YY 397
Cdd:PRK07514 302 GMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEV--KGPNVFKGYWRMPEKTAEEFRADgFF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 398 VTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAS-DEL 476
Cdd:PRK07514 380 ITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPGAALDeAAI 459
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1801842045 477 IQELqvfcKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:PRK07514 460 LAAL----KGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
38-517 |
5.42e-35 |
|
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: 137.48 E-value: 5.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 38 ENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVP---------SSEMLRTKDLQYR 108
Cdd:cd17651 17 EGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPldpaypaerLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 109 ITHgeidAVISFSSLTKEfenvkeydqlkkfiVAGHKEDWVSIEDEkekvNDDLKGADTTRDDLAILSYTSGTTGNPKAV 188
Cdd:cd17651 97 LTH----PALAGELAVEL--------------VAVTLLDQPGAAAG----ADAEPDPALDADDLAYVIYTSGSTGRPKGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 THSHGwGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFlSVLGMGATAFVYNG--RFHPETYLELLQNYQINVLC 266
Cdd:cd17651 155 VMPHR-SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIF-STLCAGATLVLPPEevRTDPPALAAWLDEQRISRVF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 267 CTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPL--NREVVEQFKRHFNITVRDGYGQTESTLLIGF----LKDTEPRMGS 340
Cdd:cd17651 233 LPTVALRALAEHGRPLGVRLAALRYLLTGGEQLvlTEDLREFCAGLPGLRLHNHYGPTETHVVTALslpgDPAAWPAPPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 341 MGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTKA------ASTGD-YYVTGDQAHIDNDGYFWF 413
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA--GLARGYLNRPELTAErfvpdpFVPGArMYRTGDLARWLPDGELEF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 414 EGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKY 493
Cdd:cd17651 391 LGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAA---ELRAALATHLPEYMV 467
|
490 500
....*....|....*....|....
gi 1801842045 494 PRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd17651 468 PSAFVLLDALPLTPNGKLDRRALP 491
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
171-513 |
1.26e-34 |
|
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: 133.01 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 171 DLAILSYTSGTTGNPKAVTHshgwgyAHLQ--MAPKHWlciqeNDLVWATAapGWQKWVWSPFLSVLG--MGATAFVYNG 246
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMC------AHRQtlRAAAAW-----ADCADLTE--DDRYLIINPFFHTFGykAGIVACLLTG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 247 R-------FHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNI-TVRDG 318
Cdd:cd17638 68 AtvvpvavFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFeTVLTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 319 YGQTESTL--LIGFLKDTEPRMGSMGKGIPGSFVTvIDDDGKEV--GPNVkgniavpldlpalFKGYFKDEARTKAASTG 394
Cdd:cd17638 148 YGLTEAGVatMCRPGDDAETVATTCGRACPGFEVR-IADDGEVLvrGYNV-------------MQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 395 DYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAS 473
Cdd:cd17638 214 DGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLT 293
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1801842045 474 DEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:cd17638 294 EE---DVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
170-513 |
1.39e-34 |
|
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: 132.78 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILsYTSGTTGNPKAVTHSHG-WGYAHLQMApkHWLCIQENDLVWATAapgwqkwvwsPFLSVLGMG-ATAFVYNG- 246
Cdd:cd17637 1 DPFVII-HTAAVAGRPRGAVLSHGnLIAANLQLI--HAMGLTEADVYLNML----------PLFHIAGLNlALATFHAGg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 247 ------RFHPETYLELLQNYQINVLCCTPTeyrMMAK-LSHLEQYNLEyLHS--AVSAGEplNREVVEQFKRHFNITVRD 317
Cdd:cd17637 68 anvvmeKFDPAEALELIEEEKVTLMGSFPP---ILSNlLDAAEKSGVD-LSSlrHVLGLD--APETIQRFEETTGATFWS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 318 GYGQTESTLLIGFLKDTEpRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYY 397
Cdd:cd17637 142 LYGQTETSGLVTLSPYRE-RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVV--RGPLVFQGYWNLPELTAYTFRNGWH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 398 VTGDQAHIDNDGYFWFEGRR--DDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYE-ASD 474
Cdd:cd17637 219 HTGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATlTAD 298
|
330 340 350
....*....|....*....|....*....|....*....
gi 1801842045 475 ELIQelqvFCKNEVAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:cd17637 299 ELIE----FVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
37-516 |
4.58e-34 |
|
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: 134.64 E-value: 4.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 37 HENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSsemlrtkDLQY---RITH-- 111
Cdd:cd12117 18 YGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPL-------DPELpaeRLAFml 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 112 --GEIDAVISFSSLTKefenvkeydqlkkfIVAGHKEDWVSIEDEKEKVNDDLKGADTTrDDLAILSYTSGTTGNPK--A 187
Cdd:cd12117 91 adAGAKVLLTDRSLAG--------------RAGGLEVAVVIDEALDAGPAGNPAVPVSP-DDLAYVMYTSGSTGRPKgvA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 188 VTHShgwGYAHLQMAPKhWLCIQENDLVWATAAPGWQKW---VWSPFLSvlgmGATAFVYNGRF--HPETYLELLQNYQI 262
Cdd:cd12117 156 VTHR---GVVRLVKNTN-YVTLGPDDRVLQTSPLAFDAStfeIWGALLN----GARLVLAPKGTllDPDALGALIAEEGV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 263 NVLCCTPTEYRMMAKLsHLEQynLEYLHSAVSAGEPLNREVVEQF-KRHFNITVRDGYGQTESTLligF-----LKDTEP 336
Cdd:cd12117 228 TVLWLTAALFNQLADE-DPEC--FAGLRELLTGGEVVSPPHVRRVlAACPGLRLVNGYGPTENTT---FttshvVTELDE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 337 RMGS--MGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTKA-------ASTGDYYVTGDQAHIDN 407
Cdd:cd12117 302 VAGSipIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGD--GLALGYLNRPALTAErfvadpfGPGERLYRTGDLARWLP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 408 DGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAsdeliQELQVFCKNE 487
Cdd:cd12117 380 DGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDA-----AELRAFLRER 454
|
490 500
....*....|....*....|....*....
gi 1801842045 488 VAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd12117 455 LPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
169-513 |
5.05e-34 |
|
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: 131.61 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 169 RDDLAILsYTSGTTGNPKAVTHSHGWGYA---HLQMAPKHWLcIQENDLVWATAAPGWQKWvWSpfLSVLGMGATAFVYN 245
Cdd:cd17635 1 EDPLAVI-FTSGTTGEPKAVLLANKTFFAvpdILQKEGLNWV-VGDVTYLPLPATHIGGLW-WI--LTCLIHGGLCVTGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 246 GRFHPETYLELLQNYQINVLCCTPTeyrMMAKLSHLEQYNLEYLHS----AVSAGEPLNRE--VVEQFKrhfNITVRDGY 319
Cdd:cd17635 76 ENTTYKSLFKILTTNAVTTTCLVPT---LLSKLVSELKSANATVPSlrliGYGGSRAIAADvrFIEATG---LTNTAQVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 320 GQTEST--LLIGFLKDTEpRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYY 397
Cdd:cd17635 150 GLSETGtaLCLPTDDDSI-EINAVGRPYPGVDVYLAATDGIAGPSASFGTIWI--KSPANMLGYWNNPERTAEVLIDGWV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 398 VTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDdyEASDELI 477
Cdd:cd17635 227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASA--ELDENAI 304
|
330 340 350
....*....|....*....|....*....|....*.
gi 1801842045 478 QELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:cd17635 305 RALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
58-518 |
6.27e-34 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 135.53 E-value: 6.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 58 FLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVI---SFSSLTKEFENV--KE 132
Cdd:PLN03102 56 LISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFvdrSFEPLAREVLHLlsSE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 133 YDQLKKFIVAGHKEDWVSIEDEKEKVNDDL--KGADT-----------TRDDLAILSYTSGTTGNPKAVTHSHGWGYAHL 199
Cdd:PLN03102 136 DSNLNLPVIFIHEIDFPKRPSSEELDYECLiqRGEPTpslvarmfriqDEHDPISLNYTSGTTADPKGVVISHRGAYLST 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 200 QMAPKHW---LCIqendlVWATAAPGWQKWVWSPFLSVLGMGATAFVYNGRFHPETYlELLQNYQINVLCCTPTEYRMMA 276
Cdd:PLN03102 216 LSAIIGWemgTCP-----VYLWTLPMFHCNGWTFTWGTAARGGTSVCMRHVTAPEIY-KNIEMHNVTHMCCVPTVFNILL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 277 KLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRhFNITVRDGYGQTESTLLIGFLK-----DTEPRMGSMG----KGIpg 347
Cdd:PLN03102 290 KGNSLDLSPRSGPVHVLTGGSPPPAALVKKVQR-LGFQVMHAYGLTEATGPVLFCEwqdewNRLPENQQMElkarQGV-- 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 348 SFVTVIDDDGKevgpNVKGNIAVPLD----------LPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRR 417
Cdd:PLN03102 367 SILGLADVDVK----NKETQESVPRDgktmgeivikGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRS 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 418 DDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQV-------FCKNEVAP 490
Cdd:PLN03102 443 KDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVDKLVTrerdlieYCRENLPH 522
|
490 500
....*....|....*....|....*...
gi 1801842045 491 YKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PLN03102 523 FMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
43-517 |
4.07e-33 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 132.41 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSS 122
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 LTKEFENVKEYDQLKKFIVAGHKEDWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHG---WGYAHL 199
Cdd:PLN02246 132 YVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKglvTSVAQQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 200 QMAPKHWLCIQENDLVwataapgwqkwvwspfLSVLGM----------------GAtAFVYNGRFHPETYLELLQNYQIN 263
Cdd:PLN02246 212 VDGENPNLYFHSDDVI----------------LCVLPMfhiyslnsvllcglrvGA-AILIMPKFEIGALLELIQRHKVT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 264 VLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQTES----TLLIGFLKdtEP-- 336
Cdd:PLN02246 275 IAPFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKELEDAFRAKLpNAVLGQGYGMTEAgpvlAMCLAFAK--EPfp 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 337 -RMGSMGKGIPGSFVTVID-DDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWF 413
Cdd:PLN02246 353 vKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICI--RGPQIMKGYLNDPEATANTIDKDGWLhTGDIGYIDDDDELFI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 414 EGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQElqvFCKNEVAPYKY 493
Cdd:PLN02246 431 VDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQ---FVAKQVVFYKR 507
|
490 500
....*....|....*....|....
gi 1801842045 494 PRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PLN02246 508 IHKVFFVDSIPKAPSGKILRKDLR 531
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
171-518 |
4.16e-33 |
|
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: 128.60 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 171 DLAILSYTSGTTGNPKAVTHSHgwgYAHL-----------QMAPKHWLCIQEndLV-WATAAPGWqKWVWSPFLSVLGMG 238
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTA---ANLLasaaglhsrlgFGGGDSWLLSLP--LYhVGGLAILV-RSLLAGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 239 ATAFVYNGRFHPETYLELlqnyqinvlccTPTE-YRMMAklSHLEQYNLEYLHSAVSAGEPLNREVVEQF-KRHFNITVr 316
Cdd:cd17630 75 NQALAEDLAPPGVTHVSL-----------VPTQlQRLLD--SGQGPAALKSLRAVLLGGAPIPPELLERAaDRGIPLYT- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 317 dGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPnvkgniavpldlPALFKGYFKDEARTKAASTGdY 396
Cdd:cd17630 141 -TYGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVEDGEIWVGG------------ASLAMGYLRGQLVPEFNEDG-W 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 397 YVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFiilqddYEASDEL 476
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAV------IVGRGPA 280
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1801842045 477 I-QELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd17630 281 DpAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
37-513 |
5.36e-33 |
|
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: 131.03 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 37 HENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMM---PRAIVTYelyIAALKLGIAIVPSSEMLRTKDLQYRITHGE 113
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGenrPEWGIAF---FAIWTYGAIAVPILAEFTADEVHHILNHSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 114 idAVISFSSltkefenvkeydqlkkfivaghkedwvsieDEkekvnddlkgadttrDDLAILSYTSGTTGNPKAV--THS 191
Cdd:cd05914 80 --AKAIFVS------------------------------DE---------------DDVALINYTSGTTGNSKGVmlTYR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 192 HGWGYAHlqmAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATaFVYNGRFhPETYLELLQNYQI--NVLCCTP 269
Cdd:cd05914 113 NIVSNVD---GVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAH-VVFLDKI-PSAKIIALAFAQVtpTLGVPVP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 270 TE-------------------YRMMAKLSHLEQYNLEY--LHSA--------VSAGEPLNREVvEQFKRHFNITVRDGYG 320
Cdd:cd05914 188 LViekifkmdiipkltlkkfkFKLAKKINNRKIRKLAFkkVHEAfggnikefVIGGAKINPDV-EEFLRTIGFPYTIGYG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 321 QTESTLLIGFLKDTEPRMGSMGKGIPGSFVTvIDDDGKEVGPN---VKGniavpldlPALFKGYFKDEARTKAASTGD-Y 396
Cdd:cd05914 267 MTETAPIISYSPPNRIRLGSAGKVIDGVEVR-IDSPDPATGEGeiiVRG--------PNVMKGYYKNPEATAEAFDKDgW 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 397 YVTGDQAHIDNDGYFWFEGRRDDIII-SSGYTIGPFEVEDALTNHAAVKECAVVASPHDIrgnivKAFIILQDDYEASDE 475
Cdd:cd05914 338 FHTGDLGKIDAEGYLYIRGRKKEMIVlSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL-----VALAYIDPDFLDVKA 412
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1801842045 476 LIQ---------ELQVFCKNEVAPYKYPRAIEFV-ENLPKTNSGKIRR 513
Cdd:cd05914 413 LKQrniidaikwEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
36-518 |
9.72e-33 |
|
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: 129.74 E-value: 9.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 36 EHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPssemLRTKDLQYRIthgeiD 115
Cdd:cd17653 17 ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP----LDAKLPSARI-----Q 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 116 AVISFSSltkefenvkeydqlKKFIVAghkedwvsiedekekvnddlkgaDTTRDDLAILSYTSGTTGNPKAVTHSHGwG 195
Cdd:cd17653 88 AILRTSG--------------ATLLLT-----------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHR-G 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 196 YAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFlSVLGMGATAFVyngRFHPETYLELLQnyQINVLCCTPTeyrmm 275
Cdd:cd17653 130 VLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIF-STLCNGGTLVL---ADPSDPFAHVAR--TVDALMSTPS----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 276 aKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKrhFNITVRDGYGQTESTLLIGFlkdTEPRMG---SMGKGIPGSFVTV 352
Cdd:cd17653 199 -ILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWS--PGRRLYNAYGPTECTISSTM---TELLPGqpvTIGKPIPNSTCYI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 353 IDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEART--KAASTGDY-----YVTGDQAHIDNDGYFWFEGRRDDIIISSG 425
Cdd:cd17653 273 LDADLQPVPEGVVGEICI--SGVQVARGYLGNPALTasKFVPDPFWpgsrmYRTGDYGRWTEDGGLEFLGREDNQVKVRG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 426 YTIGPFEVED-ALTNHAAVKECAVVASphdiRGNIVkAFIILQDDYEASdeliqeLQVFCKNEVAPYKYPRAIEFVENLP 504
Cdd:cd17653 351 FRINLEEIEEvVLQSQPEVTQAAAIVV----NGRLV-AFVTPETVDVDG------LRSELAKHLPSYAVPDRIIALDSFP 419
|
490
....*....|....
gi 1801842045 505 KTNSGKIRRVELRD 518
Cdd:cd17653 420 LTANGKVDRKALRE 433
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
41-518 |
1.17e-32 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 131.25 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIvtyELYIAALKL---GIAIVPSSEMLRTKDLQYRITHGEIDAV 117
Cdd:PLN02330 55 AVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVA---EYGIVALGImaaGGVFSGANPTALESEIKKQAEAAGAKLI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 ISfssltkefeNVKEYDQLKKF----IVAGHKE-----DWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAV 188
Cdd:PLN02330 132 VT---------NDTNYGKVKGLglpvIVLGEEKiegavNWKELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 THSHGWGYAHLQMApkhwLCIQENDLVWATAAPGWqkwvwSPFLSVLGMGATAF---------VYNGRFHPETYLELLQN 259
Cdd:PLN02330 203 MLTHRNLVANLCSS----LFSVGPEMIGQVVTLGL-----IPFFHIYGITGICCatlrnkgkvVVMSRFELRTFLNALIT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 260 YQINVLCCTPTEYRMMAKLSHLEQYNLEYL--HSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQTESTLLIgfLKDTEP 336
Cdd:PLN02330 274 QEVSFAPIVPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAPELLTAFEAKFpGVQVQEAYGLTEHSCIT--LTHGDP 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 337 RMG-------SMGKGIPGSFVTVID-DDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTKAASTGDYYV-TGDQAHIDN 407
Cdd:PLN02330 352 EKGhgiakknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ--CVMQGYYNNKEETDRTIDEDGWLhTGDIGYIDD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 408 DGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQElqvFCKNE 487
Cdd:PLN02330 430 DGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILN---FVAAN 506
|
490 500 510
....*....|....*....|....*....|.
gi 1801842045 488 VAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PLN02330 507 VAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
38-516 |
3.04e-32 |
|
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: 129.37 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 38 ENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIvtyELYI---AALKLGIAIVP---------SSEMLRTKDL 105
Cdd:cd17655 19 EDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSL---EMIVgilGILKAGGAYLPidpdypeerIQYILEDSGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 106 QYRITHGEIDAVISFsslTKEFENVKEyDQLKkfivaghkedwvsiEDEKEKVNDDLKGadttrDDLAILSYTSGTTGNP 185
Cdd:cd17655 96 DILLTQSHLQPPIAF---IGLIDLLDE-DTIY--------------HEESENLEPVSKS-----DDLAYVIYTSGSTGKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 186 KAVTHSHGwGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLgMGATAFVYNG--RFHPETYLELLQNYQIN 263
Cdd:cd17655 153 KGVMIEHR-GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLL-SGNTLYIVRKetVLDGQALTQYIRQNRIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 264 VLCCTPTEYRMMAKLSHLEQYNLEYLhsaVSAGEPLNREVVEQFKRHF--NITVRDGYGQTESTL-----LIGFLKDTEP 336
Cdd:cd17655 231 IIDLTPAHLKLLDAADDSEGLSLKHL---IVGGEALSTELAKKIIELFgtNPTITNAYGPTETTVdasiyQYEPETDQQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 337 RMgSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTKA-------ASTGDYYVTGDQAHIDNDG 409
Cdd:cd17655 308 SV-PIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE--GVARGYLNRPELTAEkfvddpfVPGERMYRTGDLARWLPDG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 410 YFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDeliqeLQVFCKNEVA 489
Cdd:cd17655 385 NIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQ-----LREFLARELP 459
|
490 500
....*....|....*....|....*..
gi 1801842045 490 PYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd17655 460 DYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
43-525 |
1.88e-31 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 127.95 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSS 122
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDLT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 LTKEFENVKeyDQL---KKFIVAGHKE--------DWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHS 191
Cdd:PRK06018 121 FVPILEKIA--DKLpsvERYVVLTDAAhmpqttlkNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 192 HGWGYAHLQMA-PKHWLCIQENDLVWATAaPGWQKWVWSPFLSVLGMGATAFVYNGRFHPETYLELLQNYQINVLCCTPT 270
Cdd:PRK06018 199 HRSNVLHALMAnNGDALGTSAADTMLPVV-PLFHANSWGIAFSAPSMGTKLVMPGAKLDGASVYELLDTEKVTFTAGVPT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 271 EYRMMakLSHLEQYNLE--YLHSAVSAGEPLNREVVEQFKRhFNITVRDGYGQTESTLL--IGFLKDT------EPRMGS 340
Cdd:PRK06018 278 VWLML--LQYMEKEGLKlpHLKMVVCGGSAMPRSMIKAFED-MGVEVRHAWGMTEMSPLgtLAALKPPfsklpgDARLDV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 341 MGK-GIP--GSFVTVIDDDGKEVGPNVK--GNIAVplDLPALFKGYFKdeARTKAASTGDYYVTGDQAHIDNDGYFWFEG 415
Cdd:PRK06018 355 LQKqGYPpfGVEMKITDDAGKELPWDGKtfGRLKV--RGPAVAAAYYR--VDGEILDDDGFFDTGDVATIDAYGYMRITD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 416 RRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAS-DELIQelqvFCKNEVAPYKYP 494
Cdd:PRK06018 431 RSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATrEEILK----YMDGKIAKWWMP 506
|
490 500 510
....*....|....*....|....*....|.
gi 1801842045 495 RAIEFVENLPKTNSGKIRRVELRDaEIKKYQ 525
Cdd:PRK06018 507 DDVAFVDAIPHTATGKILKTALRE-QFKDYK 536
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
41-518 |
5.99e-31 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 126.49 E-value: 5.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELI----SNANKVGNVFlnhGLKKGDKVLIMMPRAIVTYELYIAALKLGiAIV----PSSEML----RTKDLQYR 108
Cdd:PLN02574 66 SISYSELQplvkSMAAGLYHVM---GVRQGDVVLLLLPNSVYFPVIFLAVLSLG-GIVttmnPSSSLGeikkRVVDCSVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 109 ITHGEIDAVISFSSLTKEFENVKEYDQLKKFIVAGHKEDWVSIEDekekvNDDLKGADTTRDDLAILSYTSGTTGNPKAV 188
Cdd:PLN02574 142 LAFTSPENVEKLSPLGVPVIGVPENYDFDSKRIEFPKFYELIKED-----FDFVPKPVIKQDDVAAIMYSSGTTGASKGV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 THSHGWGYAHLQMAPKHWLCIQEN---DLVWATAAPGWQKWVWSPF-LSVLGMGATAFVYNgRFHPETYLELLQNYQINV 264
Cdd:PLN02574 217 VLTHRNLIAMVELFVRFEASQYEYpgsDNVYLAALPMFHIYGLSLFvVGLLSLGSTIVVMR-RFDASDMVKVIDRFKVTH 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 265 LCCTPTeyrMMAKLSHLEQ----YNLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQTESTLL--IGFLKDTEPR 337
Cdd:PLN02574 296 FPVVPP---ILMALTKKAKgvcgEVLKSLKQVSCGAAPLSGKFIQDFVQTLpHVDFIQGYGMTESTAVgtRGFNTEKLSK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 338 MGSMGKGIPGSFVTVID-DDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEG 415
Cdd:PLN02574 373 YSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELW--IQGPGVMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVD 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 416 RRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQElqvFCKNEVAPYKYPR 495
Cdd:PLN02574 451 RLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVIN---YVAKQVAPYKKVR 527
|
490 500
....*....|....*....|...
gi 1801842045 496 AIEFVENLPKTNSGKIRRVELRD 518
Cdd:PLN02574 528 KVVFVQSIPKSPAGKILRRELKR 550
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
36-516 |
1.05e-30 |
|
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: 124.29 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 36 EHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRA--IVTYELyiAALKLGIAIVPSsemlrtkDLQY---RIT 110
Cdd:cd17652 7 VFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSaeLVVAIL--AVLKAGAAYLPL-------DPAYpaeRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 111 HGEIDAVISFssltkefenvkeydqlkkfIVaghkedwvsiedekekvnddlkgadTTRDDLAILSYTSGTTGNPK--AV 188
Cdd:cd17652 78 YMLADARPAL-------------------LL-------------------------TTPDNLAYVIYTSGSTGRPKgvVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 THShgwGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSpFLSVLGMGATAFVY--NGRFHPETYLELLQNYQINVLC 266
Cdd:cd17652 114 THR---GLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWE-LLMALLAGATLVLApaEELLPGEPLADLLREHRITHVT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 267 CTPteyrmmAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQF---KRHFNitvrdGYGQTESTLLIGFLK-DTEPRMGSMG 342
Cdd:cd17652 190 LPP------AALAALPPDDLPDLRTLVVAGEACPAELVDRWapgRRMIN-----AYGPTETTVCATMAGpLPGGGVPPIG 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 343 KGIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTK--------AASTGDYYVTGDQAHIDNDGYFWFE 414
Cdd:cd17652 259 RPVPGTRVYVLDARLRPVPPGVPGELY--IAGAGLARGYLNRPGLTAerfvadpfGAPGSRMYRTGDLARWRADGQLEFL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 415 GRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliqELQVFCKNEVAPYKYP 494
Cdd:cd17652 337 GRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAA---ELRAHLAERLPGYMVP 413
|
490 500
....*....|....*....|..
gi 1801842045 495 RAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd17652 414 AAFVVLDALPLTPNGKLDRRAL 435
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
172-513 |
3.36e-30 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 124.85 E-value: 3.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 172 LAILsYTSGTTGNPKAVTHSHGwgyAHLQMAPKHWLCIQENDL---VWATAAPGWQKWvWSPFLSVLGMGATAFVYNGRF 248
Cdd:PTZ00237 257 LYIL-YTSGTTGNSKAVVRSNG---PHLVGLKYYWRSIIEKDIptvVFSHSSIGWVSF-HGFLYGSLSLGNTFVMFEGGI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 249 ----HPETYL-ELLQNYQINVLCCTPTEYRMMAKL----SHLE-QYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDG 318
Cdd:PTZ00237 332 iknkHIEDDLwNTIEKHKVTHTLTLPKTIRYLIKTdpeaTIIRsKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 319 YGQTES--TLLIGFLKDTEPRMGSmgkGIPGSFV--TVIDDDGKEVGPNVKGNIAVPLDLPALFKG-YFKDEARTKAAST 393
Cdd:PTZ00237 412 YGQTEIgiTYLYCYGHINIPYNAT---GVPSIFIkpSILSEDGKELNVNEIGEVAFKLPMPPSFATtFYKNDEKFKQLFS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 394 G--DYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIIL-QDDY 470
Cdd:PTZ00237 489 KfpGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLkQDQS 568
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1801842045 471 EASDELIQ---ELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:PTZ00237 569 NQSIDLNKlknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPR 614
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
165-518 |
3.47e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 124.02 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 165 ADTTRDDLAILSYTSGTTGNPKAVTHSHG-WGYAHLQMAPK--------HWLCI---QENDLV--WATAAPG------WQ 224
Cdd:PRK07867 147 RVADPDDLFMLIFTSGTSGDPKAVRCTHRkVASAGVMLAQRfglgpddvCYVSMplfHSNAVMagWAVALAAgasialRR 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 225 KWVWSPFLS-VLGMGATAFVYNGRfhPETYLellqnyqinvlCCTP-------TEYRMMaklshleqynleYLHSAVSAG 296
Cdd:PRK07867 227 KFSASGFLPdVRRYGATYANYVGK--PLSYV-----------LATPerpddadNPLRIV------------YGNEGAPGD 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 297 eplnrevVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPrmGSMGKGIPGsfVTVID-DDGKEVGPNV-------KGNI 368
Cdd:PRK07867 282 -------IARFARRFGCVVVDGFGSTEGGVAITRTPDTPP--GALGPLPPG--VAIVDpDTGTECPPAEdadgrllNADE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 369 A----VPLDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVK 444
Cdd:PRK07867 351 AigelVNTAGPGGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDAT 430
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801842045 445 ECAVVASPHDIRGNIVKAFIILQD----DYEASDELIQElqvfcKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK07867 431 EVAVYAVPDPVVGDQVMAALVLAPgakfDPDAFAEFLAA-----QPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
172-509 |
1.44e-29 |
|
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: 118.94 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 172 LAIlsYTSGTTGNPKAVTHSH-GWGYAHLQMAPKHWLciqENDLVWATAAPGWQKWVWSPFLSVLGMGATAfVYNGRFHP 250
Cdd:cd17636 4 LAI--YTAAFSGRPNGALLSHqALLAQALVLAVLQAI---DEGTVFLNSGPLFHIGTLMFTLATFHAGGTN-VFVRRVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 251 ETYLELLQNYQinvlcCT------PTEYRMMaKLSHLEQYNLEYLHSAVSAGE--PLNREVVEQFKRHFNitvrdGYGQT 322
Cdd:cd17636 78 EEVLELIEAER-----CThafllpPTIDQIV-ELNADGLYDLSSLRSSPAAPEwnDMATVDTSPWGRKPG-----GYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 323 ESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQ 402
Cdd:cd17636 147 EVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVA--RGPTVMAGYWNRPEVNARRTRGGWHHTNDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 403 AHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAS-DELIQElq 481
Cdd:cd17636 225 GRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTeAELIEH-- 302
|
330 340
....*....|....*....|....*...
gi 1801842045 482 vfCKNEVAPYKYPRAIEFVENLPKTNSG 509
Cdd:cd17636 303 --CRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
36-513 |
1.95e-29 |
|
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: 120.86 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 36 EHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPR---AIVTYelyIAALKLGIAIVPSSEMLRTKDLQYRITHG 112
Cdd:cd12116 7 RDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRsarLVAAM---LAVLKAGAAYVPLDPDYPADRLRYILEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 113 EIDAVISfssltkefenvkEYDQLKKFIVAGhkedwvsieDEKEKVNDDLKGADTTR------DDLAILSYTSGTTGNPK 186
Cdd:cd12116 84 EPALVLT------------DDALPDRLPAGL---------PVLLLALAAAAAAPAAPrtpvspDDLAYVIYTSGSTGRPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 187 AVTHSHGwGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGmGATAFVYNG--RFHPETYLELLQNYQINV 264
Cdd:cd12116 143 GVVVSHR-NLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLA-GARVVIAPRetQRDPEALARLIEAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 265 LCCTPTEYRMMAKLshlEQYNLEYLHsAVSAGEPLNREVVEQFKRH----FNItvrdgYGQTESTL--LIGFLKDTEPRM 338
Cdd:cd12116 221 MQATPATWRMLLDA---GWQGRAGLT-ALCGGEALPPDLAARLLSRvgslWNL-----YGPTETTIwsTAARVTAAAGPI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 339 gSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKAA--------STGDYYVTGDQAHIDNDGY 410
Cdd:cd12116 292 -PIGRPLANTQVYVLDAALRPVPPGVPGELY--IGGDGVAQGYLGRPALTAERfvpdpfagPGSRLYRTGDLVRRRADGR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 411 FWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVkAFIILQDDYEASdelIQELQVFCKNEVAP 490
Cdd:cd12116 369 LEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVLKAGAAPD---AAALRAHLRATLPA 444
|
490 500
....*....|....*....|...
gi 1801842045 491 YKYPRAIEFVENLPKTNSGKIRR 513
Cdd:cd12116 445 YMVPSAFVRLDALPLTANGKLDR 467
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
29-516 |
1.70e-28 |
|
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: 118.35 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYkdnehENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYR 108
Cdd:cd17656 6 AVVF-----ENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 109 ITHGEIDAVISFSSLTKEFENVKEYDQLKKFIVAghKEDWVSIEDEKEKvnddlkgadttrDDLAILSYTSGTTGNPKAV 188
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSIS--QEDTSNIDYINNS------------DDLLYIIYTSGTTGKPKGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 THSHGwGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATAFVYNG-RFHPETYLELLQNYQINVLCC 267
Cdd:cd17656 147 QLEHK-NMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREEtKRDVEQLFDLVKRHNIEVVFL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 268 TPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPL--NREVVEQFKRHfNITVRDGYGQTESTLLIGFLKDTE---PRMGSMG 342
Cdd:cd17656 226 PVAFLKFIFSEREFINRFPTCVKHIITAGEQLviTNEFKEMLHEH-NVHLHNHYGPSETHVVTTYTINPEaeiPELPPIG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 343 KGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGD-------YYVTGDQAHIDNDGYFWFEG 415
Cdd:cd17656 305 KPISNTWIYILDQEQQLQPQGIVGELYI--SGASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 416 RRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEasdelIQELQVFCKNEVAPYKYPR 495
Cdd:cd17656 383 RADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN-----ISQLREYLAKQLPEYMIPS 457
|
490 500
....*....|....*....|.
gi 1801842045 496 AIEFVENLPKTNSGKIRRVEL 516
Cdd:cd17656 458 FFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
27-516 |
3.00e-28 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 118.18 E-value: 3.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYKDNeheniSVSYKELISNANKVGNVFLNHGLKKGDKVLIMMP--RAIVTYELyiAALKLGIAIVPSSEMLRTKD 104
Cdd:PRK13383 51 RTAIIDDDG-----ALSYRELQRATESLARRLTRDGVAPGRAVGVMCRngRGFVTAVF--AVGLLGADVVPISTEFRSDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 105 LQYRITHGEIDAVISfsslTKEFenvkeYDQlkkfiVAGhKEDWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGN 184
Cdd:PRK13383 124 LAAALRAHHISTVVA----DNEF-----AER-----IAG-ADDAVAVIDPATAGAEESGGRPAVAAPGRIVLLTSGTTGK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 185 PKAVTHShgwgyAHLQMAPKHWLCIQENDLV-----WATAAPGWQKWVWSPFLSVLGMGATAFVYNgRFHPETYLELLQN 259
Cdd:PRK13383 189 PKGVPRA-----PQLRSAVGVWVTILDRTRLrtgsrISVAMPMFHGLGLGMLMLTIALGGTVLTHR-HFDAEAALAQASL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 260 YQINVLCCTPTeyrMMAKLSHL-----EQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTEstLLIGFLK-- 332
Cdd:PRK13383 263 HRADAFTAVPV---VLARILELpprvrARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTE--VGIGALAtp 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 333 -DTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPAlfKGYfkDEARTKAASTGdYYVTGDQAHIDNDGYF 411
Cdd:PRK13383 338 aDLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAG--TRY--TDGGGKAVVDG-MTSTGDMGYLDNAGRL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 412 WFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQddyEASDELIQELQVFCKNEVAPY 491
Cdd:PRK13383 413 FIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLH---PGSGVDAAQLRDYLKDRVSRF 489
|
490 500
....*....|....*....|....*
gi 1801842045 492 KYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:PRK13383 490 EQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
38-513 |
4.31e-28 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 117.68 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 38 ENISVSYKELISNANKVGNVFLNHGLKKGDKVLImmpRAIVTYELYI---AALKLGIAIVPSSEMLRTKDLQYRITHGEI 114
Cdd:PRK05852 40 DRIAISYRDLARLVDDLAGQLTRSGLLPGDRVAL---RMGSNAEFVVallAASRADLVVVPLDPALPIAEQRVRSQAAGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 115 DAVISFSslTKEFENVKEYDQLKKFIVA-----GHKEDWVSIE-DEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAV 188
Cdd:PRK05852 117 RVVLIDA--DGPHDRAEPTTRWWPLTVNvggdsGPSGGTLSVHlDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 ThshgWGYAHLQmAPKHWLC----IQENDlvwATAA--PGWQ-KWVWSPFLSVLGMGATAFV-YNGRFHPETYLELLQNY 260
Cdd:PRK05852 195 P----WTHANIA-SSVRAIItgyrLSPRD---ATVAvmPLYHgHGLIAALLATLASGGAVLLpARGRFSAHTFWDDIKAV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 261 QINVLCCTPTEYRMMAKLSHLEQYN-----LEYLHSAvSAgePLNREVVEQFKRHFNITVRDGYGQTE------STLLIG 329
Cdd:PRK05852 267 GATWYTAVPTIHQILLERAATEPSGrkpaaLRFIRSC-SA--PLTAETAQALQTEFAAPVVCAFGMTEathqvtTTQIEG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 330 FLKDTEPRM--GSMGKGIpGSFVTVIDDDGKEVGPNVKGNiaVPLDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDN 407
Cdd:PRK05852 344 IGQTENPVVstGLVGRST-GAQIRIVGSDGLPLPAGAVGE--VWLRGTTVVRGYLGDPTITAANFTDGWLRTGDLGSLSA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 408 DGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQddyEASDELIQELQVFCKNE 487
Cdd:PRK05852 421 AGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPR---ESAPPTAEELVQFCRER 497
|
490 500
....*....|....*....|....*.
gi 1801842045 488 VAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:PRK05852 498 LAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
16-519 |
8.23e-28 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 117.00 E-value: 8.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 16 SEIEKYASEDHK-KAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIV 94
Cdd:cd05906 13 LELLLRAAERGPtKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 95 PS-----SEMLRTKDLQYRITHGEID--AVISFSSLTKEFENVKEYDqlkkfivaGHKEDWVSIEDEKEKVNDDLKGADT 167
Cdd:cd05906 93 PLtvpptYDEPNARLRKLRHIWQLLGspVVLTDAELVAEFAGLETLS--------GLPGIRVLSIEELLDTAADHDLPQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 168 TRDDLAILSYTSGTTGNPKAVTHSHGwgyahlQM----APKHWLCI---QENDLVWAtaapgwqkwvwsPFLSV--LGMG 238
Cdd:cd05906 165 RPDDLALLMLTSGSTGFPKAVPLTHR------NIlarsAGKIQHNGltpQDVFLNWV------------PLDHVggLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 239 ATAFVYNG--RFH---------PETYLELLQNYQINVlccTPTEYRMMAKLS-HLEQ-----YNLEYLHSAVSAGEPLNR 301
Cdd:cd05906 227 HLRAVYLGcqQVHvpteeiladPLRWLDLIDRYRVTI---TWAPNFAFALLNdLLEEiedgtWDLSSLRYLVNAGEAVVA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 302 EVVEQF----KRH-FNITV-RDGYGQTES----TLLIGFLKDT---EPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNI 368
Cdd:cd05906 304 KTIRRLlrllEPYgLPPDAiRPAFGMTETcsgvIYSRSFPTYDhsqALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 369 AVplDLPALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNdGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECA 447
Cdd:cd05906 384 QV--RGPVVTKGYYNNPEANAEAFTEDgWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 448 VVASPHDIRGNIVKAFIIL----QDDYEASDELIQELQVFCKNEVApykypRAIEFV-----ENLPKTNSGKIRRVELRD 518
Cdd:cd05906 461 TAAFAVRDPGAETEELAIFfvpeYDLQDALSETLRAIRSVVSREVG-----VSPAYLiplpkEEIPKTSLGKIQRSKLKA 535
|
.
gi 1801842045 519 A 519
Cdd:cd05906 536 A 536
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
38-516 |
8.87e-28 |
|
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: 115.88 E-value: 8.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 38 ENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRaivTYELYI---AALKLGIAIVPSSEMLRTKDLQYRITHGEI 114
Cdd:cd12115 21 GDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLER---TPDLVVallAVLKAGAAYVPLDPAYPPERLRFILEDAQA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 115 DAVIsfssltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadTTRDDLAILSYTSGTTGNPKAVTHSHGW 194
Cdd:cd12115 98 RLVL------------------------------------------------TDPDDLAYVIYTSGSTGRPKGVAIEHRN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 195 GYAHLQMAPKHWlCIQENDLVWATAAPGWQKWVWSPFLSvLGMGATAFVYNGRFHPETYLELLQNYQINVLcctPTeyrM 274
Cdd:cd12115 130 AAAFLQWAAAAF-SAEELAGVLASTSICFDLSVFELFGP-LATGGKVVLADNVLALPDLPAAAEVTLINTV---PS---A 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 275 MAKLshLEQYNLEYLHSAVS-AGEPLNREVVEQFKRHFNIT-VRDGYGQTEST-----LLIGFLKDTEPrmgSMGKGIPG 347
Cdd:cd12115 202 AAEL--LRHDALPASVRVVNlAGEPLPRDLVQRLYARLQVErVVNLYGPSEDTtystvAPVPPGASGEV---SIGRPLAN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 348 SFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKA-------ASTGDYYVTGDQAHIDNDGYFWFEGRRDDI 420
Cdd:cd12115 277 TQAYVLDRALQPVPLGVPGELY--IGGAGVARGYLGRPGLTAErflpdpfGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 421 IISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAsdeLIQELQVFCKNEVAPYKYPRAIEFV 500
Cdd:cd12115 355 VKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG---LVEDLRRHLGTRLPAYMVPSRFVRL 431
|
490
....*....|....*.
gi 1801842045 501 ENLPKTNSGKIRRVEL 516
Cdd:cd12115 432 DALPLTPNGKIDRSAL 447
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
162-511 |
2.37e-27 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 116.95 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 162 LKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQmAPKHWLCIQENDLVWATAAP----GWQKWVWSPFLSvlGM 237
Cdd:PRK08633 774 LYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDVFNLRNDDVILSSLPFfhsfGLTVTLWLPLLE--GI 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 238 GAtafVYngrfHP-----ETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFN 312
Cdd:PRK08633 851 KV---VY----HPdptdaLGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFG 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 313 ITVRDGYGQTESTLLI----------GFLKDTEPRMGSMGKGIPGSFVTVID-DDGKEVGPNVKGNIAVplDLPALFKGY 381
Cdd:PRK08633 924 IRILEGYGATETSPVAsvnlpdvlaaDFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILI--GGPQVMKGY 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 382 FKDEARTKAA----STGDYYVTGDQAHIDNDGYFWFEGR--RDDII----ISSGytigpfEVEDALtnHAAVK----ECA 447
Cdd:PRK08633 1002 LGDPEKTAEVikdiDGIGWYVTGDKGHLDEDGFLTITDRysRFAKIggemVPLG------AVEEEL--AKALGgeevVFA 1073
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801842045 448 VVASPHDIRGnivKAFIILqddYEASDELIQELQVFCKN-EVAPYKYPRAIEFVENLPKTNSGKI 511
Cdd:PRK08633 1074 VTAVPDEKKG---EKLVVL---HTCGAEDVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
29-511 |
4.13e-27 |
|
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: 114.03 E-value: 4.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKDNeheniSVSYKELISNANKVGNVFLNHGLKKGDK-VLIMMPRAIVTYELYIAALKLGIAIVPssemlrtkdlqy 107
Cdd:cd17648 5 AVVYGDK-----RLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVP------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 108 rithgeIDAvisfssltkefenvkEY-DQLKKFIVaghkedwvsiEDEKekvnddLKGADTTRDDLAILSYTSGTTGNPK 186
Cdd:cd17648 68 ------IDP---------------SYpDERIQFIL----------EDTG------ARVVITNSTDLAYAIYTSGTTGKPK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 187 AVTHSHGwGYAHLQMA-PKHWLCIQENDLVWATAApgwqKWVWSPF-----LSVLGmGATAFVYN--GRFHPETYLELLQ 258
Cdd:cd17648 111 GVLVEHG-SVVNLRTSlSERYFGRDNGDEAVLFFS----NYVFDFFveqmtLALLN-GQKLVVPPdeMRFDPDRFYAYIN 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 259 NYQINVLCCTPTEyrmmakLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTL--LIGFLKDTEP 336
Cdd:cd17648 185 REKVTYLSGTPSV------LQQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVtnHKRFFPGDQR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 337 RMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPAlfKGYFKDEART------------KAASTGDY---YVTGD 401
Cdd:cd17648 259 FDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVA--RGYLNRPELTaerflpnpfqteQERARGRNarlYKTGD 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 402 QAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVAS--PHDIRGNIVKAFI-ILQDDYEASDEliQ 478
Cdd:cd17648 337 LVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKedASQAQSRIQKYLVgYYLPEPGHVPE--S 414
|
490 500 510
....*....|....*....|....*....|...
gi 1801842045 479 ELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKI 511
Cdd:cd17648 415 DLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-526 |
6.18e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.21 E-value: 6.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFS 121
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 122 SLTKEFENVKEYDQLkkfiVAGHKEDWVSIEDEKEKVNDDlkgadttRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQ- 200
Cdd:PRK12316 4657 HLLQRLPIPDGLASL----ALDRDEDWEGFPAHDPAVRLH-------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHa 4725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 201 MAPKHWLCIQENDLVWATAAPGWQKWVWSPflsVLGMGATAFVYNGRFH-PETYLELLQNYQINVLCCTPTEYRMMAKLS 279
Cdd:PRK12316 4726 TGERYELTPDDRVLQFMSFSFDGSHEGLYH---PLINGASVVIRDDSLWdPERLYAEIHEHRVTVLVFPPVYLQQLAEHA 4802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 280 HlEQYNLEYLHSAVSAGEPLNREVVEQ-FKRHFNITVRDGYGQTEST---LLIGFLKDTEPRMGSM--GKGIPGSFVTVI 353
Cdd:PRK12316 4803 E-RDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTvtvLLWKARDGDACGAAYMpiGTPLGNRSGYVL 4881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 354 DDDGKEVGPNVKGNIAVPLDLPAlfKGYFKDEARTKA--------ASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSG 425
Cdd:PRK12316 4882 DGQLNPLPVGVAGELYLGGEGVA--RGYLERPALTAErfvpdpfgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRG 4959
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 426 YTIGPFEVEDALTNHAAVKECAVVASP----HDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVE 501
Cdd:PRK12316 4960 FRIELGEIEARLREHPAVREAVVIAQEgavgKQLVGYVVPQDPALADADEAQAELRDELKAALRERLPEYMVPAHLVFLA 5039
|
490 500
....*....|....*....|....*
gi 1801842045 502 NLPKTNSGKIRRVELRDAEIKKYQQ 526
Cdd:PRK12316 5040 RMPLTPNGKLDRKALPQPDASLLQQ 5064
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
38-518 |
1.50e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 113.30 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 38 ENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAV 117
Cdd:PRK06164 32 EDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 I---SFSSLtKEFENVKEYDQ-----LKKFIVAGHKED---------WVSIEDEKEKVNDDLKGADTTRDDLAILSYT-S 179
Cdd:PRK06164 112 VvwpGFKGI-DFAAILAAVPPdalppLRAIAVVDDAADatpapapgaRVQLFALPDPAPPAAAGERAADPDAGALLFTtS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 180 GTTGNPKAVTHS------HGWGYAHLqmapkhwLCIQENDLVWATAapgwqkwvwsPFLSVLGM-GATAFVYNGR----- 247
Cdd:PRK06164 191 GTTSGPKLVLHRqatllrHARAIARA-------YGYDPGAVLLAAL----------PFCGVFGFsTLLGALAGGAplvce 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 248 --FHPETYLELLQNYQINVLCCTPTEYRMMAK-------LSHLEQYNL--------EYLHSAVSAGEPLnrevveqfkrh 310
Cdd:PRK06164 254 pvFDAARTARALRRHRVTHTFGNDEMLRRILDtageradFPSARLFGFasfapalgELAALARARGVPL----------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 311 fnitvRDGYGQTE-STLLIGFLKDTEPRMGSMGKGIPGS---FVTVID-DDGKEVGPNVKGNIAVplDLPALFKGYFKDE 385
Cdd:PRK06164 323 -----TGLYGSSEvQALVALQPATDPVSVRIEGGGRPASpeaRVRARDpQDGALLPDGESGEIEI--RAPSLMRGYLDNP 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 386 ARTKAASTGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDirGNIVK-AF 463
Cdd:PRK06164 396 DATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD--GKTVPvAF 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801842045 464 IILQDDYEAsDEliQELQVFCKNEVAPYKYPRAIEFVENLPKT---NSGKIRRVELRD 518
Cdd:PRK06164 474 VIPTDGASP-DE--AGLMAACREALAGFKVPARVQVVEAFPVTesaNGAKIQKHRLRE 528
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
26-517 |
1.85e-26 |
|
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: 112.08 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYKDNeheniSVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSsemlrtkDL 105
Cdd:cd17649 2 DAVALVFGDQ-----SLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPL-------DP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 106 QY---RITHGEIDAVISfssltkefenvkeydqlkkfIVAGHkedwvsiedekekvnddlkgadtTRDDLAILSYTSGTT 182
Cdd:cd17649 70 EYpaeRLRYMLEDSGAG--------------------LLLTH-----------------------HPRQLAYVIYTSGST 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 183 GNPKAVTHSHGWGYAHLQMAPKHW-LCIQENDLVWAT-----AAPGWqkwvwspfLSVLGMGATAFVYN-GRFH-PETYL 254
Cdd:cd17649 107 GTPKGVAVSHGPLAAHCQATAERYgLTPGDRELQFASfnfdgAHEQL--------LPPLICGACVVLRPdELWAsADELA 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 255 ELLQNYQINVLCCTPTEYRMMAK-LSHLEQYNLEYLHSAVSAGEPLNrevVEQFKRHFNITVR--DGYGQTESTLlIGFL 331
Cdd:cd17649 179 EMVRELGVTVLDLPPAYLQQLAEeADRTGDGRPPSLRLYIFGGEALS---PELLRRWLKAPVRlfNAYGPTEATV-TPLV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 332 KDTEPRMGS------MGKGIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTK--------AASTGDYY 397
Cdd:cd17649 255 WKCEAGAARagasmpIGRPLGGRSAYILDADLNPVPVGVTGELY--IGGEGLARGYLGRPELTAerfvpdpfGAPGSRLY 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 398 VTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVkAFIILQDDyEASDELI 477
Cdd:cd17649 333 RTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAA-AAQPELR 410
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1801842045 478 QELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd17649 411 AQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
13-480 |
8.57e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 111.14 E-value: 8.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 13 NIVSEIEKYASED-HKKAII-----YKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAA 86
Cdd:PRK09274 7 NIARHLPRAAQERpDQLAVAvpggrGADGKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 87 LKLGIAIV---PSsemLRTKDLQYRITHGEIDAVI--------------SFSSLtkefenvkeydqlKKFIVAGHKEDW- 148
Cdd:PRK09274 87 FKAGAVPVlvdPG---MGIKNLKQCLAEAQPDAFIgipkahlarrlfgwGKPSV-------------RRLVTVGGRLLWg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 149 -VSIED-EKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQmAPKHWLCIQ--ENDLvwATAapgwq 224
Cdd:PRK09274 151 gTTLATlLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIE-ALREDYGIEpgEIDL--PTF----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 225 kwvwsPFLSVLG--MGATAFVYN------GRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAG 296
Cdd:PRK09274 223 -----PLFALFGpaLGMTSVIPDmdptrpATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 297 EPLNREVVEQFKRHFNITVR--DGYGQTES---------TLLIGFLKDTEPRMGS-MGKGIPGSFVTVID---------D 355
Cdd:PRK09274 298 APVPIAVIERFRAMLPPDAEilTPYGATEAlpissiesrEILFATRAATDNGAGIcVGRPVDGVEVRIIAisdapipewD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 356 DGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAA-----STGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGP 430
Cdd:PRK09274 378 DALRLATGEIGEIVV--AGPMVTRSYYNRPEATRLAkipdgQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYT 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1801842045 431 FEVEDALTNHAAVKECAVVAspHDIRGNIVKAFII--LQDDYEASDELIQEL 480
Cdd:PRK09274 456 IPCERIFNTHPGVKRSALVG--VGVPGAQRPVLCVelEPGVACSKSALYQEL 505
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
27-517 |
9.78e-26 |
|
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: 110.60 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 27 KKAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVP-----SSEML- 100
Cdd:cd05915 10 RKEVVSRLHTGEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTanprlSPKEIa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 101 ----RTKDLQYRITHGEID-AVISFSSLTKEFENVKEYDQLKKFivaghkEDWVSIEDEKEKvndDLKGADTTrdDLAIL 175
Cdd:cd05915 90 yilnHAEDKVLLFDPNLLPlVEAIRGELKTVQHFVVMDEKAPEG------YLAYEEALGEEA---DPVRVPER--AACGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 176 SYTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLGMGATAFVYNGRFHPETYLE 255
Cdd:cd05915 159 AYTTGTTGLPKGVVYSHRALVLHSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 256 LLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPlNREVVEQFKRHFNITVRDGYGQTE-----STLLIGF 330
Cdd:cd05915 239 LFDGEGVTFTAGVPTVWLALADYLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTEtspvvVQNFVKS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 331 LKDTEPRMGSM------GKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPALFKGYFKDEARTKA-ASTGDYYVTGDQA 403
Cdd:cd05915 318 HLESLSEEEKLtlkaktGLPIPLVRLRVADEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSaLTPDGFFRTGDIA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 404 HIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDELIQelqvF 483
Cdd:cd05915 398 VWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEELNE----H 473
|
490 500 510
....*....|....*....|....*....|....*
gi 1801842045 484 CKNEVAPYKY-PRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05915 474 LLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
86-518 |
1.18e-25 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 110.70 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 86 ALKLGIAIVPSSEMLRTKDLQYRITHGEIdavisfssltkefenvkEYDqlkKFIVAGHKE-DWVSIEDEKEKVnddlkg 164
Cdd:PLN02479 145 SFKPPLLIVIGDPTCDPKSLQYALGKGAI-----------------EYE---KFLETGDPEfAWKPPADEWQSI------ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 165 adttrddlaILSYTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVLG-------- 236
Cdd:PLN02479 199 ---------ALGYTSGTTASPKGVVLHHRGAYLMALSNALIWGMNEGAVYLWTLPMFHCNGWCFTWTLAALCgtniclrq 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 237 MGATAfVYNGrfhpetylelLQNYQINVLCCTPTEYRMMAK---------LSHLeqynleyLHSAVSAGEPLNREVVEQF 307
Cdd:PLN02479 270 VTAKA-IYSA----------IANYGVTHFCAAPVVLNTIVNapksetilpLPRV-------VHVMTAGAAPPPSVLFAMS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 308 KRHFNITVRDGYGQTESTLLIGFLK---DTEP---------RMGSMGKGIPGsfVTVIDD--------DGKEVGPNV-KG 366
Cdd:PLN02479 332 EKGFRVTHTYGLSETYGPSTVCAWKpewDSLPpeeqarlnaRQGVRYIGLEG--LDVVDTktmkpvpaDGKTMGEIVmRG 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 367 NiavpldlpALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKEC 446
Cdd:PLN02479 410 N--------MVMKGYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEA 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801842045 447 AVVASPHDIRGNIVKAFIILQDDYEASDE--LIQELQVFCKNEVAPYKYPRAIEFvENLPKTNSGKIRRVELRD 518
Cdd:PLN02479 482 SVVARPDERWGESPCAFVTLKPGVDKSDEaaLAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRA 554
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
165-518 |
3.49e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 108.96 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 165 ADTTRDDLAILSYTSGTTGNPKAVTHSHGW-GYAHLQMAPKHWLCIQENDLV-------------WATA-APGW-----Q 224
Cdd:PRK13388 145 REVDAMDPFMLIFTSGTTGAPKAVRCSHGRlAFAGRALTERFGLTRDDVCYVsmplfhsnavmagWAPAvASGAavalpA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 225 KWVWSPFLS-VLGMGATAFVYNGRfhPETYLellqnyqinvlcctpteyrmMAKLSHLEQynleylhsavsAGEPLNR-- 301
Cdd:PRK13388 225 KFSASGFLDdVRRYGATYFNYVGK--PLAYI--------------------LATPERPDD-----------ADNPLRVaf 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 302 ------EVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPrmGSMGKGIPGsfVTVIDDDGKEVGP----NVKGNIAVP 371
Cdd:PRK13388 272 gneaspRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTPP--GSIGRGAPG--VAIYNPETLTECAvarfDAHGALLNA 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 372 LDL---------PALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAA 442
Cdd:PRK13388 348 DEAigelvntagAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPA 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801842045 443 VKECAVVASPHDIRGNIVKAFIILQDDyeaSDELIQELQVF--CKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:PRK13388 428 INRVAVYAVPDERVGDQVMAALVLRDG---ATFDPDAFAAFlaAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
29-516 |
1.02e-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: 106.97 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKDnehenISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYR 108
Cdd:cd12114 5 AVICGD-----GTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 109 ITHGEIDAVISFSSLTKEFENVkeydqlkkfivaghkEDWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAV 188
Cdd:cd12114 80 LADAGARLVLTDGPDAQLDVAV---------------FDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 THSHgwgyahlQMAPKHWLCIQE------NDLVWATAAPGWQKWVWSPFlSVLGMGATAFVYNG--RFHPETYLELLQNY 260
Cdd:cd12114 145 MISH-------RAALNTILDINRrfavgpDDRVLALSSLSFDLSVYDIF-GALSAGATLVLPDEarRRDPAHWAELIERH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 261 QINVLCCTPTEYRMMakLSHLEQYNLEY------LHSAVSAGEPLNREVVEQFKrhfNITVRDGYGQTE----STLL-IG 329
Cdd:cd12114 217 GVTLWNSVPALLEML--LDVLEAAQALLpslrlvLLSGDWIPLDLPARLRALAP---DARLISLGGATEasiwSIYHpID 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 330 flkDTEPRMGSM--GKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLPALfkGYFKDEARTKA-----ASTGDYYVTGDQ 402
Cdd:cd12114 292 ---EVPPDWRSIpyGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVAL--GYLGDPELTAArfvthPDGERLYRTGDL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 403 AHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVA--SPHDIRgniVKAFIILQDDYEASDEliQEL 480
Cdd:cd12114 367 GRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVlgDPGGKR---LAAFVVPDNDGTPIAP--DAL 441
|
490 500 510
....*....|....*....|....*....|....*.
gi 1801842045 481 QVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd12114 442 RAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
29-522 |
1.28e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.10 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKDNEhenisVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYR 108
Cdd:PRK12467 3113 ALVFGDQQ-----LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYM 3187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 109 ITHGEIDAVISFSSLtkefenvkeYDQLKkfIVAGHKE---DWVSIEDEKEKVNDdlkgADTTRDDLAILSYTSGTTGNP 185
Cdd:PRK12467 3188 IEDSGVKLLLTQAHL---------LEQLP--APAGDTAltlDRLDLNGYSENNPS----TRVMGENLAYVIYTSGSTGKP 3252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 186 KAVTHSHGWGYAHLQ-MAPKHWLCIQENDLVWATAApgWQKWVWSpFLSVLGMGATAFVYNGR-FHPETYLELLQNYQIN 263
Cdd:PRK12467 3253 KGVGVRHGALANHLCwIAEAYELDANDRVLLFMSFS--FDGAQER-FLWTLICGGCLVVRDNDlWDPEELWQAIHAHRIS 3329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 264 VLCCTPT------EYRMMAKLSHLEQYnleylhsaVSAGEPLNREVVEQFKRHF-NITVRDGYGQTESTLLIGFLKDT-- 334
Cdd:PRK12467 3330 IACFPPAylqqfaEDAGGADCASLDIY--------VFGGEAVPPAAFEQVKRKLkPRGLTNGYGPTEAVVTVTLWKCGgd 3401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 335 ---EPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDLpaLFKGYFKDEARTK--------AASTGDYYVTGDQA 403
Cdd:PRK12467 3402 avcEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVG--LARGYHQRPSLTAerfvadpfSGSGGRLYRTGDLA 3479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 404 HIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDiRGNIVKAFIILQDDYEAsdeLIQELQVF 483
Cdd:PRK12467 3480 RYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGA-GGKQLVAYVVPADPQGD---WRETLRDH 3555
|
490 500 510
....*....|....*....|....*....|....*....
gi 1801842045 484 CKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEIK 522
Cdd:PRK12467 3556 LAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK 3594
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
41-513 |
3.18e-24 |
|
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: 105.82 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRA---IVTYelyIAALKLGIAIVPssemLRTKDLQYRITHGEIDA- 116
Cdd:cd17646 23 TLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSadlVVAL---LAVLKAGAAYLP----LDPGYPADRLAYMLADAg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 117 ---VISFSSLTKEFENVKEYDQLKKFIVAGHKedwvsiedekekvnDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSH- 192
Cdd:cd17646 96 pavVLTTADLAARLPAGGDVALLGDEALAAPP--------------ATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 193 ------GWGYAHLQMAPKhwlciqenDLVWATAAPGWQKWVWSPFLSvLGMGATAFVYNGRFH--PETYLELLQNYQINV 264
Cdd:cd17646 162 givnrlLWMQDEYPLGPG--------DRVLQKTPLSFDVSVWELFWP-LVAGARLVVARPGGHrdPAYLAALIREHGVTT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 265 LCCTPTeyrMMAKLshLEQYNLEYLHS---AVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLK---DTEPRM 338
Cdd:cd17646 233 CHFVPS---MLRVF--LAEPAAGSCASlrrVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPvrgPAETPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 339 GSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKA-------ASTGDYYVTGDQAHIDNDGYF 411
Cdd:cd17646 308 VPIGRPVPNTRLYVLDDALRPVPVGVPGELY--LGGVQLARGYLGRPALTAErfvpdpfGPGSRMYRTGDLARWRPDGAL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 412 WFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASDEliQELQVFCKNEVAPY 491
Cdd:cd17646 386 EFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDT--AALRAHLAERLPEY 463
|
490 500
....*....|....*....|..
gi 1801842045 492 KYPRAIEFVENLPKTNSGKIRR 513
Cdd:cd17646 464 MVPAAFVVLDALPLTANGKLDR 485
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
34-519 |
5.50e-24 |
|
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: 105.40 E-value: 5.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 34 DNEHENISVSYKELISNANKVGNVFLNHGlKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDlQYRITH-- 111
Cdd:cd05931 17 DEGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPGRH-AERLAAil 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 112 --GEIDAVISFSSLtkefenvkeYDQLKKFIVA--GHKEDWVSIEDEKE-KVNDDLKGADTTRDDLAILSYTSGTTGNPK 186
Cdd:cd05931 95 adAGPRVVLTTAAA---------LAAVRAFAASrpAAGTPRLLVVDLLPdTSAADWPPPSPDPDDIAYLQYTSGSTGTPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 187 AVTHSHGWGYAHLQMAPKHWLCiQEND-------------LVWATAAPgwqkwVWSPFLSVLgMGATAFVYNgrfhPETY 253
Cdd:cd05931 166 GVVVTHRNLLANVRQIRRAYGL-DPGDvvvswlplyhdmgLIGGLLTP-----LYSGGPSVL-MSPAAFLRR----PLRW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 254 LELLQNYQINV---------LCCTpteyrmMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF------NITVRDG 318
Cdd:cd05931 235 LRLISRYRATIsaapnfaydLCVR------RVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFAEAFapfgfrPEAFRPS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 319 YGQTESTLLI----------------------GFLKDTEPRMG----SMGKGIPGSFVTVIDDDG-KEVGPNVKGNIAVp 371
Cdd:cd05931 309 YGLAEATLFVsggppgtgpvvlrvdrdalagrAVAVAADDPAArelvSCGRPLPDQEVRIVDPETgRELPDGEVGEIWV- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 372 lDLPALFKGYFKDE---ARTKAASTGD----YYVTGDQAHIdNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTN-HAAV 443
Cdd:cd05931 388 -RGPSVASGYWGRPeatAETFGALAATdeggWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEaHPAL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 444 KE--CAVVASPHDIRGnivKAFIILQ----DDYEASDELIQELQ--VFCKNEVAPykypRAIEFVEN--LPKTNSGKIRR 513
Cdd:cd05931 466 RPgcVAAFSVPDDGEE---RLVVVAEvergADPADLAAIAAAIRaaVAREHGVAP----ADVVLVRPgsIPRTSSGKIQR 538
|
....*.
gi 1801842045 514 VELRDA 519
Cdd:cd05931 539 RACRAA 544
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
432-510 |
7.87e-24 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 94.92 E-value: 7.87e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801842045 432 EVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEAsdeLIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGK 510
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVEL---LEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
175-525 |
1.13e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 104.40 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 175 LSYTSGTTGNPKAVTHSHGWGYAHLQMA--PKHwLCIQENDLVWATAaPGWQKWVWSPFLSVLGMGATaFVYNG-RFHPE 251
Cdd:PRK07008 181 LCYTSGTTGNPKGALYSHRSTVLHAYGAalPDA-MGLSARDAVLPVV-PMFHVNAWGLPYSAPLTGAK-LVLPGpDLDGK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 252 TYLELLQNYQINVLCCTPTEYRMMakLSHLEQYNLEY--LHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTE------ 323
Cdd:PRK07008 258 SLYELIEAERVTFSAGVPTVWLGL--LNHMREAGLRFstLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEmsplgt 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 324 -STLLIGFLKDT-EPRMGSM---GKGIPGSFVTVIDDDGKEVGPNVK--GNIAVplDLPALFKGYFKDEArtkAASTGDY 396
Cdd:PRK07008 336 lCKLKWKHSQLPlDEQRKLLekqGRVIYGVDMKIVGDDGRELPWDGKafGDLQV--RGPWVIDRYFRGDA---SPLVDGW 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 397 YVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPH---DIRGNIVkafIILQDDYEAS 473
Cdd:PRK07008 411 FPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHpkwDERPLLV---VVKRPGAEVT 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1801842045 474 DEliqELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDaEIKKYQ 525
Cdd:PRK07008 488 RE---ELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE-QFRDYV 535
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
43-527 |
1.60e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 105.42 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSs 122
Cdd:PRK12316 3084 SYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQS- 3162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 ltkefenvkeydQLKKFIVAGHKEdwVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQmA 202
Cdd:PRK12316 3163 ------------HLRLPLAQGVQV--LDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLC-W 3227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 203 PKHWLCIQENDLVWATAAPGWQKWVWSPFLSvLGMGATAFVYNGRFH--PETYLELLQNYQINVLCCTPTEYRMMakLSH 280
Cdd:PRK12316 3228 MQQAYGLGVGDRVLQFTTFSFDVFVEELFWP-LMSGARVVLAGPEDWrdPALLVELINSEGVDVLHAYPSMLQAF--LEE 3304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 281 LEQYNLEYLHSAVSAGEPLNREVVEQFkrHFNITVRDGYGQTESTLLIGFLKDTEPRMGS--MGKGIPGSFVTVIDDDGK 358
Cdd:PRK12316 3305 EDAHRCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACYILDGSLE 3382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 359 EVGPNVKGNIAVPLDLPAlfKGYFKDEARTKA-------ASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPF 431
Cdd:PRK12316 3383 PVPVGALGELYLGGEGLA--RGYHNRPGLTAErfvpdpfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELG 3460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 432 EVEDALTNHAAVKECAVVAsphdIRGNIVKAFIILQDDyeaSDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKI 511
Cdd:PRK12316 3461 EIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDE---AGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKL 3533
|
490
....*....|....*.
gi 1801842045 512 RRVELRDAEIKKYQQQ 527
Cdd:PRK12316 3534 DRKALPRPDAALLQQD 3549
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
13-513 |
1.73e-23 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 103.82 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 13 NIVSEIEKYAsEDHKKAIIYKDNEHENisvSYKELISNANKVGNVFLNHGLKKGDKVLI---MMPRAIVTYelyIAALKL 89
Cdd:PRK04813 3 DIIETIEEFA-QTQPDFPAYDYLGEKL---TYGQLKEDSDALAAFIDSLKLPDKSPIIVfghMSPEMLATF---LGAVKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 90 GIAIVP---SSEMLRTKDLqyrITHGEIDAVISFSSLTKEFENVKEYDQlkkfivaghkedwVSIEDEKEKVNDDLKGAD 166
Cdd:PRK04813 76 GHAYIPvdvSSPAERIEMI---IEVAKPSLIIATEELPLEILGIPVITL-------------DELKDIFATGNPYDFDHA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 167 TTRDDLAILSYTSGTTGNPKAVTHSHgwgyAHLQmAPKHWLC----IQENdLVWATAAPgwqkwvWSPFLSV------LG 236
Cdd:PRK04813 140 VKGDDNYYIIFTSGTTGKPKGVQISH----DNLV-SFTNWMLedfaLPEG-PQFLNQAP------YSFDLSVmdlyptLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 237 MGATAFVY------NgrfhPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRH 310
Cdd:PRK04813 208 SGGTLVALpkdmtaN----FKQLFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLLER 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 311 F-NITVRDGYGQTESTLLIGFLKDTE------PRMgSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFK 383
Cdd:PRK04813 284 FpSATIYNTYGPTEATVAVTSIEITDemldqyKRL-PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI--SGPSVSKGYLN 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 384 DEARTKAA-STGD---YYVTGDQAHIDnDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVasPHDiRGNI 459
Cdd:PRK04813 361 NPEKTAEAfFTFDgqpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV--PYN-KDHK 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801842045 460 VK---AFIILQD-DYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRR 513
Cdd:PRK04813 437 VQyliAYVVPKEeDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
18-516 |
2.20e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 105.24 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 18 IEKYASEDHKKAIIYKDNEHenisVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSS 97
Cdd:PRK12467 518 IEAQARQHPERPALVFGEQV----LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLD 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 98 EMLRTKDLQYRITHGEIDAVISFSSLTKEFENVkeyDQLKkFIVAGHKEDWVSIEDEkekVNDDLKGADttrDDLAILSY 177
Cdd:PRK12467 594 PEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVP---AGLR-SLCLDEPADLLCGYSG---HNPEVALDP---DNLAYVIY 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 178 TSGTTGNPKAVTHSHGwGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSvLGMGATAFV--YNGRFHPETYLE 255
Cdd:PRK12467 664 TSGSTGQPKGVAISHG-ALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGA-LASGATLHLlpPDCARDAEAFAA 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 256 LLQNYQINVLCCTPTEYRMMAKLSHLEQynLEYLHSAVSAGEPLNREVVEQ-FKRHFNITVRDGYGQTESTL--LIGFLK 332
Cdd:PRK12467 742 LMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVCGGEALQVDLLARvRALGPGARLINHYGPTETTVgvSTYELS 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 333 DTEPRMGS--MGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTK--------AASTGDYYVTGDQ 402
Cdd:PRK12467 820 DEERDFGNvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGA--GLARGYHRRPALTAerfvpdpfGADGGRLYRTGDL 897
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 403 AHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDiRGNIVKAFIIL------QDDYEASDEL 476
Cdd:PRK12467 898 ARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD-AGLQLVAYLVPaavadgAEHQATRDEL 976
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1801842045 477 IQELQvfcknEVAP-YKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:PRK12467 977 KAQLR-----QVLPdYMVPAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
167-516 |
9.89e-23 |
|
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: 100.97 E-value: 9.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 167 TTRDDLAILSYTSGTTGNPKAV--THSHGWGYAHLQMAPkhwLCIQENDLVWATAAPGWQKWVWSPFLSVLGmGATAFVY 244
Cdd:cd17644 103 TQPENLAYVIYTSGSTGKPKGVmiEHQSLVNLSHGLIKE---YGITSSDRVLQFASIAFDVAAEEIYVTLLS-GATLVLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 245 NG--RFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNL-EYLHSAVSAGEPLNREVVEQFKRHF--NITVRDGY 319
Cdd:cd17644 179 PEemRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVLELLLSTIDLpSSLRLVIVGGEAVQPELVRQWQKNVgnFIQLINVY 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 320 GQTESTL---LIGFLKDTEPRMGS--MGKGIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTK----- 389
Cdd:cd17644 259 GPTEATIaatVCRLTQLTERNITSvpIGRPIANTQVYILDENLQPVPVGVPGELH--IGGVGLARGYLNRPELTAekfis 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 390 ---AASTGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVA---SPHDIRgniVKA 462
Cdd:cd17644 337 hpfNSSESErLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVredQPGNKR---LVA 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1801842045 463 FIILQDDYEASdelIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd17644 414 YIVPHYEESPS---TVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
41-519 |
2.94e-22 |
|
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: 99.92 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPR---AIVTYelyIAALKLGIAIVPSSEMLRTKDLQYRIThgEIDAV 117
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKskwAVVAM---LAVLKAGGAFVPLDPSHPLQRLQEILQ--DTGAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 ISFSSltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadtTRDDLAILSYTSGTTGNPKAV--THS---- 191
Cdd:cd05918 99 VVLTS---------------------------------------------SPSDAAYVIFTSGSTGKPKGVviEHRalst 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 192 --HGWGYAH--------LQMAPKHW-LCIQEndlvwataapgwqkwvwspFLSVLGMGATAFVyngrfhP--ETYL---- 254
Cdd:cd05918 134 saLAHGRALgltsesrvLQFASYTFdVSILE-------------------IFTTLAAGGCLCI------PseEDRLndla 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 255 ELLQNYQINVLCCTPTeyrmMAKLSHLEQY-NLEYLhsaVSAGEPLNREVVEQFKRHfnITVRDGYGQTESTLL-IGFLK 332
Cdd:cd05918 189 GFINRLRVTWAFLTPS----VARLLDPEDVpSLRTL---VLGGEALTQSDVDTWADR--VRLINAYGPAECTIAaTVSPV 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 333 DTEPRMGSMGKGIPGS-FVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTKAA-----------STGDY---Y 397
Cdd:cd05918 260 VPSTDPRNIGRPLGATcWVVDPDNHDRLVPIGAVGELL--IEGPILARGYLNDPEKTAAAfiedpawlkqeGSGRGrrlY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 398 VTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKE--CAVVASPHD--IRGNIVkAFIILQDDYEAS 473
Cdd:cd05918 338 RTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevVVEVVKPKDgsSSPQLV-AFVVLDGSSSGS 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 474 D--------------ELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:cd05918 417 GdgdslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-526 |
2.39e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 98.88 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 40 ISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVIS 119
Cdd:PRK12316 535 ETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLS 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 120 FSSLTKEFE-----NVKEYDQLKKFiVAGHKEDWVSIEdekekvnddlkgadTTRDDLAILSYTSGTTGNPKAVTHSHGW 194
Cdd:PRK12316 615 QSHLGRKLPlaagvQVLDLDRPAAW-LEGYSEENPGTE--------------LNPENLAYVIYTSGSTGKPKGAGNRHRA 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 195 GYAHLQMApKHWLCIQENDLVWATAAPGWQKWVWSPFLSvLGMGATAFVYNGRFH--PETYLELLQNYQINVLCCTPTey 272
Cdd:PRK12316 680 LSNRLCWM-QQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAAPGDHrdPAKLVELINREGVDTLHFVPS-- 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 273 rMMAKLSHLEQY-NLEYLHSAVSAGEPLNREVVEQ-FKRHFNITVRDGYGQTESTllIGFLKDTEPRMG----SMGKGIP 346
Cdd:PRK12316 756 -MLQAFLQDEDVaSCTSLRRIVCSGEALPADAQEQvFAKLPQAGLYNLYGPTEAA--IDVTHWTCVEEGgdsvPIGRPIA 832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 347 GSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTK----AASTGD---YYVTGDQAHIDNDGYFWFEGRRDD 419
Cdd:PRK12316 833 NLACYILDANLEPVPVGVLGELY--LAGRGLARGYHGRPGLTAerfvPSPFVAgerMYRTGDLARYRADGVIEYAGRIDH 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 420 IIISSGYTIGPFEVEDALTNHAAVKECAVVAsphdIRGNIVKAFIILQDdyeASDELIQELQVFCKNEVAPYKYPRAIEF 499
Cdd:PRK12316 911 QVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLES---EGGDWREALKAHLAASLPEYMVPAQWLA 983
|
490 500
....*....|....*....|....*..
gi 1801842045 500 VENLPKTNSGKIRRVELRDAEIKKYQQ 526
Cdd:PRK12316 984 LERLPLTPNGKLDRKALPAPEASVAQQ 1010
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
43-526 |
9.97e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 96.95 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISFSS 122
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRH 2109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 LTKEFENVKEYDQLkKFIVAGHKEDWVSIEDEkekvnddlkgADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMA 202
Cdd:PRK12316 2110 LLERLPLPAGVARL-PLDRDAEWADYPDTAPA----------VQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAA 2178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 203 PKHW-LCIQENDLVWATAAPGWQKWVWSPFLSVlgmGATAFVYNGR-FHPETYLELLQNYQINVLCCTPTEYRMMAKLSH 280
Cdd:PRK12316 2179 GERYeLSPADCELQFMSFSFDGAHEQWFHPLLN---GARVLIRDDElWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAE 2255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 281 LEQYNLEyLHSAVSAGEPLNREVVEQFKRHFNiTVR--DGYGQTEsTLLIGFLKDTEPRMGS------MGKGIPGSFVTV 352
Cdd:PRK12316 2256 RDGRPPA-VRVYCFGGEAVPAASLRLAWEALR-PVYlfNGYGPTE-AVVTPLLWKCRPQDPCgaayvpIGRALGNRRAYI 2332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 353 IDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTK--------AASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISS 424
Cdd:PRK12316 2333 LDADLNLLAPGMAGELY--LGGEGLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIR 2410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 425 GYTIGPFEVEDALTNHAAVKECAVVASpHDIRGNIVKAFIILQDdyeASDELIQELQVFCKNEVAPYKYPRAIEFVENLP 504
Cdd:PRK12316 2411 GFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDD---AAEDLLAELRAWLAARLPAYMVPAHWVVLERLP 2486
|
490 500
....*....|....*....|..
gi 1801842045 505 KTNSGKIRRVELRDAEIKKYQQ 526
Cdd:PRK12316 2487 LNPNGKLDRKALPKPDVSQLRQ 2508
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
41-519 |
1.62e-20 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 94.69 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLG-IAI-----VPSSEMLRTKDLQYRIT---- 110
Cdd:PRK05857 41 ALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGaIAVmadgnLPIAAIERFCQITDPAAalva 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 111 -HGEIDAvisfSSLTkefENVKEYDQLKKFIVAGHKEDWVSIEDEKEKVNDDLkGADttrDDLAILsYTSGTTGNPKAVT 189
Cdd:PRK05857 121 pGSKMAS----SAVP---EALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQ-GSE---DPLAMI-FTSGTTGEPKAVL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 190 HSHGWGYAhlqmAPKhwlCIQENDLVWATAAPGwqKWVWSPfLSVLGMGATAFVYNGRFH----------PETYLELLQN 259
Cdd:PRK05857 189 LANRTFFA----VPD---ILQKEGLNWVTWVVG--ETTYSP-LPATHIGGLWWILTCLMHgglcvtggenTTSLLEILTT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 260 YQINVLCCTPTeyrMMAKLShleqYNLEYLHSAVsagePLNREVVEQFKRHFNITVR----------DGYGQTES--TLL 327
Cdd:PRK05857 259 NAVATTCLVPT---LLSKLV----SELKSANATV----PSLRLVGYGGSRAIAADVRfieatgvrtaQVYGLSETgcTAL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 328 I-----GFLKDTEprMGSMGKGIPGSFVTVIDDDGKevGPNVKGNIAVP------LDLPALFKGYFKDEARTKAASTGDY 396
Cdd:PRK05857 328 ClptddGSIVKIE--AGAVGRPYPGVDVYLAATDGI--GPTAPGAGPSAsfgtlwIKSPANMLGYWNNPERTAEVLIDGW 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 397 YVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEASD-- 474
Cdd:PRK05857 404 VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAar 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1801842045 475 ELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDA 519
Cdd:PRK05857 484 ALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAA 528
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
25-516 |
3.92e-20 |
|
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: 93.00 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 25 DHKkAIIYKDNeheniSVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPssemlrtkd 104
Cdd:cd17645 13 DHV-AVVDRGQ-----SLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVP--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 105 lqyrithgeIDAvisfssltkefenvkEY-DQLKKFIVAghkedwvsieDEKEKVnddlkgADTTRDDLAILSYTSGTTG 183
Cdd:cd17645 78 ---------IDP---------------DYpGERIAYMLA----------DSSAKI------LLTNPDDLAYVIYTSGSTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 184 NPKAVTHSH-------GWGYAHLQMAPkhwlciQENDLVWATAapGWQKWVWSPFLSVLgMGATAFVYNgrfhPETYLEL 256
Cdd:cd17645 118 LPKGVMIEHhnlvnlcEWHRPYFGVTP------ADKSLVYASF--SFDASAWEIFPHLT-AGAALHVVP----SERRLDL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 257 --LQNY------QINVLCcTPTEYRMMAklshLEQYNLEYLhsaVSAGEPLNREVVEQFKrhfnitVRDGYGQTESTLLI 328
Cdd:cd17645 185 daLNDYfnqegiTISFLP-TGAAEQFMQ----LDNQSLRVL---LTGGDKLKKIERKGYK------LVNNYGPTENTVVA 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 329 -GFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTKAASTGD-------YYVTG 400
Cdd:cd17645 251 tSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE--GLARGYLNRPELTAEKFIVHpfvpgerMYRTG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 401 DQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIILQDDYEasdelIQEL 480
Cdd:cd17645 329 DLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIP-----HEEL 403
|
490 500 510
....*....|....*....|....*....|....*.
gi 1801842045 481 QVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd17645 404 REWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
296-525 |
1.05e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 91.59 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 296 GEPLNREVVEQFKRHfNITVRDGYGQTESTLLIGFLKDTEPRMG--SMGKGIPGSFVTVIdddgkevgPNVKGNIAVplD 373
Cdd:PRK07445 239 GAPAWPSLLEQARQL-QLRLAPTYGMTETASQIATLKPDDFLAGnnSSGQVLPHAQITIP--------ANQTGNITI--Q 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 374 LPALFKGY---FKDEARtkaastgdYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVA 450
Cdd:PRK07445 308 AQSLALGYypqILDSQG--------IFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLG 379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801842045 451 SPHDIRGNIVKAFIILQDDYEASDELIQELqvfcKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEIKKYQ 525
Cdd:PRK07445 380 LPDPHWGEVVTAIYVPKDPSISLEELKTAI----KDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLG 450
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
170-517 |
3.00e-19 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 91.01 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHgwgyahlqmapkHWLCIQ-----------ENDlVWATAAPGWQKWVWSPFLSVLGMG 238
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISH------------SALIVQslakiaivgygEDD-VYLHTAPLCHIGGLSSALAMLMVG 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 239 AtAFVYNGRFHPETYLELLQNYQINVLCCTPTeyrMMAKL---------SHLEQYNLEYLHSAVSAGEPLNREVVEQFKR 309
Cdd:PLN02860 239 A-CHVLLPKFDAKAALQAIKQHNVTSMITVPA---MMADLisltrksmtWKVFPSVRKILNGGGSLSSRLLPDAKKLFPN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 310 hfnITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVG-------PNVKGNIAVPLDL-------- 374
Cdd:PLN02860 315 ---AKLFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQTKSSSVHQPQGvcvgkpaPHVELKIGLDESSrvgriltr 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 375 -PALFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASP 452
Cdd:PLN02860 392 gPHVMLGYWGQNSETASVLSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1801842045 453 HDIRGNIVKAFIILQDDYEASD----------ELIQE-LQVFCKNE-VAPYKYPRAI-EFVENLPKTNSGKIRRVELR 517
Cdd:PLN02860 472 DSRLTEMVVACVRLRDGWIWSDnekenakknlTLSSEtLRHHCREKnLSRFKIPKLFvQWRKPFPLTTTGKIRRDEVR 549
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
29-516 |
3.97e-19 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 89.83 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 29 AIIYKDNEhenisVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYR 108
Cdd:cd17650 5 AVSDATRQ-----LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 109 ITHGEIDAVIsfssltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkgadTTRDDLAILSYTSGTTGNPKAV 188
Cdd:cd17650 80 LEDSGAKLLL------------------------------------------------TQPEDLAYVIYTSGTTGKPKGV 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 189 --THSHgwgyahlqmapkhwlciqendlvWATAAPGWQKWVWSPFLSV--LGMGATAF-VYNG----------------- 246
Cdd:cd17650 112 mvEHRN-----------------------VAHAAHAWRREYELDSFPVrlLQMASFSFdVFAGdfarsllnggtlvicpd 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 247 --RFHPETYLELLQNYQINVLCCTPTEYR-MMAKLSHlEQYNLEYLHSAV--SAGEPLN--REVVEQFKRHFNITvrDGY 319
Cdd:cd17650 169 evKLDPAALYDLILKSRITLMESTPALIRpVMAYVYR-NGLDLSAMRLLIvgSDGCKAQdfKTLAARFGQGMRII--NSY 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 320 GQTESTLLIGFLK---DTEPRMGS--MGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTKA---- 390
Cdd:cd17650 246 GVTEATIDSTYYEegrDPLGDSANvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGA--GVARGYLNRPELTAErfve 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 391 ---ASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKEcAVVASPHDIRGNI-VKAFIIl 466
Cdd:cd17650 324 npfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDE-AVVAVREDKGGEArLCAYVV- 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1801842045 467 qddyeASDEL-IQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd17650 402 -----AAATLnTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
160-515 |
5.99e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 90.06 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 160 DDLKGAD------TTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLqmapkHWLCIQ-----ENDLVWAtaapgwqkwvW 228
Cdd:PRK07768 136 ADLLAADpidpveTGEDDLALMQLTSGSTGSPKAVQITHGNLYANA-----EAMFVAaefdvETDVMVS----------W 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 229 SP---------FLSV---LGMGA---TAFVYNGRfhPETYLELLQNYQINVLCCTPTEY----RMMAKLSHLEQYNLEYL 289
Cdd:PRK07768 201 LPlfhdmgmvgFLTVpmyFGAELvkvTPMDFLRD--PLLWAELISKYRGTMTAAPNFAYallaRRLRRQAKPGAFDLSSL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 290 HSAVSAGEPLNREVVEQF----KRH-FNIT-VRDGYGQTESTLLIGF--------------------------LKDTEPR 337
Cdd:PRK07768 279 RFALNGAEPIDPADVEDLldagARFgLRPEaILPAYGMAEATLAVSFspcgaglvvdevdadllaalrravpaTKGNTRR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 338 MGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAVPLDlpALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRR 417
Cdd:PRK07768 359 LATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGE--SVTPGYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRV 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 418 DDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDiRGNIVKAFII-----LQDDYEASDELIQEL--QVFCKNEVAp 490
Cdd:PRK07768 437 KDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVavesnAFEDPAEVRRIRHQVahEVVAEVGVR- 514
|
410 420
....*....|....*....|....*..
gi 1801842045 491 ykyPRAIEFVE--NLPKTNSGKIRRVE 515
Cdd:PRK07768 515 ---PRNVVVLGpgSIPKTPSGKLRRAN 538
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
43-517 |
8.34e-19 |
|
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: 89.02 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGI--AIVPSSemLRTKDLQYRITHGEIDAVIsF 120
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVetALINSN--LRLESLLHCITVSKAKALI-F 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 SSLTKEFENVkeYDQLKKFIVAGHKEDWVSIedekekvnddlkgadttrddlailsYTSGTTGNPKA--VTHSHgwgYAH 198
Cdd:cd05939 82 NLLDPLLTQS--STEPPSQDDVNFRDKLFYI-------------------------YTSGTTGLPKAavIVHSR---YYR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 199 LQMAPKHWLCIQENDLVWA------TAApgwqkwvwspflSVLGMG-----ATAFVYNGRFHPETYLELLQNYQinvlcC 267
Cdd:cd05939 132 IAAGAYYAFGMRPEDVVYDclplyhSAG------------GIMGVGqallhGSTVVIRKKFSASNFWDDCVKYN-----C 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 268 TPTEY-----RMMAKLSHLEQYNLEYLHSAVSAGepLNREVVEQFKRHFNIT-VRDGYGQTE--STLL--------IGFL 331
Cdd:cd05939 195 TIVQYigeicRYLLAQPPSEEEQKHNVRLAVGNG--LRPQIWEQFVRRFGIPqIGEFYGATEgnSSLVnidnhvgaCGFN 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 332 ----------------KDT-EPRMGSMG------KGIPGSFVTVIDddgkevgpnvKGNiavPLdlpALFKGYFKDEART 388
Cdd:cd05939 273 srilpsvypirlikvdEDTgELIRDSDGlcipcqPGEPGLLVGKII----------QND---PL---RRFDGYVNEGATN 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 389 KAA-----STGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAV--VASPHdIRGNIV 460
Cdd:cd05939 337 KKIardvfKKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAG 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1801842045 461 KAFIILQDDYEASDELIQELQvfckNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05939 416 MAAIVDPERKVDLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQ 468
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
166-449 |
1.49e-18 |
|
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: 88.18 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 166 DTTRDDLAILSYTSGTTGNPKAVTHSHG---WGYAHL-QMAPKH----WLCIqendlvwataAPGWQKW--VWSPFLSVL 235
Cdd:cd17640 84 ENDSDDLATIIYTSGTTGNPKGVMLTHAnllHQIRSLsDIVPPQpgdrFLSI----------LPIWHSYerSAEYFIFAC 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 236 GMgatAFVYNGrfhPETYLELLQNYQINVLCCTPTE--------YRMMAKLSHLEQYNLEYLHS------AVSAGEPLNR 301
Cdd:cd17640 154 GC---SQAYTS---IRTLKDDLKRVKPHYIVSVPRLweslysgiQKQVSKSSPIKQFLFLFFLSggifkfGISGGGALPP 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 302 EVVeQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEV-GPNVKGNIAVplDLPALFKG 380
Cdd:cd17640 228 HVD-TFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGNVVlPPGEKGIVWV--RGPQVMKG 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1801842045 381 YFKDEARTKAASTGD-YYVTGDQAHIDNDGYFWFEGR-RDDIIISSGYTIGPFEVEDALTNHAAVKECAVV 449
Cdd:cd17640 305 YYKNPEATSKVLDSDgWFNTGDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
43-527 |
1.90e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.38 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQyRITHGEIDAVISFSS 122
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQ-RIIELSRTPVLVCSA 3825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 LTKEfenvKEYDQLKKFIVAGHKEDWVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPKAV-THSHGWGYAHLQM 201
Cdd:PRK05691 3826 ACRE----QARALLDELGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKGVmVEQRGMLNNQLSK 3901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 202 APkhWLCIQENDLVWATAAPGWQKWVWSpFLSVLGMGA-TAFVYNGRFH-PETYLELLQNYQINVLCCTPTEY-RMMAKl 278
Cdd:PRK05691 3902 VP--YLALSEADVIAQTASQSFDISVWQ-FLAAPLFGArVEIVPNAIAHdPQGLLAHVQAQGITVLESVPSLIqGMLAE- 3977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 279 shlEQYNLEYLHSAVSAGEPLNREVVEQF-KRHFNITVRDGYGQTESTLLIGFLK-DTEPRMGS---MGKGIPGSFVTVI 353
Cdd:PRK05691 3978 ---DRQALDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAECSDDVAFFRvDLASTRGSylpIGSPTDNNRLYLL 4054
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 354 DDDGKEVGPNVKGNIAVPLdlPALFKGYFKDEARTKAA-------STGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSG 425
Cdd:PRK05691 4055 DEALELVPLGAVGELCVAG--TGVGRGYVGDPLRTALAfvphpfgAPGErLYRTGDLARRRSDGVLEYVGRIDHQVKIRG 4132
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 426 YTIGPFEVEDALTNHAAVKEcAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPK 505
Cdd:PRK05691 4133 YRIELGEIEARLHEQAEVRE-AAVAVQEGVNGKHLVGYLVPHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPL 4211
|
490 500
....*....|....*....|..
gi 1801842045 506 TNSGKIRRVELRDAEIKKYQQQ 527
Cdd:PRK05691 4212 NANGKLDRKALPALDIGQLQSQ 4233
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
174-523 |
2.49e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 84.32 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 174 ILSYTSGTTGNPKAVTHShgWGYAHLQMAPKHWLCIQENDLVWATAAPGWQKW-VWSPFLSVLGMGATAFVYNGRfHPET 252
Cdd:PRK08308 105 LLQYSSGTTGEPKLIRRS--WTEIDREIEAYNEALNCEQDETPIVACPVTHSYgLICGVLAALTRGSKPVIITNK-NPKF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 253 YLELLQNYQINVLCCTPTEYRMMAKLSHLEqynlEYLHSAVSAGEPLNREVVEQFKRHFNITVRDgYGQTESTLLigflk 332
Cdd:PRK08308 182 ALNILRNTPQHILYAVPLMLHILGRLLPGT----FQFHAVMTSGTPLPEAWFYKLRERTTYMMQQ-YGCSEAGCV----- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 333 dteprmgsmgkgipgsfvtvidddgkEVGPNVK--GNIAVPLDLPALFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDG 409
Cdd:PRK08308 252 --------------------------SICPDMKshLDLGNPLPHVSVSAGSDENAPEEIVVKMGDKEIfTKDLGYKSERG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 410 YFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIIlqddyeaSDELIQ--ELQVFCKNE 487
Cdd:PRK08308 306 TLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI-------SHEEIDpvQLREWCIQH 378
|
330 340 350
....*....|....*....|....*....|....*.
gi 1801842045 488 VAPYKYPRAIEFVENLPKTNSGKIRRVELRDAEIKK 523
Cdd:PRK08308 379 LAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVTA 414
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
43-517 |
2.62e-17 |
|
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: 84.33 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIaivpssemlrtkdlqyrithgeIDAVISFSS 122
Cdd:cd05940 5 TYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA----------------------VAALINYNL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 LTKEFENVKEYDQLKKFIVaghkedwvsiedekekvnddlkgadttrdDLAILSYTSGTTGNPKA--VTHSHGWGYAHLQ 200
Cdd:cd05940 63 RGESLAHCLNVSSAKHLVV-----------------------------DAALYIYTSGTTGLPKAaiISHRRAWRGGAFF 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 201 MapkHWLCIQENDLVWAT-----AAPGWQKWVwspflSVLGMGATaFVYNGRFHPETYLELLQNYQinvlcCTPTEY--R 273
Cdd:cd05940 114 A---GSGGALPSDVLYTClplyhSTALIVGWS-----ACLASGAT-LVIRKKFSASNFWDDIRKYQ-----ATIFQYigE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 274 MMAKLSHLEQYNLEYLHSA-VSAGEPLNREVVEQFKRHFNI-TVRDGYGQTESTllIGFLkDTEPRMGSMG-------KG 344
Cdd:cd05940 180 LCRYLLNQPPKPTERKHKVrMIFGNGLRPDIWEEFKERFGVpRIAEFYAATEGN--SGFI-NFFGKPGAIGrnpsllrKV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 345 IPGSFVTViDDDGKEVGPNVKGN-IAVPLDLPAL----------FKGYFKDEARTKAAST-----GD-YYVTGDQAHIDN 407
Cdd:cd05940 257 APLALVKY-DLESGEPIRDAEGRcIKVPRGEPGLlisrinplepFDGYTDPAATEKKILRdvfkkGDaWFNTGDLMRLDG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 408 DGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAV--VASP-HDirGNIVKAFIILQDDYEasdELIQELQVFC 484
Cdd:cd05940 336 EGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPgTD--GRAGMAAIVLQPNEE---FDLSALAAHL 410
|
490 500 510
....*....|....*....|....*....|...
gi 1801842045 485 KNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:cd05940 411 EKNLPGYARPLFLRLQPEMEITGTFKQQKVDLR 443
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
28-516 |
1.33e-16 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 82.70 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 28 KAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGiAIVPS-SEMLRTKDLQ 106
Cdd:cd05943 85 PAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIG-AIWSScSPDFGVPGVL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 107 YRIthGEIDAVISFSSLTKEFeNVKEYDQLKK------------------FIVAGHKEDWVSIEdeKEKVNDDLKGADTT 168
Cdd:cd05943 164 DRF--GQIEPKVLFAVDAYTY-NGKRHDVREKvaelvkglpsllavvvvpYTVAAGQPDLSKIA--KALTLEDFLATGAA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 169 ----------RDDLAILsYTSGTTGNPKAVTHSHGwGYAhLQMAPKHWLC--IQEND-LVWATaAPGWQKWVWspFLSVL 235
Cdd:cd05943 239 gelefeplpfDHPLYIL-YSSGTTGLPKCIVHGAG-GTL-LQHLKEHILHcdLRPGDrLFYYT-TCGWMMWNW--LVSGL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 236 GMGATAFVYNGR-FHP--ETYLELLQNYQINVLCCTPTeYRMM---AKLSHLEQYNLEYLHSAVSAGEPLnreVVEQF-- 307
Cdd:cd05943 313 AVGATIVLYDGSpFYPdtNALWDLADEEGITVFGTSAK-YLDAlekAGLKPAETHDLSSLRTILSTGSPL---KPESFdy 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 308 ---KRHFNITVRDGYGQTEstlLIGflkdteprmGSMGkGIP--------------GSFVTVIDDDGKEVgPNVKGNIAV 370
Cdd:cd05943 389 vydHIKPDVLLASISGGTD---IIS---------CFVG-GNPllpvyrgeiqcrglGMAVEAFDEEGKPV-WGEKGELVC 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 371 PLDLPALFKGYFKDEARTKAASTgdYYVT-------GDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAV 443
Cdd:cd05943 455 TKPFPSMPVGFWNDPDGSRYRAA--YFAKypgvwahGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEV 532
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801842045 444 KECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKirRVEL 516
Cdd:cd05943 533 EDSLVVGQEWKDGDERVILFVKLREGVELDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK--KVEV 603
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
15-517 |
1.71e-16 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 82.52 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 15 VSEIEKYASEDHKKAII--YKDNEHENISvsYKELISNANKVGNVFLNH-GLKKGDKVLIMMPRAIVTYELYIAALKLGI 91
Cdd:PRK05620 12 LTRILEYGSTVHGDTTVttWGGAEQEQTT--FAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 92 AIVPSSEMLRTKDLQYRITHGEIDAVISFSSLTKEF-ENVKEYDQLKKFIVAG---------------HKEDWVSIEDEK 155
Cdd:PRK05620 90 VFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLgEILKECPCVRAVVFIGpsdadsaaahmpegiKVYSYEALLDGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 156 EKVNDdlkGADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAH-LQMAPKHWLCIQeNDLVWATAAPGWQKWVWSPFLSV 234
Cdd:PRK05620 170 STVYD---WPELDETTAAAICYSTGTTGAPKGVVYSHRSLYLQsLSLRTTDSLAVT-HGESFLCCVPIYHVLSWGVPLAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 235 LgMGATAFVYNGR-FHPETYLELLQNYQINVLCCTPTEYrmMAKLSHLEQYNLE--YLHSAVSAGEPLNREVVEQFKRHF 311
Cdd:PRK05620 246 F-MSGTPLVFPGPdLSAPTLAKIIATAMPRVAHGVPTLW--IQLMVHYLKNPPErmSLQEIYVGGSAVPPILIKAWEERY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 312 NITVRDGYGQTEsTLLIGFLkdTEPRMGSMGKG----------IPGSFVTVIDDDGKEVGPN--------VKGNIAV--- 370
Cdd:PRK05620 323 GVDVVHVWGMTE-TSPVGTV--ARPPSGVSGEArwayrvsqgrFPASLEYRIVNDGQVMESTdrnegeiqVRGNWVTasy 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 371 ------PLDLPA-LFKGYFKDEARTKAASTGdYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAV 443
Cdd:PRK05620 400 yhspteEGGGAAsTFRGEDVEDANDRFTADG-WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEV 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801842045 444 KECAVVASPHDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK05620 479 VECAVIGYPDDKWGERPLAVTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLR 552
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
43-449 |
1.82e-16 |
|
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: 81.74 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVIsfss 122
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 123 ltkefenvkeydqlkkfivaghkedwvsiedekekvnddlkGADTTRDDLAILsYTSGTTGNPKAVTHSHGWGYAHLQmA 202
Cdd:cd05910 80 -----------------------------------------GIPKADEPAAIL-FTSGSTGTPKGVVYRHGTFAAQID-A 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 203 PKHWLCIQENDLVWATAAPgwqkwvWSPFLSVLGMGATA----FVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKL 278
Cdd:cd05910 117 LRQLYGIRPGEVDLATFPL------FALFGPALGLTSVIpdmdPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 279 SHLEQYNLEYLHSAVSAGEPLNREVVEQFKR--HFNITVRDGYGQTEStLLIGFLKD----------TEPRMGS-MGKGI 345
Cdd:cd05910 191 CAQHGITLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEA-LPVSSIGSrellatttaaTSGGAGTcVGRPI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 346 PGSFVTVID---------DDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGD-----YYVTGDQAHIDNDGYF 411
Cdd:cd05910 270 PGVRVRIIEiddepiaewDDTLELPRGEIGEITV--TGPTVTPTYVNRPVATALAKIDDnsegfWHRMGDLGYLDDEGRL 347
|
410 420 430
....*....|....*....|....*....|....*...
gi 1801842045 412 WFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVV 449
Cdd:cd05910 348 WFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
24-517 |
3.84e-16 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 81.19 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 24 EDHKKAIIykDNEHeniSVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRaivTYELYI---AALKLGIAIV------ 94
Cdd:PRK10946 36 ASDAIAVI--CGER---QFSYRELNQASDNLACSLRRQGIKPGDTALVQLGN---VAEFYItffALLKLGVAPVnalfsh 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 95 PSSEM----------LRTKDLQYRITHGeiDAVISfssltkefENVKEYDQLKKFIVAGHKEDwVSIEDEKEKVNDDLKG 164
Cdd:PRK10946 108 QRSELnayasqiepaLLIADRQHALFSD--DDFLN--------TLVAEHSSLRVVLLLNDDGE-HSLDDAINHPAEDFTA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 165 ADTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHL-------QMAPK-HWLC---IQENdlvWATAAPGwqkwvwspFLS 233
Cdd:PRK10946 177 TPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVrrsveicGFTPQtRYLCalpAAHN---YPMSSPG--------ALG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 234 VLGMGATAfVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYN--LEYLHSAVSAGEPLNREVVEQFKRHF 311
Cdd:PRK10946 246 VFLAGGTV-VLAPDPSATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSRaqLASLKLLQVGGARLSETLARRIPAEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 312 NITVRDGYGQTEStlLIGF--LKDTEPRM-GSMGKGI-PGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEAR 387
Cdd:PRK10946 325 GCQLQQVFGMAEG--LVNYtrLDDSDERIfTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMT--RGPYTFRGYYKSPQH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 388 TKAASTGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAFIIL 466
Cdd:PRK10946 401 NASAFDANgFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1801842045 467 QDDYEASdeliqELQVFCKNE-VAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK10946 481 KEPLKAV-----QLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
41-516 |
4.22e-16 |
|
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: 81.18 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNH-GLKKGDKVLIMMPRAIVTYELYIAALKLG--IAIVPSSemLRTKDLQYRITHGEIDAV 117
Cdd:cd05938 5 TYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNTN--IRSKSLLHCFRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 ISFSSLtkeFENVKEY------DQLKKFIVAGHK--EDWVSIEDEKEKVNDDLKGAD----TTRDDLAILSYTSGTTGNP 185
Cdd:cd05938 83 VVAPEL---QEAVEEVlpalraDGVSVWYLSHTSntEGVISLLDKVDAASDEPVPASlrahVTIKSPALYIYTSGTTGLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 186 KAVTHSHgwgYAHLQMAPKHWLC-IQENDLVWATAapgwqkwvwsP----------FLSVLGMGATaFVYNGRFHPETYL 254
Cdd:cd05938 160 KAARISH---LRVLQCSGFLSLCgVTADDVIYITL----------PlyhssgfllgIGGCIELGAT-CVLKPKFSASQFW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 255 ELLQNYQINV----------LCCTPteyrmmaklshleQYNLEYLHSA-VSAGEPLNREVVEQFKRHF-NITVRDGYGQT 322
Cdd:cd05938 226 DDCRKHNVTViqyigellryLCNQP-------------QSPNDRDHKVrLAIGNGLRADVWREFLRRFgPIRIREFYGST 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 323 ESTllIGFLKDTEpRMGSMGKG-------IPGSFVT--------VIDDDGK--EVGPNVKGNIAVPLDLPALFKGYFKDE 385
Cdd:cd05938 293 EGN--IGFFNYTG-KIGAVGRVsylykllFPFELIKfdvekeepVRDAQGFciPVAKGEPGLLVAKITQQSPFLGYAGDK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 386 ARTKAA------STGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAV--VASP-HDi 455
Cdd:cd05938 370 EQTEKKllrdvfKKGDvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPgHE- 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801842045 456 rGNIVKAFIILQDDYEASDEliqelQVF--CKNEVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd05938 449 -GRIGMAAVKLKPGHEFDGK-----KLYqhVREYLPAYARPRFLRIQDSLEITGTFKQQKVRL 505
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
170-481 |
2.96e-15 |
|
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: 78.28 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHGwGYAHLQMAPKHWLCIQEND--LVWATAAPGWQK------WVWSPFLSVLGMGATA 241
Cdd:cd05932 137 EQLATLIYTSGTTGQPKGVMLTFG-SFAWAAQAGIEHIGTEENDrmLSYLPLAHVTERvfveggSLYGGVLVAFAESLDT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 242 FVYNGRFHPETYL----ELLQNYQINVLCCTPTeyrmmAKLSHL---------------EQYNLEYLHSAVSAGEPLNRE 302
Cdd:cd05932 216 FVEDVQRARPTLFfsvpRLWTKFQQGVQDKIPQ-----QKLNLLlkipvvnslvkrkvlKGLGLDQCRLAGCGSAPVPPA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 303 VVEQFkRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTvIDDDGKevgpnvkgniaVPLDLPALFKGYF 382
Cdd:cd05932 291 LLEWY-RSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVR-ISEDGE-----------ILVRSPALMMGYY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 383 KDEARTKAASTGD-YYVTGDQAHIDNDGYFWFEGRRDDII-ISSGYTIGPFEVEDALTNHAAVKECAVVAS--PHDIRGN 458
Cdd:cd05932 358 KDPEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFkTSKGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALV 437
|
330 340
....*....|....*....|...
gi 1801842045 459 IVKAFIILQDDYEASDELIQELQ 481
Cdd:cd05932 438 VLSEEARLRADAFARAELEASLR 460
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
41-527 |
2.31e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 76.75 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISF 120
Cdd:PRK05691 2213 TLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSD 2292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 SSLtkeFENVKEY-DQLKKFIVaghKEDWVSIEDEKEKVNDDLKGADttrdDLAILSYTSGTTGNPKAVTHSHGWGYAHL 199
Cdd:PRK05691 2293 RAL---FEALGELpAGVARWCL---EDDAAALAAYSDAPLPFLSLPQ----HQAYLIYTSGSTGKPKGVVVSHGEIAMHC 2362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 200 Q-------MAPK----HWLCIQENdlvwatAApgwQKWVWSPFLSvlgmGATAFVY-NGRFHPETYLELLQNYQINVLCC 267
Cdd:PRK05691 2363 QavierfgMRADdcelHFYSINFD------AA---SERLLVPLLC----GARVVLRaQGQWGAEEICQLIREQQVSILGF 2429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 268 TPTEYRMMAKlsHLE-QYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVR-DGYGQTESTL--LIGFLKDT-EPRMGS-- 340
Cdd:PRK05691 2430 TPSYGSQLAQ--WLAgQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFfNAYGPTETVVmpLACLAPEQlEEGAASvp 2507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 341 MGKGIPGSFVTVIDDDGKEVGPNVKGNIAVplDLPALFKGYFKDEARTK--------AASTGDYYVTGDQAHIDNDGYFW 412
Cdd:PRK05691 2508 IGRVVGARVAYILDADLALVPQGATGELYV--GGAGLAQGYHDRPGLTAerfvadpfAADGGRLYRTGDLVRLRADGLVE 2585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 413 FEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVA----SPHDIRGNIVKAfiILQDDYEASDELIQELQVFCKNEV 488
Cdd:PRK05691 2586 YVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAldtpSGKQLAGYLVSA--VAGQDDEAQAALREALKAHLKQQL 2663
|
490 500 510
....*....|....*....|....*....|....*....
gi 1801842045 489 APYKYPRAIEFVENLPKTNSGKIRRVELRDAEIKKYQQQ 527
Cdd:PRK05691 2664 PDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQA 2702
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
26-517 |
2.59e-14 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 75.68 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 26 HKKAIIYKDNeheniSVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLG--IAIVPSSemLRTK 103
Cdd:PRK08279 52 DRPALLFEDQ-----SISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGavVALLNTQ--QRGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 104 DLQYRITHGEIDAVISFSSLTKEFENVKEYdqlkkfiVAGHKEDWVSIEDEKEKVN--DDLKGA-------------DTT 168
Cdd:PRK08279 125 VLAHSLNLVDAKHLIVGEELVEAFEEARAD-------LARPPRLWVAGGDTLDDPEgyEDLAAAaagapttnpasrsGVT 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 169 RDDLAILSYTSGTTGNPKAVTHSHG-W-----GYAHLqmapkhwLCIQENDLVW----------ATAAPGwqkwvwspfl 232
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMSHMrWlkamgGFGGL-------LRLTPDDVLYcclplyhntgGTVAWS---------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 233 SVLGMG----------------------ATAFVYNGrfhpetylELlqnyqinvlcCTpteYRMMAKLSHLEQYNleYLH 290
Cdd:PRK08279 261 SVLAAGatlalrrkfsasrfwddvrryrATAFQYIG--------EL----------CR---YLLNQPPKPTDRDH--RLR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 291 SAVSAGepLNREVVEQFKRHFNIT-VRDGYGQTESTllIGFLkDTEPRMGSMG-----KGIPGSFVT--------VIDDD 356
Cdd:PRK08279 318 LMIGNG--LRPDIWDEFQQRFGIPrILEFYAASEGN--VGFI-NVFNFDGTVGrvplwLAHPYAIVKydvdtgepVRDAD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 357 G--KEVGPNVKGNIAVPLDLPALFKGYfKDEARTKAA------STGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYT 427
Cdd:PRK08279 393 GrcIKVKPGEVGLLIGRITDRGPFDGY-TDPEASEKKilrdvfKKGDaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGEN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 428 IGPFEVEDALTNHAAVKECAV--VASP-HDirGNIVKAFIILQDDyEASDelIQELQVFCKNEVAPYKYPRAIEFVENLP 504
Cdd:PRK08279 472 VATTEVENALSGFPGVEEAVVygVEVPgTD--GRAGMAAIVLADG-AEFD--LAALAAHLYERLPAYAVPLFVRLVPELE 546
|
570
....*....|...
gi 1801842045 505 KTNSGKIRRVELR 517
Cdd:PRK08279 547 TTGTFKYRKVDLR 559
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
168-530 |
1.17e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 73.50 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 168 TRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMAPKHWLCIQENDlvwatAAPGWQKW---------VWSPF---LSVL 235
Cdd:PRK09192 174 TPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDGLKVRPGD-----RCVSWLPFyhdmglvgfLLTPVatqLSVD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 236 GMGATAFVYngrfHPETYLELLQNYQINVLCCTPTEYRMMAK---LSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFN 312
Cdd:PRK09192 249 YLPTRDFAR----RPLQWLDLISRNRGTISYSPPFGYELCARrvnSKDLAELDLSCWRVAGIGADMIRPDVLHQFAEAFA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 313 ITVRDG------YGQTESTLLIGFL------------------------KDTEPRMGSM----GKGIPGSFVTVIDDDGK 358
Cdd:PRK09192 325 PAGFDDkafmpsYGLAEATLAVSFSplgsgivveevdrdrleyqgkavaPGAETRRVRTfvncGKALPGHEIEIRNEAGM 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 359 EVGPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIdNDGYFWFEGRRDDIIISSGYTIGPFEVEDALT 438
Cdd:PRK09192 405 PLPERVVGHICV--RGPSLMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAKDLIIINGRNIWPQDIEWIAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 439 NHAAvkecavvasphdIRGNIVKAFIILQDDYEA---------SDE-----LIQELQ--------VFCKNEVAPykyPRA 496
Cdd:PRK09192 482 QEPE------------LRSGDAAAFSIAQENGEKivllvqcriSDEerrgqLIHALAalvrsefgVEAAVELVP---PHS 546
|
410 420 430
....*....|....*....|....*....|....*...
gi 1801842045 497 iefvenLPKTNSGKIRRVELRDA----EIKKYQQQNSS 530
Cdd:PRK09192 547 ------LPRTSSGKLSRAKAKKRylsgAFASLDVAASL 578
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
173-514 |
1.59e-13 |
|
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: 73.16 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 173 AILSYTSGTTGNPKAVTHSHG---W----GYAHLQMAPK--------------H--------WLCIQENDLVWaTAAPGW 223
Cdd:cd05933 153 CTLIYTSGTTGMPKGVMLSHDnitWtakaASQHMDLRPAtvgqesvvsylplsHiaaqildiWLPIKVGGQVY-FAQPDA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 224 QKW-------------------VWSPFLSVL--------GMGATAFVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMA 276
Cdd:cd05933 232 LKGtlvktlrevrptafmgvprVWEKIQEKMkavgaksgTLKRKIASWAKGVGLETNLKLMGGESPSPLFYRLAKKLVFK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 277 KLShlEQYNLEYLHSAVSAGEPLNREVVEQFkRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVI--D 354
Cdd:cd05933 312 KVR--KALGLDRCQKFFTGAAPISRETLEFF-LSLNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHnpD 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 355 DDGKevgpnvkGNIAVPLDLpaLFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDIII-SSGYTIGPFE 432
Cdd:cd05933 389 ADGI-------GEICFWGRH--VFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKELIItAGGENVPPVP 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 433 VEDaltnhaAVKECAVVASPHDIRGNIVKAFIIL--------QDDYEASDELIQELQVFCK---------NEVAPYKYPR 495
Cdd:cd05933 460 IED------AVKKELPIISNAMLIGDKRKFLSMLltlkcevnPETGEPLDELTEEAIEFCRklgsqatrvSEIAGGKDPK 533
|
410
....*....|....*....
gi 1801842045 496 AIEFVENlpktnsgKIRRV 514
Cdd:cd05933 534 VYEAIEE-------GIKRV 545
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
170-518 |
2.06e-13 |
|
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: 72.46 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 170 DDLAILSYTSGTTGNPKAVTHSHGWGYAHLQMAPkHWLCIQENDlVWATAAPGWQKWVWS-PFLSVLGMGATAFVYN--- 245
Cdd:cd05937 87 DDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLS-HDLNLKNGD-RTYTCMPLYHGTAAFlGACNCLMSGGTLALSRkfs 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 246 -GRFHPETYLELLQNYQ-INVLCctptEYRMMAKLSHLEQynleyLHSAVSA-GEPLNREVVEQFKRHFNI-TVRDGYGQ 321
Cdd:cd05937 165 aSQFWKDVRDSGATIIQyVGELC----RYLLSTPPSPYDR-----DHKVRVAwGNGLRPDIWERFRERFNVpEIGEFYAA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 322 TEstlliGFLKDTEPRMGSMGKGIPGS-------------FVTVIDDDGKEVGPNVK------------GNI--AVPLDL 374
Cdd:cd05937 236 TE-----GVFALTNHNVGDFGAGAIGHhglirrwkfenqvVLVKMDPETDDPIRDPKtgfcvrapvgepGEMlgRVPFKN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 375 PALFKGYFKDEARTKAA------STGD-YYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECA 447
Cdd:cd05937 311 REAFQGYLHNEDATESKlvrdvfRKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEAN 390
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801842045 448 V--VASP-HDirGNIVKAFIILQDDYEASDELI-QELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELRD 518
Cdd:cd05937 391 VygVKVPgHD--GRAGCAAITLEESSAVPTEFTkSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
43-517 |
2.31e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 72.82 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVfLNHGLKKGDKVLIMMPRAIVTyelyiAALKLGIAI---VPSseMLR----TKDLQYRITHGEID 115
Cdd:PRK08043 233 SYRKLLKKTLFVGRI-LEKYSVEGERIGLMLPNATIS-----AAVIFGASLrrrIPA--MMNytagVKGLTSAITAAEIK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 116 AVisFSS--------LTKEFENVKEYDqlkkfivaghkedWVSIEDEKEKVN--DDL---------KGADTTR--DDLAI 174
Cdd:PRK08043 305 TI--FTSrqfldkgkLWHLPEQLTQVR-------------WVYLEDLKDDVTtaDKLwifahllmpRLAQVKQqpEDAAL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 175 LSYTSGTTGNPKAVTHSHGWGYAHLQMAPkhwlCIQE---NDLvWATAAP-----GWQKWVWSPFLSvlgmGATAFVYNG 246
Cdd:PRK08043 370 ILFTSGSEGHPKGVVHSHKSLLANVEQIK----TIADftpNDR-FMSALPlfhsfGLTVGLFTPLLT----GAEVFLYPS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 247 RFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHleQYNLEYLHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTL 326
Cdd:PRK08043 441 PLHYRIVPELVYDRNCTVLFGTSTFLGNYARFAN--PYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECAP 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 327 LIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGKEVGPNVKgniavpLDLPALFKGYFKDEA----RTKAASTGD------Y 396
Cdd:PRK08043 519 VVSINVPMAAKPGTVGRILPGMDARLLSVPGIEQGGRLQ------LKGPNIMNGYLRVEKpgvlEVPTAENARgemergW 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 397 YVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDIRGnivKAFIILQDDYEASDEl 476
Cdd:PRK08043 593 YDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKG---EALVLFTTDSELTRE- 668
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1801842045 477 iQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK08043 669 -KLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLK 708
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
166-416 |
9.20e-13 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 70.62 E-value: 9.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 166 DTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHlQMAPKHWLCIQENDLVWATAAP----GWQKWVWSPFLSVLgmgATA 241
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLAN-QRACLKFFSPKEDDVMMSFLPPfhayGFNSCTLFPLLSGV---PVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 242 FVYNgRFHPETYLELLQNYQINVLCCTPTEYRMMAKLSHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYG 320
Cdd:PRK06334 255 FAYN-PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFpHIQLRQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 321 QTESTLLIGFLKDTEPRMGS-MGKGIPGSFVTVIDDDGK-EVGPNVKGNIAVPLDlpALFKGYF-KDEARTKAASTGD-Y 396
Cdd:PRK06334 334 TTECSPVITINTVNSPKHEScVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGT--SLFSGYLgEDFGQGFVELGGEtW 411
|
250 260
....*....|....*....|
gi 1801842045 397 YVTGDQAHIDNDGYFWFEGR 416
Cdd:PRK06334 412 YVTGDLGYVDRHGELFLKGR 431
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
43-527 |
1.03e-12 |
|
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: 70.32 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDK-------------VLIMMprAIVTYelyiaalklGIAIVPSSEMLRTKDLQYRI 109
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGKPAPAsfvgiysinrpewIISEL--ACYAY---------SLVTVPLYDTLGPEAIEYIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 110 THGEIDAV-----ISFSSLtKEFENVKEyDQLKKFIVAghkedwvsiedekekvnddlkgadtTRDDLAILSYTSGTTGN 184
Cdd:cd05927 76 NHAEISIVfcdagVKVYSL-EEFEKLGK-KNKVPPPPP-------------------------KPEDLATICYTSGTTGN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 185 PKAVTHSHG---WGYAHLQMAPKHWLCIQENDlvwataapgwqkwVWSPFL------------SVLGMGATAFVYNGrfH 249
Cdd:cd05927 129 PKGVMLTHGnivSNVAGVFKILEILNKINPTD-------------VYISYLplahifervveaLFLYHGAKIGFYSG--D 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 250 PETYLELLQNYQINVLCCTPTEY------------------RMM------AKLSHLEQYNLEY----------------- 288
Cdd:cd05927 194 IRLLLDDIKALKPTVFPGVPRVLnriydkifnkvqakgplkRKLfnfalnYKLAELRSGVVRAspfwdklvfnkikqalg 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 289 --LHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTlLIGFLKDT-EPRMGSMGKGIPGSFVTVID----------D 355
Cdd:cd05927 274 gnVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECT-AGATLTLPgDTSVGHVGGPLPCAEVKLVDvpemnydakdP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 356 DGK-EV---GPNVkgniavpldlpalFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDGYFWFEGRRDDII-ISSGYTIG 429
Cdd:cd05927 353 NPRgEVcirGPNV-------------FSGYYKDPEKTAEALDEDgWLHTGDIGEWLPNGTLKIIDRKKNIFkLSQGEYVA 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 430 PFEVEDALTNHAAVKE-------------CAVVASPHDI------RGNIVKAFIILQDDYEASDELIQEL-QVFCKNEVA 489
Cdd:cd05927 420 PEKIENIYARSPFVAQifvygdslksflvAIVVPDPDVLkewaasKGGGTGSFEELCKNPEVKKAILEDLvRLGKENGLK 499
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1801842045 490 PYKYPRAIEF------VENLPKTNSGKIRRVELRdaeiKKYQQQ 527
Cdd:cd05927 500 GFEQVKAIHLepepfsVENGLLTPTFKLKRPQLK----KYYKKQ 539
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
140-517 |
3.34e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 67.76 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 140 IVAGHKEDWVSI----EDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNPK-------AVTHSHGWGYAHLQmAPKHWLc 208
Cdd:PRK07824 1 ALAGRAPALLPVpaqdERRAALLRDALRVGEPIDDDVALVVATSGTTGTPKgamltaaALTASADATHDRLG-GPGQWL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 209 iqendlvwaTAAP-----GWQKWVWSpflSVLGMGATAFVYNGRFHPE-------------TYLELlqnyqinvlccTPT 270
Cdd:PRK07824 79 ---------LALPahhiaGLQVLVRS---VIAGSEPVELDVSAGFDPTalpravaelgggrRYTSL-----------VPM 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 271 EyrmMAK-LSHLEQYN-LEYLHSAVSAGEPLNREVVEQFKRhFNITVRDGYGQTESTLliGFLKDteprmgsmGKGIPGS 348
Cdd:PRK07824 136 Q---LAKaLDDPAATAaLAELDAVLVGGGPAPAPVLDAAAA-AGINVVRTYGMSETSG--GCVYD--------GVPLDGV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 349 FVTVIDddgkevgpnvkGNIAvpLDLPALFKGYFKDEARTKAASTGdYYVTGDQAHIDnDGYFWFEGRRDDIIISSGYTI 428
Cdd:PRK07824 202 RVRVED-----------GRIA--LGGPTLAKGYRNPVDPDPFAEPG-WFRTDDLGALD-DGVLTVLGRADDAISTGGLTV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 429 GPFEVEDALTNHAAVKECAVVASPHDIRGNIVKAfIILQDDYEAsdELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNS 508
Cdd:PRK07824 267 LPQVVEAALATHPAVADCAVFGLPDDRLGQRVVA-AVVGDGGPA--PTLEALRAHVARTLDRTAAPRELHVVDELPRRGI 343
|
....*....
gi 1801842045 509 GKIRRVELR 517
Cdd:PRK07824 344 GKVDRRALV 352
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
28-526 |
2.23e-11 |
|
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: 65.97 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 28 KAIIYKDNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSemlrtkdlqy 107
Cdd:cd05908 2 EGIIFILGDKKEKFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVS---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 108 rithgeidavisfssltkeFENVKEYdQLKKFIVAGHKEDWVSIEDEKekVNDDLKgadttrDDLAILSYTSGTTGNPKA 187
Cdd:cd05908 72 -------------------IGSNEEH-KLKLNKVWNTLKNPYLITEEE--VLCELA------DELAFIQFSSGSTGDPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 188 VTHSHGwGYAHLQMAPKHWLCIQENDLVWAtaapgwqkwvWSPFLSVLGMGA-----------TAFVYNGRF--HPETYL 254
Cdd:cd05908 124 VMLTHE-NLVHNMFAILNSTEWKTKDRILS----------WMPLTHDMGLIAfhlapliagmnQYLMPTRLFirRPILWL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 255 ELLQNYQINVLCCTPTEYRMMAKL---SHLEQYNLEYLHSAVSAGEPLNREVVEQFKRHFNI------TVRDGYGQTEST 325
Cdd:cd05908 193 KKASEHKATIVSSPNFGYKYFLKTlkpEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKyglkrnAILPVYGLAEAS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 326 LLIGFLKDTEP----------------------------RMGSMGKGIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPAL 377
Cdd:cd05908 273 VGASLPKAQSPfktitlgrrhvthgepepevdkkdseclTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQ--IRGKNV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 378 FKGYFKDEARTKAASTGDYYV-TGDQAHIDNdGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVA-SPHD- 454
Cdd:cd05908 351 TPGYYNNPEATAKVFTDDGWLkTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcGVNNs 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 455 -IRGNIVKAFII----LQDDYEASDELIQELQVFCK---NEVAPykypraiefVENLPKTNSGKIRRVELRdaeiKKYQQ 526
Cdd:cd05908 430 nTRNEEIFCFIEhrksEDDFYPLGKKIKKHLNKRGGwqiNEVLP---------IRRIPKTTSGKVKRYELA----QRYQS 496
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
34-516 |
6.63e-11 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 64.42 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 34 DNEHENISVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVP---------SSEMLRTKD 104
Cdd:cd17654 9 DQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPidpaspeqrSLTVMKKCH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 105 LQYRITHGEIDavISFSSLTKEfenvkeydqlkkfivaghkedwvsiedekeKVNDDLKgadtTRDDLAILSYTSGTTGN 184
Cdd:cd17654 89 VSYLLQNKELD--NAPLSFTPE------------------------------HRHFNIR----TDECLAYVIHTSGTTGT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 185 PKAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATAApgwqkwVWSPFLSVLGM----GAT-------AFVYNGRFHPETY 253
Cdd:cd17654 133 PKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPL------TFDPSVVEIFLslssGATllivptsVKVLPSKLADILF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 254 lellQNYQINVLCCTPTEYRMMAK-------LSHLEqyNLEYLhsaVSAGEPLNREVVEQFKRH-------FNItvrdgY 319
Cdd:cd17654 207 ----KRHRITVLQATPTLFRRFGSqsikstvLSATS--SLRVL---ALGGEPFPSLVILSSWRGkgnrtriFNI-----Y 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 320 GQTESTLLIGFLKDTEPRMG-SMGKGIPGSFVTVIDDDGKEVGPNVKgniavpldLPALFKGYFKDEARTKAASTgdYYV 398
Cdd:cd17654 273 GITEVSCWALAYKVPEEDSPvQLGSPLLGTVIEVRDQNGSEGTGQVF--------LGGLNRVCILDDEVTVPKGT--MRA 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 399 TGDQAHIDNDGYFwFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVASPHDirgNIVkAFIILQddyEASDELIQ 478
Cdd:cd17654 343 TGDFVTVKDGELF-FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ---RLI-AFIVGE---SSSSRIHK 414
|
490 500 510
....*....|....*....|....*....|....*...
gi 1801842045 479 ELQvfcKNEVAPYKYPRAIEFVENLPKTNSGKIRRVEL 516
Cdd:cd17654 415 ELQ---LTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
165-449 |
1.66e-10 |
|
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: 63.60 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 165 ADTTRDDLAILSYTSGTTGNPKAVTHSHG----WGYAHLQMAPKH------------WL------------------CIQ 210
Cdd:cd17641 153 AAGKGEDVAVLCTTSGTTGKPKLAMLSHGnflgHCAAYLAADPLGpgdeyvsvlplpWIgeqmysvgqalvcgfivnFPE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 211 E-----NDL-------------VW-ATAAPGWQKWVWSP----FLSVLGMGATAFVYNGRFHPETY-LELLQNYQInvlc 266
Cdd:cd17641 233 EpetmmEDLreigptfvllpprVWeGIAADVRARMMDATpfkrFMFELGMKLGLRALDRGKRGRPVsLWLRLASWL---- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 267 CTPTEYRMMAklshlEQYNLEYLHSAVSAGEPLNREVVeQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIP 346
Cdd:cd17641 309 ADALLFRPLR-----DRLGFSRLRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFP 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 347 GSFVTvIDDDGKEVgpnVKGniavpldlPALFKGYFKDEARTKAASTGDYYV-TGDQAHIDNDGYFWFEGRRDDI-IISS 424
Cdd:cd17641 383 GTEVR-IDEVGEIL---VRS--------PGVFVGYYKNPEATAEDFDEDGWLhTGDAGYFKENGHLVVIDRAKDVgTTSD 450
|
330 340
....*....|....*....|....*
gi 1801842045 425 GYTIGPFEVEDALTNHAAVKEcAVV 449
Cdd:cd17641 451 GTRFSPQFIENKLKFSPYIAE-AVV 474
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
172-516 |
3.72e-10 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 62.51 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 172 LAILsYTSGTTGNPKAVTHSHGwG--YAHLQMAPKHWlCIQEND-LVWATaAPGWQKWVWspFLSVLGMGATAFVYNGR- 247
Cdd:PRK03584 266 LWIL-YSSGTTGLPKCIVHGHG-GilLEHLKELGLHC-DLGPGDrFFWYT-TCGWMMWNW--LVSGLLVGATLVLYDGSp 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 248 FHP--ETYLELLQNYQINVLCCTPTEYRMMAK--LSHLEQYNLEYLHSAVSAGEPLNRE----VVEQFKRH---FNITvr 316
Cdd:PRK03584 340 FYPdpNVLWDLAAEEGVTVFGTSAKYLDACEKagLVPGETHDLSALRTIGSTGSPLPPEgfdwVYEHVKADvwlASIS-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 317 dgyGQTE--STLLIGflKDTEP-RMGSM-GKGIpGSFVTVIDDDGKEVGpNVKGNIAVPLDLPALFKGYFKDE--ARTKA 390
Cdd:PRK03584 418 ---GGTDicSCFVGG--NPLLPvYRGEIqCRGL-GMAVEAWDEDGRPVV-GEVGELVCTKPFPSMPLGFWNDPdgSRYRD 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 391 AstgdYYVT-------GDQAHIDNDGYFWFEGRRDDIIISSGYTIG-----------PfEVEDALtnhaavkecaVVASP 452
Cdd:PRK03584 491 A----YFDTfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGGVRIGtaeiyrqvealP-EVLDSL----------VIGQE 555
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801842045 453 HDIRGNIVKAFIILQDDYEASDELIQELQVFCKNEVAPYKYPRAIEFVENLPKTNSGKIrrVEL 516
Cdd:PRK03584 556 WPDGDVRMPLFVVLAEGVTLDDALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKK--VEL 617
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
41-516 |
6.27e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 62.49 E-value: 6.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 41 SVSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVISF 120
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQ 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 121 SSLTKEFENVK-----EYDQLkkfivagHKEDWVSiedekekvndDLKGADTTRDDLAILSYTSGTTGNPKAVTHSHGwg 195
Cdd:PRK05691 1236 SHLLERLPQAEgvsaiALDSL-------HLDSWPS----------QAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHA-- 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 196 yahlQMAPK-HWL----CIQENDLVWATAAPGWQKWVWSPFLSVLgMGATAFVYNGRFH--PETYLELLQNYQINVLCCT 268
Cdd:PRK05691 1297 ----ALAERlQWMqatyALDDSDVLMQKAPISFDVSVWECFWPLI-TGCRLVLAGPGEHrdPQRIAELVQQYGVTTLHFV 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 269 PTEYRMMAKLSHLEQYNleYLHSAVSAGEPLNREVVEQFKRHF-NITVRDGYGQTESTLLIGF----LKDTEprMGSMGK 343
Cdd:PRK05691 1372 PPLLQLFIDEPLAAACT--SLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHwqcqAEDGE--RSPIGR 1447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 344 GIPGSFVTVIDDDGKEVGPNVKGNIAvpLDLPALFKGYFKDEARTK----AASTGD----YYVTGDQAHIDNDGYFWFEG 415
Cdd:PRK05691 1448 PLGNVLCRVLDAELNLLPPGVAGELC--IGGAGLARGYLGRPALTAerfvPDPLGEdgarLYRTGDRARWNADGALEYLG 1525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 416 RRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVasphdIRGNIVKAFIILQDDYEASDELIQE-LQVFCKNEVAPYKYP 494
Cdd:PRK05691 1526 RLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLVGYYTGEAGQEAEAErLKAALAAELPEYMVP 1600
|
490 500
....*....|....*....|..
gi 1801842045 495 RAIEFVENLPKTNSGKIRRVEL 516
Cdd:PRK05691 1601 AQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
22-517 |
2.07e-09 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 60.36 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 22 ASEDH--KKAIIykdNEHENISVSYKELISNANKVGNVfLNHGLKKGDKVLIMMPRAIvtyelyiaalklGIAIVPSSEM 99
Cdd:PRK06814 640 AAKIHgfKKLAV---EDPVNGPLTYRKLLTGAFVLGRK-LKKNTPPGENVGVMLPNAN------------GAAVTFFALQ 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 100 lrtkdlqyriTHGEIDAVISFSSLTKEFENVKEYDQLK------KFIVAGHKEDWVS----------IEDEKEKVN--DD 161
Cdd:PRK06814 704 ----------SAGRVPAMINFSAGIANILSACKAAQVKtvltsrAFIEKARLGPLIEalefgiriiyLEDVRAQIGlaDK 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 162 LKG---------ADTTR--DDLAILSYTSGTTGNPKAVTHSHGWGYAHL-QMAPKhwLCIQENDLVWaTAAPgwqkwVWS 229
Cdd:PRK06814 774 IKGllagrfplvYFCNRdpDDPAVILFTSGSEGTPKGVVLSHRNLLANRaQVAAR--IDFSPEDKVF-NALP-----VFH 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 230 PFLSVLGM------GATAFVYNGRFHPETYLELLqnYQIN--VLCCTPTEYRMMAKLSH-LEQYNLEYlhsaVSAG-EPL 299
Cdd:PRK06814 846 SFGLTGGLvlpllsGVKVFLYPSPLHYRIIPELI--YDTNatILFGTDTFLNGYARYAHpYDFRSLRY----VFAGaEKV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 300 NREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPG-----SFVTVIDDDGKEV--GPNVkgniavpl 372
Cdd:PRK06814 920 KEETRQTWMEKFGIRILEGYGVTETAPVIALNTPMHNKAGTVGRLLPGieyrlEPVPGIDEGGRLFvrGPNV-------- 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 373 dlpalFKGYFKDEA-RTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDIIISSGYTIGPFEVEDALTNHAAVKECAVVAS 451
Cdd:PRK06814 992 -----MLGYLRAENpGVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSI 1066
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801842045 452 PHDIRGnivKAFIILQDDYEASDEliqELQVFCKNEVAPYKY-PRAIEFVENLPKTNSGKIRRVELR 517
Cdd:PRK06814 1067 PDARKG---ERIILLTTASDATRA---AFLAHAKAAGASELMvPAEIITIDEIPLLGTGKIDYVAVT 1127
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
166-453 |
3.66e-09 |
|
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: 59.15 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 166 DTTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHL----QMAPKHwlcIQENDLVWAtaapgwqkwvWSPFLSVLGMGAT- 240
Cdd:cd17639 84 DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIaglgDRVPEL---LGPDDRYLA----------YLPLAHIFELAAEn 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 241 -AFVYNGRF---HPETYLEL--------LQNYQINVLCCTP----TEYR-MMAKLS-----------HLEQYNLEYLHS- 291
Cdd:cd17639 151 vCLYRGGTIgygSPRTLTDKskrgckgdLTEFKPTLMVGVPaiwdTIRKgVLAKLNpmgglkrtlfwTAYQSKLKALKEg 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 292 ------------------------AVSAGEPLNREVveqfKRHFNITVRD---GYGQTESTLLIGFLKDTEPRMGSMGKG 344
Cdd:cd17639 231 pgtplldelvfkkvraalggrlryMLSGGAPLSADT----QEFLNIVLCPviqGYGLTETCAGGTVQDPGDLETGRVGPP 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 345 IPGSFVTVID-DDGKEV--GPNVKGNIAvpLDLPALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDGYFWFEGRRDDI 420
Cdd:cd17639 307 LPCCEIKLVDwEEGGYStdKPPPRGEIL--IRGPNVFKGYYKNPEKTKEAFDGDgWFHTGDIGEFHPDGTLKIIDRKKDL 384
|
330 340 350
....*....|....*....|....*....|....
gi 1801842045 421 I-ISSGYTIGPFEVEDALTNHAAVKECAVVASPH 453
Cdd:cd17639 385 VkLQNGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
173-523 |
7.00e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 58.29 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 173 AILsYTSGTTGNPKAVTHSH---------GWgyAHLQMAPKHWLCiqendlvWATAApgwqKWVWSPFL--SVLGMGATA 241
Cdd:PLN03051 123 NIL-FSSGTTGEPKAIPWTHlsplrcasdGW--AHMDIQPGDVVC-------WPTNL----GWMMGPWLlySAFLNGATL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 242 FVYNGRFHPETYLELLQNYQINVLCCTPTEYRMMAK--LSHLEQYNLEYLHSAVSAGEPLNREVVeqfkrHFNITVRdGY 319
Cdd:PLN03051 189 ALYGGAPLGRGFGKFVQDAGVTVLGLVPSIVKAWRHtgAFAMEGLDWSKLRVFASTGEASAVDDV-----LWLSSVR-GY 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 320 --------GQTE-------STLLI--GFLKDTEPRMGsmgkgipGSFVtVIDDDGKE--VGPNVKGNIAV-PLDLPALFK 379
Cdd:PLN03051 263 ykpvieycGGTElasgyisSTLLQpqAPGAFSTASLG-------TRFV-LLNDNGVPypDDQPCVGEVALaPPMLGASDR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 380 GYFKDEARTKAASTGDYYVTGDQAHIDND-------GYFWFEGRRDDIIISSGYTIGPFEVEDALTN-HAAVKECAVVAS 451
Cdd:PLN03051 335 LLNADHDKVYYKGMPMYGSKGMPLRRHGDimkrtpgGYFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGV 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 452 PHDIRGN----IVKAFIILQDDYEASDEliQELQVFC----KNEVAP-YKYPRaIEFVENLPKTNSGKIRRVELRDaEIK 522
Cdd:PLN03051 415 APPDGGPellvIFLVLGEEKKGFDQARP--EALQKKFqeaiQTNLNPlFKVSR-VKIVPELPRNASNKLLRRVLRD-QLK 490
|
.
gi 1801842045 523 K 523
Cdd:PLN03051 491 K 491
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
167-409 |
2.46e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 56.52 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 167 TTRDDLAILSYTSGTTGNPKAVTHSHGWGYAHLqMAPKHWLciqeNDLVwatAAPGWQKWVWS--PFLSVLGMGATA-FV 243
Cdd:PTZ00216 261 ENNDDLALIMYTSGTTGDPKGVMHTHGSLTAGI-LALEDRL----NDLI---GPPEEDETYCSylPLAHIMEFGVTNiFL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 244 YNGRF----HPETYLEL-------LQNYQINVLCCTPTEYRMM-----AKL-----------SHLEQYNLEYLH------ 290
Cdd:PTZ00216 333 ARGALigfgSPRTLTDTfarphgdLTEFRPVFLIGVPRIFDTIkkaveAKLppvgslkrrvfDHAYQSRLRALKegkdtp 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 291 -------------------SAVSAGEPLNREVVEQFKRHFNITVRdGYGQTESTLL--IGFLKDTEPrmGSMGKGIPGSF 349
Cdd:PTZ00216 413 ywnekvfsapravlggrvrAMLSGGGPLSAATQEFVNVVFGMVIQ-GWGLTETVCCggIQRTGDLEP--NAVGQLLKGVE 489
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1801842045 350 VTVIDDDG-KEVG-PNVKGNIAvpLDLPALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDG 409
Cdd:PTZ00216 490 MKLLDTEEyKHTDtPEPRGEIL--LRGPFLFKGYYKQEELTREVLDEDgWFHTGDVGSIAANG 550
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
293-448 |
4.24e-08 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 55.88 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 293 VSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVID--------DDgkevGPNV 364
Cdd:PLN02736 382 SSGASPLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDNLSGHVGSPNPACEVKLVDvpemnytsED----QPYP 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 365 KGNIAVplDLPALFKGYFKDEARTKAAstgdyyvtgdqahIDNDGYF-------WFEGRRDDII--------ISSGYTIG 429
Cdd:PLN02736 458 RGEICV--RGPIIFKGYYKDEVQTREV-------------IDEDGWLhtgdiglWLPGGRLKIIdrkknifkLAQGEYIA 522
|
170
....*....|....*....
gi 1801842045 430 PFEVEDALTNHAAVKECAV 448
Cdd:PLN02736 523 PEKIENVYAKCKFVAQCFV 541
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
173-517 |
8.19e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.77 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 173 AILSYTSGTTGNPK-------AVTHSHGWGYAHLQMAPKH-----WLCIQeNDLVWAT-------AAPGWQkwvwSPfls 233
Cdd:PRK05851 155 AVLQGTAGSTGTPRtailspgAVLSNLRGLNARVGLDAATdvgcsWLPLY-HDMGLAFlltaalaGAPLWL----AP--- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 234 vlgmgATAFVYNgrfhPETYLELLQNYQINVLCCTPTEYRMMAKLS-HLEQYNLEYLHSAVSAGEPLNrevVEQFKRHFN 312
Cdd:PRK05851 227 -----TTAFSAS----PFRWLSWLSDSRATLTAAPNFAYNLIGKYArRVSDVDLGALRVALNGGEPVD---CDGFERFAT 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 313 ITVRDG---------YGQTESTLLI-------GFLKD--TEP------RMGSMGKGIPGSFVTV------IDDDGKEVGP 362
Cdd:PRK05851 295 AMAPFGfdagaaapsYGLAESTCAVtvpvpgiGLRVDevTTDdgsgarRHAVLGNPIPGMEVRIspgdgaAGVAGREIGE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 363 -NVKGNiavpldlpALFKGYFKDEArtkaASTGDYYVTGDQAHIDNDGYFwFEGRRDDIIISSGYTIGPFEVEDALTNHA 441
Cdd:PRK05851 375 iEIRGA--------SMMSGYLGQAP----IDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVR 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 442 AVKECAVVASPHDIR----GNIVKAFIILQDDYEASDELIQELQVFCKnevapyKYPRAIEFVE--NLPKTNSGKIRRVE 515
Cdd:PRK05851 442 GVREGAVVAVGTGEGsarpGLVIAAEFRGPDEAGARSEVVQRVASECG------VVPSDVVFVApgSLPRTSSGKLRRLA 515
|
..
gi 1801842045 516 LR 517
Cdd:PRK05851 516 VK 517
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
178-330 |
1.07e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.92 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 178 TSGTTGNPKAVTHSH------GWGYAH-LQMAPkhwlcIQENDLVWATAAPGWqkwvWSPFLSV-LG---MGATAFVY-N 245
Cdd:COG1541 91 SSGTTGKPTVVGYTRkdldrwAELFARsLRAAG-----VRPGDRVQNAFGYGL----FTGGLGLhYGaerLGATVIPAgG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 246 GRfhPETYLELLQNYQINVLCCTPTEYRMMAKlsHLEQYNLEY----LHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQ 321
Cdd:COG1541 162 GN--TERQLRLMQDFGPTVLVGTPSYLLYLAE--VAEEEGIDPrdlsLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGL 237
|
....*....
gi 1801842045 322 TESTLLIGF 330
Cdd:COG1541 238 TEVGPGVAY 246
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
42-401 |
2.61e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 46.80 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVPSSEM--LRTKD---LQY---RITHGE 113
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAysLVSQDfgkLRHvleLLTPGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 114 IdavisFSSLTKEFEN---VKEYDQLKKFIVAGHKED-----WVSIEDEKEKVNDDLKGADTTRDDLAILSYTSGTTGNP 185
Cdd:PRK08180 150 V-----FADDGAAFARalaAVVPADVEVVAVRGAVPGraatpFAALLATPPTAAVDAAHAAVGPDTIAKFLFTSGSTGLP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 186 KAVTHSHGWGYAHLQMAPKHWLCIQENDLVWATAAPgwqkwvWSPFL---SVLGM----GATAFVYNGRFHPETYLELLQ 258
Cdd:PRK08180 225 KAVINTHRMLCANQQMLAQTFPFLAEEPPVLVDWLP------WNHTFggnHNLGIvlynGGTLYIDDGKPTPGGFDETLR 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 259 N-------YQINVlcctPTEYRMMAKlsHLEQ---------YNLEYLHSAvSAGEP---LNR--EVVEQFKRHfNITVRD 317
Cdd:PRK08180 299 NlreisptVYFNV----PKGWEMLVP--ALERdaalrrrffSRLKLLFYA-GAALSqdvWDRldRVAEATCGE-RIRMMT 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 318 GYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDGK-EV---GPNVkgniavpldlpalFKGYFKDEARTKAAST 393
Cdd:PRK08180 371 GLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPVGGKlEVrvkGPNV-------------TPGYWRAPELTAEAFD 437
|
....*....
gi 1801842045 394 GD-YYVTGD 401
Cdd:PRK08180 438 EEgYYRSGD 446
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
43-465 |
2.38e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 43.86 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIM---MPRAIVTYElyiAALKLGIAIVPSSEMLRTKDLQYRITHGEIDAVI- 118
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYganSPEWIISME---ACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFv 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 119 ---SFSSLTKEFENVKEYdqLKKFIVAGHkedwVSIE--DEKEKV-------NDDLKGADTTRDDLAI--------LSYT 178
Cdd:PLN02614 158 eekKISELFKTCPNSTEY--MKTVVSFGG----VSREqkEEAETFglviyawDEFLKLGEGKQYDLPIkkksdictIMYT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 179 SGTTGNPKAVTHSHG------WGYAHLQMAPKHWLCIQENDLVWATAAPGWQKWVWSPFLSVlgmGATAFVYNGRFhpET 252
Cdd:PLN02614 232 SGTTGDPKGVMISNEsivtliAGVIRLLKSANAALTVKDVYLSYLPLAHIFDRVIEECFIQH---GAAIGFWRGDV--KL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 253 YLELLQNYQINVLCCTPteyRMMAKL-SHLEQ------------------YNLEYL---HSAVSAGEPLNREVVEQFKRH 310
Cdd:PLN02614 307 LIEDLGELKPTIFCAVP---RVLDRVySGLQKklsdggflkkfvfdsafsYKFGNMkkgQSHVEASPLCDKLVFNKVKQG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 311 FNITVR--------------------------DGYGQTESTL-LIGFLKDTEPRMGSMGKGIPGSFV---TVIDDDGKEV 360
Cdd:PLN02614 384 LGGNVRiilsgaaplashvesflrvvacchvlQGYGLTESCAgTFVSLPDELDMLGTVGPPVPNVDIrleSVPEMEYDAL 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 361 GPNVKGNIAVplDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDII-ISSGYTIGPFEVEDALTN 439
Cdd:PLN02614 464 ASTPRGEICI--RGKTLFSGYYKREDLTKEVLIDGWLHTGDVGEWQPNGSMKIIDRKKNIFkLSQGEYVAVENIENIYGE 541
|
490 500
....*....|....*....|....*.
gi 1801842045 440 HAAVKECAVVasphdirGNIVKAFII 465
Cdd:PLN02614 542 VQAVDSVWVY-------GNSFESFLV 560
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
127-325 |
2.40e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 43.77 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 127 FENVKEYdqLKKFIVAG-HKEDWVSIED-------EKEKVNDD-----LKGAdttRDDLAILSYTSGTTGNPKAVthshg 193
Cdd:cd05913 27 YENVPFY--RRKFAAAGiDPDDIKSLDDlrklpftTKEDLRDNypfglFAVP---REKVVRIHASSGTTGKPTVV----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 194 wGYAHlqmapkhwlciqeNDL-VWA-------TAAPGWQKWV------WSPFLSVLG-------MGATAF-VYNGRfhPE 251
Cdd:cd05913 97 -GYTK-------------NDLdVWAelvarclDAAGVTPGDRvqnaygYGLFTGGLGfhygaerLGALVIpAGGGN--TE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801842045 252 TYLELLQNYQINVLCCTPTeyrMMAKL-SHLEQYNLEY----LHSAVSAGEPLNREVVEQFKRHFNITVRDGYGQTEST 325
Cdd:cd05913 161 RQLQLIKDFGPTVLCCTPS---YALYLaEEAEEEGIDPrelsLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEII 236
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
43-199 |
4.21e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 42.94 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 43 SYKELISNANKVGNVFLNHGLKKGDKVLIMMPRAIVTYELYIAALKLGIAIVP----SSEMLRTKDL-QYRITHGEI-DA 116
Cdd:PRK09029 30 TWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPlnpqLPQPLLEELLpSLTLDFALVlEG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 117 VISFSSLTkefenvkeyDQLKKFIVAGHKEDWvsiedekekvnddlkgaDTTRddLAILSYTSGTTGNPKAVTHSHGwgy 196
Cdd:PRK09029 110 ENTFSALT---------SLHLQLVEGAHAVAW-----------------QPQR--LATMTLTSGSTGLPKAAVHTAQ--- 158
|
...
gi 1801842045 197 AHL 199
Cdd:PRK09029 159 AHL 161
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
35-191 |
5.45e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 42.72 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 35 NEHENISVSYKELISNANKVGNVFLNH-GLKKGDKVLIMMPRAIVtyelYIAA----LKLGIAIVPSSEMLRTKDLQYRI 109
Cdd:cd05905 8 KGKEATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLD----FVAAfygcLYAGVVPIPIEPPDISQQLGFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 110 THGEIDAVISFSSLTKEF----ENVKEYDQLKKFIVAGHKEDWVSIEDEKEKVNDDLKGADTTRD-DLAILSYTSGTTG- 183
Cdd:cd05905 84 GTCKVRVALTVEACLKGLpkklLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTRDgDTAYIEYSFSSDGs 163
|
....*....
gi 1801842045 184 -NPKAVTHS 191
Cdd:cd05905 164 lSGVAVSHS 172
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
294-452 |
1.01e-03 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 42.03 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 294 SAGEPLNREVveqfKRHFNIT----VRDGYGQTESTLLIGFLKDTEPRMGSMGKGIPGSFVTVIDDDgkEVG------PN 363
Cdd:PLN02387 427 SGGAPLSGDT----QRFINIClgapIGQGYGLTETCAGATFSEWDDTSVGRVGPPLPCCYVKLVSWE--EGGylisdkPM 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 364 VKGNIAVplDLPALFKGYFKDEARTKAASTGD-----YYVTGDQAHIDNDGYFWFEGRRDDII-ISSGYTIGPFEVEDAL 437
Cdd:PLN02387 501 PRGEIVI--GGPSVTLGYFKNQEKTDEVYKVDergmrWFYTGDIGQFHPDGCLEIIDRKKDIVkLQHGEYVSLGKVEAAL 578
|
170
....*....|....*
gi 1801842045 438 TNHAAVKECAVVASP 452
Cdd:PLN02387 579 SVSPYVDNIMVHADP 593
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
285-416 |
1.30e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 41.63 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 285 NLEYLhsaVSAGEPLNREVVEQFKRHFNITVRDGYGQTESTLLIgFLKDTEP-RMGSMGKGI-PGSFVTVID---DDGKE 359
Cdd:PTZ00342 462 NLEVI---LNGGGKLSPKIAEELSVLLNVNYYQGYGLTETTGPI-FVQHADDnNTESIGGPIsPNTKYKVRTwetYKATD 537
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801842045 360 VGPnvKGNIAVPLDlpALFKGYFKDEARTKAASTGD-YYVTGDQAHIDNDGYFWFEGR 416
Cdd:PTZ00342 538 TLP--KGELLIKSD--SIFSGYFLEKEQTKNAFTEDgYFKTGDIVQINKNGSLTFLDR 591
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
42-465 |
1.89e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 40.98 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 42 VSYKELISNANKVGNVFLNHGLKKGDKVLIM---MPRAIVTYElyiAALKLGIAIVPSSEMLRTKDLQYRITHGEID-AV 117
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYgsnCPEWIIAME---ACNSQGITYVPLYDTLGANAVEFIINHAEVSiAF 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 118 ISFSSLTKEFENVKE-YDQLKKFIVAGHKEDWVSIEDEKEKV------------NDDLKGADTTRDDLAILSYTSGTTGN 184
Cdd:PLN02861 155 VQESKISSILSCLPKcSSNLKTIVSFGDVSSEQKEEAEELGVscfsweefslmgSLDCELPPKQKTDICTIMYTSGTTGE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 185 PKAVTHSHGWGYAHLqMAPKHWLciQENDLVWATAapgwqkwvwSPFLSVLGMG-------ATAFVYNG------RFHPE 251
Cdd:PLN02861 235 PKGVILTNRAIIAEV-LSTDHLL--KVTDRVATEE---------DSYFSYLPLAhvydqviETYCISKGasigfwQGDIR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 252 TYLELLQNYQINVLCCTPTEYR-----MMAKLS-------HLEQYNLEY------------------------------- 288
Cdd:PLN02861 303 YLMEDVQALKPTIFCGVPRVYDriytgIMQKISsggmlrkKLFDFAYNYklgnlrkglkqeeasprldrlvfdkikeglg 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 289 --LHSAVSAGEPLNREvVEQFKRHFNI-TVRDGYGQTESTL-LIGFLKDTEPRMGSMgkGIPGSFVTVIDDDGKEVGPNV 364
Cdd:PLN02861 383 grVRLLLSGAAPLPRH-VEEFLRVTSCsVLSQGYGLTESCGgCFTSIANVFSMVGTV--GVPMTTIEARLESVPEMGYDA 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801842045 365 KGNIA---VPLDLPALFKGYFKDEARTKAASTGDYYVTGDQAHIDNDGYFWFEGRRDDII-ISSGYTIGPFEVEDALTnh 440
Cdd:PLN02861 460 LSDVPrgeICLRGNTLFSGYHKRQDLTEEVLIDGWFHTGDIGEWQPNGAMKIIDRKKNIFkLSQGEYVAVENLENTYS-- 537
|
490 500
....*....|....*....|....*
gi 1801842045 441 aavkECAVVASPHdIRGNIVKAFII 465
Cdd:PLN02861 538 ----RCPLIASIW-VYGNSFESFLV 557
|
|
| |
