|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
49-552 |
0e+00 |
|
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: 1030.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 49 VPEYFNFAHDVLDVWSRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEW 128
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 129 WLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRELLR 208
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 209 EASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAW-TLFSAWP 287
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 288 NGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELY 367
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 368 EGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRPTRPFCFFNCYLDNPEKTAASEQ 447
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 448 GDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSH 527
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500
....*....|....*....|....*
gi 1024336653 528 DPEALTRELQEHVKRVTAPYKYPRK 552
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRK 505
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
49-552 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 550.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 49 VPEYFNFAHDVLDVWsrleeAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEW 128
Cdd:COG0365 4 VGGRLNIAYNCLDRH-----AEGRGDKVALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 129 WLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD---------SLAPRVDAISAECPSLQTKLLV----SDS 195
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 196 SRPGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESDIFWNTTDTGW 275
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 276 VKAAW-TLFSAWPNGSCIFVHE--LPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQED---LTRYQFQSLRHCLTGGEA 349
Cdd:COG0365 238 ATGHSyIVYGPLLNGATVVLYEgrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 350 LNPDVREKWKHQTGVELYEGYGQSETV-VICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRirptRP 428
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK----GP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 429 F-CFFNCYLDNPEKTAASEQGDF---YITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS 504
Cdd:COG0365 394 WpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1024336653 505 SPDPIRGEVVKAFIVLTPAYSshDPEALTRELQEHVKRVTAPYKYPRK 552
Cdd:COG0365 474 VPDEIRGQVVKAFVVLKPGVE--PSDELAKELQAHVREELGPYAYPRE 519
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
48-551 |
0e+00 |
|
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: 544.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 48 LVPEYFNFAHDVLDVWSRLEeaghrPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPE 127
Cdd:cd05970 11 NVPENFNFAYDVVDAMAKEY-----PDKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 128 WWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT--SDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRE 205
Cdd:cd05970 85 FWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 206 LLREASTE----HNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSsYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAW- 280
Cdd:cd05970 165 LIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWg 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 281 TLFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKH 360
Cdd:cd05970 244 KIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 361 QTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRPTRPFCFFNCYLDNPE 440
Cdd:cd05970 324 KTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 441 KTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 520
Cdd:cd05970 404 KTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVL 483
|
490 500 510
....*....|....*....|....*....|.
gi 1024336653 521 TPAYSShdPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05970 484 AKGYEP--SEELKKELQDHVKKVTAPYKYPR 512
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
90-552 |
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: 541.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 90 WSFEELGKQSRKAANVLGGaCGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 170 DSlaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksrDPLAIYFTSGTTGAPKMVEHSqSSYGL 249
Cdd:cd05972 80 AE---------------------------------------------------DPALIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 250 GFVASGRRWVALTESDIFWNTTDTGWVKAAW-TLFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLV 328
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 329 QEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEG 408
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 409 NVLPPGEEGNVAVRIRPTRPFCFfncYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVE 488
Cdd:cd05972 268 RELPPGEEGDIAIKLPPPGLFLG---YVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024336653 489 SALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSshDPEALTRELQEHVKRVTAPYKYPRK 552
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPRE 406
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
54-551 |
6.38e-122 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 371.54 E-value: 6.38e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 54 NFAHDVLDvwsRlEEAGHRPPNPAFWWVNGTGAEiKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSV 133
Cdd:PRK04319 43 NIAYEAID---R-HADGGRKDKVALRYLDASRKE-KYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 134 ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVdaISAECPSLQTKLLVSDSSR--PGWLNFRELLREAS 211
Cdd:PRK04319 117 GALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLDFNALMEQAS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 212 TEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRrWVA-LTESDIFWNTTDTGWVKA-AWTLFSAWPNG 289
Cdd:PRK04319 195 DEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAM-LQHYQTGK-YVLdLHEDDVYWCTADPGWVTGtSYGIFAPWLNG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 290 SCIFVHElPRVDAKVILNTLSKFPITTLCCVPTIFRLLV---QEDLTRYQFQSLRHCLTGGEALNPDVReKWKHQT-GVE 365
Cdd:PRK04319 273 ATNVIDG-GRFSPERWYRILEDYKVTVWYTAPTAIRMLMgagDDLVKKYDLSSLRHILSVGEPLNPEVV-RWGMKVfGLP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 366 LYEGYGQSET--VVICaNPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAvrIRPTRPfCFFNCYLDNPEKTA 443
Cdd:PRK04319 351 IHDNWWMTETggIMIA-NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLA--IKKGWP-SMMRGIWNNPEKYE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 444 ASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPA 523
Cdd:PRK04319 427 SYFAGDWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPG 506
|
490 500
....*....|....*....|....*....
gi 1024336653 524 YsshDP-EALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK04319 507 Y---EPsEELKEEIRGFVKKGLGAHAAPR 532
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
91-570 |
2.39e-115 |
|
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: 349.94 E-value: 2.39e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd05974 2 SFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SlaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLG 250
Cdd:cd05974 81 N-----------------------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 251 FVASgRRWVALTESDIFWNTTDTGWVKAAWT-LFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQ 329
Cdd:cd05974 114 HLST-MYWIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 330 EDLTRYQFqSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGN 409
Cdd:cd05974 193 QDLASFDV-KLREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 410 vlpPGEEGNVAVRIRPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVES 489
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 490 ALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALtrELQEHVKRVTAPYKYPRKncqRRFLERSKGVNCEV 569
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETAL--EIFRFSRERLAPYKRIRR---LEFAELPKTISGKI 423
|
.
gi 1024336653 570 R 570
Cdd:cd05974 424 R 424
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
90-552 |
2.46e-112 |
|
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: 342.56 E-value: 2.46e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 170 DSLAPRVDAisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksRDPLAIYFTSGTTGAPKMVEHSQSSYGL 249
Cdd:cd05969 80 EELYERTDP-------------------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 250 GFVaSGRRWVALTESDIFWNTTDTGWVK-AAWTLFSAWPNGSCIFVHElPRVDAKVILNTLSKFPITTLCCVPTIFRLLV 328
Cdd:cd05969 117 YYF-TGKYVLDLHPDDIYWCTADPGWVTgTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 329 QED---LTRYQFQSLRHCLTGGEALNPDVReKWKHQT-GVELYEGYGQSETVVIC-ANPKGMKIKSGSMGKASPPYDVQI 403
Cdd:cd05969 195 KEGdelARKYDLSSLRFIHSVGEPLNPEAI-RWGMEVfGVPIHDTWWQTETGSIMiANYPCMPIKPGSMGKPLPGVKAAV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 404 VDDEGNVLPPGEEGNVAvrIRPTRPfCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIG 483
Cdd:cd05969 274 VDENGNELPPGTKGILA--LKPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024336653 484 PVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDpeALTRELQEHVKRVTAPYKYPRK 552
Cdd:cd05969 351 PFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD--ELKEEIINFVRQKLGAHVAPRE 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
57-552 |
1.66e-104 |
|
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: 322.53 E-value: 1.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 57 HDVLDVWsrleeAGHRPPNPAFwwvngTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACM 136
Cdd:COG0318 2 ADLLRRA-----AARHPDRPAL-----VFGGRRLTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 137 RTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSdslaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehnc 216
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVTA----------------------------------------------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 217 mrtksrdplAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFWNTT----DTGWVkaaWTLFSAWPNGSCI 292
Cdd:COG0318 104 ---------LILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGLT---VGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 293 FVheLPRVDAKVILNTLSKFPITTLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYG 371
Cdd:COG0318 171 VL--LPRFDPERVLELIERERVTVLFGVPTMLaRLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 372 QSET-VVICANPKGMK-IKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRirptrPFCFFNCYLDNPEKTAASEQGD 449
Cdd:COG0318 249 LTETsPVVTVNPEDPGeRRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 450 FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDP 529
Cdd:COG0318 324 WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDA 402
|
490 500
....*....|....*....|...
gi 1024336653 530 EALTRELQEHVkrvtAPYKYPRK 552
Cdd:COG0318 403 EELRAFLRERL----ARYKVPRR 421
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
85-551 |
3.78e-99 |
|
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: 308.21 E-value: 3.78e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 85 GAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAK 164
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 165 SIITsdslaprvDAisaecpslqtkllvsdssrpgwlnfrellreastehncmrtkSRDPLAIYFTSGTTGAPKMVEHSQ 244
Cdd:cd05971 81 ALVT--------DG------------------------------------------SDDPALIIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 S-------SYGLGFVASGRRwvalteSDIFWNTTDTGWVKAAW-TLFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITT 316
Cdd:cd05971 111 RvllghlpGVQFPFNLFPRD------GDLYWTPADWAWIGGLLdVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 317 LCCVPTIFRLLVQEDLTRYQFQ-SLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET-VVICANPKGMKIKSGSMGK 394
Cdd:cd05971 185 AFLPPTALKMMRQQGEQLKHAQvKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECnLVIGNCSALFPIKPGSMGK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 395 ASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrPFCFFNcYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDV 474
Cdd:cd05971 265 PIPGHRVAIVDDNGTPLPPGEVGEIAVE-LPD-PVAFLG-YWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 475 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSshDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05971 342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPR 416
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
223-552 |
1.56e-97 |
|
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: 300.36 E-value: 1.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHelPRVDA 302
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 303 KVILNTLSKFPITTLCCVPTIFRLLVQEDL-TRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET--VVIC 379
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPEsAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 380 ANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIrPTRpfcfFNCYLDNPEKTAASEQGDFYITGDRARM 459
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRG-PSV----MKGYWNNPEATAAVDEDGWYRTGDLGRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 460 DKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAyssHDPEAltRELQEH 539
Cdd:cd04433 233 DEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG---ADLDA--EELRAH 307
|
330
....*....|...
gi 1024336653 540 VKRVTAPYKYPRK 552
Cdd:cd04433 308 VRERLAPYKVPRR 320
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
66-552 |
1.76e-93 |
|
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: 294.47 E-value: 1.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 66 LEE-AGHRPPNPAFWWvngTGAeiKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:cd05936 5 LEEaARRFPDKTALIF---MGR--KLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 145 GVTQLTEKDLKYRLQASRAKSIITSDSlaprvdaisaecpslqtkllvsdssrpgwlnFRELLRE-ASTEHNCMRTKSrD 223
Cdd:cd05936 79 LNPLYTPRELEHILNDSGAKALIVAVS-------------------------------FTDLLAAgAPLGERVALTPE-D 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 224 PLAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWV--ALTESDIFwnttdtgwVKA-------AWT--LFSAWPNGSCI 292
Cdd:cd05936 127 VAVLQYTSGTTGVPKGAMLTHRNL-VANALQIKAWLedLLEGDDVV--------LAAlplfhvfGLTvaLLLPLALGATI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 293 FVheLPRVDAKVILNTLSKFPITTLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYG 371
Cdd:cd05936 198 VL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYiALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 372 QSETV-VICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTRpfcfFNCYLDNPEKTAASEQGDF 450
Cdd:cd05936 276 LTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-GPQV----MKGYWNRPEETAEAFVDGW 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 451 YITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLtpayssHDPE 530
Cdd:cd05936 351 LRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL------KEGA 424
|
490 500
....*....|....*....|...
gi 1024336653 531 ALT-RELQEHVKRVTAPYKYPRK 552
Cdd:cd05936 425 SLTeEEIIAFCREQLAGYKVPRQ 447
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
51-551 |
6.13e-92 |
|
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: 291.97 E-value: 6.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 51 EYFNFAHDVLDvwsRLEEAghRPPNPAFWWVNGTgaeikWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWL 130
Cdd:cd05959 1 EKYNAATLVDL---NLNEG--RGDKTAFIDDAGS-----LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 131 VSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRV-DAISAECPSLQTkLLVSDSSRP--GWLNFRELL 207
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLaAALTKSEHTLVV-LIVSGGAGPeaGALLLAELV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 208 REASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESDIFWNTTdtgwvkaawTLFSAWP 287
Cdd:cd05959 149 AAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAA---------KLFFAYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 288 NG-SCIF--------VHELPRVDAKVILNTLSKFPITTLCCVPTIFR-LLVQEDLTRYQFQSLRHCLTGGEALNPDVREK 357
Cdd:cd05959 220 LGnSLTFplsvgattVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGER 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 358 WKHQTGVELYEGYGQSETVVI-CANPKGmKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRPTRPFcffncYL 436
Cdd:cd05959 300 WKARFGLDILDGIGSTEMLHIfLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM-----YW 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 437 DNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 516
Cdd:cd05959 374 NNRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKA 453
|
490 500 510
....*....|....*....|....*....|....*
gi 1024336653 517 FIVLTPAYSshDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05959 454 FVVLRPGYE--DSEALEEELKEFVKDRLAPYKYPR 486
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
91-551 |
2.12e-88 |
|
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: 280.17 E-value: 2.12e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd05973 2 TFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SLAPRVDAisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksrDPLAIYFTSGTTGAPKMVEHSQSsYGLG 250
Cdd:cd05973 81 ANRHKLDS--------------------------------------------DPFVMMFTSGTTGLPKGVPVPLR-ALAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 251 FVASGRRWVALTESDIFWNTTDTGWvkaAWTLFSAWPN----GSCIFVHELPrVDAKVILNTLSKFPITTLCCVPTIFRL 326
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGW---AYGLYYAITGplalGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 327 LVQ---EDLTRYQFqSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICANPKGMK--IKSGSMGKASPPYDV 401
Cdd:cd05973 192 LMAagaEVPARPKG-RLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 402 QIVDDEGNVLPPGEEGNVAVRIRPTrPFCFFNCYLDNPEKTAAseqGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYR 481
Cdd:cd05973 271 AVLDDDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024336653 482 IGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAyssHDP-EALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05973 347 IGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG---HEGtPALADELQLHVKKRLSAHAYPR 414
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
87-551 |
2.20e-83 |
|
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: 267.42 E-value: 2.20e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 87 EIKWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSI 166
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 167 ITSDSLaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrTKSRDPLAIYFTSGTTGAPKMVEHSQSS 246
Cdd:cd05958 88 LCAHAL----------------------------------------------TASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 247 YGLGFVASGRRWVALTESDIFwnttdTGWVKAAWT------LFSAWPNG-SCIFvheLPRVDAKVILNTLSKFPITTLCC 319
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRF-----VGSPPLAFTfglggvLLFPFGVGaSGVL---LEEATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 320 VPTIFRLLV------QEDLTryqfqSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICANPKGMKIKSGSMG 393
Cdd:cd05958 194 APTAYRAMLahpdaaGPDLS-----SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 394 KASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcffNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDD 473
Cdd:cd05958 269 KPVPGYEAKVVDDEGNPVPDGTIGRLAVR-GPT------GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDD 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024336653 474 VINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAyssHDP-EALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05958 342 MIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPG---VIPgPVLARELQDHAKAHIAPYKYPR 417
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
66-478 |
1.45e-78 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 254.16 E-value: 1.45e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 66 LEEAGHRPPN-PAFwwvnGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:pfam00501 1 LERQAARTPDkTAL----EVGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 145 GVTQLTEKDLKYRLQASRAKSIITSDSL-APRVDAISAECPSLQTKLLVSdssRPGWLNFRELLREASTEHNCMRT---- 219
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLD---RDPVLKEEPLPEEAKPADVPPPPpppp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 220 KSRDPLAIYFTSGTTGAPKMVEHSQSSY---GLGFVASGRRWVALTESDIFWNTTDTGWVkAAWTLFSAWP--NGSCI-F 293
Cdd:pfam00501 153 DPDDLAYIIYTSGTTGKPKGVMLTHRNLvanVLSIKRVRPRGFGLGPDDRVLSTLPLFHD-FGLSLGLLGPllAGATVvL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 294 VHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQ-EDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQ 372
Cdd:pfam00501 232 PPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEaGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 373 SETVVICANPKGMKIK---SGSMGKASPPYDVQIVDDE-GNVLPPGEEGNVAVRiRPtrpfCFFNCYLDNPEKTAAS-EQ 447
Cdd:pfam00501 312 TETTGVVTTPLPLDEDlrsLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR-GP----GVMKGYLNDPELTAEAfDE 386
|
410 420 430
....*....|....*....|....*....|.
gi 1024336653 448 GDFYITGDRARMDKDGYFWFMGRNDDVINSS 478
Cdd:pfam00501 387 DGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
89-552 |
4.81e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 253.19 E-value: 4.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:PRK06187 31 RTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSLAPRVDAISAECPSLQTKLLVSDSSRPG----WLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQ 244
Cdd:PRK06187 110 DSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSH 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 SSYGLGfVASGRRWVALTESDIFWNTTDTGWVkAAWTL-FSAWPNGSCIFVHElpRVDAKVILNTLSKFPITTLCCVPTI 323
Cdd:PRK06187 190 RNLFLH-SLAVCAWLKLSRDDVYLVIVPMFHV-HAWGLpYLALMAGAKQVIPR--RFDPENLLDLIETERVTFFFAVPTI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 324 FRLLVQEDLTR-YQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET--VVICANP----KGMKIKSGSMGKAS 396
Cdd:PRK06187 266 WQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETspVVSVLPPedqlPGQWTKRRSAGRPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 397 PPYDVQIVDDEGNVLPP--GEEGNVAVRirptRPfCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDV 474
Cdd:PRK06187 346 PGVEARIVDDDGDELPPdgGEVGEIIVR----GP-WLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLYITDRIKDV 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024336653 475 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHVkrvtAPYKYPRK 552
Cdd:PRK06187 421 IISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG-ATLDAKELRAFLRGRL----AKFKLPKR 493
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
54-551 |
1.50e-74 |
|
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: 248.65 E-value: 1.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 54 NFAHDVLDvwSRLEEAGHRPpnpAFWWVNGTGAEIK-WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVS 132
Cdd:cd17634 53 NLAANALD--RHLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 133 VACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD---------SLAPRVD-AISAECPSLQTKLLVSDSSRP---- 198
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVDdALNPNVTSVEHVIVLKRTGSDidwq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 199 --GWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESDIFWNTTDTGWV 276
Cdd:cd17634 207 egRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 277 KA-AWTLFSAWPNGSCIFVHELPRV--DAKVILNTLSKFPITTLCCVPTIFRLLVQED---LTRYQFQSLRHCLTGGEAL 350
Cdd:cd17634 287 TGhSYLLYGPLACGATTLLYEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 351 NPDVRE-KWKH--QTGVELYEGYGQSETVVICANPKGMKI--KSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIR- 424
Cdd:cd17634 367 NPEAYEwYWKKigKEKCPVVDTWWQTETGGFMITPLPGAIelKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPw 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 425 PTRPFCFFNcylDNPE--KTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV 502
Cdd:cd17634 447 PGQTRTLFG---DHERfeQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1024336653 503 VSSPDPIRGEVVKAFIVLTPAYSshDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd17634 524 VGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPD 570
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
54-552 |
1.33e-73 |
|
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: 246.32 E-value: 1.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 54 NFAHDVLDVWsrLEEAGHRPpnpAFWWV-NGTGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVS 132
Cdd:cd05966 53 NISYNCLDRH--LKERGDKV---AIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 133 VACMRTG---TVMIPGvtqLTEKDLKYRLQASRAKSIITSDS---------LAPRVDAISAECPSLQTKLLVSDSSRPGW 200
Cdd:cd05966 127 LACARIGavhSVVFAG---FSAESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALEKCPSVEKVLVVKRTGGEVP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 201 LN------FRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGfVASGRRWV-ALTESDIFWNTTDT 273
Cdd:cd05966 204 MTegrdlwWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLY-AATTFKYVfDYHPDDIYWCTADI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 274 GWVKA-AWTLFSAWPNGSCIFVHE----LPrvDAKVILNTLSKFPITTLCCVPTIFRLLVQ---EDLTRYQFQSLRHCLT 345
Cdd:cd05966 283 GWITGhSYIVYGPLANGATTVMFEgtptYP--DPGRYWDIVEKHKVTIFYTAPTAIRALMKfgdEWVKKHDLSSLRVLGS 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 346 GGEALNPdvrEKWKHqtgveLYEGYG-----------QSET--VVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLP 412
Cdd:cd05966 361 VGEPINP---EAWMW-----YYEVIGkercpivdtwwQTETggIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 413 PGEEGNVAVRiRPTrPFCFFNCYLDNP--EKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESA 490
Cdd:cd05966 433 GEVEGYLVIK-RPW-PGMARTIYGDHEryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024336653 491 LAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDpeALTRELQEHVKRVTAPYKYPRK 552
Cdd:cd05966 511 LVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDK 570
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
69-552 |
4.56e-73 |
|
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: 240.20 E-value: 4.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 69 AGHRPPNPAFWWVNGTgaeikWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQ 148
Cdd:cd17631 5 ARRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 149 LTEKDLKYRLQASRAKSIItsdslaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksRDPLAIY 228
Cdd:cd17631 79 LTPPEVAYILADSGAKVLF------------------------------------------------------DDLALLM 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 229 FTSGTTGAPKMVEHSQSSygLGFVASGrrwvALTESDIfwNTTDTGWVKA---------AWTLFSAWPNGSCIFvheLPR 299
Cdd:cd17631 105 YTSGTTGRPKGAMLTHRN--LLWNAVN----ALAALDL--GPDDVLLVVAplfhigglgVFTLPTLLRGGTVVI---LRK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 300 VDAKVILNTLSKFPITTLCCVPTIFRLLVQ-EDLTRYQFQSLRHCLTGGEALNPDVREKWKhQTGVELYEGYGQSETV-V 377
Cdd:cd17631 174 FDPETVLDLIERHRVTSFFLVPTMIQALLQhPRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSpG 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 378 ICANPKGMKI-KSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTRpfcfFNCYLDNPEKTAASEQGDFYITGDR 456
Cdd:cd17631 253 VTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GPHV----MAGYWNRPEATAAAFRDGWFHTGDL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 457 ARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPaysSHDPEALtrEL 536
Cdd:cd17631 328 GRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP---GAELDED--EL 402
|
490
....*....|....*.
gi 1024336653 537 QEHVKRVTAPYKYPRK 552
Cdd:cd17631 403 IAHCRERLARYKIPKS 418
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
91-552 |
2.93e-71 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 240.61 E-value: 2.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTG---TVMIPGvtqLTEKDLKYRLQASRAKSII 167
Cdd:TIGR02188 90 TYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGaihSVVFGG---FSAEALADRINDAGAKLVI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 168 TSDS---------LAPRVDAISAECPSLQTKLLV---SDSSRPGW-----LNFRELLREASTEHNCMRTKSRDPLAIYFT 230
Cdd:TIGR02188 166 TADEglrggkvipLKAIVDEALEKCPVSVEHVLVvrrTGNPVVPWvegrdVWWHDLMAKASAYCEPEPMDSEDPLFILYT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 231 SGTTGAPKMVEHSQSSYGLGFVASGRrWV-ALTESDIFWNTTDTGWVKA-AWTLFSAWPNGSCIFVHE-LPRV-DAKVIL 306
Cdd:TIGR02188 246 SGSTGKPKGVLHTTGGYLLYAAMTMK-YVfDIKDGDIFWCTADVGWITGhSYIVYGPLANGATTVMFEgVPTYpDPGRFW 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 307 NTLSKFPITTLCCVPTIFRLLVQ---EDLTRYQFQSLRHCLTGGEALNPDVREkWKH----QTGVELYEGYGQSET--VV 377
Cdd:TIGR02188 325 EIIEKHKVTIFYTAPTAIRALMRlgdEWVKKHDLSSLRLLGSVGEPINPEAWM-WYYkvvgKERCPIVDTWWQTETggIM 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 378 ICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVrIRPTRPFCFFNCYLDnPE---KTAASEQGDFYITG 454
Cdd:TIGR02188 404 ITPLPGATPTKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLV-IKQPWPGMLRTIYGD-HErfvDTYFSPFPGYYFTG 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 455 DRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDpeALTR 534
Cdd:TIGR02188 482 DGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDD--ELRK 559
|
490
....*....|....*...
gi 1024336653 535 ELQEHVKRVTAPYKYPRK 552
Cdd:TIGR02188 560 ELRKHVRKEIGPIAKPDK 577
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
91-551 |
6.44e-70 |
|
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: 231.97 E-value: 6.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd05919 12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 slaprvDAISAecpslqtkllvsdssrpgWLnfrellreastehncmrtksrdplaiyFTSGTTGAPKMVEHSQSSYgLG 250
Cdd:cd05919 91 ------DDIAY------------------LL---------------------------YSSGTTGPPKGVMHAHRDP-LL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 251 FV-ASGRRWVALTESDIFWNTTDT--GWVKAAWTLFSAWPNGSCIFVHElpRVDAKVILNTLSKFPITTLCCVPTIF-RL 326
Cdd:cd05919 119 FAdAMAREALGLTPGDRVFSSAKMffGYGLGNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVLYGVPTFYaNL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 327 LVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET--VVICANPKgmKIKSGSMGKASPPYDVQIV 404
Cdd:cd05919 197 LDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVghIFLSNRPG--AWRLGSTGRPVPGYEIRLV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 405 DDEGNVLPPGEEGNVAVRIrPTRpfcfFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGP 484
Cdd:cd05919 275 DEEGHTIPPGEEGDLLVRG-PSA----AVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 485 VEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHdpEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPR 414
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
52-552 |
5.40e-69 |
|
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: 234.52 E-value: 5.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 52 YFNFAHDVLDVWSrleEAGhRPPNPAFWWVNG-TGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWL 130
Cdd:cd05967 48 RLNTCYNALDRHV---EAG-RGDQIALIYDSPvTGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIYMPMIPEAAI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 131 VSVACMRTG---TVMIPGvtqLTEKDLKYRLQASRAKSIITSD---------SLAPRVD-AIS------AECPSLQTKLL 191
Cdd:cd05967 123 AMLACARIGaihSVVFGG---FAAKELASRIDDAKPKLIVTAScgiepgkvvPYKPLLDkALElsghkpHHVLVLNRPQV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 192 VSDSSRPG-WLNFRELLREAsTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESDIFWNT 270
Cdd:cd05967 200 PADLTKPGrDLDWSELLAKA-EPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAA 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 271 TDTGWV-------------KAAWTLFSAWPNGScifvhelPrvDAKVILNTLSKFPITTLCCVPTIFRLLVQED-----L 332
Cdd:cd05967 279 SDVGWVvghsyivygpllhGATTVLYEGKPVGT-------P--DPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 333 TRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET-VVICANPKG---MKIKSGSMGKASPPYDVQIVDDEG 408
Cdd:cd05967 350 KKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgWPITANPVGlepLPIKAGSPGKPVPGYQVQVLDEDG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 409 NVLPPGEEGNVAVRiRPTRPFCFFNCYLDNP--EKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVE 486
Cdd:cd05967 430 EPVGPNELGNIVIK-LPLPPGCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGE 508
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024336653 487 VESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSShDPEALTRELQEHVKRVTAPYKYPRK 552
Cdd:cd05967 509 MEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKI-TAEELEKELVALVREQIGPVAAFRL 573
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
51-551 |
1.59e-68 |
|
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: 230.11 E-value: 1.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 51 EYFNFAHDVLDvwsRLEEAGhRPPNPAFwwVNGTGAeikWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWL 130
Cdd:TIGR02262 1 EKYNAAEDLLD---RNVVEG-RGGKTAF--IDDISS---LSYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 131 VSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSsRPGWLNFRELLREA 210
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGRP-EAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 211 STEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESDIfwnttdtgwVKAAWTLFSAWPNGS 290
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDV---------CFSAAKLFFAYGLGN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 291 CIF-----------VHELPRVDAkvILNTLSKFPITTLCCVPTIFR-LLVQEDLTRYQFQSLRHCLTGGEALNPDVREKW 358
Cdd:TIGR02262 221 ALTfpmsvgattvlMGERPTPDA--VFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 359 KHQTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTRPFCFFNcyldN 438
Cdd:TIGR02262 299 QARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQDVADGEPGELLIS-GPSSATMYWN----N 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 439 PEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFI 518
Cdd:TIGR02262 374 RAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFV 453
|
490 500 510
....*....|....*....|....*....|...
gi 1024336653 519 VLTPAYsshdpEALTRELQEHVKRVTAPYKYPR 551
Cdd:TIGR02262 454 VLRPGQ-----TALETELKEHVKDRLAPYKYPR 481
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
62-551 |
2.88e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 227.92 E-value: 2.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 62 VWSRLEEAGHRPPN-PAFWWVngtGAEIkwSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGT 140
Cdd:PRK08314 12 LFHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 141 VMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRV------------------DAISAECP-----SLQTKLLVSDSSR 197
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 198 PGWLNFRELLREAST--EHncmrTKSRDPLAIY-FTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFWNTTD-- 272
Cdd:PRK08314 167 GGVVAWKEALAAGLAppPH----TAGPDDLAVLpYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlf 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 273 --TGWVKAawtLFSAWPNGSCIFVheLPRVDAKVILNTLSKFPITTLCCVPT-IFRLLVQEDLTRYQFQSLRhCLTGGEA 349
Cdd:PRK08314 242 hvTGMVHS---MNAPIYAGATVVL--MPRWDREAAARLIERYRVTHWTNIPTmVVDFLASPGLAERDLSSLR-YIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 350 LNPD-VREKWKHQTGVELYEGYGQSETVV-ICANPKGmKIKSGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVRiRPT 426
Cdd:PRK08314 316 AMPEaVAERLKELTGLDYVEGYGLTETMAqTHSNPPD-RPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-GPQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 427 rpfcFFNCYLDNPEKTAAS----EQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV 502
Cdd:PRK08314 394 ----VFKGYWNRPEATAEAfieiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACV 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1024336653 503 VSSPDPIRGEVVKAFIVLTPAYSSHDPEAltrELQEHVKRVTAPYKYPR 551
Cdd:PRK08314 470 IATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPR 515
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
89-548 |
7.14e-67 |
|
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: 225.17 E-value: 7.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSLAPRVDAISAECPSlQTKLLVSDSSRPGWLNFRELLREASTEHN-----CMRTKSRDPLAIYFTSGTTGAPKMVE-- 241
Cdd:cd05911 89 DPDGLEKVKEAAKELGP-KDKIIVLDDKPDGVLSIEDLLSPTLGEEDedlppPLKDGKDDTAAILYSSGTTGLPKGVCls 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 242 ------HSQSSYGLGFVASGRRWVALTESDIFWNTTDTgwvkaaWTLFSAWpNGSCIFVHelPRVDAKVILNTLSKFPIT 315
Cdd:cd05911 168 hrnliaNLSQVQTFLYGNDGSNDVILGFLPLYHIYGLF------TTLASLL-NGATVIIM--PKFDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 316 TLCCVPTIFRLLVQ-EDLTRYQFQSLRHCLTGGEALNPDVREKW-KHQTGVELYEGYGQSETVVICANPKGMKIKSGSMG 393
Cdd:cd05911 239 FLYLVPPIAAALAKsPLLDKYDLSSLRVILSGGAPLSKELQELLaKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 394 KASPPYDVQIVDDEGN-VLPPGEEGNVAVRIrptrPFCFfNCYLDNPEKTAAS--EQGdFYITGDRARMDKDGYFWFMGR 470
Cdd:cd05911 319 RLLPNVEAKIVDDDGKdSLGPNEPGEICVRG----PQVM-KGYYNNPEATKETfdEDG-WLHTGDIGYFDEDGYLYIVDR 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024336653 471 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPaysshDPEALTRELQEHV-KRVtAPYK 548
Cdd:cd05911 393 KKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP-----GEKLTEKEVKDYVaKKV-ASYK 465
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
89-551 |
2.09e-66 |
|
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: 222.17 E-value: 2.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 sdslaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksrDPLAIYFTSGTTGAPKMVEHSQSSYg 248
Cdd:cd05934 82 ------------------------------------------------------DPASILYTSGTTGPPKGVVITHANL- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 249 LGFVASGRRWVALTESDIFWNTTDTGWVKA-AWTLFSAWPNGSCIFVheLPRVDAKVILNTLSKFPITTLCCVPTIFR-L 326
Cdd:cd05934 107 TFAGYYSARRFGLGEDDVYLTVLPLFHINAqAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSyL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 327 LVQEDLTRYQFQSLRhcLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDD 406
Cdd:cd05934 185 LAQPPSPDDRAHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 407 EGNVLPPGEEGNVAvrIRPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVE 486
Cdd:cd05934 263 DGQELPAGEPGELV--IRGLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024336653 487 VESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHVkrvtAPYKYPR 551
Cdd:cd05934 341 VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFAFCEGQL----AYFKVPR 400
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
91-546 |
8.30e-65 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 223.48 E-value: 8.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTG---TVMIPGvtqLTEKDLKYRLQASRAKSII 167
Cdd:PRK00174 100 TYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGavhSVVFGG---FSAEALADRIIDAGAKLVI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 168 TSD---------SLAPRVDAISAECPSLQTKLLVS--------DSSRPGWLNfrELLREASTEHNCMRTKSRDPLAIYFT 230
Cdd:PRK00174 176 TADegvrggkpiPLKANVDEALANCPSVEKVIVVRrtggdvdwVEGRDLWWH--ELVAGASDECEPEPMDAEDPLFILYT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 231 SGTTGAPKMVEHSQSSYgLGFVASGRRWV-ALTESDIFWNTTDTGWVKA-AWTLFSAWPNGSCIFVHE----LPRVD--A 302
Cdd:PRK00174 254 SGSTGKPKGVLHTTGGY-LVYAAMTMKYVfDYKDGDVYWCTADVGWVTGhSYIVYGPLANGATTLMFEgvpnYPDPGrfW 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 303 KVIlntlSKFPITTLCCVPTIFRLLVQ---EDLTRYQFQSLRhcLTG--GEALNPdvrEKWKHqtgveLYEGYG------ 371
Cdd:PRK00174 333 EVI----DKHKVTIFYTAPTAIRALMKegdEHPKKYDLSSLR--LLGsvGEPINP---EAWEW-----YYKVVGgercpi 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 372 -----QSET--VVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVR------IRptrpfcffNCYLDn 438
Cdd:PRK00174 399 vdtwwQTETggIMITPLPGATPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKdpwpgmMR--------TIYGD- 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 439 PE---KTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK 515
Cdd:PRK00174 470 HErfvKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIY 549
|
490 500 510
....*....|....*....|....*....|.
gi 1024336653 516 AFIVLTPAYSSHDpeALTRELQEHVKRVTAP 546
Cdd:PRK00174 550 AFVTLKGGEEPSD--ELRKELRNWVRKEIGP 578
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
64-552 |
2.98e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 219.01 E-value: 2.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 64 SRLEEAGHR-PPNPAFWwvngTGAEiKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVM 142
Cdd:PRK07656 9 ELLARAARRfGDKEAYV----FGDQ-RLTYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 143 IPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLV----SDSSRPGWLNFRELLREASTEHNCMR 218
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 219 TKSRDPLAIYFTSGTTGAPK--MVEHSQ--SSYG-----LGFVASGRRWVALTESDIFwnttdtGWvKAAWTlfSAWPNG 289
Cdd:PRK07656 163 VDPDDVADILFTSGTTGRPKgaMLTHRQllSNAAdwaeyLGLTEGDRYLAANPFFHVF------GY-KAGVN--APLMRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 290 SCIFVHelPRVDAKVILNTLSKFPITTLCCVPTIFR-LLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVE-LY 367
Cdd:PRK07656 234 ATILPL--PVFDPDEVFRLIETERITVLPGPPTMYNsLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDiVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 368 EGYGQSETV-VICANPKG--MKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRirptrpfcFFNC---YLDNPEK 441
Cdd:PRK07656 312 TGYGLSEASgVTTFNRLDddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR--------GPNVmkgYYDDPEA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 442 TAASEQGDFYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 520
Cdd:PRK07656 384 TAAAIDADGWLhTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVL 463
|
490 500 510
....*....|....*....|....*....|...
gi 1024336653 521 TPAysshdpEALTRE-LQEHVKRVTAPYKYPRK 552
Cdd:PRK07656 464 KPG------AELTEEeLIAYCREHLAKYKVPRS 490
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
89-552 |
3.06e-60 |
|
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: 206.37 E-value: 3.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYrlqasraksiit 168
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 sdslaprvdaisaecpslqtklLVSDSSRPGWLnfrellreastehncmrtksrDPLAIYFTSGTTGAPKMVEHSQSSyg 248
Cdd:cd05941 79 ----------------------VITDSEPSLVL---------------------DPALILYTSGTTGRPKGVVLTHAN-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 249 lgfVASGRRwvALTESdifWNTTDT-------------GWVKAawTLFSAWPNGSCIFvheLPRVDAKVILNTLSKFPIT 315
Cdd:cd05941 114 ---LAANVR--ALVDA---WRWTEDdvllhvlplhhvhGLVNA--LLCPLFAGASVEF---LPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 316 TLCCVPTIFRLLVQ---------EDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICANPKGMK 386
Cdd:cd05941 181 VFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 387 IKSGSMGKASPPYDVQIVDDEGN-VLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGD-FYITGDRARMDKDGY 464
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEYWNKPEATKEEFTDDgWFKTGDLGVVDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 465 FWFMGR-NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEaltrELQEHVKRV 543
Cdd:cd05941 336 YWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE----ELKEWAKQR 411
|
....*....
gi 1024336653 544 TAPYKYPRK 552
Cdd:cd05941 412 LAPYKRPRR 420
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
54-542 |
4.29e-60 |
|
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: 210.04 E-value: 4.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 54 NFAHDVLDVWSRleeagHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSV 133
Cdd:cd05968 61 NIVEQLLDKWLA-----DTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLR-ALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 134 ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD---------SLAPRVDAISAECPSLQTKLLVSDSSRP-GWLNF 203
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTVEKVVVVRHLGNDfTPAKG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 204 REL---LREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESD-IFWnTTDTGWVKAA 279
Cdd:cd05968 215 RDLsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTW-FTDLGWMMGP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 280 WTLFSAWPNGSCIFVHE----LPrvDAKVILNTLSKFPITTLCCVPTIFRLLV---QEDLTRYQFQSLRHCLTGGEALNP 352
Cdd:cd05968 294 WLIFGGLILGATMVLYDgapdHP--KADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNP 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 353 dvrEKWKHqtgveLYEGYGQSEtVVICANPKGMKIKSGSMGK-------------ASPPYDVQIVDDEGNVLPPgEEGNV 419
Cdd:cd05968 372 ---EPWNW-----LFETVGKGR-NPIINYSGGTEISGGILGNvlikpikpssfngPVPGMKADVLDESGKPARP-EVGEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 420 AVR---IRPTRPFC-----FFNCYLDNPEktaaseqgDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESAL 491
Cdd:cd05968 442 VLLapwPGMTRGFWrdedrYLETYWSRFD--------NVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVL 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1024336653 492 AEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSshDPEALTRELQEHVKR 542
Cdd:cd05968 514 NAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERVAD 562
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
66-551 |
3.11e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 204.46 E-value: 3.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 66 LEEAGHR-PPNPAFWWVngtGAEIkwSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PRK05605 38 YDNAVARfGDRPALDFF---GATT--TYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 145 GVTQLTEKDLKYRLQASRAKSIITSDSLAPR---------------VDAISA-----------ECPSLQTKLLVSDSSRP 198
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGARVAIVWDKVAPTverlrrttpletivsVNMIAAmpllqrlalrlPIPALRKARAALTGPAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 199 GWLNFRELLREA----STEHNCMRTKSRDPLAIYFTSGTTGAPK--MVEHSQSSYGLgfvASGRRWV-ALTESDifwntt 271
Cdd:PRK05605 192 GTVPWETLVDAAiggdGSDVSHPRPTPDDVALILYTSGTTGKPKgaQLTHRNLFANA---AQGKAWVpGLGDGP------ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 272 DTgwVKAAWTLFSAWPNGSCIFVHE--------LPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQE------DLTryqf 337
Cdd:PRK05605 263 ER--VLAALPMFHAYGLTLCLTLAVsiggelvlLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLS---- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 338 qSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETV-VICANPKGMKIKSGSMGKASPPYDVQIVD--DEGNVLPPG 414
Cdd:PRK05605 337 -GVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 415 EEGNVAVRIRPTrpfcfFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEH 494
Cdd:PRK05605 416 EEGELLVRGPQV-----FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREH 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 495 PAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHVKRvtapYKYPR 551
Cdd:PRK05605 491 PGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEGLRAYCREHLTR----YKVPR 542
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
61-522 |
1.33e-56 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 198.75 E-value: 1.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 61 DVWSRLeeAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGT 140
Cdd:PRK08008 11 QMWDDL--ADVYGHKTALIFESSGGVVRRYSYLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 141 VMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRP---GWLNFRELLREASTEHNCM 217
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPaddGVSSFTQLKAQQPATLCYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 218 RTKSRDPLA-IYFTSGTTGAPKMVEHSQssYGLGFVASGRRW-VALTESDIFWNTTDTGWV----KAAWTLFSAwpnGSC 291
Cdd:PRK08008 168 PPLSTDDTAeILFTSGTTSRPKGVVITH--YNLRFAGYYSAWqCALRDDDVYLTVMPAFHIdcqcTAAMAAFSA---GAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 292 IFVHElpRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQslrHCLTggEA---LNPDVREK--WKHQTGVEL 366
Cdd:PRK08008 243 FVLLE--KYSARAFWGQVCKYRATITECIPMMIRTLMVQPPSANDRQ---HCLR--EVmfyLNLSDQEKdaFEERFGVRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 367 YEGYGQSETVV-ICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRPTRpfCFFNCYLDNPEKTAAS 445
Cdd:PRK08008 316 LTSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGK--TIFKEYYLDPKATAKV 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024336653 446 EQGDFYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTP 522
Cdd:PRK08008 394 LEADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNE 471
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
87-552 |
4.96e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 197.08 E-value: 4.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 87 EIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSI 166
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 167 ITSDSLAPRVDAISAECPSLQTKLLVSDSSRP---GWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHS 243
Cdd:PRK08316 113 LVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAMLT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 244 QSS----YGLGFVASGrrwvaLTESDIFWNttdtgwvkaAWTLF-SAWPN---GSCIFV----HELPRVDAKVILNTLSK 311
Cdd:PRK08316 193 HRAliaeYVSCIVAGD-----MSADDIPLH---------ALPLYhCAQLDvflGPYLYVgatnVILDAPDPELILRTIEA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 312 FPITTLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEALNPDV-REKWKHQTGVELYEGYGQSE-----TVVicaNPKG 384
Cdd:PRK08316 259 ERITSFFAPPTVWiSLLRHPDFDTRDLSSLRKGYYGASIMPVEVlKELRERLPGLRFYNCYGQTEiaplaTVL---GPEE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 385 MKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRirpTRPFCffNCYLDNPEKTAASEQGDFYITGDRARMDKDGY 464
Cdd:PRK08316 336 HLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR---SPQLM--LGYWDDPEKTAEAFRGGWFHSGDLGVMDEEGY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 465 FWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEaltrELQEHVKRVT 544
Cdd:PRK08316 411 ITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-ATVTED----ELIAHCRARL 485
|
....*...
gi 1024336653 545 APYKYPRK 552
Cdd:PRK08316 486 AGFKVPKR 493
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
44-561 |
5.47e-56 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 197.96 E-value: 5.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 44 LGRQLVPEYfnfahdvLDVWSRLeeaghRPPNPAFWWVngtGAEIkwSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLP 123
Cdd:PRK06178 30 HGERPLTEY-------LRAWARE-----RPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 124 RLPEWWLVSVACMRTGTVMIPgVTQLT-EKDLKYRLQASRAKSIITSDSLAPRVDAISAEC-----------------PS 185
Cdd:PRK06178 92 NCPQFHIVFFGILKLGAVHVP-VSPLFrEHELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaePT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 186 LQTKLLVSDSSR--PGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQ-------SSYGLGFVASGR 256
Cdd:PRK06178 171 LPLPDSLRAPRLaaAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQrdmvytaAAAYAVAVVGGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 257 RWVALTESDIFW-NTTDTGWVkaaWTLFSawpnGSCIFVheLPRVDAKVILNTLSKFPIT-TLCCVPTIFRLLVQEDLTR 334
Cdd:PRK06178 251 DSVFLSFLPEFWiAGENFGLL---FPLFS----GATLVL--LARWDAVAFMAAVERYRVTrTVMLVDNAVELMDHPRFAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 335 YQFQSLRH--CLTGGEALNPDVREKWKHQTGVELYEG-YGQSETVVICANPKGMKikSGSM---------GKASPPYDVQ 402
Cdd:PRK06178 322 YDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAGFQ--DDDFdllsqpvfvGLPVPGTEFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 403 IVD-DEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYR 481
Cdd:PRK06178 400 ICDfETGELLPLGAEGEIVVR-TPS----LLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 482 IGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHVkrvtAPYKYPrkncQRRFLER 561
Cdd:PRK06178 475 VFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG-ADLTAAALQAWCRENM----AVYKVP----EIRIVDA 545
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
84-552 |
9.06e-56 |
|
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: 195.61 E-value: 9.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 84 TGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 164 KSIITSDS-------LAPRVDAISAECPSLQTKLLVSDSSRPgwLNFRELLREASTEHNCMRtkSRDPLAIYFTSGTTGA 236
Cdd:cd05926 88 KLVLTPKGelgpasrAASKLGLAILELALDVGVLIRAPSAES--LSNLLADKKNAKSEGVPL--PDDLALILHTSGTTGR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 237 PKMVEHSQssygLGFVASGR---RWVALTESDIFWNTTDT----GWVKAAW-TLFSawpnGSCIFVHelPRVDAKVILNT 308
Cdd:cd05926 164 PKGVPLTH----RNLAASATnitNTYKLTPDDRTLVVMPLfhvhGLVASLLsTLAA----GGSVVLP--PRFSASTFWPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 309 LSKFPITTLCCVPTIFRLLVQ--EDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETV-VICANP-KG 384
Cdd:cd05926 234 VRDYNATWYTAVPTIHQILLNrpEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhQMTSNPlPP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 385 MKIKSGSMGKASPPyDVQIVDDEGNVLPPGEEGNVAVR----IRPtrpfcffncYLDNPEKTAAS-EQGDFYITGDRARM 459
Cdd:cd05926 314 GPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRgpnvTRG---------YLNNPEANAEAaFKDGWFRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 460 DKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSshdpeALTRELQEH 539
Cdd:cd05926 384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGAS-----VTEEELRAF 458
|
490
....*....|...
gi 1024336653 540 VKRVTAPYKYPRK 552
Cdd:cd05926 459 CRKHLAAFKVPKK 471
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
84-552 |
1.96e-55 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 195.09 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 84 TGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:PRK07514 23 TPDGLRYTYGDLDAASARLANLLVAL-GVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 164 KSIITSDSLAPRVDAISAECPSLQTKLLvsDSSRPGWLNfrELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPK--MVE 241
Cdd:PRK07514 102 ALVVCDPANFAWLSKIAAAAGAPHVETL--DADGTGSLL--EAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 242 HsqssyglGFVASGrrwvALTESDiFWNTTDTG--------------WVKAAWTLFSAwpnGSCIFvheLPRVDAKVILN 307
Cdd:PRK07514 178 H-------GNLLSN----ALTLVD-YWRFTPDDvlihalpifhthglFVATNVALLAG---ASMIF---LPKFDPDAVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 308 TLSKfpITTLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICANPKGMK 386
Cdd:PRK07514 240 LMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 387 IKSGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGD-FYITGDRARMDKDGY 464
Cdd:PRK07514 318 RRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-GPN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 465 FWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHVkrvt 544
Cdd:PRK07514 393 VHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL---- 467
|
....*...
gi 1024336653 545 APYKYPRK 552
Cdd:PRK07514 468 ARFKQPKR 475
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
91-551 |
6.65e-54 |
|
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: 189.23 E-value: 6.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SLaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksrDPLA-IYFTSGTTGAPKMVEHSQSSYgL 249
Cdd:cd05935 82 EL--------------------------------------------------DDLAlIPYTSGTTGLPKGCMHTHFSA-A 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 250 GFVASGRRWVALTESDIFWNTTD----TGWVKaawTLFSAWPNGSCIFVheLPRVDAKVILNTLSKFPITTLCCVPT-IF 324
Cdd:cd05935 111 ANALQSAVWTGLTPSDVILACLPlfhvTGFVG---SLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTmLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 325 RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVV-ICANPKGmKIKSGSMGKASPPYDVQI 403
Cdd:cd05935 186 DLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSqTHTNPPL-RPKLQCLGIP*FGVDARV 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 404 VDDE-GNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGD----FYITGDRARMDKDGYFWFMGRNDDVINSS 478
Cdd:cd05935 265 IDIEtGRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEESFIEIkgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVS 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024336653 479 SYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSShdpEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05935 340 GFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRG---KVTEEDIIEWAREQMAAYKYPR 409
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
83-551 |
4.92e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 188.57 E-value: 4.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 83 GTGAEikWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASR 162
Cdd:PRK08276 7 PSGEV--VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 163 AKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLaiyFTSGTTGAPKMVEH 242
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGADML---YSSGTTGRPKGIKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 243 SQSSYGLGFVASGRRWVALTEsdiFWNTTDTGWVKAAwTLFSAWPNGSCIFVHEL-------PRVDAKVILNTLSKFPIT 315
Cdd:PRK08276 161 PLPGLDPDEAPGMMLALLGFG---MYGGPDSVYLSPA-PLYHTAPLRFGMSALALggtvvvmEKFDAEEALALIERYRVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 316 TLCCVPTIF-RLLV--QEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVIC-ANPKGMKIKSGS 391
Cdd:PRK08276 237 HSQLVPTMFvRMLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSEGGGVTvITSEDWLAHPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 392 MGKASPPyDVQIVDDEGNVLPPGEEGNVAVRiRPTRPFCffncYLDNPEKTAASEQG-DFYITGDRARMDKDGYFWFMGR 470
Cdd:PRK08276 317 VGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPFE----YHNDPEKTAAARNPhGWVTVGDVGYLDEDGYLYLTDR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 471 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLTPAYSSHDPEALTRELQEHVKRVTAPYKYP 550
Cdd:PRK08276 391 KSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPADGADAGDALAAELIAWLRGRLAHYKCP 468
|
.
gi 1024336653 551 R 551
Cdd:PRK08276 469 R 469
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
89-551 |
9.55e-53 |
|
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: 186.19 E-value: 9.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWwLVSV-ACMRTGTVMIPgvtqLtekDLKY---RLQAsrak 164
Cdd:cd05930 12 SLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEM-VVAIlAVLKAGAAYVP----L---DPSYpaeRLAY---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 165 siITSDSlaprvdaisaecpslQTKLLVSDSSrpgwlnfrellreastehncmrtksrDPLAIYFTSGTTGAPK--MVEH 242
Cdd:cd05930 79 --ILEDS---------------GAKLVLTDPD--------------------------DLAYVIYTSGSTGKPKgvMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 243 SqssyGLG-FVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCI-FVHELPRVDAKVILNTLSKFPITTLCCV 320
Cdd:cd05930 116 R----GLVnLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLvVLPEEVRKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 321 PTIFRLLVQEdLTRYQFQSLRHCLTGGEALNPDVREKW-KHQTGVELYEGYGQSETVVICAnpkGMKIKSGSMGKASPP- 398
Cdd:cd05930 192 PSLLRLLLQE-LELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDAT---YYRVPPDDEEDGRVPi 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 399 ------YDVQIVDDEGNVLPPGEEG-------NVAvrirptrpfcffNCYLDNPEKTAAS------EQGD-FYITGDRAR 458
Cdd:cd05930 268 grpipnTRVYVLDENLRPVPPGVPGelyiggaGLA------------RGYLNRPELTAERfvpnpfGPGErMYRTGDLVR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 459 MDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVltpaySSHDPEALTRELQE 538
Cdd:cd05930 336 WLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV-----PDEGGELDEEELRA 410
|
490
....*....|...
gi 1024336653 539 HVKRVTAPYKYPR 551
Cdd:cd05930 411 HLAERLPDYMVPS 423
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
57-552 |
1.18e-51 |
|
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: 184.75 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 57 HDVLDVWSrLEEAGHRPPNPAFwwVNG-TGAEIkwSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVAC 135
Cdd:cd05904 4 DLPLDSVS-FLFASAHPSRPAL--IDAaTGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 136 MRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVdaisaecPSLQTKLLVSDSSR-PGWLNFRELLREASTEH 214
Cdd:cd05904 78 LSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKL-------ASLALPVVLLDSAEfDSLSFSDLLFEADEAEP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 215 NCMRTKSRDPLAIYFTSGTTGAPK--MVEHSqssyglGFVASgrrwVALTESDIFWNTTDTGWVKAAWTLF--------- 283
Cdd:cd05904 151 PVVVIKQDDVAALLYSSGTTGRSKgvMLTHR------NLIAM----VAQFVAGEGSNSDSEDVFLCVLPMFhiyglssfa 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 284 -SAWPNGSCIFVheLPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLT-RYQFQSLRHCLTGGEALNPDV----REK 357
Cdd:cd05904 221 lGLLRLGATVVV--MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELieafRAK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 358 WKHqtgVELYEGYGQSET---VVICANPKGMKIKSGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVRirptRPfCFFN 433
Cdd:cd05904 299 FPN---VDLGQGYGMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR----GP-SIMK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 434 CYLDNPEKTAAS--EQGdFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRG 511
Cdd:cd05904 371 GYLNNPEATAATidKEG-WLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAG 449
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1024336653 512 EVVKAFIVLTPAYSshdpeaLT-RELQEHV-KRVtAPYKYPRK 552
Cdd:cd05904 450 EVPMAFVVRKPGSS------LTeDEIMDFVaKQV-APYKKVRK 485
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
66-551 |
1.98e-51 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 185.64 E-value: 1.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 66 LEEAGHRPPN-PAFwwVNgTGAEIkwSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIp 144
Cdd:PRK08974 29 FEQAVARYADqPAF--IN-MGEVM--TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 145 GVTQL-TEKDLKYRLQASRAKSIITSDSLAPRVDAISAECP-----------SLQT-------------KLLVSDSSRPG 199
Cdd:PRK08974 103 NVNPLyTPRELEHQLNDSGAKAIVIVSNFAHTLEKVVFKTPvkhviltrmgdQLSTakgtlvnfvvkyiKRLVPKYHLPD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 200 WLNFRELLREASTEHNCMRTKSRDPLA-IYFTSGTTGAPK--MVEHS-------QSSYGLG-FVASGRRWV--ALTESDI 266
Cdd:PRK08974 183 AISFRSALHKGRRMQYVKPELVPEDLAfLQYTGGTTGVAKgaMLTHRnmlanleQAKAAYGpLLHPGKELVvtALPLYHI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 267 FwnttdtgwvkaAWTLfsawpngSCIFVHEL---------PRvDAKVILNTLSKFPITTLCCVPTIFRLLVQ-EDLTRYQ 336
Cdd:PRK08974 263 F-----------ALTV-------NCLLFIELggqnllitnPR-DIPGFVKELKKYPFTAITGVNTLFNALLNnEEFQELD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 337 FQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSE-TVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGE 415
Cdd:PRK08974 324 FSSLKLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 416 EGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHP 495
Cdd:PRK08974 404 PGELWVK-GPQ----VMLGYWQRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHP 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 496 AVLESAVVSSPDPIRGEVVKAFIVltpaysSHDPeALTR-ELQEHVKRVTAPYKYPR 551
Cdd:PRK08974 479 KVLEVAAVGVPSEVSGEAVKIFVV------KKDP-SLTEeELITHCRRHLTGYKVPK 528
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
72-551 |
1.39e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 182.67 E-value: 1.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 72 RPPNPAFWWVngtGAEIKWSfeELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTE 151
Cdd:PRK07786 30 QPDAPALRFL---GNTTTWR--ELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 152 KDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLAIYFTS 231
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 232 GTTGAPK--MVEHS----QSSYGLgfvasgRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRVDAKVI 305
Cdd:PRK07786 184 GTTGRPKgaVLTHAnltgQAMTCL------RTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 306 LNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRhCLTGGEALNPD--VREKWKHQTGVELYEGYGQSE-TVVICA-N 381
Cdd:PRK07786 258 LDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALR-VLSWGAAPASDtlLRQMAATFPEAQILAAFGQTEmSPVTCMlL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 382 PKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRARMDK 461
Cdd:PRK07786 337 GEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEATAEAFAGGWFHSGDLVRQDE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 462 DGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALTRELQEHVK 541
Cdd:PRK07786 412 EGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRLA 491
|
490
....*....|
gi 1024336653 542 RvtapYKYPR 551
Cdd:PRK07786 492 R----YKHPK 497
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
91-503 |
2.17e-50 |
|
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: 179.00 E-value: 2.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SLAPRVDAISAE--CPSLQTKLLVSDSSRPGWLNfrellreastehncMRTKSRDPLAIYFTSGTTGAPK--MVEHSQSS 246
Cdd:TIGR01733 81 ALASRLAGLVLPviLLDPLELAALDDAPAPPPPD--------------APSGPDDLAYVIYTSGSTGRPKgvVVTHRSLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 247 YglgFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFV--HELPRVDAKVILNTLSKFPITTLCCVPTIF 324
Cdd:TIGR01733 147 N---LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVppEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 325 RLLVQEDLTRyqFQSLRHCLTGGEALNPDVREKWKHQTG-VELYEGYGQSETVVICAnpkgMKIKSGSM---------GK 394
Cdd:TIGR01733 224 ALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWST----ATLVDPDDaprespvpiGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 395 ASPPYDVQIVDDEGNVLPPGEEG-------NVAVRirptrpfcffncYLDNPEKTAA---------SEQGDFYITGDRAR 458
Cdd:TIGR01733 298 PLANTRLYVLDDDLRPVPVGVVGelyiggpGVARG------------YLNRPELTAErfvpdpfagGDGARLYRTGDLVR 365
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1024336653 459 MDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVlESAVV 503
Cdd:TIGR01733 366 YLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
73-551 |
2.53e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 181.36 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 73 PPNPAFWwVNGTGAEIkwSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEK 152
Cdd:PRK13390 11 PDRPAVI-VAETGEQV--SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 153 DLKYRLQASRAKSIITSDSLaprvDAISAECPSLQTKLLVSDSSRPGWLNFRELLREAS---TEHNCmrtksrdPLAIYF 229
Cdd:PRK13390 87 EADYIVGDSGARVLVASAAL----DGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGprlTEQPC-------GAVMLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 230 TSGTTGAPKMV-----EHSQSSYGLGFVASGRRWVALTESDIFWNTTdtgwvkaawTLFSAWPNGSCIFVHEL------- 297
Cdd:PRK13390 156 SSGTTGFPKGIqpdlpGRDVDAPGDPIVAIARAFYDISESDIYYSSA---------PIYHAAPLRWCSMVHALggtvvla 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 298 PRVDAKVILNTLSKFPITTLCCVPTIF-RLLVQED--LTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSE 374
Cdd:PRK13390 227 KRFDAQATLGHVERYRITVTQMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 375 T--VVICANPKGMKiKSGSMGKaSPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTRPFCffncYLDNPEKTAASEQ--GDF 450
Cdd:PRK13390 307 AhgMTFIDSPDWLA-HPGSVGR-SVLGDLHICDDDGNELPAGRIGTVYFE-RDRLPFR----YLNDPEKTAAAQHpaHPF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 451 YIT-GDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYsshDP 529
Cdd:PRK13390 380 WTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI---RG 456
|
490 500
....*....|....*....|...
gi 1024336653 530 -EALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK13390 457 sDELARELIDYTRSRIAHYKAPR 479
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
56-551 |
1.20e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 180.61 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 56 AHDVLDVWSRLEEAGHR-PPNPAFWWVngtGAEIkwSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVA 134
Cdd:PRK06710 20 SYDIQPLHKYVEQMASRyPEKKALHFL---GKDI--TFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNCPQAVIGYYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 135 CMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAEC----------------------PSLQTK--- 189
Cdd:PRK06710 94 TLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSATkiehvivtriadflpfpknllyPFVQKKqsn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 190 --LLVSDSSRPGWLNFRELLREASTEHNCmrTKSRDPLAIYFTSGTTGAPKmvehsqssyglGFVASGRRWVALTESDIF 267
Cdd:PRK06710 174 lvVKVSESETIHLWNSVEKEVNTGVEVPC--DPENDLALLQYTGGTTGFPK-----------GVMLTHKNLVSNTLMGVQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 268 W--NTTDTGWVKAAWTLF------SAWPNGSCIFVHEL---PRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTR-Y 335
Cdd:PRK06710 241 WlyNCKEGEEVVLGVLPFfhvygmTAVMNLSIMQGYKMvliPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKeY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 336 QFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETV-VICANPKGMKIKSGSMGKASPPYDVQIVDDE-GNVLPP 413
Cdd:PRK06710 321 DISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSLEtGEALPP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 414 GEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAE 493
Cdd:PRK06710 401 GEIGEIVVK-GPQ----IMKGYWNKPEETAAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024336653 494 HPAVLESAVVSSPDPIRGEVVKAFIVLtpaysSHDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK06710 476 HEKVQEVVTIGVPDPYRGETVKAFVVL-----KEGTECSEEELNQFARKYLAAYKVPK 528
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
54-543 |
1.51e-49 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 181.69 E-value: 1.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 54 NFAHDVLDVWsrLEEaghRPPNPAFWWVNG-TGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVS 132
Cdd:PRK10524 53 NLCHNAVDRH--LAK---RPEQLALIAVSTeTDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 133 VACMRTG---TVMIPGvtqLTEKDLKYRLQASRAKSIITSDSLA---------PRVDAISAECPSLQTKLLVSD------ 194
Cdd:PRK10524 127 LACARIGaihSVVFGG---FASHSLAARIDDAKPVLIVSADAGSrggkvvpykPLLDEAIALAQHKPRHVLLVDrglapm 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 195 SSRPGWLNFRELLREASTEHN--CMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESDIFWNTTD 272
Cdd:PRK10524 204 ARVAGRDVDYATLRAQHLGARvpVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFFCASD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 273 TGWVKA-AWTLFSAWPNGSCIFVHE-LP-RVDAKVILNTLSKFPITTLCCVPTIFRLLVQED---LTRYQFQSLRHCLTG 346
Cdd:PRK10524 284 IGWVVGhSYIVYAPLLAGMATIMYEgLPtRPDAGIWWRIVEKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLRALFLA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 347 GEALN-PDVRekWKHQT-GVELYEGYGQSET-VVICANPKG---MKIKSGSMGKASPPYDVQIVDDE-GNVLPPGEEGNV 419
Cdd:PRK10524 364 GEPLDePTAS--WISEAlGVPVIDNYWQTETgWPILAIARGvedRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 420 AVRiRPTRPFC----------FFNCYLdnpekTAASEQgdFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVES 489
Cdd:PRK10524 442 VIE-GPLPPGCmqtvwgdddrFVKTYW-----SLFGRQ--VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEE 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1024336653 490 ALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALTRELQEHVKRV 543
Cdd:PRK10524 514 SISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREARLALEKEIMALV 567
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
90-545 |
1.63e-48 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 178.61 E-value: 1.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVM-IPGV---TQLTEkdlkyRLQASRAKS 165
Cdd:PRK07529 59 WTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANpINPLlepEQIAE-----LLRAAGAKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 166 IIT------SDsLAPRVDAISAECPSLQTKLLVsDSSR--PGW----------------LNF-RELLREASTEHNCMRTK 220
Cdd:PRK07529 133 LVTlgpfpgTD-IWQKVAEVLAALPELRTVVEV-DLARylPGPkrlavplirrkahariLDFdAELARQPGDRLFSGRPI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 221 SRDPLAIYF-TSGTTGAPKMVEHSQSsyglGFVASGrrWVAltESDIFWNTTDTgwVKAAWTLF----------SAWPNG 289
Cdd:PRK07529 211 GPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WLG--ALLLGLGPGDT--VFCGLPLFhvnallvtglAPLARG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 290 scifvhelprvdAKVILNT----------------LSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPD 353
Cdd:PRK07529 281 ------------AHVVLATpqgyrgpgvianfwkiVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 354 VREKWKHQTGVELYEGYGQSE-TVVICANPKGMKIKSGSMGKASPPYDVQIV--DDEGNVL---PPGEEGNVAVRiRPTr 427
Cdd:PRK07529 349 VFRRFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GPN- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 428 pfcFFNCYLdNPEKTAASE-QGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSP 506
Cdd:PRK07529 427 ---VFSGYL-EAAHNKGLWlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRP 502
|
490 500 510
....*....|....*....|....*....|....*....
gi 1024336653 507 DPIRGEVVKAFIVLTPAySSHDPEaltrELQEHVKRVTA 545
Cdd:PRK07529 503 DAHAGELPVAYVQLKPG-ASATEA----ELLAFARDHIA 536
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
91-551 |
2.00e-48 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 177.38 E-value: 2.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SLAPRVDAISAECPSLQT------------------------KLLVSDSSRPGWLNFRELLREAStEHNcMRTKSRDPLA 226
Cdd:PRK08751 132 NFGTTVQQVIADTPVKQVittglgdmlgfpkaalvnfvvkyvKKLVPEYRINGAIRFREALALGR-KHS-MPTLQIEPDD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 IYF---TSGTTGAPK------------MVEHSQSSYGLGFVASGRRWV--ALTESDIFwNTTDTGWVKAAWtlfsawpnG 289
Cdd:PRK08751 210 IAFlqyTGGTTGVAKgamlthrnlvanMQQAHQWLAGTGKLEEGCEVVitALPLYHIF-ALTANGLVFMKI--------G 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 290 SCIFVHELPRvDAKVILNTLSKFPITTLCCVPTIFR-LLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYE 368
Cdd:PRK08751 281 GCNHLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNgLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 369 GYGQSETV-VICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQ 447
Cdd:PRK08751 360 AYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-GPQ----VMKGYWKRPEETAKVMD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 448 GDFYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVltpaysS 526
Cdd:PRK08751 435 ADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------K 508
|
490 500
....*....|....*....|....*
gi 1024336653 527 HDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK08751 509 KDPALTAEDVKAHARANLTGYKQPR 533
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
86-534 |
1.11e-47 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 174.95 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 86 AEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKS 165
Cdd:PRK06155 43 GGTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 166 IITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGW-LNFRELLREASTEH-NCMRTKSRDPLAIYFTSGTTGAPKMV--E 241
Cdd:PRK06155 122 LVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpAGWSTAPLPPLDAPaPAAAVQPGDTAAILYTSGTTGPSKGVccP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 242 HSQSsYGLGFVASgrRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVheLPRVDAKVILNTLSKFPITT---LC 318
Cdd:PRK06155 202 HAQF-YWWGRNSA--EDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATVtylLG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 319 CVPTIfrLLVQEDLTRYQFQSLRHCLTGGEAlnPDVREKWKHQTGVELYEGYGQSETVVICANPKGMKiKSGSMGKASPP 398
Cdd:PRK06155 277 AMVSI--LLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLAPG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 399 YDVQIVDDEGNVLPPGEEGNVAVRIRPtrPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSS 478
Cdd:PRK06155 352 FEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRR 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024336653 479 SYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTR 534
Cdd:PRK06155 430 GENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPVALVR 484
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
72-546 |
3.96e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 170.17 E-value: 3.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 72 RPPNPAFWWVNGTgaeikWSFEELGKQSRKAANVLGgACGLQPGDR-MMLVLPRlPEWWLVSVACMRTGTVMIPGVTQLT 150
Cdd:PRK06188 25 YPDRPALVLGDTR-----LTYGQLADRISRYIQAFE-ALGLGTGDAvALLSLNR-PEVLMAIGAAQLAGLRRTALHPLGS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 151 EKDLKYRLQASRAKS-IITSDSLAPRVDAISAECPSLQTKLLVSDSsrPGWLNFRELLREASTEHNCMRTKSRDPLAIYF 229
Cdd:PRK06188 98 LDDHAYVLEDAGISTlIVDPAPFVERALALLARVPSLKHVLTLGPV--PDGVDLLAAAAKFGPAPLVAAALPPDIAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 230 TSGTTGAPKMVEHSQSSYGlGFVAsgrrwVALTESDI-----FWNTTDTGWVKAAWTLFSAWPNGScifVHELPRVDAKV 304
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIA-TMAQ-----IQLAEWEWpadprFLMCTPLSHAGGAFFLPTLLRGGT---VIVLAKFDPAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 305 ILNTLSKFPITTLCCVPT-IFRLLVQEDLTRYQFQSLRHCLTGGEALNPD-VREKWKhQTGVELYEGYGQSETV-VICAN 381
Cdd:PRK06188 247 VLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPVrLAEAIE-RFGPIFAQYYGQTEAPmVITYL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 382 PKGMKIKS-----GSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRirptRPFcFFNCYLDNPEKTAASEQGDFYITGDR 456
Cdd:PRK06188 326 RKRDHDPDdpkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR----GPL-VMDGYWNRPEETAEAFRDGWLHTGDV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 457 ARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEaltrEL 536
Cdd:PRK06188 401 AREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-AAVDAA----EL 475
|
490
....*....|....
gi 1024336653 537 QEHVKR----VTAP 546
Cdd:PRK06188 476 QAHVKErkgsVHAP 489
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
87-551 |
5.68e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 170.34 E-value: 5.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 87 EIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSI 166
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 167 ITSD------------SLAP------RVDAISAECPSLQTKLLVSDSSRPGWLNFRELLREA---STEHNCMRTKS---R 222
Cdd:PRK12583 122 ICADafktsdyhamlqELLPglaegqPGALACERLPELRGVVSLAPAPPPGFLAWHELQARGetvSREALAERQASldrD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPK--MVEHSQSSYGLGFVAsgrRWVALTESDI------FWNTTdtGWVKAAWTLFSAwpnGSCIfV 294
Cdd:PRK12583 202 DPINIQYTSGTTGFPKgaTLSHHNILNNGYFVA---ESLGLTEHDRlcvpvpLYHCF--GMVLANLGCMTV---GACL-V 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 295 HELPRVDAKVILNTLSKFPITTLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKW---KHQTGVELyeGY 370
Cdd:PRK12583 273 YPNEAFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVmdeMHMAEVQI--AY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 371 GQSETVVI---CANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAvrirpTRPFCFFNCYLDNPEKTAASEQ 447
Cdd:PRK12583 351 GMTETSPVslqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMKGYWNNPEATAESID 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 448 GDFYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSs 526
Cdd:PRK12583 426 EDGWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHA- 504
|
490 500
....*....|....*....|....*
gi 1024336653 527 hdpeALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK12583 505 ----ASEEELREFCKARIAHFKVPR 525
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
66-552 |
8.35e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 169.45 E-value: 8.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 66 LEEAGHRPPN-PAFWWvngtgAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PRK07470 13 LRQAARRFPDrIALVW-----GDRSWTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 145 GVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLqtKLLVSDSSRPGWLNFRELLRE--------ASTEHNc 216
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDL--THVVAIGGARAGLDYEALVARhlgarvanAAVDHD- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 217 mrtksrDPLAIYFTSGTTGAPK--MVEHSQssygLGFVASGRRwvalteSDIFWNTT--DTGWVKAawtlfsawPNGSCI 292
Cdd:PRK07470 164 ------DPCWFFFTSGTTGRPKaaVLTHGQ----MAFVITNHL------ADLMPGTTeqDASLVVA--------PLSHGA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 293 FVHELPRV--DAKVILNTLSKFPI------------TTLCCVPTIFRLLVQ-EDLTRYQFQSLRHCLTGGEalnPDVREK 357
Cdd:PRK07470 220 GIHQLCQVarGAATVLLPSERFDPaevwalverhrvTNLFTVPTILKMLVEhPAVDRYDHSSLRYVIYAGA---PMYRAD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 358 WKH---QTGVELYEGYGQSE-TVVICANPKGM-------KIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRPT 426
Cdd:PRK07470 297 QKRalaKLGKVLVQYFGLGEvTGNITVLPPALhdaedgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 427 rpfcfFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSP 506
Cdd:PRK07470 377 -----FAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVP 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1024336653 507 DPIRGEVVKAFIVltpAYSSHDPEAltRELQEHVKRVTAPYKYPRK 552
Cdd:PRK07470 452 DPVWGEVGVAVCV---ARDGAPVDE--AELLAWLDGKVARYKLPKR 492
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
85-552 |
1.14e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 168.11 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 85 GAEIKWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAK 164
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 165 SIITSDSLAPRVDAISAecpslqtkllVSDSSRPGWLNFRELLREASTEhNCMRTKSRDPLAIYFTSGTTGAPKmvehsq 244
Cdd:PRK06839 103 VLFVEKTFQNMALSMQK----------VSYVQRVISITSLKEIEDRKID-NFVEKNESASFIICYTSGTTGKPK------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 ssyglGFVasgrrwvaLTESDIFWN------TTDTGWVKAAWTL-------------FSAWPNGSCIFVHElpRVDAKVI 305
Cdd:PRK06839 166 -----GAV--------LTQENMFWNalnntfAIDLTMHDRSIVLlplfhiggiglfaFPTLFAGGVIIVPR--KFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 306 LNTLSKFPITTLCCVPTIFRLLVQE-DLTRYQFQSLRHCLTGGeALNPDVREKWKHQTGVELYEGYGQSET--VVICANP 382
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQSVRWFYNGG-APCPEELMREFIDRGFLFGQGFGMTETspTVFMLSE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 383 KGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRARMDKD 462
Cdd:PRK06839 310 EDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRPDATEETIQDGWLCTGDLARVDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 463 GYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSshdpeALTRELQEHVKR 542
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSV-----LIEKDVIEHCRL 459
|
490
....*....|
gi 1024336653 543 VTAPYKYPRK 552
Cdd:PRK06839 460 FLAKYKIPKE 469
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
84-550 |
3.57e-45 |
|
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: 166.73 E-value: 3.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 84 TGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:cd05920 35 VDGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 164 KSIITSDSLAPrvdaisaecpslqtkllvsdssrpgwLNFRELLREastehncMRTKSRDPLAIYFTSGTTGAPKMVEHS 243
Cdd:cd05920 114 VAYIVPDRHAG--------------------------FDHRALARE-------LAESIPEVALFLLSGGTTGTPKLIPRT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 244 QSSYGLGFVASGRrWVALTESDIFW--NTTDTGWVKAAWTLFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITTLccVP 321
Cdd:cd05920 161 HNDYAYNVRASAE-VCGLDQDTVYLavLPAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTAL--VP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 322 TIFRLLVQE-DLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICA---NPKgmKIKSGSMGKASP 397
Cdd:cd05920 238 ALVSLWLDAaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTrldDPD--EVIIHTQGRPMS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 398 PYD-VQIVDDEGNVLPPGEEGNVAVRIRPTrpfcfFNCYLDNPEKTAAS--EQGdFYITGDRARMDKDGYFWFMGRNDDV 474
Cdd:cd05920 316 PDDeIRVVDEEGNPVPPGEEGELLTRGPYT-----IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPDGYLVVEGRIKDQ 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 475 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTpaysshDPEALTRELQEHVK-RVTAPYKYP 550
Cdd:cd05920 390 INRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLReRGLAAYKLP 460
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
91-551 |
6.57e-45 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 167.50 E-value: 6.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIpGVTQL-TEKDLKYRLQASRAKSIITS 169
Cdd:PRK07059 50 TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV-NVNPLyTPRELEHQLKDSGAEAIVVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 170 DSLAPRVDAISAECP-------SL----------------QTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLA 226
Cdd:PRK07059 128 ENFATTVQQVLAKTAvkhvvvaSMgdllgfkghivnfvvrRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 -IYFTSGTTGapkmvehsqssyglgfVASGrrwVALTESDIFWNTTDTG-WVKAAwtlFSAWPN-GSCIFVHELP----- 298
Cdd:PRK07059 208 fLQYTGGTTG----------------VSKG---ATLLHRNIVANVLQMEaWLQPA---FEKKPRpDQLNFVCALPlyhif 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 299 ----------RVDAKVIL-----------NTLSKFPITTLCCVPTIFR-LLVQEDLTRYQFQSLRHCLTGGEALNPDVRE 356
Cdd:PRK07059 266 altvcgllgmRTGGRNILipnprdipgfiKELKKYQVHIFPAVNTLYNaLLNNPDFDKLDFSKLIVANGGGMAVQRPVAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 357 KWKHQTGVELYEGYGQSETV-VICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCY 435
Cdd:PRK07059 346 RWLEMTGCPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-GPQ----VMAGY 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 436 LDNPEKTAASEQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVV 514
Cdd:PRK07059 421 WNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAV 500
|
490 500 510
....*....|....*....|....*....|....*...
gi 1024336653 515 KAFIVltpaysSHDPeALTRE-LQEHVKRVTAPYKYPR 551
Cdd:PRK07059 501 KLFVV------KKDP-ALTEEdVKAFCKERLTNYKRPK 531
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
57-550 |
9.14e-45 |
|
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: 166.47 E-value: 9.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 57 HDVLDVWSRleeagHRPPNPAFwwvngTGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACM 136
Cdd:COG1021 28 GDLLRRRAE-----RHPDRIAV-----VDGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 137 RTGtvMIPgVTQL-----TEkdLKYRLQASRAKSIITSDS-----LAPRVDAISAECPSLQTKLLVSDSSrpGWLNFREL 206
Cdd:COG1021 97 RAG--AIP-VFALpahrrAE--ISHFAEQSEAVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVVGDAG--EFTSLDAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 207 LREASTEHNCmRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWvALTESDIFwnttdtgwvkaawtlFSAW 286
Cdd:COG1021 170 LAAPADLSEP-RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEIC-GLDADTVY---------------LAAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 287 PNG-----SCIFVHELPRVDAKVIL----NTLSKFP------ITTLCCVPTIFRLLVQ-EDLTRYQFQSLRHCLTGGEAL 350
Cdd:COG1021 233 PAAhnfplSSPGVLGVLYAGGTVVLapdpSPDTAFPliererVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 351 NPDVREKWKHQTGVELYEGYGQSETVVIC----------ANpkgmkiksgSMGKASPPYD-VQIVDDEGNVLPPGEEGNV 419
Cdd:COG1021 313 SPELARRVRPALGCTLQQVFGMAEGLVNYtrlddpeeviLT---------TQGRPISPDDeVRIVDEDGNPVPPGEVGEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 420 AVR----IRPtrpfcffncYLDNPEKTAAS--EQGdFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAE 493
Cdd:COG1021 384 LTRgpytIRG---------YYRAPEHNARAftPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 494 HPAVLESAVVSSPDPIRGEVVKAFIVLTPAysSHDPEALTRELQEhvkRVTAPYKYP 550
Cdd:COG1021 454 HPAVHDAAVVAMPDEYLGERSCAFVVPRGE--PLTLAELRRFLRE---RGLAAFKLP 505
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
66-551 |
9.69e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 166.86 E-value: 9.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 66 LEEAGHRPPN-PAFWWVNGTgaeikWSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PRK05677 30 LKQSCQRFADkPAFSNLGKT-----LTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 145 GVTQLTEKDLKYRLQASRAKSIITSDSLA-------PRVD---AISAECPSL--------------QTKLLVSDSSRPGW 200
Cdd:PRK05677 105 TNPLYTAREMEHQFNDSGAKALVCLANMAhlaekvlPKTGvkhVIVTEVADMlpplkrllinavvkHVKKMVPAYHLPQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 201 LNFRELL----REASTEHNCmrtKSRDPLAIYFTSGTTGAPK--MVEHSQssyglgFVASGRRWVALTESDIfwnttdtg 274
Cdd:PRK05677 185 VKFNDALakgaGQPVTEANP---QADDVAVLQYTGGTTGVAKgaMLTHRN------LVANMLQCRALMGSNL-------- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 275 wVKAAWTLFSAWP-------NGSCIFV-----HEL----PRvDAKVILNTLSKFPITTLCCVPTIFRLLVQ-EDLTRYQF 337
Cdd:PRK05677 248 -NEGCEILIAPLPlyhiyafTFHCMAMmlignHNIlisnPR-DLPAMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 338 QSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETV-VICANPKGmKIKSGSMGKASPPYDVQIVDDEGNVLPPGEE 416
Cdd:PRK05677 326 SALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTETSpVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 417 GNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHP 495
Cdd:PRK05677 405 GELCVK-GPQ----VMKGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALP 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 496 AVLESAVVSSPDPIRGEVVKAFIVLTPAysshdpEALTRE-LQEHVKRVTAPYKYPR 551
Cdd:PRK05677 480 GVLQCAAIGVPDEKSGEAIKVFVVVKPG------ETLTKEqVMEHMRANLTGYKVPK 530
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
90-547 |
1.29e-44 |
|
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: 170.42 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWwLVSV-ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:COG1020 502 LTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEM-VVALlAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLT 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSLAPRVDAISAECPSLQTKLLVSDSSRPgwlnfreLLREASTEHncmrtksrdpLA-IYFTSGTTGAPK--MVEHSqs 245
Cdd:COG1020 580 QSALAARLPELGVPVLALDALALAAEPATN-------PPVPVTPDD----------LAyVIYTSGSTGRPKgvMVEHR-- 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 246 syGLG-FVASGRRWVALTESDIF-WNTT---DTgwvkAAWTLFSAWPNG-SCIFVHELPRVDAKVILNTLSKFPITTLCC 319
Cdd:COG1020 641 --ALVnLLAWMQRRYGLGPGDRVlQFASlsfDA----SVWEIFGALLSGaTLVLAPPEARRDPAALAELLARHRVTVLNL 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 320 VPTIFRLLVQEDLTryQFQSLRHCLTGGEALNPDVREKW-KHQTGVELYEGYGQSETVVICAnpkGMKIKSGSMGKASPP 398
Cdd:COG1020 715 TPSLLRALLDAAPE--ALPSLRLVLVGGEALPPELVRRWrARLPGARLVNLYGPTETTVDST---YYEVTPPDADGGSVP 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 399 Y-------DVQIVDDEGNVLPPGEEG-------NVAvrirptrpfcffNCYLDNPEKTAA-------SEQGD-FYITGDR 456
Cdd:COG1020 790 IgrpiantRVYVLDAHLQPVPVGVPGelyiggaGLA------------RGYLNRPELTAErfvadpfGFPGArLYRTGDL 857
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 457 ARMDKDGYFWFMGRNDD-V-INSssYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTR 534
Cdd:COG1020 858 ARWLPDGNLEFLGRADDqVkIRG--FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAG-AAAAAALLRL 934
|
490
....*....|...
gi 1024336653 535 ELQEHVKRVTAPY 547
Cdd:COG1020 935 ALALLLPPYMVPA 947
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
82-542 |
1.94e-44 |
|
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: 165.11 E-value: 1.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 82 NGTGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDR---MMLVLPRLPEWWLvSVACMrtGTVMIPGVTQLTEKDLKYRL 158
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRvatLAWNTHRHLELYY-AVPGM--GAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 159 QASRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSR------PGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSG 232
Cdd:cd12119 94 NHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 233 TTGAPKMVEHSQSS---YGLGFVASGRrwVALTESDIFWNTTDTGWVkAAWTL-FSAWPNGSCiFVHELPRVDAKVILNT 308
Cdd:cd12119 174 TTGNPKGVVYSHRSlvlHAMAALLTDG--LGLSESDVVLPVVPMFHV-NAWGLpYAAAMVGAK-LVLPGPYLDPASLAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 309 LSKFPITTLCCVPTIFRLLVQE-DLTRYQFQSLRHCLTGGEALNPDVREKWKhQTGVELYEGYGQSET--VVICANPKGM 385
Cdd:cd12119 250 IEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFE-ERGVRVIHAWGMTETspLGTVARPPSE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 386 KIKSG---------SMGKASPPYDVQIVDDEGNVLP--PGEEGNVAVR---IRPTrpfcffncYLDNPEKTAASEQGDFY 451
Cdd:cd12119 329 HSNLSedeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRgpwVTKS--------YYKNDEESEALTEDGWL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 452 ITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEA 531
Cdd:cd12119 401 RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEG-ATVTAEE 479
|
490
....*....|.
gi 1024336653 532 LTRELQEHVKR 542
Cdd:cd12119 480 LLEFLADKVAK 490
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
90-550 |
1.51e-43 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 163.38 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT- 168
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 ----SDSLAPRVDAISAECPSLQTKLLVsDSSRPGW--LNFRELL-REASTEHNCMrTKSRDPLAIYFTSGTTGAPK--M 239
Cdd:PRK06087 129 tlfkQTRPVDLILPLQNQLPQLQQIVGV-DKLAPATssLSLSQIIaDYEPLTTAIT-THGDELAAVLFTSGTEGLPKgvM 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 240 VEHSQssyglgFVASGRRWVA---LTESDIFWnttdtgwvkaawtlFSAWPNGSCIFVHELPR---VDAKVILntLSKF- 312
Cdd:PRK06087 207 LTHNN------ILASERAYCArlnLTWQDVFM--------------MPAPLGHATGFLHGVTApflIGARSVL--LDIFt 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 313 PITTL-------C-CV----PTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPD-VREKWKHqtGVELYEGYGQSETVV-I 378
Cdd:PRK06087 265 PDACLalleqqrCtCMlgatPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKvARECQQR--GIKLLSVYGSTESSPhA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 379 CANP-KGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRirptRPFCFFNcYLDNPEKTAAS--EQGDFYiTGD 455
Cdd:PRK06087 343 VVNLdDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASR----GPNVFMG-YLDEPELTARAldEEGWYY-SGD 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 456 RARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALTRE 535
Cdd:PRK06087 417 LCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAF 496
|
490
....*....|....*
gi 1024336653 536 LQEhvKRVtAPYKYP 550
Cdd:PRK06087 497 FSR--KRV-AKYKYP 508
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
69-539 |
2.24e-43 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 163.73 E-value: 2.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 69 AGHRPPNPAFWWVNGtGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQ 148
Cdd:COG1022 21 AARFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 149 LTEKDLKYRLQASRAKSIITSD-SLAPRVDAISAECPSLQtKLLVSD----SSRPGWLNFRELLREASTEHNCMRTKSR- 222
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVLDprglRDDPRLLSLDELLALGREVADPAELEARr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 ------DPLAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIF------WnttdtgWVKA-AWTLFSAWpNG 289
Cdd:COG1022 178 aavkpdDLATIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRTlsflplA------HVFErTVSYYALA-AG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 290 SCIFVHElprvDAKVILNTLSKFPITTLCCVP----------------------TIFRLLVQ--EDLTRYQFQS------ 339
Cdd:COG1022 250 ATVAFAE----SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeagglkrKLFRWALAvgRRYARARLAGkspsll 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 340 -----------------------LRHCLTGGEALNPDVrEKWKHQTGVELYEGYGQSET-VVICANPKGmKIKSGSMGKA 395
Cdd:COG1022 326 lrlkhaladklvfsklrealggrLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETsPVITVNRPG-DNRIGTVGPP 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 396 SPPYDVQIvDDEGNVLPPGEegNVavrirptrpfcfFNCYLDNPEKTAAS--EQGDFYiTGDRARMDKDGYFWFMGRNDD 473
Cdd:COG1022 404 LPGVEVKI-AEDGEILVRGP--NV------------MKGYYKNPEATAEAfdADGWLH-TGDIGELDEDGFLRITGRKKD 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 474 VI-NSSSYRIGPVEVESALAEHPAVLESAVVsspdpirGE---VVKAFIVLtpaysshDPEALTRELQEH 539
Cdd:COG1022 468 LIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpFLAALIVP-------DFEALGEWAEEN 523
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
91-551 |
6.18e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 161.02 E-value: 6.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT-S 169
Cdd:PRK12406 13 SFDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 170 DSLAPRVDAISAEC--------PSLQTKLLVSDSSR---PGWLNFRELL--REASTEhncmrTKSRDPLAIYFTSGTTGA 236
Cdd:PRK12406 92 DLLHGLASALPAGVtvlsvptpPEIAAAYRISPALLtppAGAIDWEGWLaqQEPYDG-----PPVPQPQSMIYTSGTTGH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 237 PKMVEHSQSSYGLgfVASGRRWVALtesdIFWNTTDtgwVKAAWT--LFSAWPNGSCIFVHEL-------PRVDAKVILN 307
Cdd:PRK12406 167 PKGVRRAAPTPEQ--AAAAEQMRAL----IYGLKPG---IRALLTgpLYHSAPNAYGLRAGRLggvlvlqPRFDPEELLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 308 TLSKFPITTLCCVPTIF-RL--LVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET-VVICANPK 383
Cdd:PRK12406 238 LIERHRITHMHMVPTMFiRLlkLPEEVRAKYDVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESgAVTFATSE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 384 GMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRPTRPFCffncYLDNPEKTAASEQGDFYITGDRARMDKDG 463
Cdd:PRK12406 318 DALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFT----YHNKPEKRAEIDRGGFITSGDVGYLDADG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 464 YFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHVkrv 543
Cdd:PRK12406 394 YLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLDEADIRAQLKARL--- 469
|
....*...
gi 1024336653 544 tAPYKYPR 551
Cdd:PRK12406 470 -AGYKVPK 476
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
89-551 |
6.66e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 158.51 E-value: 6.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:PRK07798 28 RLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSLAPRVDAISAECPSLQTKLLVSDSS----RPGWLNFRELLREASTEHNcMRTKSRDPLAIYFTSGTTGAPKMVEHSQ 244
Cdd:PRK07798 107 EREFAPRVAEVLPRLPKLRTLVVVEDGSgndlLPGAVDYEDALAAGSPERD-FGERSPDDLYLLYTGGTTGMPKGVMWRQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 SSYglgFVAS--GRRWV----ALTESDIFWNTTDTG---WVKAA--------WTLFSAWPNGSCIFVHELPRVDAKVILN 307
Cdd:PRK07798 186 EDI---FRVLlgGRDFAtgepIEDEEELAKRAAAGPgmrRFPAPplmhgagqWAAFAALFSGQTVVLLPDVRFDADEVWR 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 308 TLSKFPITTLCCVPTIF-RLLVQE--DLTRYQFQSLRHCLTGGEALNPDVREKW-KHQTGVELYEGYGQSETvviCANPK 383
Cdd:PRK07798 263 TIEREKVNVITIVGDAMaRPLLDAleARGPYDLSSLFAIASGGALFSPSVKEALlELLPNVVLTDSIGSSET---GFGGS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 384 GMKiKSGSMGKASPPY----DVQIVDDEGNVLPPGEE--------GNVAVRirptrpfcffncYLDNPEKTAAS---EQG 448
Cdd:PRK07798 340 GTV-AKGAVHTGGPRFtigpRTVVLDEDGNPVEPGSGeigwiarrGHIPLG------------YYKDPEKTAETfptIDG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 449 DFY-ITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSH 527
Cdd:PRK07798 407 VRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARP 485
|
490 500
....*....|....*....|....
gi 1024336653 528 DPEaltrELQEHVKRVTAPYKYPR 551
Cdd:PRK07798 486 DLA----ELRAHCRSSLAGYKVPR 505
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
111-551 |
1.28e-41 |
|
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: 156.06 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 111 GLQPGDRMMLVLPRLPEW-WL---VSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSL 186
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELsfaVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 187 QTKLLVSdssrpGWLNFRELLREASTEHNcmrtksrDPLAIYFTSGTTGAPK--MVEHSQSSYGLGFVASgrrWVALTES 264
Cdd:cd05922 94 GTVLDAD-----GIRAARASAPAHEVSHE-------DLALLLYTSGSTGSPKlvRLSHQNLLANARSIAE---YLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 265 DIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRVDAKVIlNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCL 344
Cdd:cd05922 159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 345 TGGEALNPDV----REKWKhqtGVELYEGYGQSETVVICA--NPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGN 418
Cdd:cd05922 238 QAGGRLPQETiarlRELLP---GAQVYVMYGQTEATRRMTylPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 419 VAVRirptRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVL 498
Cdd:cd05922 315 IVHR----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLII 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1024336653 499 ESAVVSSPDPIrGEVVKAFIVLTPAYsshDPEALTRELQEhvkrVTAPYKYPR 551
Cdd:cd05922 391 EAAAVGLPDPL-GEKLALFVTAPDKI---DPKDVLRSLAE----RLPPYKVPA 435
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
54-548 |
2.49e-41 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 158.91 E-value: 2.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 54 NFAHDVLDvwsRLEEAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSV 133
Cdd:PLN02654 88 NICYNCLD---RNVEAGNGDKIAIYWEGNEPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAML 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 134 ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDS---------LAPRVDAISAE----------CPSLQTKLLVSD 194
Cdd:PLN02654 164 ACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITCNAvkrgpktinLKDIVDAALDEsakngvsvgiCLTYENQLAMKR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 195 SSRPgWLNFREL-----LREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESDIFWN 269
Cdd:PLN02654 244 EDTK-WQEGRDVwwqdvVPNYPTKCEVEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWC 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 270 TTDTGWVKA-AWTLFSAWPNGSCIFVHE-LPRV-DAKVILNTLSKFPITTLCCVPTIFRLLVQED---LTRYQFQSLRHC 343
Cdd:PLN02654 323 TADCGWITGhSYVTYGPMLNGATVLVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 344 LTGGEALNPDVREKWKHQTG---VELYEGYGQSET--VVICANPKGMKIKSGSmgKASPPYDVQ--IVDDEGNVLppgeE 416
Cdd:PLN02654 403 GSVGEPINPSAWRWFFNVVGdsrCPISDTWWQTETggFMITPLPGAWPQKPGS--ATFPFFGVQpvIVDEKGKEI----E 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 417 GNVA--VRIRPTRPFCFFNCYLDNP--EKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALA 492
Cdd:PLN02654 477 GECSgyLCVKKSWPGAFRTLYGDHEryETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024336653 493 EHPAVLESAVVSSPDPIRGEVVKAFIVLTPA--YSSHDPEALTRELQEHVKRVTAPYK 548
Cdd:PLN02654 557 SHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGvpYSEELRKSLILTVRNQIGAFAAPDK 614
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
72-551 |
4.33e-41 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 155.62 E-value: 4.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 72 RPPNPAFWwVNGTGAEIkwSFEELGKQSRKAANVLGGAcGLQPGDRMMLVL---PRLPEwwlVSVACMRTGTVMIPGVTQ 148
Cdd:PRK13391 10 TPDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 149 LTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPSLQTKLLV-SDSSRPGWLNFRELLReastehNCMRTKSRD-PL- 225
Cdd:PRK13391 83 LTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVA------GLPATPIADeSLg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 226 -AIYFTSGTTGAPKMVE----HSQSSYGLGFVASGRRWVALTESDIFWNTTdtgwvkaawTLFSAWPNGSCIFVHEL--- 297
Cdd:PRK13391 157 tDMLYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGFRSDMVYLSPA---------PLYHSAPQRAVMLVIRLggt 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 298 ----PRVDAKVILNTLSKFPITTLCCVPTIF-RLLV--QEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGY 370
Cdd:PRK13391 228 vivmEHFDAEQYLALIEEYGVTHTQLVPTMFsRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 371 GQSETVVICA-NPKGMKIKSGSMGKASPPyDVQIVDDEGNVLPPGEEGNVAvrIRPTRPFCFFNcyldNPEKTAAS--EQ 447
Cdd:PRK13391 308 AATEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIW--FEGGRPFEYLN----DPAKTAEArhPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 448 GDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLTPAYSSH 527
Cdd:PRK13391 381 GTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKA--VVQPVDGVD 458
|
490 500
....*....|....*....|....
gi 1024336653 528 DPEALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK13391 459 PGPALAAELIAFCRQRLSRQKCPR 482
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
57-552 |
4.73e-41 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 156.37 E-value: 4.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 57 HDVLDvwsrlEEAGHRPPNPAFWWVN-GTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDrmmLVLPRLPEWWLVSV-- 133
Cdd:PRK13295 27 NDDLD-----ACVASCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGD---VVSCQLPNWWEFTVly 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 134 -ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIItsdslAPR----------VDAISAECPSLQTKLLV----SDS--- 195
Cdd:PRK13295 98 lACSRIGAVLNPLMPIFRERELSFMLKHAESKVLV-----VPKtfrgfdhaamARRLRPELPALRHVVVVggdgADSfea 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 196 --SRPGWlnfrELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRwVALTESD-IFWNTT- 271
Cdd:PRK13295 173 llITPAW----EQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER-LGLGADDvILMASPm 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 272 --DTGW---------VKAAWTLFSAWPngscifvhelPRVDAKVILNTLSKFpitTLCCVPTIFRLLVQEDLTRYQFQSL 340
Cdd:PRK13295 248 ahQTGFmyglmmpvmLGATAVLQDIWD----------PARAAELIRTEGVTF---TMASTPFLTDLTRAVKESGRPVSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 341 RHCLTGGEALNPDVREKWKHQTGVELYEGYGQSE----TVVICANPKgmKIKSGSMGKASPPYDVQIVDDEGNVLPPGEE 416
Cdd:PRK13295 315 RTFLCAGAPIPGALVERARAALGAKIVSAWGMTEngavTLTKLDDPD--ERASTTDGCPLPGVEVRVVDADGAPLPAGQI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 417 GNVAVRIrptrpfCF-FNCYLDNPEKTAASEQGdFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHP 495
Cdd:PRK13295 393 GRLQVRG------CSnFGGYLKRPQLNGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHP 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 496 AVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHvkRVTAPYkYPRK 552
Cdd:PRK13295 466 AIAQVAIVAYPDERLGERACAFVVPRPG-QSLDFEEMVEFLKAQ--KVAKQY-IPER 518
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
89-552 |
5.62e-41 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 154.73 E-value: 5.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLA-ALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSLAprvDAISAECPSLQTKLLVSDSSRPGWLNFRELLREAStehncmrtksrdplaIYFTSGTTGAPKMVehsQSSYG 248
Cdd:PRK03640 106 DDDFE---AKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVAT---------------IMYTSGTTGKPKGV---IQTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 249 LGFvasgrrWVA--------LTESDifwnttdtGWVkAAWTLFSAwpNG------SCIF---VHELPRVDAKVILNTLSK 311
Cdd:PRK03640 165 NHW------WSAvgsalnlgLTEDD--------CWL-AAVPIFHI--SGlsilmrSVIYgmrVVLVEKFDAEKINKLLQT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 312 FPITTLCCVPTIF-RLLVQEDLTRYQfQSLRHCLTGGEALNPDVREKWKhQTGVELYEGYGQSETVV-ICA-NPKGMKIK 388
Cdd:PRK03640 228 GGVTIISVVSTMLqRLLERLGEGTYP-SSFRCMLLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETASqIVTlSPEDALTK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 389 SGSMGKASPPYDVQIVDDeGNVLPPGEEGNVAVR---IRPTrpfcffncYLDNPEKTAASEQGDFYITGDRARMDKDGYF 465
Cdd:PRK03640 306 LGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKgpnVTKG--------YLNREDATRETFQDGWFKTGDIGYLDEEGFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 466 WFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLtpaySSHDPEAltrELQEHVKRVTA 545
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK----SGEVTEE---ELRHFCEEKLA 449
|
....*..
gi 1024336653 546 PYKYPRK 552
Cdd:PRK03640 450 KYKVPKR 456
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
87-552 |
6.20e-41 |
|
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: 154.76 E-value: 6.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 87 EIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSI 166
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 167 ITsdslaprvdaisaecpslqtkllvsDSSrpgwLNFRELLREASTEHNCMRTKS-RDPLAIYFTSGTTGAPKMVEHSQS 245
Cdd:cd12118 106 FV-------------------------DRE----FEYEDLLAEGDPDFEWIPPADeWDPIALNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 246 SYGLGFVASGRRWVALTESDIFWNTTD---TGWVkAAWTLFSAWPNGSCifvheLPRVDAKVILNTLSKFPITTLCCVPT 322
Cdd:cd12118 157 GAYLNALANILEWEMKQHPVYLWTLPMfhcNGWC-FPWTVAAVGGTNVC-----LRKVDAKAIYDLIEKHKVTHFCGAPT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 323 IFRLLVQ-EDLTRYQFQSLRHCLTGGEALNPDVREKwKHQTGVELYEGYGQSET---VVICA-NPK----------GMKI 387
Cdd:cd12118 231 VLNMLANaPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVCAwKPEwdelpteeraRLKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 388 KSGSMGKASPPYDVqiVDDEGNVLPP--GEE-GNVAVRIRPTrpfcfFNCYLDNPEKTAASEQGDFYITGDRARMDKDGY 464
Cdd:cd12118 310 RQGVRYVGLEEVDV--LDPETMKPVPrdGKTiGEIVFRGNIV-----MKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 465 FWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYsshdpEALTRELQEHVKRVT 544
Cdd:cd12118 383 IEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA-----KVTEEEIIAFCREHL 457
|
....*...
gi 1024336653 545 APYKYPRK 552
Cdd:cd12118 458 AGFMVPKT 465
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
67-540 |
1.22e-40 |
|
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: 153.97 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 67 EEAGHRPPNPAfwwVNGTGAEIkwSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGV 146
Cdd:cd17646 6 EQAARTPDAPA---VVDEGRTL--TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 147 TQLTEKDLKYRLQASRAKSIITSDSLAprvDAISAEcpslqtkLLVSDSSRPGWLNFRELLREASTEhncmrtksRDPLA 226
Cdd:cd17646 80 PGYPADRLAYMLADAGPAVVLTTADLA---ARLPAG-------GDVALLGDEALAAPPATPPLVPPR--------PDNLA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 -IYFTSGTTGAPK--MVEHSQssyglgfVASGRRWV----ALTESDIFWNTTDTGWVKAAWTLFsaWP--NGSCIFVHEl 297
Cdd:cd17646 142 yVIYTSGSTGRPKgvMVTHAG-------IVNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWELF--WPlvAGARLVVAR- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 298 P--RVDAKVILNTLSKFPITTLCCVPTIFRLLVQEdLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET 375
Cdd:cd17646 212 PggHRDPAYLAALIREHGVTTCHFVPSMLRVFLAE-PAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 376 VV-----ICANPKGMKikSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRP-TRPfcffncYLDNPEKTAAS---- 445
Cdd:cd17646 291 AIdvthwPVRGPAETP--SVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQlARG------YLGRPALTAERfvpd 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 446 --EQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTP 522
Cdd:cd17646 363 pfGPGSrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAA 442
|
490
....*....|....*...
gi 1024336653 523 AYSSHDPEALTRELQEHV 540
Cdd:cd17646 443 GAAGPDTAALRAHLAERL 460
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
85-539 |
1.30e-40 |
|
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: 153.13 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 85 GAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAK 164
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 165 SIITSDSlaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksRDPLAIYFTSGTTGAPKMVEHSQ 244
Cdd:cd05907 80 ALFVEDP--------------------------------------------------DDLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 SSYgLGFVASGRRWVALTESD----------IFWNTTDTGWVKAAwtlfsawpnGSCIFVHElprvDAKVILNTLSKFPI 314
Cdd:cd05907 110 RNI-LSNALALAERLPATEGDrhlsflplahVFERRAGLYVPLLA---------GARIYFAS----SAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 315 TTLCCVPTIFR----LLVQEDLTRYQ--------FQSLRHCLTGGEALNPDVREKWkHQTGVELYEGYGQSETV-VICAN 381
Cdd:cd05907 176 TVFLAVPRVWEkvyaAIKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAELLHFF-RALGIPVYEGYGLTETSaVVTLN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 382 PKGmKIKSGSMGKASPPYDVQIVDDeGNVLPPGEegNVavrirptrpfcfFNCYLDNPEKTAASEQGD-FYITGDRARMD 460
Cdd:cd05907 255 PPG-DNRIGTVGKPLPGVEVRIADD-GEILVRGP--NV------------MLGYYKNPEATAEALDADgWLHTGDLGEID 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 461 KDGYFWFMGRNDDVI-NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPirgeVVKAFIVLtpaysshDPEALTRELQEH 539
Cdd:cd05907 319 EDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP-------DPEALEAWAEEH 387
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
89-555 |
7.06e-40 |
|
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: 150.19 E-value: 7.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKsiit 168
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLA-ALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 sdslaprVDAISAecpslqtkllvsdssrpgwlnfrellreastehncmrtksrdplaIYFTSGTTGAPKMVE-----HS 243
Cdd:cd05912 76 -------LDDIAT---------------------------------------------IMYTSGTTGKPKGVQqtfgnHW 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 244 QSSYG----LGFVASGRRWVALTesdIFWnttdtgwVKAAWTLFSAWPNGSCIFVHElpRVDAKVILNTLSKFPITTLCC 319
Cdd:cd05912 104 WSAIGsalnLGLTEDDNWLCALP---LFH-------ISGLSILMRSVIYGMTVYLVD--KFDAEQVLHLINSGKVTIISV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 320 VPTIFRLLVQEDLTRYQfQSLRHCLTGGEALNPDVREKWKhQTGVELYEGYGQSETV--VICANPKGMKIKSGSMGKASP 397
Cdd:cd05912 172 VPTMLQRLLEILGEGYP-NNLRCILLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKPLF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 398 PYDVQIVDDEGnvlPPGEEGNVAVR---IRPTrpfcffncYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDV 474
Cdd:cd05912 250 PVELKIEDDGQ---PPYEVGEILLKgpnVTKG--------YLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDL 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 475 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHdpealtrELQEHVKRVTAPYKYPRKNC 554
Cdd:cd05912 319 IISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEE-------ELIAYCSEKLAKYKVPKKIY 391
|
.
gi 1024336653 555 Q 555
Cdd:cd05912 392 F 392
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
91-552 |
7.24e-40 |
|
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: 150.99 E-value: 7.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd05903 3 TYSELDTRADRLAAGLA-ALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SlaprvdaisaecpslqtkllvsdssrpgwlnFRellreaSTEHNCMrtkSRDPLAIYFTSGTTGAPKMVEHSQSSYGLG 250
Cdd:cd05903 82 R-------------------------------FR------QFDPAAM---PDAVALLLFTSGTTGEPKGVMHSHNTLSAS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 251 FVASGRRWvALTESDIFWNTTD----TGWVKAAWTLFSAwpnGSCifVHELPRVDAKVILNTLSKFPITTLCCVPT-IFR 325
Cdd:cd05903 122 IRQYAERL-GLGPGDVFLVASPmahqTGFVYGFTLPLLL---GAP--VVLQDIWDPDKALALMREHGVTFMMGATPfLTD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 326 LLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSE---TVVICANPKGMKIkSGSMGKASPPYDVQ 402
Cdd:cd05903 196 LLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEcpgAVTSITPAPEDRR-LYTDGRPLPGVEIK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 403 IVDDEGNVLPPGEEGNVAVRIRPTrpfcfFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRI 482
Cdd:cd05903 275 VVDDTGATLAPGVEGELLSRGPSV-----FLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENI 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1024336653 483 GPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLtpayssHDPEALT-RELQEHVKRV-TAPYKYPRK 552
Cdd:cd05903 350 PVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT------KSGALLTfDELVAYLDRQgVAKQYWPER 415
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
88-551 |
1.85e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 150.73 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 88 IKWSFEELGKQSRKAANVLGGAcGLQPGDRMMlVLPRLPEWWLV-SVACMRTGTVMIPgvtqltekdLKYRLQASRaksi 166
Cdd:PRK09088 21 RRWTYAELDALVGRLAAVLRRR-GCVDGERLA-VLARNSVWLVAlHFACARVGAIYVP---------LNWRLSASE---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 167 itsdslaprVDAISAECpslQTKLLVSDSS----RPGWLNFRELLREASTeHNCMRTKSRDPLA---IYFTSGTTGAPKM 239
Cdd:PRK09088 86 ---------LDALLQDA---EPRLLLGDDAvaagRTDVEDLAAFIASADA-LEPADTPSIPPERvslILFTSGTSGQPKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 240 V---EHSQSSYGLGFVASGR---RWVALTESDIFwnttdtGWVKAAWTLFSAWPNGSCIFVHelPRVDAKVILNTLS--K 311
Cdd:PRK09088 153 VmlsERNLQQTAHNFGVLGRvdaHSSFLCDAPMF------HIIGLITSVRPVLAVGGSILVS--NGFEPKRTLGRLGdpA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 312 FPITTLCCVPTIFRLL-VQEDLTRYQFQSLRHCLTGGeALNPDVREKWKHQTGVELYEGYGQSE--TVV-ICANPKGMKI 387
Cdd:PRK09088 225 LGITHYFCVPQMAQAFrAQPGFDAAALRHLTALFTGG-APHAAEDILGWLDDGIPMVDGFGMSEagTVFgMSVDCDVIRA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 388 KSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGD-FYITGDRARMDKDGYFW 466
Cdd:PRK09088 304 KAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFW 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 467 FMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEaltrELQEHVKRVTAP 546
Cdd:PRK09088 379 VVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSHLSTRLAK 453
|
....*
gi 1024336653 547 YKYPR 551
Cdd:PRK09088 454 YKVPK 458
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
133-551 |
2.86e-39 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 151.06 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 133 VACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPslQTKLLVSDSSRPGWLNFrELLREAST 212
Cdd:PRK13382 111 LAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALADCP--QATRIVAWTDEDHDLTV-EVLIAAHA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 213 EHNCMRTKSRDPLaIYFTSGTTGAPKMVEHSQS-SYG-LGFVASGRRWVALTESDIfwnttdtgwvkaAWTLFSAWPNGS 290
Cdd:PRK13382 188 GQRPEPTGRKGRV-ILLTSGTTGTPKGARRSGPgGIGtLKAILDRTPWRAEEPTVI------------VAPMFHAWGFSQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 291 CIFVHELP-------RVDAKVILNTLSKFPITTLCCVPTIFRL---LVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKH 360
Cdd:PRK13382 255 LVLAASLActivtrrRFDPEATLDLIDRHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMD 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 361 QTGVELYEGYGQSETVVIC-ANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRptrpfCFFNCYldNP 439
Cdd:PRK13382 335 QFGDVIYNNYNATEAGMIAtATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRND-----TQFDGY--TS 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 440 EKTAASEQGdFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 519
Cdd:PRK13382 408 GSTKDFHDG-FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVV 486
|
410 420 430
....*....|....*....|....*....|..
gi 1024336653 520 LTPaysshDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK13382 487 LKP-----GASATPETLKQHVRDNLANYKVPR 513
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-551 |
7.86e-39 |
|
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: 145.88 E-value: 7.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPK--MVEHsqssYGL---GFVAsGRRwVALTESDI----------FwnttdtGWVKAawTLFSAWP 287
Cdd:cd05917 3 DVINIQFTSGTTGSPKgaTLTH----HNIvnnGYFI-GER-LGLTEQDRlcipvplfhcF------GSVLG--VLACLTH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 288 NGSCIFVHelPRVDAKVILNTLSKFPITTLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGV-E 365
Cdd:cd05917 69 GATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 366 LYEGYGQSETVVICANPK---GMKIKSGSMGKASPPYDVQIVDDEGNVLPP-GEEGNVAVRirptrPFCFFNCYLDNPEK 441
Cdd:cd05917 147 VTIAYGMTETSPVSTQTRtddSIEKRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 442 TAASEQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 520
Cdd:cd05917 222 TAEAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL 301
|
330 340 350
....*....|....*....|....*....|.
gi 1024336653 521 TPaysshDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05917 302 KE-----GAELTEEDIKAYCKGKIAHYKVPR 327
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
72-552 |
7.96e-39 |
|
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: 148.16 E-value: 7.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 72 RPPNPAFWWVNGTgaeikWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPgvtqlte 151
Cdd:cd05945 4 NPDRPAVVEGGRT-----LTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 152 kdlkyrlqasraksiITSDSLAPRVDAISAECpslQTKLLVSDSSrpgwlnfrellreastehncmrtksrDPLAIYFTS 231
Cdd:cd05945 71 ---------------LDASSPAERIREILDAA---KPALLIADGD--------------------------DNAYIIFTS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 232 GTTGAPKMVEHSQSSyglgfVASGRRWV----ALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVheLPR---VDAKV 304
Cdd:cd05945 107 GSTGRPKGVQISHDN-----LVSFTNWMlsdfPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVP--VPRdatADPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 305 ILNTLSKFPITTLCCVPTIFRLLVQ-EDLTRYQFQSLRHCLTGGEALNPDVREKWKHQT-GVELYEGYGQSETVVICAnp 382
Cdd:cd05945 180 LFRFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVT-- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 383 kGMKI--------KSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRirptRPfCFFNCYLDNPEKTAAS----EQGDF 450
Cdd:cd05945 258 -YIEVtpevldgyDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVIS----GP-SVSKGYLNNPEKTAAAffpdEGQRA 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 451 YITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPayssHDPE 530
Cdd:cd05945 332 YRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP----GAEA 407
|
490 500
....*....|....*....|..
gi 1024336653 531 ALTRELQEHVKRVTAPYKYPRK 552
Cdd:cd05945 408 GLTKAIKAELAERLPPYMIPRR 429
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
219-539 |
2.89e-38 |
|
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: 147.48 E-value: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 219 TKSRDPLAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFWNTTDT----GWVKAAWTLFSAwpnGSCIFV 294
Cdd:cd05909 144 VQPDDPAVILFTSGSEGLPKGVVLSHKNL-LANVEQITAIFDPNPEDVVFGALPFfhsfGLTGCLWLPLLS---GIKVVF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 295 HELPrVDAKVILNTLSKFPITTLCCVPTIFRLLVQEdLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSE 374
Cdd:cd05909 220 HPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 375 TV-VICANPKGMKIKSGSMGKASPPYDVQIVDDEGNV-LPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYI 452
Cdd:cd05909 298 CSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVR-GPN----VMLGYLNEPELTSFAFGDGWYD 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 453 TGDRARMDKDGYFWFMGRnddviNSSSYRIG----PVE-VESALAEH-PAVLESAVVSSPDPIRGEVVKAFIVLTPAyss 526
Cdd:cd05909 373 TGDIGKIDGEGFLTITGR-----LSRFAKIAgemvSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLLTTTTDT--- 444
|
330
....*....|...
gi 1024336653 527 hDPEALTRELQEH 539
Cdd:cd05909 445 -DPSSLNDILKNA 456
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
223-551 |
3.89e-38 |
|
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: 143.56 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPK--MVEHSqssyglGFVASGRRWVA---LTESDIFWNTT---DTGWVKAAWTLFSAwpnGSCIFV 294
Cdd:cd17637 1 DPFVIIHTAAVAGRPRgaVLSHG------NLIAANLQLIHamgLTEADVYLNMLplfHIAGLNLALATFHA---GGANVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 295 heLPRVDAKVILNTLSKFPITTLCCVPTI-FRLLVQEDLTRYQFQSLRHcLTGGEAlnPDVREKWKHQTGVELYEGYGQS 373
Cdd:cd17637 72 --MEKFDPAEALELIEEEKVTLMGSFPPIlSNLLDAAEKSGVDLSSLRH-VLGLDA--PETIQRFEETTGATFWSLYGQT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 374 ETV-VICANPkgMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYI 452
Cdd:cd17637 147 ETSgLVTLSP--YRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR-GPL----VFQGYWNLPELTAYTFRNGWHH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 453 TGDRARMDKDGYFWFMGRN--DDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAysshdpE 530
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG------A 293
|
330 340
....*....|....*....|..
gi 1024336653 531 ALT-RELQEHVKRVTAPYKYPR 551
Cdd:cd17637 294 TLTaDELIEFVGSRIARYKKPR 315
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
89-550 |
7.43e-38 |
|
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: 146.19 E-value: 7.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEwwlvSVACM----RTGTVMIPGVTQLTEKDLKYRLQASRAK 164
Cdd:cd12117 22 SLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPE----LVVALlavlKAGAAYVPLDPELPAERLAFMLADAGAK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 165 SIITSDSLAPRVDAisaecpsLQTKLLVSDSSRPGwlnfrellreasTEHNCMRTKSRDPLA-IYFTSGTTGAPK--MVE 241
Cdd:cd12117 97 VLLTDRSLAGRAGG-------LEVAVVIDEALDAG------------PAGNPAVPVSPDDLAyVMYTSGSTGRPKgvAVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 242 HsqssYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRV-DAKVILNTLSKFPITTLCCV 320
Cdd:cd12117 158 H----RGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 321 PTIFRLLVQEDLTRyqFQSLRHCLTGGEALNPD-VREKWKHQTGVELYEGYGQSE-TVVICA---NPKGMKIKSGSMGKA 395
Cdd:cd12117 234 AALFNQLADEDPEC--FAGLRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTEnTTFTTShvvTELDEVAGSIPIGRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 396 SPPYDVQIVDDEGNVLPPGEEGNVavrirptrpfcffnC---------YLDNPEKTAAS-------EQGDFYITGDRARM 459
Cdd:cd12117 312 IANTRVYVLDEDGRPVPPGVPGEL--------------YvggdglalgYLNRPALTAERfvadpfgPGERLYRTGDLARW 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 460 DKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVsspdPIRGEVVKAFIVltpAYSSHDPEALTRELQEH 539
Cdd:cd12117 378 LPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVV----VREDAGGDKRLV---AYVVAEGALDAAELRAF 450
|
490
....*....|.
gi 1024336653 540 VKRVTAPYKYP 550
Cdd:cd12117 451 LRERLPAYMVP 461
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
91-551 |
7.61e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 147.00 E-value: 7.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMlVLPRLPEWWLVS-VACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:PRK07788 76 TYAELDEQSNALARGLL-ALGVRAGDGVA-VLARNHRGFVLAlYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 170 DSLAPRVDAISAECPSLQTKLLVSDS---SRPGWLNFRELLREASTEHncMRTKSRDPLAIYFTSGTTGAPKMVEHSQSS 246
Cdd:PRK07788 154 DEFTDLLSALPPDLGRLRAWGGNPDDdepSGSTDETLDDLIAGSSTAP--LPKPPKPGGIVILTSGTTGTPKGAPRPEPS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 247 yGLGFVAS-------GRRWVALTESDIFWNTtdtGWvkAAWTLfsAWPNGSCIFVHElpRVDAKVILNTLSKFPITTLCC 319
Cdd:PRK07788 232 -PLAPLAGllsrvpfRAGETTLLPAPMFHAT---GW--AHLTL--AMALGSTVVLRR--RFDPEATLEDIAKHKATALVV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 320 VPTIFRLLV---QEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSE-TVVICANPKGMKIKSGSMGKA 395
Cdd:PRK07788 302 VPVMLSRILdlgPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvAFATIATPEDLAEAPGTVGRP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 396 SPPYDVQIVDDEGNVLPPGEEGNVAVRIRPTrpfcfFNCYLDNPEKTAAseqGDFYITGDRARMDKDGYFWFMGRNDDVI 475
Cdd:PRK07788 382 PKGVTVKILDENGNEVPRGVVGRIFVGNGFP-----FEGYTDGRDKQII---DGLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024336653 476 NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEaltrELQEHVKRVTAPYKYPR 551
Cdd:PRK07788 454 VSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG-AALDED----AIKDYVRDNLARYKVPR 524
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
84-540 |
9.29e-38 |
|
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: 145.95 E-value: 9.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 84 TGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP-GVTQLTEKdLKYRLQASR 162
Cdd:cd17651 15 VAEGRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPlDPAYPAER-LAFMLADAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 163 AKSIITSDSLAPRVDAISAecpslqtkllvsdssrPGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEH 242
Cdd:cd17651 93 PVLVLTHPALAGELAVELV----------------AVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 243 SQSSYgLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCI-FVHELPRVDAKVILNTLSKFPITtLCCVP 321
Cdd:cd17651 157 PHRSL-ANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLvLPPEEVRTDPPALAAWLDEQRIS-RVFLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 322 TIFRLLVQEDLTRY--QFQSLRHCLTGGEAL--NPDVREKWKHQTGVELYEGYGQSETVVICA----NPKGMKIKSGSMG 393
Cdd:cd17651 235 TVALRALAEHGRPLgvRLAALRYLLTGGEQLvlTEDLREFCAGLPGLRLHNHYGPTETHVVTAlslpGDPAAWPAPPPIG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 394 KASPPYDVQIVDDEGNVLPPGEEGNVAVRirptrPFCFFNCYLDNPEKTAA-------SEQGDFYITGDRARMDKDGYFW 466
Cdd:cd17651 315 RPIDNTRVYVLDAALRPVPPGVPGELYIG-----GAGLARGYLNRPELTAErfvpdpfVPGARMYRTGDLARWLPDGELE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024336653 467 FMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHV 540
Cdd:cd17651 390 FLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-APVDAAELRAALATHL 462
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
91-551 |
4.11e-36 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 142.27 E-value: 4.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:PRK12492 51 SYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SLAPRVDAISAEC--------------PSLQ----------TKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLA 226
Cdd:PRK12492 131 MFGKLVQEVLPDTgieylieakmgdllPAAKgwlvntvvdkVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 IY-FTSGTTGAPK--MVEHSQSSYGLGFVASGRRWVALTESDIFWNTTDtgwVKAA----WTLFSAWPNGSCIFV---HE 296
Cdd:PRK12492 211 VLqYTGGTTGLAKgaMLTHGNLVANMLQVRACLSQLGPDGQPLMKEGQE---VMIAplplYHIYAFTANCMCMMVsgnHN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 297 L----PRvDAKVILNTLSKFPITTLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYG 371
Cdd:PRK12492 288 VlitnPR-DIPGFIKELGKWRFSALLGLNTLFvALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 372 QSETV-VICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGD- 449
Cdd:PRK12492 367 LTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GPQ----VMKGYWQQPEATAEALDAEg 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 450 FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVltpaysSHDP 529
Cdd:PRK12492 442 WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV------ARDP 515
|
490 500
....*....|....*....|..
gi 1024336653 530 EALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK12492 516 GLSVEELKAYCKENFTGYKVPK 537
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
220-562 |
4.57e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 138.67 E-value: 4.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 220 KSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGfVASGRRWVALTESDIFW------NTTDTGWVKAA--------WTLFSA 285
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQEDIFRM-LMGGADFGTGEFTPSEDahkaaaAAAGTVMFPAPplmhgtgsWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 286 WPNGSCIFVHElPRVDAKVILNTLSKFPITTLCCVPTIF-RLLVQE--DLTRYQFQSLRHCLTGGEALNPDVREKW-KHQ 361
Cdd:cd05924 80 LLGGQTVVLPD-DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlrDAGPYDLSSLFAISSGGALLSPEVKQGLlELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 362 TGVELYEGYGQSET-VVICANPKGMKIKSGSMGKASPpyDVQIVDDEGNVLPPGEEGNVAVRIRPTRPfcffNCYLDNPE 440
Cdd:cd05924 159 PNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGGVGWIARRGHIP----LGYYGDEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 441 KTAAS--EQGD--FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 516
Cdd:cd05924 233 KTAETfpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1024336653 517 FIVLTPAyssHDPEAltRELQEHVKRVTAPYKYPRKNCQRRFLERS 562
Cdd:cd05924 313 VVQLREG---AGVDL--EELREHCRTRIARYKLPKQVVFVDEIERS 353
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
111-552 |
1.00e-35 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 142.48 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 111 GLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVdaisAECPSLQTKL 190
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRF----QPSRVAEAAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 191 LVSDSSRPGWLNFRELLREASTehncmrtksrdpLAIYfTSGTTGAPKMVEHSQSSYgLGFV-ASGRRWVALTESDIFWN 269
Cdd:PRK06060 127 LMSEAARVAPGGYEPMGGDALA------------YATY-TSGTTGPPKAAIHRHADP-LTFVdAMCRKALRLTPEDTGLC 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 270 TTDT----GWVKAAWTLFSAwpnGSCIFVHELPrVDAKVILNTLSKFPITTLCCVPTIFRLLVqEDLTRYQFQSLRHCLT 345
Cdd:PRK06060 193 SARMyfayGLGNSVWFPLAT---GGSAVINSAP-VTPEAAAILSARFGPSVLYGVPNFFARVI-DSCSPDSFRSLRCVVS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 346 GGEALNPDVREKW-KHQTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiR 424
Cdd:PRK06060 268 AGEALELGLAERLmEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVR-G 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 425 PTrpfcFFNCYLDNPEKTAasEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS 504
Cdd:PRK06060 347 PA----IAKGYWNRPDSPV--ANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVA 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1024336653 505 SPDPIRGEVVKAFIVltPAYSSHDPEALTRELQEHVKRVTAPYKYPRK 552
Cdd:PRK06060 421 VRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHR 466
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
223-546 |
4.60e-35 |
|
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: 135.69 E-value: 4.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYF-TSGTTGAPKMVEHSQSsyglGFVASGrrWVALTESDifWNTTDTgwVKAAWTLFSAwpNGSCIFVHELPRVD 301
Cdd:cd05944 2 DDVAAYFhTGGTTGTPKLAQHTHS----NEVYNA--WMLALNSL--FDPDDV--LLCGLPLFHV--NGSVVTLLTPLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 302 AKVILNT----------------LSKFPITTLCCVPTIFRLLVQEDLTRyQFQSLRHCLTGGEALNPDVREKWKHQTGVE 365
Cdd:cd05944 70 AHVVLAGpagyrnpglfdnfwklVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 366 LYEGYGQSE-TVVICANPKGMKIKSGSMGKASPPYDVQIV--DDEGNVL---PPGEEGNVAVRIRPTrpfcfFNCYLDNP 439
Cdd:cd05944 149 VVEGYGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLrdcAPDEVGEICVAGPGV-----FGGYLYTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 440 EKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 519
Cdd:cd05944 224 GNKNAFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQ 303
|
330 340
....*....|....*....|....*...
gi 1024336653 520 LTPAySSHDPEALTRELQEHV-KRVTAP 546
Cdd:cd05944 304 LKPG-AVVEEEELLAWARDHVpERAAVP 330
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
88-551 |
2.28e-34 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 137.25 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 88 IKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMipgVT-----QLTEkdLKYRLQASR 162
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL---VTinpayRLSE--LEYALNQSG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 163 AKSIITSDS------------LAP------RVDAISAECPSLQTKLLVSDSSRPGWLNFRELLREASTEHN-----CMRT 219
Cdd:PRK08315 116 CKALIAADGfkdsdyvamlyeLAPelatcePGQLQSARLPELRRVIFLGDEKHPGMLNFDELLALGRAVDDaelaaRQAT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 220 -KSRDPLAIYFTSGTTGAPK--MVEHsqssYGLG----FVASGRRwvaLTESD---I-------FwnttdtGWVKAAWTL 282
Cdd:PRK08315 196 lDPDDPINIQYTSGTTGFPKgaTLTH----RNILnngyFIGEAMK---LTEEDrlcIpvplyhcF------GMVLGNLAC 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 283 FSAwpnGSCIfVHELPRVDAKVILNTLSKFPITTLCCVPTIF-RLLVQEDLTRYQFQSLRhclTGGEALNP-------DV 354
Cdd:PRK08315 263 VTH---GATM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLR---TGIMAGSPcpievmkRV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 355 REKWkHQTGVELyeGYGQSETV-VICA----NPkgMKIKSGSMGKASPPYDVQIVDDE-GNVLPPGEEGNVAvrirpTRP 428
Cdd:PRK08315 336 IDKM-HMSEVTI--AYGMTETSpVSTQtrtdDP--LEKRVTTVGRALPHLEVKIVDPEtGETVPRGEQGELC-----TRG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 429 FCFFNCYLDNPEKTAASEQGDFYI-TGDRARMDKDGYFWFMGRNDDVI-----NsssyrIGPVEVESALAEHPAVLESAV 502
Cdd:PRK08315 406 YSVMKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIirggeN-----IYPREIEEFLYTHPKIQDVQV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1024336653 503 VSSPDPIRGEVVKAFIVLtpayssHDPEALTRE-LQEHVKRVTAPYKYPR 551
Cdd:PRK08315 481 VGVPDEKYGEEVCAWIIL------RPGATLTEEdVRDFCRGKIAHYKIPR 524
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
226-551 |
3.21e-34 |
|
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: 135.58 E-value: 3.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 226 AIYFTSGTTGAPKMVEHSQSSyGLGFVASGRRWvalteSDIFWNTTDTGWVKAAwTLFSAWPNGSCIFVHEL-------P 298
Cdd:cd05929 129 KMLYSGGTTGRPKGIKRGLPG-GPPDNDTLMAA-----ALGFGPGADSVYLSPA-PLYHAAPFRWSMTALFMggtlvlmE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 299 RVDAKVILNTLSKFPITTLCCVPTIF-RLLVQEDLTR--YQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET 375
Cdd:cd05929 202 KFDPEEFLRLIERYRVTFAQFVPTMFvRLLKLPEAVRnaYDLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 376 VVICAnpkgmkIKS-------GSMGKASPPyDVQIVDDEGNVLPPGEEGNVAVRIRPTrpfcfFNcYLDNPEKTAASEQG 448
Cdd:cd05929 282 QGLTI------INGeewlthpGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG-----FE-YTNDPEKTAAARNE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 449 DFYIT-GDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLTPAYSSH 527
Cdd:cd05929 349 GGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGAD 426
|
330 340
....*....|....*....|....
gi 1024336653 528 DPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd05929 427 AGTALAEELIAFLRDRLSRYKCPR 450
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
223-551 |
2.86e-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: 129.76 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPKMVEHSQ-----SSYG----LGFVASGRRWVALTESDIfwnttdTG------WVKAAWTLfsawp 287
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAanllaSAAGlhsrLGFGGGDSWLLSLPLYHV------GGlailvrSLLAGAEL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 288 ngscifvHELPRVDAkvILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQtGVELY 367
Cdd:cd17630 70 -------VLLERNQA--LAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 368 EGYGQSETVV-ICANPKGMKiKSGSMGKASPPYDVQIVDDeGNVLPPGEegnvavrirptrpfCFFNCYLDNPEKTAASE 446
Cdd:cd17630 140 TTYGMTETASqVATKRPDGF-GRGGVGVLLPGRELRIVED-GEIWVGGA--------------SLAMGYLRGQLVPEFNE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 447 QGDFYiTGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLtpayss 526
Cdd:cd17630 204 DGWFT-TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG------ 276
|
330 340
....*....|....*....|....*
gi 1024336653 527 hDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd17630 277 -RGPADPAELRAWLKDKLARFKLPK 300
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
90-539 |
3.13e-33 |
|
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: 132.41 E-value: 3.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 90 WSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 170 DSLAPRVDAISaecpslqtkllvsdssrPGWLnfRELLREASTEHNCMRTKSRDPLA-IYFTSGTTGAPKMVEHSQSSYg 248
Cdd:cd12116 92 DALPDRLPAGL-----------------PVLL--LALAAAAAAPAAPRTPVSPDDLAyVIYTSGSTGRPKGVVVSHRNL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 249 LGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFsaWP---NGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPTIFR 325
Cdd:cd12116 152 VNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELL--LPllaGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 326 LLVQEdltryQFQSLR--HCLTGGEALNPDVREKWKHQTGvELYEGYGQSETVV------ICANPKGMKIksgsmGKASP 397
Cdd:cd12116 230 MLLDA-----GWQGRAglTALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI-----GRPLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 398 PYDVQIVDDEGNVLPPGEEGN-------VAVRirptrpfcffncYLDNPEKTAAS--------EQGDFYITGDRARMDKD 462
Cdd:cd12116 299 NTQVYVLDAALRPVPPGVPGElyiggdgVAQG------------YLGRPALTAERfvpdpfagPGSRLYRTGDLVRRRAD 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 463 GYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLtPAYSSHDPEALTRELQEH 539
Cdd:cd12116 367 GRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALRAHLRAT 441
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
91-562 |
4.00e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 132.70 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SLaprvDAIsaecPSLQTKLLV------SDSSRPGWLNFRELLREASTEHNCMRtksrdplaIYFTSGTTGAPKMVEHSQ 244
Cdd:PRK06145 108 EF----DAI----VALETPKIVidaaaqADSRRLAQGGLEIPPQAAVAPTDLVR--------LMYTSGTTDRPKGVMHSY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 SSY---------GLGFVASGRRWVALTESDIfwNTTDTGWVKAAWtlfsawpNGSCIFVHElpRVDAKVILNTLSKFPIT 315
Cdd:PRK06145 172 GNLhwksidhviALGLTASERLLVVGPLYHV--GAFDLPGIAVLW-------VGGTLRIHR--EFDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 316 TLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEAlNPD--VREKWKHQTGVELYEGYGQSETvviCANPKGMKI----- 387
Cdd:PRK06145 241 CAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET---CSGDTLMEAgreie 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 388 KSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVR-IRPTRPfcffncYLDNPEKTAASEQGDFYITGDRARMDKDGYFW 466
Cdd:PRK06145 317 KIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRgPKVTKG------YWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 467 FMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPealtrELQEHVKRVTAP 546
Cdd:PRK06145 391 LTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE-----ALDRHCRQRLAS 465
|
490
....*....|....*.
gi 1024336653 547 YKYPRKNCQRRFLERS 562
Cdd:PRK06145 466 FKVPRQLKVRDELPRN 481
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
227-551 |
1.29e-32 |
|
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: 128.00 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 IYFTSGTTGAPK--MVEHSQSsygLGFVASGRRWVALTESD------IFWNTTdtGWvKAAWtlFSAWPNGSCIFVHELp 298
Cdd:cd17638 5 IMFTSGTTGRSKgvMCAHRQT---LRAAAAWADCADLTEDDryliinPFFHTF--GY-KAGI--VACLLTGATVVPVAV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 299 rVDAKVILNTLSKFPITTLCCVPTIFR-LLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVE-LYEGYGQSETV 376
Cdd:cd17638 76 -FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGLTEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 377 V--ICANPKGMKIKSGSMGKASPPYDVQIVDDeGNVLPPGEegNVAVRirptrpfcffncYLDNPEKTAASEQGDFYI-T 453
Cdd:cd17638 155 VatMCRPGDDAETVATTCGRACPGFEVRIADD-GEVLVRGY--NVMQG------------YLDDPEATAEAIDADGWLhT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 454 GDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALT 533
Cdd:cd17638 220 GDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTLTEEDVI 298
|
330
....*....|....*...
gi 1024336653 534 RELQEHVkrvtAPYKYPR 551
Cdd:cd17638 299 AWCRERL----ANYKVPR 312
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
222-552 |
1.92e-32 |
|
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: 127.76 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 222 RDPLAIYFTSGTTGAPKMVEHSQSSYGLG---FVASGRRWValTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHElp 298
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVpdiLQKEGLNWV--VGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 299 RVDAKVILNTLSKFPITTLCCVPTIFRLLVQE--DLTRYQfQSLRHCLTGGE-ALNPDVRE-KWKHQTGVELYegYGQSE 374
Cdd:cd17635 77 NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSElkSANATV-PSLRLIGYGGSrAIAADVRFiEATGLTNTAQV--YGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 375 TVVICANPKGMKIKS-GSMGKASPPYDVQIVDDEGNVLPPGEEGNVAvrIRPTRpfcFFNCYLDNPEKTAASEQGDFYIT 453
Cdd:cd17635 154 TGTALCLPTDDDSIEiNAVGRPYPGVDVYLAATDGIAGPSASFGTIW--IKSPA---NMLGYWNNPERTAEVLIDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 454 GDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLtpaySSHDPEALT 533
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA----SAELDENAI 304
|
330
....*....|....*....
gi 1024336653 534 RELQEHVKRVTAPYKYPRK 552
Cdd:cd17635 305 RALKHTIRRELEPYARPST 323
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
61-550 |
7.16e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 129.48 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 61 DVWSRL-EEAGHRPPNPAFwwvngTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTG 139
Cdd:PRK06164 11 TLASLLdAHARARPDAVAL-----IDEDRPLSRAELRALVDRLAAWLA-AQGVRRGDRVAVWLPNCIEWVVLFLACARLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 140 TVMIPGVTQLTEKDLKYRLQASRAKSIITSDS-----LAPRVDAIS-AECPSLQTKLLVSDSSR--PGWLNFR-----EL 206
Cdd:PRK06164 85 ATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAAVPpDALPPLRAIAVVDDAADatPAPAPGArvqlfAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 207 LREASTEHNCMRTKSRDPLAIYFT-SGTTGAPKMVEHSQS-----------SYGLGfvASGRRWVALTESDIFwnttdtG 274
Cdd:PRK06164 165 PDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQAtllrharaiarAYGYD--PGAVLLAALPFCGVF------G 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 275 WVKAAWTLFSAWPngscifVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCltGGEALNPDV 354
Cdd:PRK06164 237 FSTLLGALAGGAP------LVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF--GFASFAPAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 355 RE--KWKHQTGVELYEGYGQSETVVICA-----NPKGMKIKSGSMgKASPPYDVQIVD-DEGNVLPPGEEGNVAVRiRPT 426
Cdd:PRK06164 309 GElaALARARGVPLTGLYGSSEVQALVAlqpatDPVSVRIEGGGR-PASPEARVRARDpQDGALLPDGESGEIEIR-APS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 427 RpfcfFNCYLDNPEKTAASEQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSS 505
Cdd:PRK06164 387 L----MRGYLDNPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1024336653 506 pdPIRGE-VVKAFIVLTPAYSShDPEALTRELQEHVkrvtAPYKYP 550
Cdd:PRK06164 463 --TRDGKtVPVAFVIPTDGASP-DEAGLMAACREAL----AGFKVP 501
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
227-560 |
8.13e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 128.57 E-value: 8.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 IYFTSGTTGAPKmvehsqssyglGFVASgRRWVAltesdifwntTDTGWVKAAWtlfsAWpNGSCIFVHELP-------- 298
Cdd:PRK07787 133 IVYTSGTTGPPK-----------GVVLS-RRAIA----------ADLDALAEAW----QW-TADDVLVHGLPlfhvhglv 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 299 -------RVDAKVIlnTLSKF-----------PITTLCCVPTIF-RLLVQEDLTRyQFQSLRHCLTGGEALNPDVREKWK 359
Cdd:PRK07787 186 lgvlgplRIGNRFV--HTGRPtpeayaqalseGGTLYFGVPTVWsRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 360 HQTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEE--GNVAVRiRPTrpfcFFNCYLD 437
Cdd:PRK07787 263 ALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVR-GPT----LFDGYLN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 438 NPEKTAASEQGD-FYITGDRARMDKDGYFWFMGRND-DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK 515
Cdd:PRK07787 338 RPDATAAAFTADgWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIV 417
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1024336653 516 AFIVltpaysSHDPEALTrELQEHVKRVTAPYKYPRkncQRRFLE 560
Cdd:PRK07787 418 AYVV------GADDVAAD-ELIDFVAQQLSVHKRPR---EVRFVD 452
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
91-550 |
1.39e-31 |
|
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: 128.21 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd17655 24 TYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SLAPRVDAIsaecpslQTKLLVSDSsrpgwlNFRELlREASTEHNCmrtKSRDPLAIYFTSGTTGAPK--MVEHSQ-SSY 247
Cdd:cd17655 103 HLQPPIAFI-------GLIDLLDED------TIYHE-ESENLEPVS---KSDDLAYVIYTSGSTGKPKgvMIEHRGvVNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 248 GLGF----VASGRRWVALTESDIFwnttDTgwvkAAWTLFSAWPNGSCIFV--HElPRVDAKVILNTLSKFPITTLCCVP 321
Cdd:cd17655 166 VEWAnkviYQGEHLRVALFASISF----DA----SVTEIFASLLSGNTLYIvrKE-TVLDGQALTQYIRQNRITIIDLTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 322 TIFRLLVQEDLTryQFQSLRHCLTGGEALNPDVREKWKHQ--TGVELYEGYGQSETVVICA--NPKGMKIKSGS--MGKA 395
Cdd:cd17655 237 AHLKLLDAADDS--EGLSLKHLIVGGEALSTELAKKIIELfgTNPTITNAYGPTETTVDASiyQYEPETDQQVSvpIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 396 SPPYDVQIVDDEGNVLPPGEEGN-------VAvrirptrpfcffNCYLDNPEKTAAS------EQGD-FYITGDRARMDK 461
Cdd:cd17655 315 LGNTRIYILDQYGRPQPVGVAGElyiggegVA------------RGYLNRPELTAEKfvddpfVPGErMYRTGDLARWLP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 462 DGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVltpayssHDPEALTRELQEHVK 541
Cdd:cd17655 383 DGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIV-------SEKELPVAQLREFLA 455
|
....*....
gi 1024336653 542 RVTAPYKYP 550
Cdd:cd17655 456 RELPDYMIP 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
87-561 |
1.68e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 131.23 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 87 EIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSI 166
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALI-ARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 167 ITSDSLAPRV---DAISAecpslqtklLVSDSSRPgWLNFrellreasTEHNCMRTKSRDPLA-IYFTSGTTGAPKMVEH 242
Cdd:PRK12316 4653 LTQSHLLQRLpipDGLAS---------LALDRDED-WEGF--------PAHDPAVRLHPDNLAyVIYTSGSTGRPKGVAV 4714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 243 SQSSYGLGFVASGRRWvALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPT 322
Cdd:PRK12316 4715 SHGSLVNHLHATGERY-ELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPV 4793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 323 IFRLLVQEDLTRYQFQSLRHCLTGGEALNPD-VREKWKHQTGVELYEGYGQSETVVIC---ANPKGMKIKSGSM--GKAS 396
Cdd:PRK12316 4794 YLQQLAEHAERDGEPPSLRVYCFGGEAVAQAsYDLAWRALKPVYLFNGYGPTETTVTVllwKARDGDACGAAYMpiGTPL 4873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 397 PPYDVQIVDDEGNVLPPGEEGNVAVRIRptrpfCFFNCYLDNPEKTAA-------SEQGD-FYITGDRARMDKDGYFWFM 468
Cdd:PRK12316 4874 GNRSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAErfvpdpfGAPGGrLYRTGDLARYRADGVIDYL 4948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 469 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPE--ALTRELQEHVKRVTAP 546
Cdd:PRK12316 4949 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAqaELRDELKAALRERLPE 5028
|
490
....*....|....*
gi 1024336653 547 YKYPrknCQRRFLER 561
Cdd:PRK12316 5029 YMVP---AHLVFLAR 5040
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
90-551 |
2.17e-31 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 128.17 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 90 WSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 170 DSLAPRVDAIsaECPSLqtklLVSDSSRPGWLNFRELLREASTEHNCMRTK---SRDPLAIYFTSGTTGAPK--MVEHSQ 244
Cdd:PLN02330 135 DTNYGKVKGL--GLPVI----VLGEEKIEGAVNWKELLEAADRAGDTSDNEeilQTDLCALPFSSGTTGISKgvMLTHRN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 -------SSYGLGFVASGRRwVALTESDIFWNTTDTGwvkaawTLFSAWPNGSCIFVheLPRVDAKVILNTLSKFPITTL 317
Cdd:PLN02330 209 lvanlcsSLFSVGPEMIGQV-VTLGLIPFFHIYGITG------ICCATLRNKGKVVV--MSRFELRTFLNALITQEVSFA 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 318 CCVPTIFRLLVQE------DLTRYQFQSLrhcLTGGEALNPDVREKWKHQ-TGVELYEGYGQSETVVIC---ANP-KGMK 386
Cdd:PLN02330 280 PIVPPIILNLVKNpiveefDLSKLKLQAI---MTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITlthGDPeKGHG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 387 I-KSGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVRIRptrpfCFFNCYLDNPEKTAASEQGDFYI-TGDRARMDKDG 463
Cdd:PLN02330 357 IaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRTIDEDGWLhTGDIGYIDDDG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 464 YFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALtrelqEHVKRV 543
Cdd:PLN02330 432 DIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDIL-----NFVAAN 506
|
....*...
gi 1024336653 544 TAPYKYPR 551
Cdd:PLN02330 507 VAHYKKVR 514
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
227-550 |
3.16e-31 |
|
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: 126.33 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 IYfTSGTTGAPKMVEHSQSSYGLGFVASGRRWvALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPR-VDAKVI 305
Cdd:cd17649 100 IY-TSGSTGTPKGVAVSHGPLAAHCQATAERY-GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELwASADEL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 306 LNTLSKFPITTLCCVPTIFRLLVQE--DLTRYQFQSLRHCLTGGEALNPDVREKWKhQTGVELYEGYGQSETVV---ICA 380
Cdd:cd17649 178 AEMVRELGVTVLDLPPAYLQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEATVtplVWK 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 381 NPKGMKIKSGSM--GKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRptrpfCFFNCYLDNPEKTA--------ASEQGDF 450
Cdd:cd17649 257 CEAGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGELYIGGE-----GLARGYLGRPELTAerfvpdpfGAPGSRL 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 451 YITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLTPAysshDPE 530
Cdd:cd17649 332 YRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLRAA----AAQ 406
|
330 340
....*....|....*....|.
gi 1024336653 531 ALTRE-LQEHVKRVTAPYKYP 550
Cdd:cd17649 407 PELRAqLRTALRASLPDYMVP 427
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
111-563 |
3.37e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 127.99 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 111 GLQPGDRMMLVLPRlPEW---WLVSVACMrtGTVMIPgvtqltekdLKYRLQASRAKSII------------TSDSLAPR 175
Cdd:PLN02860 53 GLRNGDVVAIAALN-SDLyleWLLAVACA--GGIVAP---------LNYRWSFEEAKSAMllvrpvmlvtdeTCSSWYEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 176 VDaiSAECPSLQTKLLV---SDSSRPGWLNF---RELLREASTEHNCMRTKSRDPLA-IYFTSGTTGAPKMVEHSQSSY- 247
Cdd:PLN02860 121 LQ--NDRLPSLMWQVFLespSSSVFIFLNSFlttEMLKQRALGTTELDYAWAPDDAVlICFTSGTTGRPKGVTISHSALi 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 248 --GLGFVASgrrwVALTESDIFWNTT---DTGWVKAAWTLFSAwpnGSC-IFvheLPRVDAKVILNTLSKFPITTLCCVP 321
Cdd:PLN02860 199 vqSLAKIAI----VGYGEDDVYLHTAplcHIGGLSSALAMLMV---GAChVL---LPKFDAKAALQAIKQHNVTSMITVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 322 TIFRLLV---QEDLTRYQFQSLRHCLTGGEALNPD-VREKWKHQTGVELYEGYGQSET----------VVICANPK---- 383
Cdd:PLN02860 269 AMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRlLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhDPTLESPKqtlq 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 384 -GMKIKSGS--------MGKASPPYDVQIVDDEgnvlpPGEEGNVAvrirpTRPFCFFNCYLDNPEKTAASEQGDFYI-T 453
Cdd:PLN02860 349 tVNQTKSSSvhqpqgvcVGKPAPHVELKIGLDE-----SSRVGRIL-----TRGPHVMLGYWGQNSETASVLSNDGWLdT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 454 GDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEALT 533
Cdd:PLN02860 419 GDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKEN 498
|
490 500 510
....*....|....*....|....*....|
gi 1024336653 534 RELQEHVKRVTApykypRKNCQRRFLERSK 563
Cdd:PLN02860 499 AKKNLTLSSETL-----RHHCREKNLSRFK 523
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
223-551 |
3.91e-31 |
|
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: 126.27 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPK--MVEHSQSsygLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFV--HELP 298
Cdd:cd17643 94 DLAYVIYTSGSTGRPKgvVVSHANV---LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVvpYEVA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 299 RvDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQ-SLRHCLTGGEALNPDVREKWKHQTGV---ELYEGYGQSE 374
Cdd:cd17643 171 R-SPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 375 TVV----ICANPKGMKIKSGS-MGKASPPYDVQIVDDEGNVLPPGEEGNVAV-RIRPTRPfcffncYLDNPEKTA----- 443
Cdd:cd17643 250 TTVhvtfRPLDAADLPAAAASpIGRPLPGLRVYVLDADGRPVPPGVVGELYVsGAGVARG------YLGRPELTAerfva 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 444 --ASEQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVl 520
Cdd:cd17643 324 npFGGPGSrMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVV- 402
|
330 340 350
....*....|....*....|....*....|.
gi 1024336653 521 tpaySSHDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd17643 403 ----ADDGAAADIAELRALLKELLPDYMVPA 429
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
69-552 |
8.89e-31 |
|
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: 125.70 E-value: 8.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 69 AGHRPPNPAFWWVNGTGAEIKWSfEELGKQSRKAANVLggACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQ 148
Cdd:cd05923 10 AASRAPDACAIADPARGLRLTYS-ELRARIEAVAARLH--ARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 149 LTEKDLKYRLQASRAKSIITSDSlAPRVDAISaecpsLQTKLLVSDSSRPGwlnfrelLREASTEHNCMRTKSRDPLA-- 226
Cdd:cd05923 87 LKAAELAELIERGEMTAAVIAVD-AQVMDAIF-----QSGVRVLALSDLVG-------LGEPESAGPLIEDPPREPEQpa 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 -IYFTSGTTGAPK---------------MVEHSQSSYGlgfvaSGRRWVALTEsdiFWNTTDTGWVKAAWTLFsawpNGS 290
Cdd:cd05923 154 fVFYTSGTTGLPKgavipqraaesrvlfMSTQAGLRHG-----RHNVVLGLMP---LYHVIGFFAVLVAALAL----DGT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 291 CIFVHELPRVDAkviLNTLSKFPITTLCCVPTIFRLLV-QEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEG 369
Cdd:cd05923 222 YVVVEEFDPADA---LKLIEQERVTSLFATPTHLDALAaAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 370 YGQSETVVICANPKgmkIKSGSMGKASPPYDVQIVDDEGNV---LPPGEEGNVAVRIRPTRPFcffNCYLDNPEKTAASE 446
Cdd:cd05923 299 YGTTEAMNSLYMRD---ARTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 447 QGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAyss 526
Cdd:cd05923 373 QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG--- 449
|
490 500
....*....|....*....|....*...
gi 1024336653 527 hdpeALTRELQEHVKRVT--APYKYPRK 552
Cdd:cd05923 450 ----TLSADELDQFCRASelADFKRPRR 473
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
289-551 |
4.50e-30 |
|
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: 120.87 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 289 GSCIFVhelPRVDAKVILNTLSKFPIT-TLCCVPTIFRLLVQEDLTRYQFQSLRHCLT--GGEALNPDVREKWKHQTGve 365
Cdd:cd17636 67 GTNVFV---RRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPG-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 366 lyeGYGQSETV-VICANPKGMKIKsGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAA 444
Cdd:cd17636 142 ---GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEVNAR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 445 SEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPay 524
Cdd:cd17636 213 RTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKP-- 290
|
250 260
....*....|....*....|....*..
gi 1024336653 525 sshDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:cd17636 291 ---GASVTEAELIEHCRARIASYKKPK 314
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
82-545 |
1.54e-29 |
|
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: 122.19 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 82 NGTGAEIKWSfeELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQAS 161
Cdd:cd05932 1 GGQVVEFTWG--EVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 162 RAKSIITSdslapRVDAISAECPSLQTKLLVSDSSRPGWLNFRE----LLREASTEHNCMRTKSRDPLAIYFTSGTTGAP 237
Cdd:cd05932 78 ESKALFVG-----KLDDWKAMAPGVPEGLISISLPPPSAANCQYqwddLIAQHPPLEERPTRFPEQLATLIYTSGTTGQP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 238 KMVEHSQSSYGLGfVASGRRWVALTESD----------IFWNT-TDTGWVKAAWTLFsaWPNGSCIFVHEL--------- 297
Cdd:cd05932 153 KGVMLTFGSFAWA-AQAGIEHIGTEENDrmlsylplahVTERVfVEGGSLYGGVLVA--FAESLDTFVEDVqrarptlff 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 298 --PRVDAKVILNTLSKFP---ITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREkWKHQTGVELYEGYGQ 372
Cdd:cd05932 230 svPRLWTKFQQGVQDKIPqqkLNLLLKIPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNILEAYGM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 373 SETVVICANPKGMKIKSGSMGKASPPYDVQIvddegnvlppGEEGNVAVRIRPTrpfcfFNCYLDNPEKTAASEQGD-FY 451
Cdd:cd05932 309 TENFAYSHLNYPGRDKIGTVGNAGPGVEVRI----------SEDGEILVRSPAL-----MMGYYKDPEATAEAFTADgFL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 452 ITGDRARMDKDGYFWFMGRNDDVINSSSYR-IGPVEVESALAEHPAVLESAVVSS--PDPIRGEVVKAFIVLTPAYSshD 528
Cdd:cd05932 374 RTGDKGELDADGNLTITGRVKDIFKTSKGKyVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRADAF--A 451
|
490
....*....|....*..
gi 1024336653 529 PEALTRELQEHVKRVTA 545
Cdd:cd05932 452 RAELEASLRAHLARVNS 468
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
223-547 |
1.84e-29 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 121.88 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPK--MVEHSQssyglgFVASgrrwvALTESDIFWNTTDTGWVK-AAWT-------LFSAWPNGSCI 292
Cdd:cd05918 107 DAAYVIFTSGSTGKPKgvVIEHRA------LSTS-----ALAHGRALGLTSESRVLQfASYTfdvsileIFTTLAAGGCL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 293 FV-HELPRVD--AKVIlntlSKFPITTLCCVPTIFRLLVQEDLTryqfqSLRHCLTGGEALNPDVREKWKHqtGVELYEG 369
Cdd:cd05918 176 CIpSEEDRLNdlAGFI----NRLRVTWAFLTPSVARLLDPEDVP-----SLRTLVLGGEALTQSDVDTWAD--RVRLINA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 370 YGQSETVVIC-ANPKGMKIKSGSMGkasPPYDVQ--IVD--DEGNVLPPGEEG-------NVAvrirptrpfcffNCYLD 437
Cdd:cd05918 245 YGPAECTIAAtVSPVVPSTDPRNIG---RPLGATcwVVDpdNHDRLVPIGAVGelliegpILA------------RGYLN 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 438 NPEKTAAS--------------EQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 503
Cdd:cd05918 310 DPEKTAAAfiedpawlkqegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVV 389
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1024336653 504 SSPDPIRGEVVK---AFIVLTPAYS------------SHDPEALTRELQEHVKRVTAPY 547
Cdd:cd05918 390 EVVKPKDGSSSPqlvAFVVLDGSSSgsgdgdslflepSDEFRALVAELRSKLRQRLPSY 448
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-550 |
2.63e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 124.12 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 33 QKIVATWEAislgrqlvPEYFNFAHDVLDVWSRleEAGHRPPNPAFwwvngTGAEIKWSFEELGKQSRKAANVLGGAcGL 112
Cdd:PRK12467 496 ARELVRWNA--------PATEYAPDCVHQLIEA--QARQHPERPAL-----VFGEQVLSYAELNRQANRLAHVLIAA-GV 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 113 QPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDaisaecpslqtkllV 192
Cdd:PRK12467 560 GPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLP--------------V 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 193 SDSSRPGWLNFRELLREASTEHNCMRTKSRDPLA-IYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFWNTT 271
Cdd:PRK12467 626 PAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAyVIYTSGSTGQPKGVAISHGAL-ANYVCVIAERLQLAADDSMLMVS 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 272 DTGWVKAAWTLFSAWPNGSCifVHELPR---VDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRyQFQSLRHCLTGGE 348
Cdd:PRK12467 705 TFAFDLGVTELFGALASGAT--LHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVA-LPRPQRALVCGGE 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 349 ALNPDVREKWKH-QTGVELYEGYGQSETVVICA----NPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAV-- 421
Cdd:PRK12467 782 ALQVDLLARVRAlGPGARLINHYGPTETTVGVStyelSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIgg 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 422 ----RIRPTRPFCFFNCYLDNPEKTAAseqGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAV 497
Cdd:PRK12467 862 aglaRGYHRRPALTAERFVPDPFGADG---GRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1024336653 498 LESAVVSSPDPIRGEVVkAFIVLTPAYSSHDPEALTRELQEHVKRVTAPYKYP 550
Cdd:PRK12467 939 REAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVP 990
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
87-552 |
8.70e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 120.44 E-value: 8.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 87 EIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSI 166
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 167 ITSDSLAPRVDAISAECPSLqtKLLVSD--------SSRPGWLNFRELLREASTEHNCMRTKSR-DPLAIYFTSGTTGAP 237
Cdd:PRK08162 120 IVDTEFAEVAREALALLPGP--KPLVIDvddpeypgGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSGTTGNP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 238 K-MVEHSQSSY--GLGFVAS---GRRWVALTESDIF-WNttdtGWVkAAWTLFSAWPNGSCifvheLPRVDAKVILNTLS 310
Cdd:PRK08162 198 KgVVYHHRGAYlnALSNILAwgmPKHPVYLWTLPMFhCN----GWC-FPWTVAARAGTNVC-----LRKVDPKLIFDLIR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 311 KFPITTLCCVPTIFRLLVQ-EDLTRYQFQSLRHCLTGGEALNPDVREKWKhQTGVELYEGYGQSET---VVICANPKG-- 384
Cdd:PRK08162 268 EHGVTHYCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAKME-EIGFDLTHVYGLTETygpATVCAWQPEwd 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 385 ---MKIKSGSMGKASPPYDVQivdDEGNVLPP-------------GE---EGNVAVRirptrpfcffnCYLDNPEKTAAS 445
Cdd:PRK08162 347 alpLDERAQLKARQGVRYPLQ---EGVTVLDPdtmqpvpadgetiGEimfRGNIVMK-----------GYLKNPKATEEA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 446 EQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYS 525
Cdd:PRK08162 413 FAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGAS 492
|
490 500
....*....|....*....|....*..
gi 1024336653 526 shdpeALTRELQEHVKRVTAPYKYPRK 552
Cdd:PRK08162 493 -----ATEEEIIAHCREHLAGFKVPKA 514
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
91-549 |
2.76e-28 |
|
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: 117.41 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:cd17653 24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SlaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtkSRDPLAIYFTSGTTGAPK--MVEH------ 242
Cdd:cd17653 103 S-------------------------------------------------PDDLAYIIFTSGSTGIPKgvMVPHrgvlny 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 243 -SQSSYGLgFVASGRRwVALTESDIFWnttdtgwvKAAWTLFSAWPNGScIFVHELPRVDAKVILNTLSKFPITtlccvP 321
Cdd:cd17653 134 vSQPPARL-DVGPGSR-VAQVLSIAFD--------ACIGEIFSTLCNGG-TLVLADPSDPFAHVARTVDALMST-----P 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 322 TIFRLLVQEDltryqFQSLRHCLTGGEALNPDVREKWKHqtGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDV 401
Cdd:cd17653 198 SILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTC 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 402 QIVDDEGNVLPPGEEGNVAVR-IRPTRPfcffncYLDNPEKTAASEQGD-------FYITGDRARMDKDGYFWFMGRNDD 473
Cdd:cd17653 271 YILDADLQPVPEGVVGEICISgVQVARG------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGREDN 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1024336653 474 VINSSSYRIGPVEVESALAEHPAVLESAVVSSpdpIRGEVVkAFIvlTPAysSHDPEALTRELQEHVKRVTAPYKY 549
Cdd:cd17653 345 QVKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFV--TPE--TVDVDGLRSELAKHLPSYAVPDRI 412
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
86-520 |
3.81e-28 |
|
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: 118.40 E-value: 3.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 86 AEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKS 165
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALK-KYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 166 IITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLA--------IYFTSGTTGAP 237
Cdd:cd17642 120 VFCSKKGLQKVLNVQKKLKIIKTIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDFKPPSFdrdeqvalIMNSSGSTGLP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 238 KMVEHSQSSYGLGFvaSGRRwvalteSDIFWNTT--DTGWVKA-----AWTLFSAWPNGSCIF-VHELPRVDAKVILNTL 309
Cdd:cd17642 200 KGVQLTHKNIVARF--SHAR------DPIFGNQIipDTAILTVipfhhGFGMFTTLGYLICGFrVVLMYKFEEELFLRSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 310 SKFPITTLCCVPTIFRLLVQEDLT-RYQFQSLRHCLTGGEALNPDVREKWKHQTGVE-LYEGYGQSE-TVVICANPKGmK 386
Cdd:cd17642 272 QDYKVQSALLVPTLFAFFAKSTLVdKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTEtTSAILITPEG-D 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 387 IKSGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVRirptRPFcFFNCYLDNPEKTAASEQGDFYI-TGDRARMDKDGY 464
Cdd:cd17642 351 DKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK----GPM-IMKGYVNNPEATKALIDKDGWLhSGDIAYYDEDGH 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024336653 465 FWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 520
Cdd:cd17642 426 FFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL 481
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
66-522 |
3.84e-28 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 118.54 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 66 LEEAGHRPPNPAFwwVNG-TGAEikWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PLN02246 30 FERLSEFSDRPCL--IDGaTGRV--YTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 145 GVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPslqTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDP 224
Cdd:PLN02246 105 ANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDG---VTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 225 LAIYFTSGTTGAPK--MVEHSqssyglGFVASGRRWVALTESDIFWNTTDTgwVKAAWTLF----------SAWPNGSCI 292
Cdd:PLN02246 182 VALPYSSGTTGLPKgvMLTHK------GLVTSVAQQVDGENPNLYFHSDDV--ILCVLPMFhiyslnsvllCGLRVGAAI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 293 FVheLPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQED-LTRYQFQSLRHCLTG----GEALNPDVREKWKhqtGVELY 367
Cdd:PLN02246 254 LI--MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGaaplGKELEDAFRAKLP---NAVLG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 368 EGYGQSETVVICA-------NPkgMKIKSGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVR---IrptrpfcfFNCYL 436
Cdd:PLN02246 329 QGYGMTEAGPVLAmclafakEP--FPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRgpqI--------MKGYL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 437 DNPEKTAASEQGDFYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK 515
Cdd:PLN02246 399 NDPEATANTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPV 478
|
....*..
gi 1024336653 516 AFIVLTP 522
Cdd:PLN02246 479 AFVVRSN 485
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
5-503 |
1.19e-27 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 118.61 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 5 LRHLVLQALRNSRAFCGShgkpAPLPVPQKivatweaislgRQLVPEYFNFAHDVLDVW--SRLEEAGHRPPN-PAFwwv 81
Cdd:PRK10252 416 LKALIAQFAADPALLCGD----VDILLPGE-----------YAQLAQVNATAVEIPETTlsALVAQQAAKTPDaPAL--- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 82 ngTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQAS 161
Cdd:PRK10252 478 --ADARYQFSYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDA 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 162 RAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPgwlnfrellreastehnCMRTKSRDPLAIYFTSGTTGAPK--M 239
Cdd:PRK10252 555 RPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAP-----------------LQLSQPHHTAYIIFTSGSTGRPKgvM 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 240 VEHS---------QSSYGlgfvasgrrwvaLTESDIFWNTTDTGWVKAAWTLFsaWP--NGSCIFV-----HELPRVDAK 303
Cdd:PRK10252 618 VGQTaivnrllwmQNHYP------------LTADDVVLQKTPCSFDVSVWEFF--WPfiAGAKLVMaepeaHRDPLAMQQ 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 304 VIlntlSKFPITTLCCVPTIFRLLVQE---DLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVV-IC 379
Cdd:PRK10252 684 FF----AEYGVTTTHFVPSMLAAFVASltpEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdVS 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 380 ANPKG----MKIKSGSMGKASPPYDVQ--IVDDEGNVLPPGEEGNVAVR-IRPTRPfcffncYLDNPEKTA-------AS 445
Cdd:PRK10252 760 WYPAFgeelAAVRGSSVPIGYPVWNTGlrILDARMRPVPPGVAGDLYLTgIQLAQG------YLGRPDLTAsrfiadpFA 833
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1024336653 446 EQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVlESAVV 503
Cdd:PRK10252 834 PGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDV-EQAVT 890
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
91-552 |
1.27e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 117.25 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPR---LPEWWLVSVACMRTGTVMIPgVTQLTEkdlkyrlqaSRAKSII 167
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNsvyFPVIFLAVLSLGGIVTTMNP-SSSLGE---------IKKRVVD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 168 TSDSLAPRVDAISAECPSLQTK-LLVS-----DSSRPGWLNFRELLREASTEhnCMR--TKSRDPLAIYFTSGTTGAPKM 239
Cdd:PLN02574 138 CSVGLAFTSPENVEKLSPLGVPvIGVPenydfDSKRIEFPKFYELIKEDFDF--VPKpvIKQDDVAAIMYSSGTTGASKG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 240 VEHSQSSyglgFVASGRRWVALTESDIFWNTTDTGWVkAAWTLFSAW----------PNGSCIFVheLPRVDAKVILNTL 309
Cdd:PLN02574 216 VVLTHRN----LIAMVELFVRFEASQYEYPGSDNVYL-AALPMFHIYglslfvvgllSLGSTIVV--MRRFDASDMVKVI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 310 SKFPITTLCCVPTIFRLLVQ--EDLTRYQFQSLRHCLTGGEALN----PDVREKWKHqtgVELYEGYGQSETVVICA--- 380
Cdd:PLN02574 289 DRFKVTHFPVVPPILMALTKkaKGVCGEVLKSLKQVSCGAAPLSgkfiQDFVQTLPH---VDFIQGYGMTESTAVGTrgf 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 381 NPKGMKiKSGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYI-TGDRAR 458
Cdd:PLN02574 366 NTEKLS-KYSSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ-GPG----VMKGYLNNPKATQSTIDKDGWLrTGDIAY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 459 MDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAysshdpEALTRE-LQ 537
Cdd:PLN02574 440 FDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVI 513
|
490
....*....|....*
gi 1024336653 538 EHVKRVTAPYKYPRK 552
Cdd:PLN02574 514 NYVAKQVAPYKKVRK 528
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
223-552 |
3.22e-27 |
|
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: 112.11 E-value: 3.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPKMVEHSQSSYGLGFVAsgrrwvalTESDIFWNTTDTgwVKAAWTLFSAWPNGSCIF-------VH 295
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVC--------NEDLFNISGEDA--ILAPGPLSHSLFLYGAISalylggtFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 296 ELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLrhcLTGGEALNPDVREKWKHQT-GVELYEGYGQSE 374
Cdd:cd17633 71 GQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIEFYGTSE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 375 TVVICANPKGMKIKSGSMGKASPPYDVQIVDDEGnvlppGEEGNVAVRIRptrpfCFFNCYLDNPEktaaSEQGDFYITG 454
Cdd:cd17633 148 LSFITYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSE-----MVFSGYVRGGF----SNPDGWMSVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 455 DRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAysshDPEALTR 534
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKL----TYKQLKR 289
|
330
....*....|....*...
gi 1024336653 535 ELQEHVKRvtapYKYPRK 552
Cdd:cd17633 290 FLKQKLSR----YEIPKK 303
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
109-550 |
5.93e-27 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 114.98 E-value: 5.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 109 ACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITsDSLAP-RVDAISAECPSLQ 187
Cdd:PRK05852 62 RSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI-DADGPhDRAEPTTRWWPLT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 188 TKLLVSDSSRPGWLnfrELLREASTEHNCMRTKSR----DPLAIYFTSGTTGAPKMVEHSQ-----------SSYGLGfv 252
Cdd:PRK05852 141 VNVGGDSGPSGGTL---SVHLDAATEPTPATSTPEglrpDDAMIMFTGGTTGLPKMVPWTHaniassvraiiTGYRLS-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 253 aSGRRWVALTEsdiFWNttDTGWVKAawtLFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQ--- 329
Cdd:PRK05852 216 -PRDATVAVMP---LYH--GHGLIAA---LLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLEraa 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 330 EDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETV--VICANPKGM------KIKSGSMGKASPPyDV 401
Cdd:PRK05852 287 TEPSGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAThqVTTTQIEGIgqtenpVVSTGLVGRSTGA-QI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 402 QIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYR 481
Cdd:PRK05852 366 RIVGSDGLPLPAGAVGEVWLR-GTT----VVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEK 440
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024336653 482 IGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVltPAYSSHdPEAltRELQEHVKRVTAPYKYP 550
Cdd:PRK05852 441 ISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAP-PTA--EELVQFCRERLAAFEIP 504
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
219-538 |
2.52e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 114.64 E-value: 2.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 219 TKSRDPLAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFWNT---------TDTGWVKAAwtlfsawpNG 289
Cdd:PRK08633 779 FKPDDTATIIFSSGSEGEPKGVMLSHHNI-LSNIEQISDVFNLRNDDVILSSlpffhsfglTVTLWLPLL--------EG 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 290 -SCIFvHELPrVDAKVILNTLSKFPITTLCCVPTIFRLLVQED-LTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELY 367
Cdd:PRK08633 850 iKVVY-HPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKFGIRIL 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 368 EGYGQSETV-VICANPKGMKI---------KSGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVRiRPTRpfcfFNCYL 436
Cdd:PRK08633 928 EGYGATETSpVASVNLPDVLAadfkrqtgsKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-GPQV----MKGYL 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 437 DNPEKTAA----SEQGDFYITGDRARMDKDGYFWFMGRnddviNSSSYRIG----PV-EVESALAE--HPAVLESAVVSS 505
Cdd:PRK08633 1003 GDPEKTAEvikdIDGIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemvPLgAVEEELAKalGGEEVVFAVTAV 1077
|
330 340 350
....*....|....*....|....*....|...
gi 1024336653 506 PDPIRGEVVkafIVLTpAYSSHDPEALTRELQE 538
Cdd:PRK08633 1078 PDEKKGEKL---VVLH-TCGAEDVEELKRAIKE 1106
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
204-537 |
1.06e-25 |
|
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: 110.10 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 204 RELLREASTEHncMRTKSRDPLAIYFTSGTTGAPKMV--EHSQssyglgfVASGRRWVALTESDIFWN----TTDTGWVK 277
Cdd:cd12115 89 RFILEDAQARL--VLTDPDDLAYVIYTSGSTGRPKGVaiEHRN-------AAAFLQWAAAAFSAEELAgvlaSTSICFDL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 278 AAWTLFSAWPNGSCIFVHE-------LPRVDAKVILNTlskfpittlccVPTIFR-LLVQEDLTryqfQSLRHCLTGGEA 349
Cdd:cd12115 160 SVFELFGPLATGGKVVLADnvlalpdLPAAAEVTLINT-----------VPSAAAeLLRHDALP----ASVRVVNLAGEP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 350 LNPD-VREKWKHQTGVELYEGYGQSETVV---ICANPKGMKiKSGSMGKASPPYDVQIVDDEGNVLPPGEEGN------- 418
Cdd:cd12115 225 LPRDlVQRLYARLQVERVVNLYGPSEDTTystVAPVPPGAS-GEVSIGRPLANTQAYVLDRALQPVPLGVPGElyiggag 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 419 VAVrirptrpfcffnCYLDNPEKTAAS------EQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESAL 491
Cdd:cd12115 304 VAR------------GYLGRPGLTAERflpdpfGPGArLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAAL 371
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1024336653 492 AEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSShDPEALTRELQ 537
Cdd:cd12115 372 RSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG-LVEDLRRHLG 416
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
87-550 |
2.66e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 109.69 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 87 EIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGV-----TQLTEkdlkYRLQ-- 159
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALfshqrSELNA----YASQie 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 160 -----ASRAKSIITSDSlapRVDAISAECPSLQTKLLVSDssrPGWLNFRELLREASTEHNCMRTKSrDPLAIYFTSG-T 233
Cdd:PRK10946 121 palliADRQHALFSDDD---FLNTLVAEHSSLRVVLLLND---DGEHSLDDAINHPAEDFTATPSPA-DEVAFFQLSGgS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 234 TGAPKMVEHSQSSYglgfVASGRRWValtesDIFWNTTDTGWVKA-------------AWTLFSAwpnGSCifvhelprv 300
Cdd:PRK10946 194 TGTPKLIPRTHNDY----YYSVRRSV-----EICGFTPQTRYLCAlpaahnypmsspgALGVFLA---GGT--------- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 301 dakVILNT----LSKFP------ITTLCCVPTIFRLLVQ---EDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELY 367
Cdd:PRK10946 253 ---VVLAPdpsaTLCFPliekhqVNVTALVPPAVSLWLQaiaEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 368 EGYGQSETVV----------ICANPKGMKIksgsmgkaSPPYDVQIVDDEGNVLPPGEEGNVAVRIRPTrpfcfFNCYLD 437
Cdd:PRK10946 330 QVFGMAEGLVnytrlddsdeRIFTTQGRPM--------SPDDEVWVADADGNPLPQGEVGRLMTRGPYT-----FRGYYK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 438 NPEKTAAS--EQGdFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK 515
Cdd:PRK10946 397 SPQHNASAfdANG-FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSC 475
|
490 500 510
....*....|....*....|....*....|....*
gi 1024336653 516 AFIVLTPAYSshdPEALTRELQEhvkRVTAPYKYP 550
Cdd:PRK10946 476 AFLVVKEPLK---AVQLRRFLRE---QGIAEFKLP 504
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
117-552 |
4.29e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 108.71 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 117 RMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDaiSAECPSLQtkllvsdss 196
Cdd:PRK07638 52 TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLP--DEEGRVIE--------- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 197 rpgWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKmvehsqssyglGFVASGRRWV---ALTESDIFWNTTDT 273
Cdd:PRK07638 121 ---IDEWKRMIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPK-----------AFLRAQQSWLhsfDCNVHDFHMKREDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 274 gwVKAAWTLFSA---WPNGSCIF----VHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLrhcLTG 346
Cdd:PRK07638 187 --VLIAGTLVHSlflYGAISTLYvgqtVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKENRVIENKMKI---ISS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 347 GEALNPDVREKWKHQ-TGVELYEGYGQSETVVICA-NPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRir 424
Cdd:PRK07638 262 GAKWEAEAKEKIKNIfPYAKLYEFYGASELSFVTAlVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVK-- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 425 ptRPFcFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS 504
Cdd:PRK07638 340 --SPQ-FFMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIG 416
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1024336653 505 SPDPIRGEVVKAFIvltpaysshDPEALTRELQEHVKRVTAPYKYPRK 552
Cdd:PRK07638 417 VPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKE 455
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
89-538 |
4.63e-25 |
|
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: 108.03 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGGaCGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 -SDSLAprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksrdplAIYFTSGTTGAPK--MVEHSQS 245
Cdd:cd17645 102 nPDDLA----------------------------------------------------YVIYTSGSTGLPKgvMIEHHNL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 246 sygLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCifVHELP---RVDAkVILNTLSKFPITTLCCVPT 322
Cdd:cd17645 130 ---VNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAA--LHVVPserRLDL-DALNDYFNQEGITISFLPT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 323 ifrlLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKhqtgveLYEGYGQSE-TVVICANPKGMKIKSGSMGKASPPYDV 401
Cdd:cd17645 204 ----GAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYK------LVNNYGPTEnTVVATSFEIDKPYANIPIGKPIDNTRV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 402 QIVDDEGNVLPPGEEGNVAVRIRPtrpfcFFNCYLDNPEKTAASEQGD-------FYITGDRARMDKDGYFWFMGRNDDV 474
Cdd:cd17645 274 YILDEALQLQPIGVAGELCIAGEG-----LARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLGRLDQQ 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024336653 475 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVltpAYSSHDPEALTRELQE 538
Cdd:cd17645 349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT---APEEIPHEELREWLKN 409
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
100-552 |
4.66e-25 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 109.34 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 100 RKAANVLggACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAI 179
Cdd:PLN03102 51 RLAASLI--SLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 180 SAECPSLQTKL-----LVSDSSRPGWLNFRELLREA---------STEHNCMRTKSR-DPLAIYFTSGTTGAPKMVEHSQ 244
Cdd:PLN03102 129 LHLLSSEDSNLnlpviFIHEIDFPKRPSSEELDYECliqrgeptpSLVARMFRIQDEhDPISLNYTSGTTADPKGVVISH 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 SSYGLGFVASGRRWVALTESDIFWNTTD---TGWVkAAWTLFSAWPNGSCIfvhelPRVDAKVILNTLSKFPITTLCCVP 321
Cdd:PLN03102 209 RGAYLSTLSAIIGWEMGTCPVYLWTLPMfhcNGWT-FTWGTAARGGTSVCM-----RHVTAPEIYKNIEMHNVTHMCCVP 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 322 TIFRLLVQEDLTRYQFQSLR-HCLTGGEAlNPDVREKWKHQTGVELYEGYGQSET---VVIC---------ANPKGMKIK 388
Cdd:PLN03102 283 TVFNILLKGNSLDLSPRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCewqdewnrlPENQQMELK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 389 SGSMGKASPPYDVQIVDDEGNVLPPgEEGNVAVRIRpTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFWFM 468
Cdd:PLN03102 362 ARQGVSILGLADVDVKNKETQESVP-RDGKTMGEIV-IKGSSIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 469 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAYSSHDPEA---LTRE--LQEHVKRV 543
Cdd:PLN03102 440 DRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVdklVTRErdLIEYCREN 519
|
....*....
gi 1024336653 544 TAPYKYPRK 552
Cdd:PLN03102 520 LPHFMCPRK 528
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
86-550 |
1.46e-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: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 86 AEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP-GVTQLTEKdLKYRLQASRAK 164
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPvDIDQPAAR-REAILADAGAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 165 SIITSDSLAprvdaisAECPSLQTKLLVSDSSRPGWLNFRELLREAStehncmrtksrDPLAIYFTSGTTGAPK--MVEH 242
Cdd:cd12114 87 LVLTDGPDA-------QLDVAVFDVLILDLDALAAPAPPPPVDVAPD-----------DLAYVIFTSGSTGTPKgvMISH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 243 SQSS---------YGLGfvaSGRRWVALTE-------SDIFwnttdtgwvkaawTLFSAwpNGSCIFVHELPRVDAKVIL 306
Cdd:cd12114 149 RAALntildinrrFAVG---PDDRVLALSSlsfdlsvYDIF-------------GALSA--GATLVLPDEARRRDPAHWA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 307 NTLSKFPITTLCCVPTIFRLLVQED-LTRYQFQSLRHCLTGGE----ALNPDVREKWKHQTGVELyeGyGQSETVvICAN 381
Cdd:cd12114 211 ELIERHGVTLWNSVPALLEMLLDVLeAAQALLPSLRLVLLSGDwiplDLPARLRALAPDARLISL--G-GATEAS-IWSI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 382 --PkgmkIKSGSMGKASPPYDV-------QIVDDEGNVLPPGEEG-------NVAvrirptrpfcffNCYLDNPEKTAAS 445
Cdd:cd12114 287 yhP----IDEVPPDWRSIPYGRplanqryRVLDPRGRDCPDWVPGelwiggrGVA------------LGYLGDPELTAAR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 446 -----EQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVL 520
Cdd:cd12114 351 fvthpDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVP 429
|
490 500 510
....*....|....*....|....*....|
gi 1024336653 521 TPAYSSHDPEALTRELQEHVKRVTAPYKYP 550
Cdd:cd12114 430 DNDGTPIAPDALRAFLAQTLPAYMIPSRVI 459
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
91-525 |
2.17e-24 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 107.18 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWW--LVSVACMrtGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSLAPRVDAISAECPSLQTKLLVSDSS--------RPGW--LNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPK 238
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPSDadsaaahmPEGIkvYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 239 MVEHSQSSYGLgfvasgrRWVALTESDIFWNTTDTGWVKA-------AWTL-FSAWPNGSCIFvheLPRVD------AKV 304
Cdd:PRK05620 198 GVVYSHRSLYL-------QSLSLRTTDSLAVTHGESFLCCvpiyhvlSWGVpLAAFMSGTPLV---FPGPDlsaptlAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 305 ILNTLSKfpitTLCCVPTIF-RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVI--CAN 381
Cdd:PRK05620 268 IATAMPR----VAHGVPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVgtVAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 382 PkgmkiKSGSMGKASPPYDV-----------QIVDDeGNVLPPGE--EGNVAVRiRPTRPFCFFNCylDNPEKTAAS--- 445
Cdd:PRK05620 344 P-----PSGVSGEARWAYRVsqgrfpasleyRIVND-GQVMESTDrnEGEIQVR-GNWVTASYYHS--PTEEGGGAAstf 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 446 -----EQGD-------FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 513
Cdd:PRK05620 415 rgedvEDANdrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGER 494
|
490
....*....|..
gi 1024336653 514 VKAFIVLTPAYS 525
Cdd:PRK05620 495 PLAVTVLAPGIE 506
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
166-536 |
2.45e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 107.03 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 166 IITSDSLAPRVDAIsaECPSLQtkLLVSDSsrPGWlnfRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQS 245
Cdd:PRK13388 103 LVTDAEHRPLLDGL--DLPGVR--VLDVDT--PAY---AELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 246 SYG-LGFVASGRRwvALTESDIFWNTT---DTGWVKAAWTlfSAWPNGSCIFVHelPRVDAKVILNTLSKFPITTLCCV- 320
Cdd:PRK13388 174 RLAfAGRALTERF--GLTRDDVCYVSMplfHSNAVMAGWA--PAVASGAAVALP--AKFSASGFLDDVRRYGATYFNYVg 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 321 PTIFRLLVQEDLTRYQFQSLRHCLtGGEAlNPDVREKWKHQTGVELYEGYGQSETVVICANPKGMKikSGSMGKASPpyD 400
Cdd:PRK13388 248 KPLAYILATPERPDDADNPLRVAF-GNEA-SPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTP--PGSIGRGAP--G 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 401 VQIVDDE-------------GNVLPPGEegnvAV-RIRPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRARMDKDGYFW 466
Cdd:PRK13388 322 VAIYNPEtltecavarfdahGALLNADE----AIgELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIY 397
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 467 FMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTREL 536
Cdd:PRK13388 398 FAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAAFL 466
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
221-527 |
3.03e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 107.13 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 221 SRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASgrrWVALTESD---IFWNTTDTGWVKAAWTLFSAWPNGSCIFVHEL 297
Cdd:PTZ00237 253 SSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYY---WRSIIEKDiptVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 298 PRVDAKV----ILNTLSKFPITTLCCVPTIFRLLVQED------LTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELY 367
Cdd:PTZ00237 330 GIIKNKHieddLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSS 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 368 EGYGQSET-VVICANPKGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIrPTRPfCFFNCYLDNPE--KTAA 444
Cdd:PTZ00237 410 RGYGQTEIgITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPP-SFATTFYKNDEkfKQLF 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 445 SEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAY 524
Cdd:PTZ00237 488 SKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQ 567
|
...
gi 1024336653 525 SSH 527
Cdd:PTZ00237 568 SNQ 570
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
91-519 |
1.16e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 106.58 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:PRK12316 2030 SYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 SLAPRVdAISAECPSLqtkllvsDSSRPGWLnfrellREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLG 250
Cdd:PRK12316 2109 HLLERL-PLPAGVARL-------PLDRDAEW------ADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 251 FVASGRRWvALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQE 330
Cdd:PRK12316 2175 CQAAGERY-ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEH 2253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 331 DLTRYQFQSLRHCLTGGEALNPDVREKWKHQT-GVELYEGYGQSETVVI-----CANPKGMKIKSGSMGKASPPYDVQIV 404
Cdd:PRK12316 2254 AERDGRPPAVRVYCFGGEAVPAASLRLAWEALrPVYLFNGYGPTEAVVTpllwkCRPQDPCGAAYVPIGRALGNRRAYIL 2333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 405 DDEGNVLPPGEEGNVAVRIRptrpfCFFNCYLDNPEKTA--------ASEQGDFYITGDRARMDKDGYFWFMGRNDDVIN 476
Cdd:PRK12316 2334 DADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQVK 2408
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1024336653 477 SSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIV 519
Cdd:PRK12316 2409 IRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV 2450
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
91-550 |
1.20e-23 |
|
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: 103.87 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPgvtqltekdlkyrlqasraksiitsd 170
Cdd:cd17652 14 TYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLP-------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 slaprvdaISAECPSLQTKLLVSDSsRPGwlnfrellreastehnCMRTKSRDPLAIYFTSGTTGAPK--MVEHSqssyG 248
Cdd:cd17652 67 --------LDPAYPAERIAYMLADA-RPA----------------LLLTTPDNLAYVIYTSGSTGRPKgvVVTHR----G 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 249 L-GFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVhelprVDAKVIL------NTLSKFPITTLCCVP 321
Cdd:cd17652 118 LaNLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVL-----APAEELLpgeplaDLLREHRITHVTLPP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 322 TIFRLLVQEDLTryqfqSLRHCLTGGEALNPDVREKWKhqTGVELYEGYGQSETVViCANPKGMKIKSGS--MGKASPPY 399
Cdd:cd17652 193 AALAALPPDDLP-----DLRTLVVAGEACPAELVDRWA--PGRRMINAYGPTETTV-CATMAGPLPGGGVppIGRPVPGT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 400 DVQIVDDEGNVLPPGEEGNVAVR-IRPTRPfcffncYLDNPEKTA--------ASEQGDFYITGDRARMDKDGYFWFMGR 470
Cdd:cd17652 265 RVYVLDARLRPVPPGVPGELYIAgAGLARG------YLNRPGLTAerfvadpfGAPGSRMYRTGDLARWRADGQLEFLGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 471 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPaysshDPEALTRELQEHVKRVTAPYKYP 550
Cdd:cd17652 339 ADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVP 413
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
67-561 |
1.48e-23 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 106.40 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 67 EEAGHRPPNPAFwwvngTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGV 146
Cdd:PRK12467 1582 DQAAATPEAVAL-----VFGEQELTYGELNRRANRLAHRLI-ALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLD 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 147 TQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAecpslqTKLLVSDSSRpGWLnfrellrEASTEHNCMRTKSRDPLA 226
Cdd:PRK12467 1656 PEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDG------LRSLVLDQED-DWL-------EGYSDSNPAVNLAPQNLA 1721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 --IYfTSGTTGAPKMVEHSQSSYGLGFVASgRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFV--HELPRvDA 302
Cdd:PRK12467 1722 yvIY-TSGSTGRPKGAGNRHGALVNRLCAT-QEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIapPGAHR-DP 1798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 303 KVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTG-VELYEGYGQSETVV---- 377
Cdd:PRK12467 1799 EQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVdvth 1878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 378 -IC--ANPKGMkiKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAV------RirptrpfcffnCYLDNPEKTA----- 443
Cdd:PRK12467 1879 wTCrrKDLEGR--DSVPIGQPIANLSTYILDASLNPVPIGVAGELYLggvglaR-----------GYLNRPALTAerfva 1945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 444 ---ASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIVL 520
Cdd:PRK12467 1946 dpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVP 2024
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1024336653 521 TPA---YSSHDPEALTRELQEHVKRVTAPYKYPRkncQRRFLER 561
Cdd:PRK12467 2025 TDPglvDDDEAQVALRAILKNHLKASLPEYMVPA---HLVFLAR 2065
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
84-503 |
1.83e-23 |
|
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: 103.68 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 84 TGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:cd05914 2 YYGGEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 164 KSIITSDSlaprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksRDPLAIYFTSGTTGAPK--MVE 241
Cdd:cd05914 81 KAIFVSDE--------------------------------------------------DDVALINYTSGTTGNSKgvMLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 242 HSQSsygLGFVASGRRWVALTESDIFWNTTDTGWV-KAAWTLFSAWPNGSCI-FVHELPrvDAKVILNTLSKFPITTLCC 319
Cdd:cd05914 111 YRNI---VSNVDGVKEVVLLGKGDKILSILPLHHIyPLTFTLLLPLLNGAHVvFLDKIP--SAKIIALAFAQVTPTLGVP 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 320 VP------TIFRLLVQEDLTRYQF--------QSLRHCL----------------TGGEALNPDVrEKWKHQTGVELYEG 369
Cdd:cd05914 186 VPlviekiFKMDIIPKLTLKKFKFklakkinnRKIRKLAfkkvheafggnikefvIGGAKINPDV-EEFLRTIGFPYTIG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 370 YGQSETV-VICANPKGmKIKSGSMGKASPPYDVQIVDDEgnvlPPGEEGNVAVRIRptrpfcffNC---YLDNPEKTAA- 444
Cdd:cd05914 265 YGMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP--------NVmkgYYKNPEATAEa 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024336653 445 -SEQGDFYiTGDRARMDKDGYFWFMGRNDDVINSSSYR-IGPVEVESALAEHPAVLESAVV 503
Cdd:cd05914 332 fDKDGWFH-TGDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPFVLESLVV 391
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
66-552 |
4.42e-23 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 103.16 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 66 LEEAGHRPPNPAFWWVNGTGAeikWSFEEL-GKQSRKAANVLGGAcgLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIP 144
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGTSA---LRYRELvAEVGGLAADLRAQS--VSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 145 GVTQLTEKDLKYRLQASRAKSIITSDslAPRVDAIS-AECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNcmrTKSRD 223
Cdd:PRK05857 96 ADGNLPIAAIERFCQITDPAAALVAP--GSKMASSAvPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNAD---QGSED 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 224 PLAIYFTSGTTGAPKMVEHSQSSYglgFV------ASGRRWVALTESDIFWN---TTDTG--WvkaaWTLFSAWPNGSCI 292
Cdd:PRK05857 171 PLAMIFTSGTTGEPKAVLLANRTF---FAvpdilqKEGLNWVTWVVGETTYSplpATHIGglW----WILTCLMHGGLCV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 293 FVHElprvDAKVILNTLSKFPITTLCCVPTIFRLLVQE-DLTRYQFQSLRHCLTGG-EALNPDVRekWKHQTGVELYEGY 370
Cdd:PRK05857 244 TGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAADVR--FIEATGVRTAQVY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 371 GQSET--VVICA---NPKGMKIKSGSMGKASPPYDVQIVDDEG---NVLPPGEE---GNVAVRiRPTRPFCFFNcyldNP 439
Cdd:PRK05857 318 GLSETgcTALCLptdDGSIVKIEAGAVGRPYPGVDVYLAATDGigpTAPGAGPSasfGTLWIK-SPANMLGYWN----NP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 440 EKTAASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 519
Cdd:PRK05857 393 ERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVV 472
|
490 500 510
....*....|....*....|....*....|...
gi 1024336653 520 LTPAYSSHDPEALTRELQEHVKRVTAPYKYPRK 552
Cdd:PRK05857 473 ASAELDESAARALKHTIAARFRRESEPMARPST 505
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-561 |
1.25e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 103.50 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 86 AEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKS 165
Cdd:PRK12316 3079 GEQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQL 3157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 166 IITSDSLA-PRVDAISAECPSLQTkllvsdssrpgwlnfrellrEASTEHNCMRTKSRDPLA-IYFTSGTTGAPKMVEHS 243
Cdd:PRK12316 3158 LLSQSHLRlPLAQGVQVLDLDRGD--------------------ENYAEANPAIRTMPENLAyVIYTSGSTGKPKGVGIR 3217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 244 QSSYGLGFVASGRRWvALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRVDA-KVILNTLSKFPITTLCCVPT 322
Cdd:PRK12316 3218 HSALSNHLCWMQQAY-GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDpALLVELINSEGVDVLHAYPS 3296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 323 IFRLLVQEDLTRyQFQSLRHCLTGGEALNPDVREKWkhQTGVELYEGYGQSETVVICANPKGMKIKSGS--MGKASPPYD 400
Cdd:PRK12316 3297 MLQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRA 3373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 401 VQIVDDEGNVLPPGEEGNVAV------RIRPTRPFCFFNCYLDNPektaASEQGDFYITGDRARMDKDGYFWFMGRNDDV 474
Cdd:PRK12316 3374 CYILDGSLEPVPVGALGELYLggeglaRGYHNRPGLTAERFVPDP----FVPGERLYRTGDLARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 475 INSSSYRIGPVEVESALAEHPAVLESAVVSspdpIRGEVVKAFIVLTPAYSshdpeALTRELQEHVKRVTAPYKYPrknC 554
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDEAG-----DLREALKAHLKASLPEYMVP---A 3517
|
....*..
gi 1024336653 555 QRRFLER 561
Cdd:PRK12316 3518 HLLFLER 3524
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
227-550 |
2.61e-22 |
|
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: 100.20 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 IYFTSGTTGAPK--MVEH-SQSSYGLGFVASgrrwVALTESDIFWNTTDTGWVKAAWTLFSAWPNG-SCIFVHELPRVDA 302
Cdd:cd17644 111 VIYTSGSTGKPKgvMIEHqSLVNLSHGLIKE----YGITSSDRVLQFASIAFDVAAEEIYVTLLSGaTLVLRPEEMRSSL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 303 KVILNTLSKFPITTLCCVPTIFRLLVQEDL--TRYQFQSLRHCLTGGEALNPDVREKWKHQTG--VELYEGYGQSETVV- 377
Cdd:cd17644 187 EDFVQYIQQWQLTVLSLPPAYWHLLVLELLlsTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEATIa 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 378 -ICANPK---GMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAV-RIRPTRPfcffncYLDNPEKTA--------- 443
Cdd:cd17644 267 aTVCRLTqltERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIgGVGLARG------YLNRPELTAekfishpfn 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 444 ASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVltPA 523
Cdd:cd17644 341 SSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV--PH 418
|
330 340
....*....|....*....|....*..
gi 1024336653 524 YSShdpEALTRELQEHVKRVTAPYKYP 550
Cdd:cd17644 419 YEE---SPSTVELRQFLKAKLPDYMIP 442
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-561 |
2.94e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 102.34 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 33 QKIVATWEAislgrqlVPEYFNFAHDVLDVWSRLEEAGHRPPNPAFwwvngtgAEIKWSFEELGKQSRKAANVLGgACGL 112
Cdd:PRK12316 494 GQLVEGWNA-------TAAEYPLQRGVHRLFEEQVERTPEAPALAF-------GEETLDYAELNRRANRLAHALI-ERGV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 113 QPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAPRVDaisaecpsLQTKLLV 192
Cdd:PRK12316 559 GPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLP--------LAAGVQV 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 193 SDSSRPG-WLnfrellrEASTEHNCMRTKSRDPLA-IYFTSGTTGAPKMVEHSQSSyglgfVASGRRWV----ALTESDI 266
Cdd:PRK12316 631 LDLDRPAaWL-------EGYSEENPGTELNPENLAyVIYTSGSTGKPKGAGNRHRA-----LSNRLCWMqqayGLGVGDT 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 267 FWNTTDTGWVKAAWTLFSAWPNGSCIFV--HELPRVDAKVIlNTLSKFPITTLCCVPTIFRLLVQEDLTRyQFQSLRHCL 344
Cdd:PRK12316 699 VLQKTPFSFDVSVWEFFWPLMSGARLVVaaPGDHRDPAKLV-ELINREGVDTLHFVPSMLQAFLQDEDVA-SCTSLRRIV 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 345 TGGEALNPDVREKWKHQTGV-ELYEGYGQSETVVICANPKGMKiksgsMGKASPPYD-------VQIVDDEGNVLPPGEE 416
Cdd:PRK12316 777 CSGEALPADAQEQVFAKLPQaGLYNLYGPTEAAIDVTHWTCVE-----EGGDSVPIGrpianlaCYILDANLEPVPVGVL 851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 417 GNVAVRIRP-TRPfcffncYLDNPEKTA----ASEQGD---FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVE 488
Cdd:PRK12316 852 GELYLAGRGlARG------YHGRPGLTAerfvPSPFVAgerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIE 925
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024336653 489 SALAEHPAVLESAVVSspdpIRGEVVKAFIVLTpaysshDPEALTRE-LQEHVKRVTAPYKYPrknCQRRFLER 561
Cdd:PRK12316 926 ARLLEHPWVREAAVLA----VDGKQLVGYVVLE------SEGGDWREaLKAHLAASLPEYMVP---AQWLALER 986
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
91-539 |
3.96e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 100.36 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTG--TVMI-PGvtqLTEKDLKYRLQASRAKSII 167
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGavPVLVdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 168 T--SDSLAPRVDAISaeCPSLQTKLLVSDSSRPGWLNFRELLRE-ASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQ 244
Cdd:PRK09274 119 GipKAHLARRLFGWG--KPSVRRLVTVGGRLLWGGTTLATLLRDgAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 SSyglgFVASGRrwvALTES-DIFWNTTDTgwvkAAWTLFSAWP---NGSCIfvheLPRVD----AKV----ILNTLSKF 312
Cdd:PRK09274 197 GM----FEAQIE---ALREDyGIEPGEIDL----PTFPLFALFGpalGMTSV----IPDMDptrpATVdpakLFAAIERY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 313 PITTLCCVPTIFRLLVQEDLTR-YQFQSLRHCLTGGEALNPDVRE---KWKHQtGVELYEGYGQSE-------------- 374
Cdd:PRK09274 262 GVTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGAPVPIAVIErfrAMLPP-DAEILTPYGATEalpissiesreilf 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 375 -TVVICANPKGMKIksgsmGKASPPYDVQIVD---------DEGNVLPPGEEGNVAVRiRP--TRpfcffnCYLDNPEKT 442
Cdd:PRK09274 341 aTRAATDNGAGICV-----GRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA-GPmvTR------SYYNRPEAT 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 443 AAS----EQGDFY-ITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPirGEVVKAF 517
Cdd:PRK09274 409 RLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRPVL 486
|
490 500
....*....|....*....|..
gi 1024336653 518 IVLTPAYSSHDPEALTRELQEH 539
Cdd:PRK09274 487 CVELEPGVACSKSALYQELRAL 508
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
89-503 |
9.78e-22 |
|
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: 98.59 E-value: 9.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSII- 167
Cdd:cd17640 5 RITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 168 --TSDSLAprvdaisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksrdplAIYFTSGTTGAPK--MVEHS 243
Cdd:cd17640 84 enDSDDLA----------------------------------------------------TIIYTSGTTGNPKgvMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 244 QSSYGLGFVASGrrwVALTESDIF------WNTTDtgwvKAAWTLFSAWpNGSCIFVhelprvDAKVILNTLSKFPITTL 317
Cdd:cd17640 112 NLLHQIRSLSDI---VPPQPGDRFlsilpiWHSYE----RSAEYFIFAC-GCSQAYT------SIRTLKDDLKRVKPHYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 318 CCVPTIFRLL---VQEDLTRYQF------------QSLRHCLTGGEALNPDVrEKWKHQTGVELYEGYGQSETVVICANP 382
Cdd:cd17640 178 VSVPRLWESLysgIQKQVSKSSPikqflflfflsgGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETSPVVSAR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 383 KGMKIKSGSMGKASPPYDVQIVDDEGN-VLPPGEEGNVAVRIRPTrpfcfFNCYLDNPEKTAASEQGD-FYITGDRARMD 460
Cdd:cd17640 257 RLKCNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDgWFNTGDLGWLT 331
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1024336653 461 KDGYFWFMGRNDDVIN-SSSYRIGPVEVESALAEHPaVLESAVV 503
Cdd:cd17640 332 CGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSP-FIEQIMV 374
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
91-546 |
1.32e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 98.53 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGdRMMLVLPRLPEWWLVSV-ACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITS 169
Cdd:PRK13383 62 SYRELQRATESLARRLTRD-GVAPG-RAVGVMCRNGRGFVTAVfAVGLLGADVVPISTEFRSDALAAALRAHHISTVVAD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 170 DSLAPRVDAISaecpslqTKLLVSDSSrpgwlnfrellrEASTEHNCMRTKSRDPLAI-YFTSGTTGAPKMVEHS-QSSY 247
Cdd:PRK13383 140 NEFAERIAGAD-------DAVAVIDPA------------TAGAEESGGRPAVAAPGRIvLLTSGTTGKPKGVPRApQLRS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 248 GLGFvasgrrWVALTESdifwNTTDTG-WVKAAWTLFSAWPNGSCIFVHEL-------PRVDAKVILNTLSKFPITTLCC 319
Cdd:PRK13383 201 AVGV------WVTILDR----TRLRTGsRISVAMPMFHGLGLGMLMLTIALggtvlthRHFDAEAALAQASLHRADAFTA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 320 VPTIF-RLLVQEDLTRYQ--FQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSETVV-ICANPKGMKIKSGSMGKA 395
Cdd:PRK13383 271 VPVVLaRILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIgALATPADLRDAPETVGKP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 396 SPPYDVQIVDDEGNVLPPGEEGNVAV--RIRPTRpfcffncYLDNPEKTAASEQGDfyiTGDRARMDKDGYFWFMGRNDD 473
Cdd:PRK13383 351 VAGCPVRILDRNNRPVGPRVTGRIFVggELAGTR-------YTDGGGKAVVDGMTS---TGDMGYLDNAGRLFIVGREDD 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1024336653 474 VINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAySSHDPEALTRELQEHVKRVTAP 546
Cdd:PRK13383 421 MIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVDAAQLRDYLKDRVSRFEQP 492
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
65-507 |
1.95e-21 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 98.41 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 65 RLEEAGHR-PPNPAFwwvngTGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTV-- 141
Cdd:PRK08279 42 VFEEAAARhPDRPAL-----LFEDQSISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVva 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 142 MIPgvTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAIsAECPSLQTKLLVSDS----SRPGWLNFRELLREASTE--HN 215
Cdd:PRK08279 116 LLN--TQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEA-RADLARPPRLWVAGGdtldDPEGYEDLAAAAAGAPTTnpAS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 216 CMRTKSRDPlAIY-FTSGTTGAPKMVEHSQS---SYGLGFVASgrrwVALTESDIFWNTT----DTGWVkAAWTlfSAWP 287
Cdd:PRK08279 193 RSGVTAKDT-AFYiYTSGTTGLPKAAVMSHMrwlKAMGGFGGL----LRLTPDDVLYCCLplyhNTGGT-VAWS--SVLA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 288 NGSCIfvhelprvdakVILNTLS---------KFPITTLCCVPTIFRLLVQEDLTRYQFQ-SLRHCLtgGEALNPDVREK 357
Cdd:PRK08279 265 AGATL-----------ALRRKFSasrfwddvrRYRATAFQYIGELCRYLLNQPPKPTDRDhRLRLMI--GNGLRPDIWDE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 358 WKHQTGVE-LYEGYGQSETVVICANPKGmkiKSGSMGKaSPP----------YDVQ----IVDDEGNVLP--PGEEGNVA 420
Cdd:PRK08279 332 FQQRFGIPrILEFYAASEGNVGFINVFN---FDGTVGR-VPLwlahpyaivkYDVDtgepVRDADGRCIKvkPGEVGLLI 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 421 VRIRPTRPfcfFNCYLDnPEKTAAS------EQGDFYI-TGDRARMDKDGYFWFMGRNDDvinssSYR-----IGPVEVE 488
Cdd:PRK08279 408 GRITDRGP---FDGYTD-PEASEKKilrdvfKKGDAWFnTGDLMRDDGFGHAQFVDRLGD-----TFRwkgenVATTEVE 478
|
490 500
....*....|....*....|.
gi 1024336653 489 SALAEHPAVLESAV--VSSPD 507
Cdd:PRK08279 479 NALSGFPGVEEAVVygVEVPG 499
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
223-536 |
2.01e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 97.83 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPKMVEHSQssyglGFVASGRRWVA----LTESDIFWNTT---DTGWVKAAWTLfsAWPNGSCIFVH 295
Cdd:PRK07867 153 DLFMLIFTSGTSGDPKAVRCTH-----RKVASAGVMLAqrfgLGPDDVCYVSMplfHSNAVMAGWAV--ALAAGASIALR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 296 elPRVDAKVILNTLSKFPITTLCCV--PTIFrLLVQEDLTRYQFQSLRhCLTGGEALNPDVrEKWKHQTGVELYEGYGQS 373
Cdd:PRK07867 226 --RKFSASGFLPDVRRYGATYANYVgkPLSY-VLATPERPDDADNPLR-IVYGNEGAPGDI-ARFARRFGCVVVDGFGST 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 374 ET-VVICANPKGmkiKSGSMGKASPpyDVQIVD-DEGNVLPPGE-------EGNVAV--RIRPTRPfCFFNCYLDNPEKT 442
Cdd:PRK07867 301 EGgVAITRTPDT---PPGALGPLPP--GVAIVDpDTGTECPPAEdadgrllNADEAIgeLVNTAGP-GGFEGYYNDPEAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 443 AASEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTP 522
Cdd:PRK07867 375 AERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAP 454
|
330
....*....|....
gi 1024336653 523 AySSHDPEALTREL 536
Cdd:PRK07867 455 G-AKFDPDAFAEFL 467
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
223-551 |
6.50e-21 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 96.45 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 223 DPLAIYFTSGTTGAPK-MVEHSQSSYgLGFVASGRRWvALTESDIFWNTTD----TGWVkAAWTLFSAWPNGSCifvheL 297
Cdd:PLN02479 196 QSIALGYTSGTTASPKgVVLHHRGAY-LMALSNALIW-GMNEGAVYLWTLPmfhcNGWC-FTWTLAALCGTNIC-----L 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 298 PRVDAKVILNTLSKFPITTLCCVPTIFRLLVQ--EDLTRYQFQSLRHCLTGGEALNPDVREKWKHQtGVELYEGYGQSET 375
Cdd:PLN02479 268 RQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNapKSETILPLPRVVHVMTAGAAPPPSVLFAMSEK-GFRVTHTYGLSET 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 376 V---VICA-NPKGMKIKSGSMGKASPPYDVQIVDDEG-------NVLPPGEEGNVAVRIrPTRPFCFFNCYLDNPEKTAA 444
Cdd:PLN02479 347 YgpsTVCAwKPEWDSLPPEEQARLNARQGVRYIGLEGldvvdtkTMKPVPADGKTMGEI-VMRGNMVMKGYLKNPKANEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 445 SEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAY 524
Cdd:PLN02479 426 AFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGV 505
|
330 340
....*....|....*....|....*..
gi 1024336653 525 SSHDPEALTRELQEHVKRVTAPYKYPR 551
Cdd:PLN02479 506 DKSDEAALAEDIMKFCRERLPAYWVPK 532
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
55-544 |
4.52e-20 |
|
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: 93.89 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 55 FAHDVLDVWSRLEE----AGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPR----LP 126
Cdd:cd05906 1 PLHRPEGAPRTLLElllrAAERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDnedfIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 127 EWWlvsvACMRTGTVMIPgVTQLTEkdlkYRLQASRAKS------------IITSDSLAPRVDAISAECPSLQTKLLVSD 194
Cdd:cd05906 80 AFW----ACVLAGFVPAP-LTVPPT----YDEPNARLRKlrhiwqllgspvVLTDAELVAEFAGLETLSGLPGIRVLSIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 195 SsrpgwlnfrelLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSygLGFVASGRRWVA-LTESDIFWNttdt 273
Cdd:cd05906 151 E-----------LLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRN--ILARSAGKIQHNgLTPQDVFLN---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 274 gWVkaawtlfsawP---NGSCIFVHELP--------RVDAKVI-------LNTLSKFPIT-TLccVPTIFRLLVQEDLTR 334
Cdd:cd05906 214 -WV----------PldhVGGLVELHLRAvylgcqqvHVPTEEIladplrwLDLIDRYRVTiTW--APNFAFALLNDLLEE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 335 -----YQFQSLRHCLTGGEALNPdvrekwkhQTGVELYE--------------GYGQSETVVIC-------ANPKGMKIK 388
Cdd:cd05906 281 iedgtWDLSSLRYLVNAGEAVVA--------KTIRRLLRllepyglppdairpAFGMTETCSGViysrsfpTYDHSQALE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 389 SGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRptrpfCFFNCYLDNPEKTAASEQGD-FYITGDRARMDkDGYFWF 467
Cdd:cd05906 353 FVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP-----VVTKGYYNNPEANAEAFTEDgWFRTGDLGFLD-NGNLTI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 468 MGRNDDVINSSSYRIGPVEVESALAEHPAVLES--AVVSSPDPIRGEVVKAfIVLTPAYSSHDP-EALTRELQEHVKRVT 544
Cdd:cd05906 427 TGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVVSREV 505
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
46-503 |
6.45e-20 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 94.85 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 46 RQLVPEYFNfahdvldvwsrlEEAGHRPPNPAFWWVNGTgaeikWSFEELGKQSRKAANVLGGaCGLQPGDRMMLVLPRL 125
Cdd:PRK05691 1130 QAWLPELLN------------EQARQTPERIALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERS 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 126 PEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSL---APRVDAISAECpsLQTKLLVSDSSRPGWLN 202
Cdd:PRK05691 1192 PQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLlerLPQAEGVSAIA--LDSLHLDSWPSQAPGLH 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 203 FrellreastehncmrtkSRDPLA-IYFTSGTTGAPKMVEHSQSSyglgfVASGRRWV----ALTESDIFWNTTDTGWVK 277
Cdd:PRK05691 1270 L-----------------HGDNLAyVIYTSGSTGQPKGVGNTHAA-----LAERLQWMqatyALDDSDVLMQKAPISFDV 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 278 AAWTLFsaWP-NGSCIFVHELP--RVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRyQFQSLRHCLTGGEALNPDV 354
Cdd:PRK05691 1328 SVWECF--WPlITGCRLVLAGPgeHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA-ACTSLRRLFSGGEALPAEL 1404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 355 REKWKHQ-TGVELYEGYGQSETVV-----ICANPKGMKIKSGSmgkasPPYDV--QIVDDEGNVLPPGEEGNVAVR-IRP 425
Cdd:PRK05691 1405 RNRVLQRlPQVQLHNRYGPTETAInvthwQCQAEDGERSPIGR-----PLGNVlcRVLDAELNLLPPGVAGELCIGgAGL 1479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 426 TRPfcffncYLDNPEKTAA-------SEQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAV 497
Cdd:PRK05691 1480 ARG------YLGRPALTAErfvpdplGEDGArLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGV 1553
|
....*.
gi 1024336653 498 LESAVV 503
Cdd:PRK05691 1554 AQAAVL 1559
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
122-546 |
1.20e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 92.19 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 122 LPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLA------PRVDAISAECPSLQTKLLVSDS 195
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 196 S-----RPGWLNFRELLREASTEHnCMR--------TKSRDPLAIYFTSGTTGAPKMVEHSQSSyGLGFVASGRRWVALT 262
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQG-SVGgneyspvyAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 263 ESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHE---LPRVDAKVIlntlSKFPITTLCCVPTIFRLLVQ---EDLTRYQ 336
Cdd:PLN03051 159 PGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGgapLGRGFGKFV----QDAGVTVLGLVPSIVKAWRHtgaFAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 337 FQSLRHCLTGGEALNPD-------VREKWK----HQTGVELYEGYGQSETVVICAnpkgmkikSGSMGKASPPYDVQIVD 405
Cdd:PLN03051 235 WSKLRVFASTGEASAVDdvlwlssVRGYYKpvieYCGGTELASGYISSTLLQPQA--------PGAFSTASLGTRFVLLN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 406 DEGNVLPPGEE--GNVAVRIrptrPFCFFNCYLDNPEKTAASEQG-DFYIT--------GDRARMDKDGYFWFMGRNDDV 474
Cdd:PLN03051 307 DNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmPMYGSkgmplrrhGDIMKRTPGGYFCVQGRADDT 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 475 INSSSYRIGPVEVESALAE-HPAVLESAVVSSPDPIRGE----VVKAFIVLTPAYSSHDPEALTRELQEHVKRVTAP 546
Cdd:PLN03051 383 MNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNLNP 459
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
89-519 |
4.95e-19 |
|
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: 90.23 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:cd17656 13 KLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSLAprvDAISAEcpsLQTKLLVSDSSrpgwlnFRELLREASTEHNcmrtkSRDPLAIYFTSGTTGAPK--MVEHSQSs 246
Cdd:cd17656 92 QRHLK---SKLSFN---KSTILLEDPSI------SQEDTSNIDYINN-----SDDLLYIIYTSGTTGKPKgvQLEHKNM- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 247 ygLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIF-VHELPRVDAKVILNTLSKFPITTLCCVPTIFR 325
Cdd:cd17656 154 --VNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIEVVFLPVAFLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 326 LLVQE-DLTRYQFQSLRHCLTGGEAL---NPDVREKWKHQtgVELYEGYGQSETVVICA---NPKGMKIKSGSMGKASPP 398
Cdd:cd17656 232 FIFSErEFINRFPTCVKHIITAGEQLvitNEFKEMLHEHN--VHLHNHYGPSETHVVTTytiNPEAEIPELPPIGKPISN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 399 YDVQIVDDEGNVLPPGEEGNVAVR-IRPTRPfcffncYLDNPEKTAASEQGD-------FYITGDRARMDKDGYFWFMGR 470
Cdd:cd17656 310 TWIYILDQEQQLQPQGIVGELYISgASVARG------YLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1024336653 471 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 519
Cdd:cd17656 384 ADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV 432
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
91-512 |
1.00e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 89.43 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLV---LPRLPEWWLvsvACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSII 167
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWY---GIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 168 TSDSLAPRVDAISAECPSLQTKLLVSDSSR------PGWLNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVE 241
Cdd:PRK06018 117 TDLTFVPILEKIADKLPSVERYVVLTDAAHmpqttlKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 242 HSQSSYGL-GFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAwPNGSCIFVHELPRVDAKVILNTLSKFPITTLCCV 320
Cdd:PRK06018 197 YSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSA-PSMGTKLVMPGAKLDGASVYELLDTEKVTFTAGV 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 321 PTIFRLLVQE-DLTRYQFQSLRHCLTGGEALnPDVREKWKHQTGVELYEGYGQSETV---VICANPKGMKIKSGS----- 391
Cdd:PRK06018 276 PTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSplgTLAALKPPFSKLPGDarldv 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 392 -MGKASPPYDVQ--IVDDEGNVLP-PGEE-GNVAVRiRPTRPFCFFNCyldnpEKTAASEQGdFYITGDRARMDKDGYFW 466
Cdd:PRK06018 355 lQKQGYPPFGVEmkITDDAGKELPwDGKTfGRLKVR-GPAVAAAYYRV-----DGEILDDDG-FFDTGDVATIDAYGYMR 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1024336653 467 FMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGE 512
Cdd:PRK06018 428 ITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDE 473
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
158-550 |
1.03e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 91.00 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 158 LQASRAKSIITSdSLAPrVDAISAECPSLQTKLL--VSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLA-IYFTSGTT 234
Cdd:PRK05691 3804 LPAQRLQRIIEL-SRTP-VLVCSAACREQARALLdeLGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAyVIYTSGST 3881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 235 GAPK--MVEHSQSsygLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAWPNGScifvhelpRVDakVILNTLSKF 312
Cdd:PRK05691 3882 GLPKgvMVEQRGM---LNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGA--------RVE--IVPNAIAHD 3948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 313 P-----------ITTLCCVPTIFRLLVQEDltRYQFQSLRHCLTGGEALNPDVREKW-KHQTGVELYEGYGQSEtvviCA 380
Cdd:PRK05691 3949 PqgllahvqaqgITVLESVPSLIQGMLAED--RQALDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAE----CS 4022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 381 N-----PKGMKIKSGSMGKASPPYD---VQIVDDEGNVLPPGEEGNVAV------RirptrpfcffnCYLDNPEKTAAS- 445
Cdd:PRK05691 4023 DdvaffRVDLASTRGSYLPIGSPTDnnrLYLLDEALELVPLGAVGELCVagtgvgR-----------GYVGDPLRTALAf 4091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 446 ------EQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFi 518
Cdd:PRK05691 4092 vphpfgAPGErLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLVGY- 4169
|
410 420 430
....*....|....*....|....*....|..
gi 1024336653 519 vLTPAYSSHDPEALTRELQEHVKRVTAPYKYP 550
Cdd:PRK05691 4170 -LVPHQTVLAQGALLERIKQRLRAELPDYMVP 4200
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
486-552 |
3.04e-18 |
|
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: 79.13 E-value: 3.04e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 486 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPaysshDPEALTRELQEHVKRVTAPYKYPRK 552
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKE 62
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
84-542 |
5.12e-18 |
|
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: 87.10 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 84 TGAEIKWSFEELGKQSRKAANVLGGaCGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRA 163
Cdd:cd05915 19 TGEVHRTTYAEVYQRARRLMGGLRA-LGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 164 KSIITSDSLAprvdAISAECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSR-DPLAIYFTSGTTGAPKMVEH 242
Cdd:cd05915 98 KVLLFDPNLL----PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRVPErAACGMAYTTGTTGLPKGVVY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 243 SQSSYGLGFVASG-RRWVALTESDIFWNTTD----TGWVkAAWTLFSAwpNGSCIFVHELPrvDAKVILNTLSKFPITTL 317
Cdd:cd05915 174 SHRALVLHSLAASlVDGTALSEKDVVLPVVPmfhvNAWC-LPYAATLV--GAKQVLPGPRL--DPASLVELFDGEGVTFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 318 CCVPTIFRLLVQ-EDLTRYQFQSLRHCLTGGEAlNPDVREKWKHQTGVELYEGYGQSETVVI------------CANPKG 384
Cdd:cd05915 249 AGVPTVWLALADyLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETSPVvvqnfvkshlesLSEEEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 385 MKIKSGSmGKASPPYDVQIVDDEGNVLPpgEEGNVaVRIRPTRPFCFFNCYLDNPEKTAASE-QGDFYITGDRARMDKDG 463
Cdd:cd05915 328 LTLKAKT-GLPIPLVRLRVADEEGRPVP--KDGKA-LGEVQLKGPWITGGYYGNEEATRSALtPDGFFRTGDIAVWDEEG 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1024336653 464 YFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAysshdpEALTRELQEHVKR 542
Cdd:cd05915 404 YVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGE------KPTPEELNEHLLK 476
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-550 |
6.00e-18 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 88.29 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 86 AEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKS 165
Cdd:PRK12467 3117 GDQQLSYAELNRRANRLAHRLI-AIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKL 3195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 166 IITSDSLAPRVDAisaecPSLQTKLLVSDSSRPGWLnfrellreastEHNCMRTKSRDPLA-IYFTSGTTGAPKMVEHSQ 244
Cdd:PRK12467 3196 LLTQAHLLEQLPA-----PAGDTALTLDRLDLNGYS-----------ENNPSTRVMGENLAyVIYTSGSTGKPKGVGVRH 3259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 245 SSyglgfVASGRRWVA----LTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRVDAKVILNTLSKFPITTLCCV 320
Cdd:PRK12467 3260 GA-----LANHLCWIAeayeLDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFP 3334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 321 PTIFRLLVQeDLTRYQFQSLRHCLTGGEALNPDVREKWK-HQTGVELYEGYGQSETVVI-----CANPKGMKIKSGSMGK 394
Cdd:PRK12467 3335 PAYLQQFAE-DAGGADCASLDIYVFGGEAVPPAAFEQVKrKLKPRGLTNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGR 3413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 395 ASPPYDVQIVDDEGNVLPPGEEGNVAV------RIRPTRPFCFFNCYLDNPEKTAAseqGDFYITGDRARMDKDGYFWFM 468
Cdd:PRK12467 3414 PVAGRSIYVLDGQLNPVPVGVAGELYIggvglaRGYHQRPSLTAERFVADPFSGSG---GRLYRTGDLARYRADGVIEYL 3490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 469 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIVLtpayssHDP-EALTRELQEHVKRVTAPY 547
Cdd:PRK12467 3491 GRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP------ADPqGDWRETLRDHLAASLPDY 3563
|
...
gi 1024336653 548 KYP 550
Cdd:PRK12467 3564 MVP 3566
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
42-542 |
7.29e-18 |
|
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: 87.33 E-value: 7.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 42 ISLGRQLVPEYF-----NFAHDVLdvwsrleeAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGD 116
Cdd:cd05943 54 VSGRIMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALR-ALGVKPGD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 117 RMMLVLPRLPEwwlVSVACMRTGTV-----------MIPGVTQltekdlkyRLQASRAKSIITSDS---------LAPRV 176
Cdd:cd05943 125 RVAGYLPNIPE---AVVAMLATASIgaiwsscspdfGVPGVLD--------RFGQIEPKVLFAVDAytyngkrhdVREKV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 177 DAISAECPSLQTKLLVSDSSRPGWLNFRE----------LLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSS 246
Cdd:cd05943 194 AELVKGLPSLLAVVVVPYTVAAGQPDLSKiakaltledfLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHGAGG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 247 YGLGFVASGRRWVALTESD-IFWNTTdTGWVKAAWtLFSAWPNG-SCIFVHELP-RVDAKVILNTLSKFPITTLCCVPTI 323
Cdd:cd05943 274 TLLQHLKEHILHCDLRPGDrLFYYTT-CGWMMWNW-LVSGLAVGaTIVLYDGSPfYPDTNALWDLADEEGITVFGTSAKY 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 324 FRLLVQEDL---TRYQFQSLRHCLTGGEALNPD----VREKWKHqtGVELYEGYGQseTVVICANPKGMKIKSGSMGKAS 396
Cdd:cd05943 352 LDALEKAGLkpaETHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGG--TDIISCFVGGNPLLPVYRGEIQ 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 397 PPY---DVQIVDDEGNVLPpGEEGN-VAVRIRPTRPFCFFNcyldnpeKTAASEQGDFYIT--------GDRARMDKDGY 464
Cdd:cd05943 428 CRGlgmAVEAFDEEGKPVW-GEKGElVCTKPFPSMPVGFWN-------DPDGSRYRAAYFAkypgvwahGDWIEITPRGG 499
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024336653 465 FWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLTPAysshdpEALTRELQEHVKR 542
Cdd:cd05943 500 VVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELDDELRKRIRS 571
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
89-508 |
1.21e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 86.30 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGGAcGLQPGDR--------------------MMLVL----PRL-PEW--WLVSVAcmrtgtv 141
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAAL-GVEPGDRvgtlawngyrhleayygvsgSGAVChtinPRLfPEQiaYIVNHA------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 142 mipgvtqlTEKDLKYRLqasraksiitsdSLAPRVDAISAECPSLQTKLLVSDSSR-PG----WLNFRELLREASTEHNC 216
Cdd:PRK07008 111 --------EDRYVLFDL------------TFLPLVDALAPQCPNVKGWVAMTDAAHlPAgstpLLCYETLVGAQDGDYDW 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 217 MRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGL-GFVASGRRWVALTESDIFWNTTDTGWVKAaWTLFSAWPNGSCIFVH 295
Cdd:PRK07008 171 PRFDENQASSLCYTSGTTGNPKGALYSHRSTVLhAYGAALPDAMGLSARDAVLPVVPMFHVNA-WGLPYSAPLTGAKLVL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 296 ELPRVDAKVILNTLSKFPITTLCCVPTIFRLL---VQEDLTRyqFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQ 372
Cdd:PRK07008 250 PGPDLDGKSLYELIEAERVTFSAGVPTVWLGLlnhMREAGLR--FSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 373 SETV---VIC-------ANPKG--MKIKSgSMGKASPPYDVQIVDDEGNVLP-PGEE-GNVAVRirptRPFCffncyLDN 438
Cdd:PRK07008 328 TEMSplgTLCklkwkhsQLPLDeqRKLLE-KQGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR----GPWV-----IDR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1024336653 439 PEKTAASEQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDP 508
Cdd:PRK07008 398 YFRGDASPLVDgWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHP 468
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
91-551 |
1.02e-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: 83.11 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEW---WL------VSVACMRtgtvmipgvTQLTEKDLKYRLQAS 161
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLglaklgCPVAFLN---------TNIRSKSLLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 162 RAKSIITSDSLAPRVDAIsaeCPSLQTK-----LLVSDSSRPGWLNFRELLREASTE------HNCMRTKSrdpLAIY-F 229
Cdd:cd05938 78 GAKVLVVAPELQEAVEEV---LPALRADgvsvwYLSHTSNTEGVISLLDKVDAASDEpvpaslRAHVTIKS---PALYiY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 230 TSGTTGAPK--MVEHSQSSYGLGFV-ASGrrwvaLTESDIFWNTTdtgwvkaawTLFSAwpNGSCIFVHELPRVDAKVIL 306
Cdd:cd05938 152 TSGTTGLPKaaRISHLRVLQCSGFLsLCG-----VTADDVIYITL---------PLYHS--SGFLLGIGGCIELGATCVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 307 NtlSKFP------------ITTLCCVPTIFRLLVQedltryQFQSLRHC-----LTGGEALNPDVREKWKHQTG-VELYE 368
Cdd:cd05938 216 K--PKFSasqfwddcrkhnVTVIQYIGELLRYLCN------QPQSPNDRdhkvrLAIGNGLRADVWREFLRRFGpIRIRE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 369 GYGQSETVVICANPKGmkiKSGSMGKAS-------P----PYDVQ----IVDDEGNVLP--PGEEGNVAVRIRPTRPfcf 431
Cdd:cd05938 288 FYGSTEGNIGFFNYTG---KIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSP--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 432 FNCYLDNPEKTAAS------EQGDFYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV-- 502
Cdd:cd05938 362 FLGYAGDKEQTEKKllrdvfKKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVyg 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1024336653 503 VSSPDpIRGEVVKAFIVLTPaysshdPEALT-RELQEHVKRVTAPYKYPR 551
Cdd:cd05938 442 VTVPG-HEGRIGMAAVKLKP------GHEFDgKKLYQHVREYLPAYARPR 484
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
89-547 |
1.24e-16 |
|
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: 82.40 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIt 168
Cdd:cd05940 3 ALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 sdslaprVDAisaecpslqtkllvsdssrpgwlnfrellreastehncmrtksrdplAIY-FTSGTTGAPK--MVEHSQS 245
Cdd:cd05940 81 -------VDA-----------------------------------------------ALYiYTSGTTGLPKaaIISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 246 SYGLGFVASgrrWVALTESDIFWNTTdtgwvkaawTLFSAwpNGSCIFVHELPRVDAKVILNtlSKFPITTLC--CVP-- 321
Cdd:cd05940 107 WRGGAFFAG---SGGALPSDVLYTCL---------PLYHS--TALIVGWSACLASGATLVIR--KKFSASNFWddIRKyq 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 322 -TIFRLLvqEDLTRYQFQS------LRHCLTG--GEALNPDVREKWKHQTGV-ELYEGYGQSETVVICANPKGmkiKSGS 391
Cdd:cd05940 171 aTIFQYI--GELCRYLLNQppkpteRKHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINFFG---KPGA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 392 MGKASPP-----------YDVQ----IVDDEGNV--LPPGEEGNVAVRIRPTRPFcffNCYLDNPEKTA-----ASEQGD 449
Cdd:cd05940 246 IGRNPSLlrkvaplalvkYDLEsgepIRDAEGRCikVPRGEPGLLISRINPLEPF---DGYTDPAATEKkilrdVFKKGD 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 450 FYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV--VSSPDpIRGEVVKAFIVLTPAYsS 526
Cdd:cd05940 323 AWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQPNE-E 400
|
490 500
....*....|....*....|.
gi 1024336653 527 HDPEALTRELQEHVKRVTAPY 547
Cdd:cd05940 401 FDLSALAAHLEKNLPGYARPL 421
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
219-555 |
2.45e-16 |
|
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: 81.68 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 219 TKSRDPLAIYFTSGTTGAPK--MVEHsQSSYGLGFVASGRRWVALTESDifwnttdtgwvkaAWTLFSAWpngscIFVHE 296
Cdd:cd17648 91 TNSTDLAYAIYTSGTTGKPKgvLVEH-GSVVNLRTSLSERYFGRDNGDE-------------AVLFFSNY-----VFDFF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 297 LPR-VDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLT----------RYQFQSLRH--CLTG-GEALNPDVREKWKHQT 362
Cdd:cd17648 152 VEQmTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTylsgtpsvlqQYDLARLPHlkRVDAaGEEFTAPVFEKLRSRF 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 363 GVELYEGYGQSETVVICANP--KGMKIKSGSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRirptrPFCFFNCYLDNPE 440
Cdd:cd17648 232 AGLIINAYGPTETTVTNHKRffPGDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLG-----GDGVARGYLNRPE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 441 KTA--------ASEQ-------GDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSS 505
Cdd:cd17648 307 LTAerflpnpfQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAK 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1024336653 506 PDP-IRGEVVKAFIVltpAYSSHDPEALTR-ELQEHVKRVTAPYKYPRKNCQ 555
Cdd:cd17648 387 EDAsQAQSRIQKYLV---GYYLPEPGHVPEsDLLSFLRAKLPRYMVPARLVR 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
67-550 |
9.25e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 81.37 E-value: 9.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 67 EEAGHRPPNPAFwwvngTGAEIKWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGV 146
Cdd:PRK05691 2196 AQAARTPQAPAL-----TFAGQTLSYAELDARANRLARALRER-GVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLD 2269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 147 TQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAE--CPSLQTKLLVSDSSRPGWLNFRELLREAStehncmrtksrdp 224
Cdd:PRK05691 2270 PEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGvaRWCLEDDAAALAAYSDAPLPFLSLPQHQA------------- 2336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 225 LAIYfTSGTTGAPKMVEHSQSSYGLGFVASGRRWvALTESDIFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRVDAKV 304
Cdd:PRK05691 2337 YLIY-TSGSTGKPKGVVVSHGEIAMHCQAVIERF-GMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEE 2414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 305 ILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLRHCLTGGEALNPD----VREKWKHQtgvELYEGYGQSETVVI-- 378
Cdd:PRK05691 2415 ICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEhlqrIRQAFAPQ---LFFNAYGPTETVVMpl 2491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 379 -CANPKGMKIKSGS--MGKASPPYDVQIVDDEGNVLPPGEEGNVAV------RIRPTRPFCFFNCYLDNPektAASEQGD 449
Cdd:PRK05691 2492 aCLAPEQLEEGAASvpIGRVVGARVAYILDADLALVPQGATGELYVggaglaQGYHDRPGLTAERFVADP---FAADGGR 2568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 450 FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLEsAVVSSPDPIRGEVVKAFIVLTPAYSSHDP 529
Cdd:PRK05691 2569 LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAVAGQDDEA 2647
|
490 500
....*....|....*....|..
gi 1024336653 530 EALTRE-LQEHVKRVTAPYKYP 550
Cdd:PRK05691 2648 QAALREaLKAHLKQQLPDYMVP 2669
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
89-559 |
1.99e-15 |
|
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: 79.39 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIIT 168
Cdd:cd17641 11 EFTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSlaPRVD---AISAECPSLQtKLLVSDSS-----RPGWLNFRELLREASTEHN----------CMRTKSRDPLAIYFT 230
Cdd:cd17641 90 EDE--EQVDkllEIADRIPSVR-YVIYCDPRgmrkyDDPRLISFEDVVALGRALDrrdpglyereVAAGKGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 231 SGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFWNTTDTGWV-KAAWTLFSAWPNGSCI-FVHEL----------- 297
Cdd:cd17641 167 SGTTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIgEQMYSVGQALVCGFIVnFPEEPetmmedlreig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 298 -------PRV-------------DA------------KVILNTL-----SKFPITTLCCVPTIFRLLVQEDL-TRYQFQS 339
Cdd:cd17641 246 ptfvllpPRVwegiaadvrarmmDAtpfkrfmfelgmKLGLRALdrgkrGRPVSLWLRLASWLADALLFRPLrDRLGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 340 LRHCLTGGEALNPDVReKWKHQTGVELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVddegnvlppgEEGNV 419
Cdd:cd17641 326 LRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRID----------EVGEI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 420 AVRIRPTrpfcfFNCYLDNPEKTAASEQGD-FYITGDRARMDKDGYFWFMGRNDDVINSS-SYRIGPVEVESALAEHPAV 497
Cdd:cd17641 395 LVRSPGV-----FVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYI 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1024336653 498 LESAVVSSPDPIrgevVKAFIVLTP------------AYSSHDPEALTRE----LQEHVKRVTApyKYPRKNCQRRFL 559
Cdd:cd17641 470 AEAVVLGAGRPY----LTAFICIDYaivgkwaeqrgiAFTTYTDLASRPEvyelIRKEVEKVNA--SLPEAQRIRRFL 541
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
206-550 |
2.44e-15 |
|
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: 78.67 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 206 LLREASTEHNCMRTKSrdPLA-IYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFS 284
Cdd:cd17654 103 LSFTPEHRHFNIRTDE--CLAyVIHTSGTTGTPKIVAVPHKCI-LPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 285 AWPNGSCIFV--HELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQF---QSLRHCLTGGEALNPDVREK-W 358
Cdd:cd17654 180 SLSSGATLLIvpTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLsatSSLRVLALGGEPFPSLVILSsW 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 359 KHQ-TGVELYEGYGQSEtVVICANPKGMKIKSGSMGKASPPYD--VQIVDDEGNvlppGEEGNVAVRIRPTRpfCFFNCY 435
Cdd:cd17654 260 RGKgNRTRIFNIYGITE-VSCWALAYKVPEEDSPVQLGSPLLGtvIEVRDQNGS----EGTGQVFLGGLNRV--CILDDE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 436 LDNPEktaaseqGDFYITGDRARMdKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDpirgEVVK 515
Cdd:cd17654 333 VTVPK-------GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRLI 400
|
330 340 350
....*....|....*....|....*....|....*
gi 1024336653 516 AFIVltpaysshDPEALTRELQEHVKRVTAPYKYP 550
Cdd:cd17654 401 AFIV--------GESSSSRIHKELQLTLLSSHAIP 427
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
227-552 |
7.07e-15 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 77.24 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 227 IYFTSGTTGAPKMVEHSQSSYgLGFV---------ASGRRWVA-------LTESDIFWNTTDTGwvkaawTLFSawpngs 290
Cdd:PRK04813 148 IIFTSGTTGKPKGVQISHDNL-VSFTnwmledfalPEGPQFLNqapysfdLSVMDLYPTLASGG------TLVA------ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 291 cifvheLPRV---DAKVILNTLSKFPITTLCCVPTIFRL-LVQEDLTRYQFQSLRHCLTGGEALnpdvrekwKHQTGVEL 366
Cdd:PRK04813 215 ------LPKDmtaNFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCGEEL--------PHKTAKKL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 367 YE---------GYGQSETVV----------ICANPKGMKIksgsmGKASPPYDVQIVDDEGNVLPPGEEGNVAVrirpTR 427
Cdd:PRK04813 281 LErfpsatiynTYGPTEATVavtsieitdeMLDQYKRLPI-----GYAKPDSPLLIIDEEGTKLPDGEQGEIVI----SG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 428 PfCFFNCYLDNPEKTAA---SEQGD-FYITGDRARMDkDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVlESAVV 503
Cdd:PRK04813 352 P-SVSKGYLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYV-ESAVV 428
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1024336653 504 SspdPI-RGEVVK---AFIVLTPayssHDPE---ALTRELQEHVKRVTAPYKYPRK 552
Cdd:PRK04813 429 V---PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRK 477
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
224-550 |
1.20e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 76.23 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 224 PLAIYFTSGTTGAPKMVEHSQS-------SYGlgfvasgrrwVALTESDifwntTDTGWVKAAWT--------LFSAWPN 288
Cdd:PRK08308 103 PSLLQYSSGTTGEPKLIRRSWTeidreieAYN----------EALNCEQ-----DETPIVACPVThsyglicgVLAALTR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 289 GSCifVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQSLrhcLTGGeALNPD-----VREKWKHqtg 363
Cdd:PRK08308 168 GSK--PVIITNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGTFQFHAV---MTSG-TPLPEawfykLRERTTY--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 364 veLYEGYGQSET--VVICANPKgmkiKSGSMGKASPPYDVQIVDDEGNvlpPGEegnVAVRIrptrpfcffncyldnpek 441
Cdd:PRK08308 239 --MMQQYGCSEAgcVSICPDMK----SHLDLGNPLPHVSVSAGSDENA---PEE---IVVKM------------------ 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 442 taaseqGDFYI-TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfivl 520
Cdd:PRK08308 289 ------GDKEIfTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA---- 358
|
330 340 350
....*....|....*....|....*....|
gi 1024336653 521 tpAYSSHDPEAlTRELQEHVKRVTAPYKYP 550
Cdd:PRK08308 359 --KVISHEEID-PVQLREWCIQHLAPYQVP 385
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
219-539 |
9.77e-14 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 73.66 E-value: 9.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 219 TKSRDPLAIYFTSGTTGAPK--MVEHS---------QSSYGLGFVASGRRWVALTESDIFwnttdtgwvkAAWTLFSAWP 287
Cdd:cd17650 90 TQPEDLAYVIYTSGTTGKPKgvMVEHRnvahaahawRREYELDSFPVRLLQMASFSFDVF----------AGDFARSLLN 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 288 NGSCIFVHELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQE-DLTRYQFQSLRHCLTGGEAlnpdVREKWKhqtgVEL 366
Cdd:cd17650 160 GGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYvYRNGLDLSAMRLLIVGSDG----CKAQDF----KTL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 367 YEGYGQSeTVVIcaNPKGMK---IKSG---------------SMGKASPPYDVQIVDDEGNVLPPGEEGN-------VAv 421
Cdd:cd17650 232 AARFGQG-MRII--NSYGVTeatIDSTyyeegrdplgdsanvPIGRPLPNTAMYVLDERLQPQPVGVAGElyiggagVA- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 422 rirptrpfcffNCYLDNPEKTAA-------SEQGDFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEH 494
Cdd:cd17650 308 -----------RGYLNRPELTAErfvenpfAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARH 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1024336653 495 PAVLESAVVSSPDPiRGEV-VKAFIVltpaySSHDPEalTRELQEH 539
Cdd:cd17650 377 PAIDEAVVAVREDK-GGEArLCAYVV-----AAATLN--TAELRAF 414
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
91-503 |
2.34e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 72.49 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIpgvtqltekdlkyrlqasraksiitsd 170
Cdd:cd05910 4 SFRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPV--------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 slapRVDaisaecPSLQTKllvsdssrpgwlNFRELLREASTEHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYG-- 248
Cdd:cd05910 56 ----LID------PGMGRK------------NLKQCLQEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAaq 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 249 -------LGFVASGRRWVALTESDIFwnttdtgwvKAAWTLFSAWPNGScifvHELP-RVDAKVILNTLSKFPITTLCCV 320
Cdd:cd05910 114 idalrqlYGIRPGEVDLATFPLFALF---------GPALGLTSVIPDMD----PTRPaRADPQKLVGAIRQYGVSIVFGS 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 321 PTIFRLLvqedlTRY------QFQSLRHCLTGGEALNPDVREKWKH--QTGVELYEGYGQSETVVICA----------NP 382
Cdd:cd05910 181 PALLERV-----ARYcaqhgiTLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSSigsrellattTA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 383 KGMKIKSGSMGKASPPYDVQIV--DDEG-------NVLPPGEEGNVAVRIRPTRPfcffnCYLDNPEKTAASE-----QG 448
Cdd:cd05910 256 ATSGGAGTCVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTP-----TYVNRPVATALAKiddnsEG 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1024336653 449 DFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 503
Cdd:cd05910 331 FWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
91-542 |
7.14e-13 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 71.65 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 91 SFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSD 170
Cdd:PLN03052 210 TLSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQD 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 171 -----------------SLAPRVDAISAECPSLQTKLLVSDSSrpgWLNFRELL--REASTEHNCMRTKSRDPLAIYFTS 231
Cdd:PLN03052 289 vivrggksiplysrvveAKAPKAIVLPADGKSVRVKLREGDMS---WDDFLARAngLRRPDEYKAVEQPVEAFTNILFSS 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 232 GTTGAPKMVEHSQSSyglGFVASGRRWVAL--TESDIFWNTTDTGWVKAAWTLFSAWPNGSCI--------------FVH 295
Cdd:PLN03052 366 GTTGEPKAIPWTQLT---PLRAAADAWAHLdiRKGDIVCWPTNLGWMMGPWLVYASLLNGATLalyngsplgrgfakFVQ 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 296 elprvDAKVilntlskfpiTTLCCVPTIFRLLVQEDLTR-YQFQSLRHCLTGGEALNPD------VREKWK----HQTGV 364
Cdd:PLN03052 443 -----DAKV----------TMLGTVPSIVKTWKNTNCMAgLDWSSIRCFGSTGEASSVDdylwlmSRAGYKpiieYCGGT 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 365 ELYEGYGQSETVvicaNPKGMKIKSG-SMGkasppYDVQIVDDEGNVLPPgeegNVAvrirptrpfCFFNCYLDnPEKTA 443
Cdd:PLN03052 508 ELGGGFVTGSLL----QPQAFAAFSTpAMG-----CKLFILDDSGNPYPD----DAP---------CTGELALF-PLMFG 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 444 ASE------------QGDFYITGDRARMDKD-------GYFWFMGRNDDVINSSSYRIGPVEVESAL-AEHPAVLESAVV 503
Cdd:PLN03052 565 ASStllnadhykvyfKGMPVFNGKILRRHGDifertsgGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAI 644
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1024336653 504 SSPDPIRG--EVVKAFIVLTPAYSSHDPEALTRELQEHVKR 542
Cdd:PLN03052 645 GVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQK 685
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
320-552 |
1.70e-12 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 69.64 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 320 VPTIFRLLVQEDLTryQFQSLRHCLTGGEALNPDVREKWKHQtGVELYEGYGQSETVV-ICA-NPKGMKIKSGSMGKASP 397
Cdd:PRK07445 214 VPTQLQRLLQLRPQ--WLAQFRTILLGGAPAWPSLLEQARQL-QLRLAPTYGMTETASqIATlKPDDFLAGNNSSGQVLP 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 398 PYDVQIVddegnvlpPGEEGNVAVRIRPTrpfcFFNCYldnPEKTAASEqgdFYITGDRARMDKDGYFWFMGRNDDVINS 477
Cdd:PRK07445 291 HAQITIP--------ANQTGNITIQAQSL----ALGYY---PQILDSQG---IFETDDLGYLDAQGYLHILGRNSQKIIT 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1024336653 478 SSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVltPAYSSHDPEaltrELQEHVKRVTAPYKYPRK 552
Cdd:PRK07445 353 GGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV--PKDPSISLE----ELKTAIKDQLSPFKQPKH 421
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
230-544 |
1.76e-11 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 66.33 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 230 TSGTTGAPKMVEHSQS-------SYGLGFVASGrrwvaLTESDIFWNTTDTGWVKAAWTLFSAwpngscifvheLPRVDA 302
Cdd:COG1541 91 SSGTTGKPTVVGYTRKdldrwaeLFARSLRAAG-----VRPGDRVQNAFGYGLFTGGLGLHYG-----------AERLGA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 303 KVI----------LNTLSKFPITTLCCVPTIFRLLVQE------DLTRYqfqSLRHCLTGGEALNPDVREKWKHQTGVEL 366
Cdd:COG1541 155 TVIpagggnterqLRLMQDFGPTVLVGTPSYLLYLAEVaeeegiDPRDL---SLKKGIFGGEPWSEEMRKEIEERWGIKA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 367 YEGYGQSETVVICANP----KGMKIKSGSMgkasppYdVQIVDDE-GNVLPPGEEGNVAV---------RIRptrpfcff 432
Cdd:COG1541 232 YDIYGLTEVGPGVAYEceaqDGLHIWEDHF------L-VEIIDPEtGEPVPEGEEGELVVttltkeampLIR-------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 433 ncyldnpektaaseqgdfYITGDRA--------------RMDKdgyfwFMGRNDDVInssSYR---IGPVEVESALAEHP 495
Cdd:COG1541 297 ------------------YRTGDLTrllpepcpcgrthpRIGR-----ILGRADDML---IIRgvnVFPSQIEEVLLRIP 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1024336653 496 AVLESAVVSSPDPIRGEVVKAFIVLTPAYSshdPEALTRELQEHVKRVT 544
Cdd:COG1541 351 EVGPEYQIVVDREGGLDELTVRVELAPGAS---LEALAEAIAAALKAVL 396
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
89-503 |
6.15e-11 |
|
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: 64.75 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 89 KWSFEELGKQSRKAANVLGGAcGLQPGDRMMLVLPRLPEW---WLvsvacmrtGTVMIPGVTQLTEKDLK-----YRLQA 160
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFvalWL--------GLAKIGVETALINSNLRlesllHCITV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 161 SRAKSIITsDSLAPRVDAISAECPSLQTKllvsdssrpgwlNFRELLreastehncmrtksrdpLAIYfTSGTTGAPK-- 238
Cdd:cd05939 74 SKAKALIF-NLLDPLLTQSSTEPPSQDDV------------NFRDKL-----------------FYIY-TSGTTGLPKaa 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 239 MVEHSQ-------SSYGLGFvasgrrwvalTESDIFWNT-----TDTGWVKAAWTLFsawpNGSCIFVHElpRVDAKVIL 306
Cdd:cd05939 123 VIVHSRyyriaagAYYAFGM----------RPEDVVYDClplyhSAGGIMGVGQALL----HGSTVVIRK--KFSASNFW 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 307 NTLSKFPITTLCCVPTIFRLLVQEDLTRYQFQslrHC--LTGGEALNPDVREKWKHQTGV-ELYEGYGQSETVVICANPK 383
Cdd:cd05939 187 DDCVKYNCTIVQYIGEICRYLLAQPPSEEEQK---HNvrLAVGNGLRPQIWEQFVRRFGIpQIGEFYGATEGNSSLVNID 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 384 GmkiKSGSMGKAS--PP--YDVQIV-----------DDEGNVLP--PGEEGNVAVRIRPTRPFCFFNCYLD---NPEKTA 443
Cdd:cd05939 264 N---HVGACGFNSriLPsvYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNegaTNKKIA 340
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1024336653 444 AS--EQGD-FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALaeHPAV-LESAVV 503
Cdd:cd05939 341 RDvfKKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGIL--SNVLgLEDVVV 402
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
335-546 |
6.90e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.37 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 335 YQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSET--VVICANPkgMKIKSGSMGKASPPYDVQIVDDEGNvlp 412
Cdd:PRK06814 904 YDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapVIALNTP--MHNKAGTVGRLLPGIEYRLEPVPGI--- 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 413 pgEEGNvavRIRPTRPfcffNC---YL--DNPEKTAASEQGdFYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEV 487
Cdd:PRK06814 979 --DEGG---RLFVRGP----NVmlgYLraENPGVLEPPADG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAV 1048
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 488 ESALAEHPAVLESAVVSSPDPIRGEVVkafIVLTpaysshDPEALTRE-LQEHVKRVTAP 546
Cdd:PRK06814 1049 EELAAELWPDALHAAVSIPDARKGERI---ILLT------TASDATRAaFLAHAKAAGAS 1099
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
344-551 |
1.01e-10 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 63.53 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 344 LTGGEALNPDVREKWKhQTGVELYEGYGQSETVVICANPkgmkiksgsmGKASPPYDVQIVDdeGNVLPPGEegNVAVRI 423
Cdd:PRK07824 157 LVGGGPAPAPVLDAAA-AAGINVVRTYGMSETSGGCVYD----------GVPLDGVRVRVED--GRIALGGP--TLAKGY 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 424 RptrpfcffncyldNPEKTAASEQGDFYITGDRARMDkDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 503
Cdd:PRK07824 222 R-------------NPVDPDPFAEPGWFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1024336653 504 SSPDPIRGEVVKAFIVLTPAysshdPEALTRELQEHVKRVTAPYKYPR 551
Cdd:PRK07824 288 GLPDDRLGQRVVAAVVGDGG-----PAPTLEALRAHVARTLDRTAAPR 330
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
69-514 |
1.83e-10 |
|
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: 63.41 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 69 AGHRPPNPAFWWVN-GTGAEIKWSFEELgkqSRKAANVlggACGLQ----PGDRMMLVLPRLPEwwLVS--VACMRTGTV 141
Cdd:cd05931 3 AAARPDRPAYTFLDdEGGREETLTYAEL---DRRARAI---AARLQavgkPGDRVLLLAPPGLD--FVAafLGCLYAGAI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 142 MIPgVTQLTEKDLKYRLQA----SRAKSIITSDSLAPRVDAISAECPSLQTKLLVSDSSRPgwlnfrelLREASTEHNCM 217
Cdd:cd05931 75 AVP-LPPPTPGRHAERLAAiladAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLP--------DTSAADWPPPS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 218 rTKSRDPLAIYFTSGTTGAPK--MVEH---------SQSSYGLGFVASGRRWVALTEsdifwnttDTGWVKAawtLFSAW 286
Cdd:cd05931 146 -PDPDDIAYLQYTSGSTGTPKgvVVTHrnllanvrqIRRAYGLDPGDVVVSWLPLYH--------DMGLIGG---LLTPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 287 PNG-SCIFVHELPRVDAKVI-LNTLSKFPITT---------LCCvptifRLLVQEDLTRYQFQSLRHCLTGGEALNPDVR 355
Cdd:cd05931 214 YSGgPSVLMSPAAFLRRPLRwLRLISRYRATIsaapnfaydLCV-----RRVRDEDLEGLDLSSWRVALNGAEPVRPATL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 356 EKW---------KHQTgveLYEGYGQSETVVICANPKG----------MKIKSG----------------SMGKASPPYD 400
Cdd:cd05931 289 RRFaeafapfgfRPEA---FRPSYGLAEATLFVSGGPPgtgpvvlrvdRDALAGravavaaddpaarelvSCGRPLPDQE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 401 VQIVDDEGN-VLPPGEEGNVAVRIRPTRPfcffnCYLDNPEKTAASEQ-------GDFYITGDRARMdKDGYFWFMGRND 472
Cdd:cd05931 366 VRIVDPETGrELPDGEVGEIWVRGPSVAS-----GYWGRPEATAETFGalaatdeGGWLRTGDLGFL-HDGELYITGRLK 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1024336653 473 DVINSSSYRIGPVEVESALAEHPAVLES---AVVSSPDPIRGEVV 514
Cdd:cd05931 440 DLIIVRGRNHYPQDIEATAEEAHPALRPgcvAAFSVPDDGEERLV 484
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
54-276 |
2.77e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 59.81 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 54 NFAHDVLdvwsrleeAGHRPPNPAFWWVNGTGAEIKWSFEELGKQSRKAANVLGgACGLQPGDRMMLVLPRLPEWWLVSV 133
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNIPETVVAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 134 ACMRTGTVM--------IPGVTQltekdlkyRLQASRAKSIITSD---------SLAPRVDAISAECPSLQTKLLVS--- 193
Cdd:PRK03584 158 ATASLGAIWsscspdfgVQGVLD--------RFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLEHVVVVPylg 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 194 ----DSSRPGWLNFRELLREAST-EHNCMRTKSRDPLAIYFTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESD-IF 267
Cdd:PRK03584 230 paaaAAALPGALLWEDFLAPAEAaELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHCDLGPGDrFF 309
|
....*....
gi 1024336653 268 WNTTdTGWV 276
Cdd:PRK03584 310 WYTT-CGWM 317
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
93-494 |
1.94e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 57.13 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 93 EELGKQS----RKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGT--VMIPGVTQLTEkdLKYRLQASRAKSI 166
Cdd:PRK06334 41 EQLGKLSynqvRKAVIALATKVSKYPDQHIGIMMPASAGAYIAYFATLLSGKipVMINWSQGLRE--VTACANLVGVTHV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 167 ITSDSLAPRVDAISAECPSLQTKLLVSDSSRPGwLNFRELLREA---STEHNCM-------RTKSRDPLAIYFTSGTTGA 236
Cdd:PRK06334 119 LTSKQLMQHLAQTHGEDAEYPFSLIYMEEVRKE-LSFWEKCRIGiymSIPFEWLmrwfgvsDKDPEDVAVILFTSGTEKL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 237 PKMVEHSQSSyglgFVASGRRWVAltesdiFWNTTDTGWVKAAWTLFSAWPNGSCIFVHELPRV---------DAKVILN 307
Cdd:PRK06334 198 PKGVPLTHAN----LLANQRACLK------FFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVpvvfaynplYPKKIVE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 308 TLSKFPITTLCCVPTIFR-LLVQEDLTRYQFQSLRHCLTGGEALNPDVREK-WKHQTGVELYEGYGQSE-TVVICANPKG 384
Cdd:PRK06334 268 MIDEAKVTFLGSTPVFFDyILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEaLKTFPHIQLRQGYGTTEcSPVITINTVN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 385 MKIKSGSMGKASPPYDVQIVDDEGNV-LPPGEEGNVAvrirpTRPFCFFNCYLDNPEKTAASEQG--DFYITGDRARMDK 461
Cdd:PRK06334 348 SPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVL-----TRGTSLFSGYLGEDFGQGFVELGgeTWYVTGDLGYVDR 422
|
410 420 430
....*....|....*....|....*....|...
gi 1024336653 462 DGYFWFMGRNDDVINSSSYRIGPVEVESALAEH 494
Cdd:PRK06334 423 HGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
126-463 |
4.79e-08 |
|
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: 55.68 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 126 PEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSIITSDSLAprvdaisaecpslqtklLVSdssrpgWLNFRE 205
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAGVK-----------------VYS------LEEFEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 206 LLREASTEHNcmrTKSRDPLA-IYFTSGTTGAPKMVEHSQSSyglgFVASGRRWVALTESDIFWNTTDTgwvkaawtLFS 284
Cdd:cd05927 100 LGKKNKVPPP---PPKPEDLAtICYTSGTTGNPKGVMLTHGN----IVSNVAGVFKILEILNKINPTDV--------YIS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 285 AWP---------------NGSCIFVHelpRVDAKVILNTLSKFPITTLCCVPTIF-RLL------VQED--LTR------ 334
Cdd:cd05927 165 YLPlahifervvealflyHGAKIGFY---SGDIRLLLDDIKALKPTVFPGVPRVLnRIYdkifnkVQAKgpLKRklfnfa 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 335 --YQFQSLRH---------------------------CLTGGEALNPDVREKWKHQTGVELYEGYGQSETVVICA--NPK 383
Cdd:cd05927 242 lnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATltLPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 384 GMKIksGSMGKASPPYDVQIVD-DEGNVLPPGEEGNVAVRIRPTrpfCFFNCYLDNPEKTA-ASEQGDFYITGDRARMDK 461
Cdd:cd05927 322 DTSV--GHVGGPLPCAEVKLVDvPEMNYDAKDPNPRGEVCIRGP---NVFSGYYKDPEKTAeALDEDGWLHTGDIGEWLP 396
|
..
gi 1024336653 462 DG 463
Cdd:cd05927 397 NG 398
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
220-546 |
5.41e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 55.87 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 220 KSRDPLAIYFTSGTTGAPKMVEHSQSSYgLGFVASGRRWVALTESDIFwnttdtgwvKAAWTLFSAW--------P--NG 289
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRF---------MSALPLFHSFgltvglftPllTG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 290 SCIFVHELP---RVDAKVIL--NTLSKFPITTLCCVPTIFRllvqedlTRYQFQSLRHCLTGGEALNPDVREKWKHQTGV 364
Cdd:PRK08043 433 AEVFLYPSPlhyRIVPELVYdrNCTVLFGTSTFLGNYARFA-------NPYDFARLRYVVAGAEKLQESTKQLWQDKFGL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 365 ELYEGYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVDdegnvLPPGEEGNvavRIRPTRPfCFFNCYL--DNPEK- 441
Cdd:PRK08043 506 RILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLLS-----VPGIEQGG---RLQLKGP-NIMNGYLrvEKPGVl 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 442 ---TAASEQGD----FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVES-ALAEHPAVLESAVVSSpDPIRGEv 513
Cdd:PRK08043 577 evpTAENARGEmergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKS-DASKGE- 654
|
330 340 350
....*....|....*....|....*....|....
gi 1024336653 514 vkAFIVLTPaysshDPEaLTRE-LQEHVKRVTAP 546
Cdd:PRK08043 655 --ALVLFTT-----DSE-LTREkLQQYAREHGVP 680
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
229-535 |
2.05e-07 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 53.97 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 229 FTSGTTGAPKMVEHSQSSYGLGFVASGRRWVALTESD------IFWNTTDTGWVKAAWTLFsawpNGSCIFVHE---LPR 299
Cdd:cd05921 172 FTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPpvlvdwLPWNHTFGGNHNFNLVLY----NGGTLYIDDgkpMPG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 300 VDAKVILNtLSKFPITTLCCVPTIFRLLVQ-----EDLTRYQFQSLRHCLTGGEALNPDVREKWK----HQTG--VELYE 368
Cdd:cd05921 248 GFEETLRN-LREISPTVYFNVPAGWEMLVAalekdEALRRRFFKRLKLMFYAGAGLSQDVWDRLQalavATVGerIPMMA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 369 GYGQSETVVICANPKGMKIKSGSMGKASPPYDVQIVddegnvlPPGeeGNVAVRIR-PTrpfcFFNCYLDNPEKTAAS-- 445
Cdd:cd05921 327 GLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV-------PSG--GKYEVRVKgPN----VTPGYWRQPELTAQAfd 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 446 EQGdFYITGDRARM----DKDGYFWFMGR--NDDVINSSSY-RIGPVEVESALAEHPAVLEsAVVSSPDpirGEVVKAFI 518
Cdd:cd05921 394 EEG-FYCLGDAAKLadpdDPAKGLVFDGRvaEDFKLASGTWvSVGPLRARAVAACAPLVHD-AVVAGED---RAEVGALV 468
|
330 340
....*....|....*....|....*
gi 1024336653 519 V--------LTPAYSSHDPEALTRE 535
Cdd:cd05921 469 FpdllacrrLVGLQEASDAEVLRHA 493
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
337-493 |
2.46e-07 |
|
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: 53.52 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 337 FQSLRHCLTGGEALNPDVREKWKhQTGVELYEGYGQSETV---VICaNPKGMKIksGSMGKASPPYDVQIV--DDEGNvl 411
Cdd:cd05933 319 LDRCQKFFTGAAPISRETLEFFL-SLNIPIMELYGMSETSgphTIS-NPQAYRL--LSCGKALPGCKTKIHnpDADGI-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 412 ppgeeGNVAVRIRPTrpfcfFNCYLDNPEKTAASEQGDFYI-TGDRARMDKDGYFWFMGRNDD-VINSSSYRIGPVEVES 489
Cdd:cd05933 393 -----GEICFWGRHV-----FMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIED 462
|
....
gi 1024336653 490 ALAE 493
Cdd:cd05933 463 AVKK 466
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
90-551 |
3.64e-07 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 52.82 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 90 WSFEELGKQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQASRAKSII-T 168
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIvD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 169 SDSLA-----------PRVDAISaecpslQTKLLVSDSSRPGWLNfrelLREASTEHNCMrtksrdPLaIYFTSGTTGAP 237
Cdd:cd05937 86 PDDPAiliytsgttglPKAAAIS------WRRTLVTSNLLSHDLN----LKNGDRTYTCM------PL-YHGTAAFLGAC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 238 KMVeHSQSSYGLGFVASGRRwvaltesdiFWNttdtgwvkaawtlfSAWPNGSCIFVHelprvdakvilntlskfpITTL 317
Cdd:cd05937 149 NCL-MSGGTLALSRKFSASQ---------FWK--------------DVRDSGATIIQY------------------VGEL 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 318 CcvptifRLLVQEDLTRYQFQSLRHCLTGgEALNPDVREKWKHQTGV-ELYEGYGQSETVVICANPKGMKIKSGSMGKAS 396
Cdd:cd05937 187 C------RYLLSTPPSPYDRDHKVRVAWG-NGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 397 P----------------PYDVQIVDDEGN----VLPPGEEGNVAVRIRPtRPFCFFNCYLDNPEKTAAS------EQGD- 449
Cdd:cd05937 260 LirrwkfenqvvlvkmdPETDDPIRDPKTgfcvRAPVGEPGEMLGRVPF-KNREAFQGYLHNEDATESKlvrdvfRKGDi 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 450 FYITGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDP-IRGEVVKAFIVLTPaySSHD 528
Cdd:cd05937 339 YFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEE--SSAV 416
|
490 500
....*....|....*....|....
gi 1024336653 529 PEALTRELQEHVKRVTAP-YKYPR 551
Cdd:cd05937 417 PTEFTKSLLASLARKNLPsYAVPL 440
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
325-545 |
4.72e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 52.69 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 325 RLLVQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTG------VELYEGYGQSET---VVICANPKGMKIKS------ 389
Cdd:PRK07768 263 RLRRQAKPGAFDLSSLRFALNGAEPIDPADVEDLLDAGArfglrpEAILPAYGMAEAtlaVSFSPCGAGLVVDEvdadll 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 390 -----------------GSMGKASPPYDVQIVDDEGNVLPPGEEGNVAVRIRPTRPFcffncYLDNPEKTAASEQGDFYI 452
Cdd:PRK07768 343 aalrravpatkgntrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG-----YLTMDGFIPAQDADGWLD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 453 TGDRARMDKDGYFWFMGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVLTPAYSSHDPEAL 532
Cdd:PRK07768 418 TGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAEV 496
|
250
....*....|...
gi 1024336653 533 TRELQEHVKRVTA 545
Cdd:PRK07768 497 RRIRHQVAHEVVA 509
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
230-417 |
1.14e-05 |
|
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: 48.00 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 230 TSGTTGAPKMVEHSQS--SYGLGFVASGRRWVALTESDIFWNTTDTGWVKAAWTLFSAwpngscifvheLPRVDAKVI-- 305
Cdd:cd05913 86 SSGTTGKPTVVGYTKNdlDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYG-----------AERLGALVIpa 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 306 --------LNTLSKFPITTLCCVPTIFRLL---VQEDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGVELYEGYGQSE 374
Cdd:cd05913 155 gggnterqLQLIKDFGPTVLCCTPSYALYLaeeAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTE 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1024336653 375 tvVI-------CANPKGMKIksgsmgkASPPYDVQIVDDE-GNVLPPGEEG 417
Cdd:cd05913 235 --IIgpgvafeCEEKDGLHI-------WEDHFIPEIIDPEtGEPVPPGEVG 276
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
220-540 |
2.16e-05 |
|
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: 47.10 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 220 KSRDPLA-IYFTSGTTGAPK--MVEHSQSSYGLGFVASGRRWvalTESDIF--WN--TTDTGWvkAAWTLFSAWPNGSCI 292
Cdd:cd05908 103 ELADELAfIQFSSGSTGDPKgvMLTHENLVHNMFAILNSTEW---KTKDRIlsWMplTHDMGL--IAFHLAPLIAGMNQY 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 293 FVH-ELPRVDAKVILNTLSKFPITTLCCVPTIFRLLVQ----EDLTRYQFQSLRHCLTGGEALNPDVREKWKHQTGV--- 364
Cdd:cd05908 178 LMPtRLFIRRPILWLKKASEHKATIVSSPNFGYKYFLKtlkpEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKygl 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 365 ---ELYEGYGQSE-TVVICANPKG--------------------MKIKSG-------SMGKASPPYDVQIVDDEGNVLPP 413
Cdd:cd05908 258 krnAILPVYGLAEaSVGASLPKAQspfktitlgrrhvthgepepEVDKKDsecltfvEVGKPIDETDIRICDEDNKILPD 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 414 GEEGNVAVRIRPTRPfcffnCYLDNPEKTAA--SEQGdFYITGDRARMdKDGYFWFMGRNDDVINSSSYRIGPVEVESAL 491
Cdd:cd05908 338 GYIGHIQIRGKNVTP-----GYYNNPEATAKvfTDDG-WLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIA 410
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1024336653 492 AEHPAVLESAVVS---SPDPIRGEVVKAFIVltPAYSSHDPEALTRELQEHV 540
Cdd:cd05908 411 EELEGVELGRVVAcgvNNSNTRNEEIFCFIE--HRKSEDDFYPLGKKIKKHL 460
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
393-544 |
3.84e-04 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 43.46 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 393 GKASPPYDVQIVDDEGNVLPPGEEGNVAVRiRPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRARMdKDGYFWFMGRND 472
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GPS----LMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1024336653 473 DVINSSSYRIGPVEVESALAEHPAVL--ESAVVSSPDPIRGEVVkafiVLTPAYSShDPE---ALTRELQEHVKRVT 544
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV----LLVQCRIS-DEErrgQLIHALAALVRSEF 533
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
81-242 |
6.44e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.78 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 81 VNGTGAEIKW-SFEELGkQSRKAANVLGGACGLQPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVTQLTEKDLKYRLQ 159
Cdd:PLN02736 69 VDGTVGEYKWmTYGEAG-TARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 160 ASRAKSIITSDSLAPRVDAISAECPSLqtKLLV----SDSSRPGW--------LNFRELLREA-STEHNCMRTKSRDPLA 226
Cdd:PLN02736 148 HAEVAAIFCVPQTLNTLLSCLSEIPSV--RLIVvvggADEPLPSLpsgtgveiVTYSKLLAQGrSSPQPFRPPKPEDVAT 225
|
170
....*....|....*...
gi 1024336653 227 IYFTSGTTGAPK--MVEH 242
Cdd:PLN02736 226 ICYTSGTTGTPKgvVLTH 243
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
69-248 |
1.49e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 41.69 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 69 AGHRPPNPAFWWVNGTGAE-IKWSFEELGKQSRKAANVLGGACGlqPGDRMMLVLPRLPEWWLVSVACMRTGTVMIPGVT 147
Cdd:PRK05691 19 AAQTPDRLALRFLADDPGEgVVLSYRDLDLRARTIAAALQARAS--FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 148 QLTEKdlkyRLQASRAKSIItsDSLAPR-VDAISAECPSLQTKLLVSDSSRPGWLNFRELLREASTEHNCMRTKSRDPLA 226
Cdd:PRK05691 97 PESAR----RHHQERLLSII--ADAEPRlLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQPDDIAF 170
|
170 180
....*....|....*....|..
gi 1024336653 227 IYFTSGTTGAPKMVehsQSSYG 248
Cdd:PRK05691 171 LQYTSGSTALPKGV---QVSHG 189
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
111-257 |
5.97e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 39.57 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 111 GLQPGDRMMLVLPRLPEWwLVSV-AC----MRTGTVMipgvTQLTEKDLKYRLQASRAKSIITSDSLAPRVDAISAECPS 185
Cdd:PTZ00216 142 GLTKGSNVAIYEETRWEW-LASIyGIwsqsMVAATVY----ANLGEDALAYALRETECKAIVCNGKNVPNLLRLMKSGGM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1024336653 186 LQTKLLVSDSSRPG----------WLNFRELLREASTEHNCMRTKSRDPLA-IYFTSGTTGAPKMVEHSQSSYGLGFVAS 254
Cdd:PTZ00216 217 PNTTIIYLDSLPASvdtegcrlvaWTDVVAKGHSAGSHHPLNIPENNDDLAlIMYTSGTTGDPKGVMHTHGSLTAGILAL 296
|
...
gi 1024336653 255 GRR 257
Cdd:PTZ00216 297 EDR 299
|
|
| |
