|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
48-576 |
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: 1019.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 48 VPEYFNFAHDVLDVWSQLEKTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEW 127
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 128 WLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFRELLR 207
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 208 VASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWA 286
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 287 NGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIH 366
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 367 EGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFCLFNCYLDNPEKTAASEQ 446
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 447 GDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSH 526
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 88196780 527 DPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:cd05928 481 DPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKEW 530
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
48-578 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 577.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 48 VPEYFNFAHDVLDVWsqLEKTGHRPpnpAFWWVNGSGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEW 127
Cdd:COG0365 4 VGGRLNIAYNCLDRH--AEGRGDKV---ALIWEGEDGEERTLTYAELRREVNRFANALR-ALGVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 128 WLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDA---------LAPHVDAISADCPSLQSRLLV----SDT 194
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 195 SRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGW 274
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 275 VKAAW-TLFSAWANGACVFVHELPQV--DAQTILNTLCRFPITTICCVPTLFRLLVQED---LTRYKFQCLRHCLAGGEA 348
Cdd:COG0365 238 ATGHSyIVYGPLLNGATVVLYEGRPDfpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 349 LNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptRP 427
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK----GP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 428 F-CLFNCYLDNPEKTAASEQGDF---YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS 503
Cdd:COG0365 394 WpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196780 504 SPDPIRGEVVKAFIVLSPAYVshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 578
Cdd:COG0365 474 VPDEIRGQVVKAFVVLKPGVE--PSDELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGR 546
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
89-572 |
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: 568.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 89 WTFEELGKQSRKAANILEGaCGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITS 168
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 169 DalaphvdaisadcpslqsrllvSDTSrpgwinfrellrvaspehnclrtrsgdsmAIYFTSGTTGTPKMVEHSQcSYGL 248
Cdd:cd05972 80 A----------------------EDPA-----------------------------LIYFTSGTTGLPKGVLHTH-SYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 249 GFVASGRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLV 327
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 328 QEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEG 407
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 408 NVLPPGKEGNIAIRIKPTRpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVE 487
Cdd:cd05972 268 RELPPGEEGDIAIKLPPPG---LFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 488 SALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvsHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGY--EPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*
gi 88196780 568 RSKLR 572
Cdd:cd05972 423 RVELR 427
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
48-575 |
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: 553.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 48 VPEYFNFAHDVLDVWSQLEktghrPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEW 127
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEY-----PDKLALVWCDDAGEERIFTFAELADYSDKTANFFK-AMGIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 128 WLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIIT--SDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFREL 205
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 206 LRVASPE----HNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQcSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAW-T 280
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDF-TYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 281 LFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQ 360
Cdd:cd05970 245 IYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 361 TGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFCLFNCYLDNPEK 440
Cdd:cd05970 325 TGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 441 TAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLS 520
Cdd:cd05970 405 TAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLA 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 88196780 521 PAYVShdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:cd05970 485 KGYEP--SEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
76-577 |
1.95e-130 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 393.11 E-value: 1.95e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 76 AFWWVnGSGTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKY 155
Cdd:PRK04319 62 ALRYL-DASRKEKYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 156 RLQAARVKSIITSDALAPHVdaISADCPSLQSRLLVSDTSR--PGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTT 233
Cdd:PRK04319 140 RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGST 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 234 GTPK--------MVEHSQcsyglgfvaSGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHElPQVDAQTI 304
Cdd:PRK04319 218 GKPKgvlhvhnaMLQHYQ---------TGKYVLDLHEDDVYWCTADPGWVTGtSYGIFAPWLNGATNVIDG-GRFSPERW 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 305 LNTLCRFPITTICCVPTLFRLLV---QEDLTRYKFQCLRHCLAGGEALNSDVRdKW-KNQTGLEIHEGYGQSET--VLIC 378
Cdd:PRK04319 288 YRILEDYKVTVWYTAPTAIRMLMgagDDLVKKYDLSSLRHILSVGEPLNPEVV-RWgMKVFGLPIHDNWWMTETggIMIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 379 gNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIriKPTRPfCLFNCYLDNPEKTAASEQGDFYITGDRAHM 458
Cdd:PRK04319 367 -NYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYM 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 459 DEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshDP-EALTRELQE 537
Cdd:PRK04319 443 DEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY---EPsEELKEEIRG 519
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 88196780 538 HVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 577
Cdd:PRK04319 520 FVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELG 559
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-575 |
2.97e-125 |
|
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: 374.98 E-value: 2.97e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARvksiitsd 169
Cdd:cd05974 2 SFAEMSARSSRVANFLR-SIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 alapHVDAISADCpslqsrllvsdtsrpgwinfrellrvaspehnclrTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLG 249
Cdd:cd05974 73 ----AVYAAVDEN-----------------------------------THADDPMLLYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 250 FVASgRRLMALTESDIFWNTTDTGWVKAAWT-LFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ 328
Cdd:cd05974 114 HLST-MYWIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 329 EDLTRYKFQcLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGN 408
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 409 vlpPGKEGNIAIRIKPTRPFCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVES 488
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 489 ALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALtrELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILR 568
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETAL--EIFRFSRERLAPYKRIRRLEF-AELPKTISGKIRR 425
|
....*..
gi 88196780 569 SKLRNQE 575
Cdd:cd05974 426 VELRRRE 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
89-575 |
3.16e-122 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 367.60 E-value: 3.16e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 89 WTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITS 168
Cdd:cd05969 1 YTFAQLKVLSARFANVLK-SLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 169 DalaphvdaisadcpslqsrllvsdtsrpgwinfrELLRVASPEhnclrtrsgDSMAIYFTSGTTGTPKMVEHSQcSYGL 248
Cdd:cd05969 80 E----------------------------------ELYERTDPE---------DPTLLHYTSGTTGTPKGVLHVH-DAMI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 249 GFVASGRRLMALTESDIFWNTTDTGWVK-AAWTLFSAWANGACVFVHElPQVDAQTILNTLCRFPITTICCVPTLFRLLV 327
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTgTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 328 QED---LTRYKFQCLRHCLAGGEALNSDVRdKW-KNQTGLEIHEGYGQSET--VLICgNFRGSTIKSGSMGKASPPYDVQ 401
Cdd:cd05969 195 KEGdelARKYDLSSLRFIHSVGEPLNPEAI-RWgMEVFGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKAA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 402 IVDEEGNVLPPGKEGNIAIriKPTRPfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRI 481
Cdd:cd05969 273 VVDENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 482 GPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshDP-EALTRELQEHVKTVTAPYKYPRKVAFISELPK 560
Cdd:cd05969 350 GPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGF---EPsDELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
|
490
....*....|....*
gi 88196780 561 TVSGKILRSKLRNQE 575
Cdd:cd05969 427 TRSGKIMRRVLKAKE 441
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
56-578 |
3.51e-117 |
|
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: 354.89 E-value: 3.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 56 HDVLDVWSQlektgHRPPNPAFwwVNGSGTevkWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACM 135
Cdd:COG0318 2 ADLLRRAAA-----RHPDRPAL--VFGGRR---LTYAELDARARRLAAALR-ALGVGPGDRVALLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 136 RTGVVMIPGISQLTQKDLKYRLQAARVKSIITsdalaphvdaisadcpslqsrllvsdtsrpgwinfrellrvaspehnc 215
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 216 lrtrsgdsMAIYFTSGTTGTPKMVEHSQ---CSYGLGFVASgrrlMALTESDIFWNTT----DTGWVkaaWTLFSAWANG 288
Cdd:COG0318 103 --------ALILYTSGTTGRPKGVMLTHrnlLANAAAIAAA----LGLTPGDVVLVALplfhVFGLT---VGLLAPLLAG 167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 289 ACVFVheLPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHE 367
Cdd:COG0318 168 ATLVL--LPRFDPERVLELIERERVTVLFGVPTMLaRLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 368 GYGQSET-VLICGNFRGS-TIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptrPFCLFNCYLDNPEKTAASE 445
Cdd:COG0318 246 GYGLTETsPVVTVNPEDPgERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAF 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 446 QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVS 525
Cdd:COG0318 321 RDGWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AE 399
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 88196780 526 HDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 578
Cdd:COG0318 400 LDAEELRAFLRERL----ARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
84-572 |
9.94e-107 |
|
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: 327.85 E-value: 9.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 84 GTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVK 163
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 164 SIITsdalaphvDAisADCPSLqsrllvsdtsrpgwinfrellrvaspehnclrtrsgdsmaIYFTSGTTGTPKMVEHSQ 243
Cdd:cd05971 81 ALVT--------DG--SDDPAL----------------------------------------IIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 cSYGLGFvASGRRL---MALTESDIFWNTTDTGWVKAAW-TLFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCV 319
Cdd:cd05971 111 -RVLLGH-LPGVQFpfnLFPRDGDLYWTPADWAWIGGLLdVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 320 PTLFRLLVQEDLTRYKFQC-LRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRG-STIKSGSMGKASPP 397
Cdd:cd05971 189 PTALKMMRQQGEQLKHAQVkLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 398 YDVQIVDEEGNVLPPGKEGNIAIRikptRP-FCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINS 476
Cdd:cd05971 269 HRVAIVDDNGTPLPPGEVGEIAVE----LPdPVAFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 477 SSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVshDPEALTRELQEHVKTVTAPYKYPRKVAFIS 556
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVN 422
|
490
....*....|....*.
gi 88196780 557 ELPKTVSGKILRSKLR 572
Cdd:cd05971 423 ELPRTATGKIRRRELR 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-572 |
4.55e-104 |
|
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: 323.17 E-value: 4.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 50 EYFNFAHDVLDvwsQLEKTghRPPNPAFWWVNGSgtevkWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWL 129
Cdd:cd05959 1 EKYNAATLVDL---NLNEG--RGDKTAFIDDAGS-----LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 130 TIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHV-DAISADCPSLQsRLLVSDTSRP--GWINFRELL 206
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLaAALTKSEHTLV-VLIVSGGAGPeaGALLLAELV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 207 RVASPEHNCLRTRSgDSMAIY-FTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWvkaAWTL---- 281
Cdd:cd05959 149 AAEAEQLKPAATHA-DDPAFWlYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAAKLFF---AYGLgnsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 282 -FSAWANGACVFVHELPQVDAqtILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKN 359
Cdd:cd05959 225 tFPLSVGATTVLMPERPTPAA--VFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 360 QTGLEIHEGYGQSETVLI-CGNFRGStIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFclfncYLDNP 438
Cdd:cd05959 303 RFGLDILDGIGSTEMLHIfLSNRPGR-VRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM-----YWNNR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 439 EKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 518
Cdd:cd05959 377 DKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 88196780 519 LSPAYvsHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05959 457 LRPGY--EDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
222-567 |
3.48e-102 |
|
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: 312.30 E-value: 3.48e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 222 DSMAIYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHelPQVDA 301
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 302 QTILNTLCRFPITTICCVPTLFRLLVQEDL-TRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET--VLIC 378
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPEsAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 379 GNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHM 458
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGP-----SVMKGYWNNPEATAAVDEDGWYRTGDLGRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 459 DEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvsHDPEAltRELQEH 538
Cdd:cd04433 233 DEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG---ADLDA--EELRAH 307
|
330 340
....*....|....*....|....*....
gi 88196780 539 VKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-573 |
6.83e-102 |
|
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: 315.23 E-value: 6.83e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQaarvksiiTSD 169
Cdd:cd05973 2 TFGELRALSARFANALQ-ELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLR--------TSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 AlaphvdaisadcpslqsRLLVSDTSrpgwinfrELLRVASpehnclrtrsgDSMAIYFTSGTTGTPKMVEHSqCSYGLG 249
Cdd:cd05973 73 A-----------------RLVVTDAA--------NRHKLDS-----------DPFVMMFTSGTTGLPKGVPVP-LRALAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 250 FVASGRRLMALTESDIFWNTTDTGWvkaAWTLFSA----WANGACVFVHELPqVDAQTILNTLCRFPITTICCVPTLFRL 325
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGW---AYGLYYAitgpLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 326 LVQ---EDLTRYKFQcLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRG--STIKSGSMGKASPPYDV 400
Cdd:cd05973 192 LMAagaEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHAleHPVHAGSAGRAMPGWRV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 401 QIVDEEGNVLPPGKEGNIAIRIKPTrPFCLFNCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYR 480
Cdd:cd05973 271 AVLDDDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 481 IGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvsHDP-EALTRELQEHVKTVTAPYKYPRKVAFISELP 559
Cdd:cd05973 347 IGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG---HEGtPALADELQLHVKKRLSAHAYPRTIHFVDELP 423
|
490
....*....|....
gi 88196780 560 KTVSGKILRSKLRN 573
Cdd:cd05973 424 KTPSGKIQRFLLRR 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
61-572 |
3.08e-98 |
|
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: 306.80 E-value: 3.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 61 VWSQLEKT-GHRPPNPAFWWvngsgTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGV 139
Cdd:cd05936 1 LADLLEEAaRRFPDKTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 140 VMIPGISQLTQKDLKYRLQaarvksiitsdalaphvdaisaDCpslQSRLLVSDTSrpgwinFRELLRV-ASPEHNCLRT 218
Cdd:cd05936 75 VVVPLNPLYTPRELEHILN----------------------DS---GAKALIVAVS------FTDLLAAgAPLGERVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 219 RsGDSMAIYFTSGTTGTPK--MVEH-------SQCSYGLGFVASGRR--LMALTESDIFwnttdtgwvkaAWT--LFSAW 285
Cdd:cd05936 124 P-EDVAVLQYTSGTTGVPKgaMLTHrnlvanaLQIKAWLEDLLEGDDvvLAALPLFHVF-----------GLTvaLLLPL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 286 ANGACVFVheLPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLE 364
Cdd:cd05936 192 ALGATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYiALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 365 IHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAA 443
Cdd:cd05936 270 IVEGYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-GPQ----VMKGYWNRPEETAE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 444 SEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspay 523
Cdd:cd05936 345 AFVDGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL---- 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 88196780 524 vsHDPEALT-RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05936 421 --KEGASLTeEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
86-572 |
1.98e-96 |
|
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: 300.93 E-value: 1.98e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALaphvdaisadcpslqsrllvsdtsrpgwinfrellrvaspehnclrTRSGDSMAIYFTSGTTGTPKMVEHSQCS 245
Cdd:cd05958 88 LCAHAL----------------------------------------------TASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 246 YGLGFVASGRRLMALTESDIFwnttdTGWVKAAWT------LFSAWANGACVFVheLPQVDAQTILNTLCRFPITTICCV 319
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRF-----VGSPPLAFTfglggvLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 320 PTLFRLLV------QEDLTrykfqCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGK 393
Cdd:cd05958 195 PTAYRAMLahpdaaGPDLS-----SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 394 ASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfclfNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDV 473
Cdd:cd05958 270 PVPGYEAKVVDDEGNPVPDGTIGRLAVR-GPT------GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 474 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShdPEALTRELQEHVKTVTAPYKYPRKVA 553
Cdd:cd05958 343 IVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAIE 420
|
490
....*....|....*....
gi 88196780 554 FISELPKTVSGKILRSKLR 572
Cdd:cd05958 421 FVTELPRTATGKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
85-576 |
2.85e-88 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 282.46 E-value: 2.85e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 85 TEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKS 164
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALR-ALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 165 IITSDALAPHVDAISADCPSLQSRLLVSDTSRPG----WINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK--- 237
Cdd:PRK06187 107 VLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKgvv 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 238 -----MVEHSqcsyglgfvASGRRLMALTESDIFWNTTDTGWVkAAWTL-FSAWANGA-CVFVHElpqVDAQTILNTLCR 310
Cdd:PRK06187 187 lshrnLFLHS---------LAVCAWLKLSRDDVYLVIVPMFHV-HAWGLpYLALMAGAkQVIPRR---FDPENLLDLIET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 311 FPITTICCVPTLFRLLVQEDLTR-YKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNF-----RG 383
Cdd:PRK06187 254 ERVTFFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLPpedqlPG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 384 STIKSGSMGKASPPYDVQIVDEEGNVLPP-GKE-GNIAIRiKPtrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDED 461
Cdd:PRK06187 334 QWTKRRSAGRPLPGVEARIVDDDGDELPPdGGEvGEIIVR-GP----WLMQGYWNRPEATAETIDGGWLHTGDVGYIDED 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 462 GYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEaltrELQEHVKT 541
Cdd:PRK06187 409 GYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG-ATLDAK----ELRAFLRG 483
|
490 500 510
....*....|....*....|....*....|....*
gi 88196780 542 VTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK06187 484 RLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-572 |
7.63e-81 |
|
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: 260.47 E-value: 7.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYrlqaarvksiitsd 169
Cdd:cd05919 12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAY-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 alaphvdaISADCpslQSRLLVsdtsrpgwinfrellrvaspehnclrtRSGDSMAIY-FTSGTTGTPKMVEHSQCSYgL 248
Cdd:cd05919 77 --------IARDC---EARLVV---------------------------TSADDIAYLlYSSGTTGPPKGVMHAHRDP-L 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 249 GFV-ASGRRLMALTESDIFWNTTDTGWvkaAW----TLFSAWANGACVFVHELPqVDAQTILNTLCRFPITTICCVPTLF 323
Cdd:cd05919 118 LFAdAMAREALGLTPGDRVFSSAKMFF---GYglgnSLWFPLAVGASAVLNPGW-PTAERVLATLARFRPTVLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 -RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQI 402
Cdd:cd05919 194 aNLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 403 VDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIG 482
Cdd:cd05919 274 VDEEGHTIPPGEEGDLLVR-GPS----AAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 483 PVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHdpEALTRELQEHVKTVTAPYKYPRKVAFISELPKTV 562
Cdd:cd05919 349 PVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTA 426
|
490
....*....|
gi 88196780 563 SGKILRSKLR 572
Cdd:cd05919 427 TGKLQRFKLR 436
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-573 |
9.97e-81 |
|
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: 265.33 E-value: 9.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 47 PVPEYF-----NFAHDVLDVWSQlektGHRPPNPAFWWVNGS-GTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLV 120
Cdd:cd05967 39 PFTRWFvggrlNTCYNALDRHVE----AGRGDQIALIYDSPVtGTERTYTYAELLDEVSRLAGVLR-KLGVVKGDRVIIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 121 LPRLPEWWLTIVACMRTGV---VMIPGISQltqKDLKYRLQAARVKSIITSDA---------LAPHVD-AIS------AD 181
Cdd:cd05967 114 MPMIPEAAIAMLACARIGAihsVVFGGFAA---KELASRIDDAKPKLIVTASCgiepgkvvpYKPLLDkALElsghkpHH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 182 CPSLQSRLLVSDTSRPG-WINFRELLRVASPeHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMAL 260
Cdd:cd05967 191 VLVLNRPQVPADLTKPGrDLDWSELLAKAEP-VDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 261 TESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHELPQV---DAQTILNTLCRFPITTICCVPTLFRLLVQED-----L 331
Cdd:cd05967 270 KPGDVWWAASDVGWVVGhSYIVYGPLLHGATTVLYEGKPVgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 332 TRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET-VLICGNFRG---STIKSGSMGKASPPYDVQIVDEEG 407
Cdd:cd05967 350 KKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgWPITANPVGlepLPIKAGSPGKPVPGYQVQVLDEDG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 408 NVLPPGKEGNIAIRIkPTRPFCLFNCYLDNP--EKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVE 485
Cdd:cd05967 430 EPVGPNELGNIVIKL-PLPPGCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGE 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 486 VESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 565
Cdd:cd05967 509 MEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEG-VKITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGK 587
|
....*...
gi 88196780 566 ILRSKLRN 573
Cdd:cd05967 588 ILRRTLRK 595
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-567 |
1.07e-80 |
|
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: 264.44 E-value: 1.07e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 53 NFAHDVLDvwSQLEKTGHRPpnpAFWWVNGSGTEVK-WTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTI 131
Cdd:cd17634 53 NLAANALD--RHLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTLL-DLGVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 132 VACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDA---------LAPHVD-AISADCPSLQSRLLVSDTSRP---- 197
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvpLKKNVDdALNPNVTSVEHVIVLKRTGSDidwq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 198 --GWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWV 275
Cdd:cd17634 207 egRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 276 KA-AWTLFSAWANGACVFVHELPQV--DAQTILNTLCRFPITTICCVPTLFRLLVQED---LTRYKFQCLRHCLAGGEAL 349
Cdd:cd17634 287 TGhSYLLYGPLACGATTLLYEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 350 NSDV-RDKWK--NQTGLEIHEGYGQSETV-LICGNFRGST-IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIK- 423
Cdd:cd17634 367 NPEAyEWYWKkiGKEKCPVVDTWWQTETGgFMITPLPGAIeLKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPw 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 424 --PTRPFclfncYLDNPE--KTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLES 499
Cdd:cd17634 447 pgQTRTL-----FGDHERfeQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196780 500 AVVSSPDPIRGEVVKAFIVLSPAYVshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:cd17634 522 AVVGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
90-572 |
8.16e-80 |
|
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: 259.77 E-value: 8.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:TIGR02262 32 SYGELEAQVRRLAAALR-RLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDAISADCPSLQSRLLVSDtSRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLG 249
Cdd:TIGR02262 111 ALLPVIKAALGKSPHLEHRVVVGR-PEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 250 FVASGRRLMALTESDIfwnttdtgwVKAAWTLFSAWANG-----------ACVFVHELPQVDAqtILNTLCRFPITTICC 318
Cdd:TIGR02262 190 AELYARNTLGIREDDV---------CFSAAKLFFAYGLGnaltfpmsvgaTTVLMGERPTPDA--VFDRLRRHQPTIFYG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 319 VPTLFR-LLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPP 397
Cdd:TIGR02262 259 VPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 398 YDVQIVDEEGNVLPPGKEGNIAIRiKPTRPfclfNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSS 477
Cdd:TIGR02262 339 YRLRLVGDGGQDVADGEPGELLIS-GPSSA----TMYWNNRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 478 SYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshdpEALTRELQEHVKTVTAPYKYPRKVAFISE 557
Cdd:TIGR02262 414 GIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ-----TALETELKEHVKDRLAPYKYPRWIVFVDD 488
|
490
....*....|....*
gi 88196780 558 LPKTVSGKILRSKLR 572
Cdd:TIGR02262 489 LPKTATGKIQRFKLR 503
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
53-573 |
3.10e-78 |
|
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: 258.65 E-value: 3.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 53 NFAHDVLDVWsqLEKTGHRPpnpAFWWV-NGSGTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTI 131
Cdd:cd05966 53 NISYNCLDRH--LKERGDKV---AIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 132 VACMRTGV---VMIPGISQltqKDLKYRLQAARVKSIITSDA---------LAPHVDAISADCPSLQSRLLVSDTSRPGW 199
Cdd:cd05966 127 LACARIGAvhsVVFAGFSA---ESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALEKCPSVEKVLVVKRTGGEVP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 200 IN------FRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTG 273
Cdd:cd05966 204 MTegrdlwWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKYVFDYHPDDIYWCTADIG 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 274 WVKA-AWTLFSAWANGACVFVHE----LPQVDaqTILNTLCRFPITTICCVPTLFRLLVQ---EDLTRYKFQCLRHCLAG 345
Cdd:cd05966 284 WITGhSYIVYGPLANGATTVMFEgtptYPDPG--RYWDIVEKHKVTIFYTAPTAIRALMKfgdEWVKKHDLSSLRVLGSV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 346 GEALNSDVrdkWK---NQTGLE---IHEGYGQSETVLIC-GNFRGST-IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGN 417
Cdd:cd05966 362 GEPINPEA---WMwyyEVIGKErcpIVDTWWQTETGGIMiTPLPGATpLKPGSATRPFFGIEPAILDEEGNEVEGEVEGY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 418 IAIRiKPTrPFCLFNCYLDNP--EKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPA 495
Cdd:cd05966 439 LVIK-RPW-PGMARTIYGDHEryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPA 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196780 496 VLESAVVSSPDPIRGEVVKAFIVLSPAYvsHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd05966 517 VAEAAVVGRPHDIKGEAIYAFVTLKDGE--EPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
69-568 |
7.74e-78 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 252.53 E-value: 7.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 69 GHRPPNPAFWWVNGSgtevkWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisql 148
Cdd:cd17631 6 RRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 149 tqkdLKYRLQAARVKSIItsdalaphvdaisADCpslQSRLLVSDTSRpgwinfrellrvaspehnclrtrsgdsmaIYF 228
Cdd:cd17631 75 ----LNFRLTPPEVAYIL-------------ADS---GAKVLFDDLAL-----------------------------LMY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 229 TSGTTGTPKMVEHSQcsYGLGFVASGrrlmALTESDIfwNTTDTGWVKA---------AWTLFSAWANGACVFvheLPQV 299
Cdd:cd17631 106 TSGTTGRPKGAMLTH--RNLLWNAVN----ALAALDL--GPDDVLLVVAplfhigglgVFTLPTLLRGGTVVI---LRKF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 300 DAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKnQTGLEIHEGYGQSETV-LI 377
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQALLQhPRFATTDLSSLRAVIYGGAPMPERLLRALQ-ARGVKFVQGYGMTETSpGV 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 378 CGNFRGSTI-KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRA 456
Cdd:cd17631 254 TFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GPH----VMAGYWNRPEATAAAFRDGWFHTGDLG 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 457 HMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvSHDPEALtrELQ 536
Cdd:cd17631 329 RLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP---GAELDED--ELI 403
|
490 500 510
....*....|....*....|....*....|..
gi 88196780 537 EHVKTVTAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:cd17631 404 AHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
65-477 |
1.07e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 251.46 E-value: 1.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 65 LEKTGHRPPN-PAFwwvnGSGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIP 143
Cdd:pfam00501 1 LERQAARTPDkTAL----EVGEGRRLTYRELDERANRLAAGLR-ALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 144 GISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDtsRPGWINFRELLRVASPEHNCLRT---RS 220
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLD--RDPVLKEEPLPEEAKPADVPPPPpppPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 221 GDSMA-IYFTSGTTGTPKMVEHSQ---CSYGLGFVASGRRLMALTESDIFWNTT----DTGWVkaaWTLFSAWANGA-CV 291
Cdd:pfam00501 154 PDDLAyIIYTSGTTGKPKGVMLTHrnlVANVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLS---LGLLGPLLAGAtVV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 292 FVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYG 370
Cdd:pfam00501 231 LPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEaGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 371 QSET---VLICGNFRGSTIKSGSMGKASPPYDVQIVDEE-GNVLPPGKEGNIAIRikptRPfCLFNCYLDNPEKTAAS-E 445
Cdd:pfam00501 311 LTETtgvVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAfD 385
|
410 420 430
....*....|....*....|....*....|..
gi 88196780 446 QGDFYITGDRAHMDEDGYFWFVGRNDDVINSS 477
Cdd:pfam00501 386 EDGWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
84-572 |
4.78e-77 |
|
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: 256.02 E-value: 4.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 84 GTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGV---VMIPGISQltqKDLKYRLQAA 160
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGAihsVVFGGFSA---EALADRINDA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 161 RVKSIITSD---------ALAPHVDAISADCPSLQSRLLV---SDTSRPGWIN-----FRELLRVASPEHNCLRTRSGDS 223
Cdd:TIGR02188 160 GAKLVITADeglrggkviPLKAIVDEALEKCPVSVEHVLVvrrTGNPVVPWVEgrdvwWHDLMAKASAYCEPEPMDSEDP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 224 MAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHE----LPQ 298
Cdd:TIGR02188 240 LFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGhSYIVYGPLANGATTVMFEgvptYPD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 299 VD--AQTILntlcRFPITTICCVPTLFRLLVQ---EDLTRYKFQCLRhcLAG--GEALNSDVRDKWKNQTGLE---IHEG 368
Cdd:TIGR02188 320 PGrfWEIIE----KHKVTIFYTAPTAIRALMRlgdEWVKKHDLSSLR--LLGsvGEPINPEAWMWYYKVVGKErcpIVDT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 369 YGQSETVLIC-GNFRGST-IKSGSMGKASPPYDVQIVDEEGNVLP-PGKEGNIAIRiKPtRPFCLFNCYLDnPE---KTA 442
Cdd:TIGR02188 394 WWQTETGGIMiTPLPGATpTKPGSATLPFFGIEPAVVDEEGNPVEgPGEGGYLVIK-QP-WPGMLRTIYGD-HErfvDTY 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 443 ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPA 522
Cdd:TIGR02188 471 FSPFPGYYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDG 550
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 88196780 523 YvSHDPEaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:TIGR02188 551 Y-EPDDE-LRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLR 598
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
90-574 |
1.14e-73 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 244.04 E-value: 1.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK07656 32 TYAELNARVRRAAAALA-ALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDAISADCPSLQSRLLVSDT----SRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK--MVEHSQ 243
Cdd:PRK07656 111 LFLGVDYSATTRLPALEHVVICETEeddpHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKgaMLTHRQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 --------CSYgLGFVASGRRLMALTESDIFwnttdtGWvKAAWTlfSAWANGACVFVHelPQVDAQTILNTLCRFPITT 315
Cdd:PRK07656 191 llsnaadwAEY-LGLTEGDRYLAANPFFHVF------GY-KAGVN--APLMRGATILPL--PVFDPDEVFRLIETERITV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 316 ICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGE----ALNSDVRDKWKNQTgleIHEGYGQSE---TVLICGNFRGSTIK 387
Cdd:PRK07656 259 LPGPPTMYNsLLQHPDRSAEDLSSLRLAVTGAAsmpvALLERFESELGVDI---VLTGYGLSEasgVTTFNRLDDDRKTV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 388 SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptrpfcLFNC---YLDNPEKTAASEQGDFYI-TGDRAHMDEDGY 463
Cdd:PRK07656 336 AGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR--------GPNVmkgYYDDPEATAAAIDADGWLhTGDLGRLDEEGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 464 FWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALTRE-LQEHVKTV 542
Cdd:PRK07656 408 LYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG------AELTEEeLIAYCREH 481
|
490 500 510
....*....|....*....|....*....|..
gi 88196780 543 TAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK07656 482 LAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
85-567 |
4.63e-72 |
|
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: 239.04 E-value: 4.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 85 TEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKS 164
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLR-KLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 165 IITSDALAPHVDAISADCPSlQSRLLVSDTSRPGWINFRELLRVAS--PEHN---CLRTRSGDSMAIYFTSGTTGTPK-- 237
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGP-KDKIIVLDDKPDGVLSIEDLLSPTLgeEDEDlppPLKDGKDDTAAILYSSGTTGLPKgv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 238 ---------MVEHSQCSYGLGFVASGRRLMALTesdIFWNTTDTgwvkaaWTLFSAWaNGACVFVHelPQVDAQTILNTL 308
Cdd:cd05911 165 clshrnliaNLSQVQTFLYGNDGSNDVILGFLP---LYHIYGLF------TTLASLL-NGATVIIM--PKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 309 CRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGL-EIHEGYGQSETVLICGNFRGSTI 386
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAKsPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 387 KSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAIRIkptrPFClFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGY 463
Cdd:cd05911 313 KPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRG----PQV-MKGYYNNPEATKETfdEDG-WLHTGDIGYFDEDGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 464 FWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVT 543
Cdd:cd05911 387 LYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP-----GEKLTEKEVKDYVAKKV 461
|
490 500
....*....|....*....|....*
gi 88196780 544 APYKYPRK-VAFISELPKTVSGKIL 567
Cdd:cd05911 462 ASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
61-578 |
9.64e-72 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 239.86 E-value: 9.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 61 VWSQLEKTGHRPPN-PAFWWVngsGTEVkwTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGV 139
Cdd:PRK08314 12 LFHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 140 VMIPGISQLTQKDLKYRLQAARVKSIITSDALAP------------HV------DAISADCP-----SLQSRLLVSDTSR 196
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELAPkvapavgnlrlrHVivaqysDYLPAEPEiavpaWLRAEPPLQALAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 197 PGWINFRELLR--VASPEHNclrTRSGDSMAIYFTSGTTGTPKMVEHSQcsyglgfvasgRRLMALTESDIFWNT-TDTG 273
Cdd:PRK08314 167 GGVVAWKEALAagLAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTH-----------RTVMANAVGSVLWSNsTPES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 274 WVKAAWTLF----------SAWANGACVFVheLPQVDAQTILNTLCRFPITTICCVPT-LFRLLVQEDLTRYKFQCLRHC 342
Cdd:PRK08314 233 VVLAVLPLFhvtgmvhsmnAPIYAGATVVL--MPRWDREAAARLIERYRVTHWTNIPTmVVDFLASPGLAERDLSSLRYI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 343 LAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTiKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAI 420
Cdd:PRK08314 311 GGGGAAMPEAVAERLKELTGLDYVEGYGLTETMaQTHSNPPDRP-KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 421 RiKPTrpfcLFNCYLDNPEKTAAS----EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAV 496
Cdd:PRK08314 390 H-GPQ----VFKGYWNRPEATAEAfieiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 497 LESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK08314 465 QEACVIATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEK 541
|
..
gi 88196780 577 GR 578
Cdd:PRK08314 542 AR 543
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
44-572 |
2.91e-71 |
|
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: 240.08 E-value: 2.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 44 GKRPVPEYF-----NFAHDVLDVWsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLM 118
Cdd:cd05968 47 GGKPWAAWFvggrmNIVEQLLDKW-----LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLR-ALGVGKGDRVG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 119 LVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDA---------LAPHVDAISADCPSLQSRL 189
Cdd:cd05968 121 IYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 190 LVSDTSRP-GWINFREL---LRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESD- 264
Cdd:cd05968 201 VVRHLGNDfTPAKGRDLsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 265 IFWnTTDTGWVKAAWTLFSAWANGACVFVHE-LPQVD-AQTILNTLCRFPITTICCVPTLFRLLV---QEDLTRYKFQCL 339
Cdd:cd05968 281 LTW-FTDLGWMMGPWLIFGGLILGATMVLYDgAPDHPkADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 340 RHCLAGGEALNSD-------VRDKWKN-----QTGLEIHEGygqsetvlICGNFRGSTIKSGSMGKASPPYDVQIVDEEG 407
Cdd:cd05968 360 RVLGSTGEPWNPEpwnwlfeTVGKGRNpiinySGGTEISGG--------ILGNVLIKPIKPSSFNGPVPGMKADVLDESG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 408 NVLPPgKEGNIAIRiKP----TRPFCLFNC-YLDnpekTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIG 482
Cdd:cd05968 432 KPARP-EVGELVLL-APwpgmTRGFWRDEDrYLE----TYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVG 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 483 PVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTV 562
Cdd:cd05968 506 PAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERVADELGKPLSPERILFVKDLPKTR 583
|
570
....*....|
gi 88196780 563 SGKILRSKLR 572
Cdd:cd05968 584 NAKVMRRVIR 593
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-572 |
2.18e-70 |
|
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: 232.57 E-value: 2.18e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqkdLKYRLQAARVKSIIT 167
Cdd:cd05934 3 RWTYAELLRESARIAAALA-ALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVP---------INTALRGDELAYIID 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 sdalapHVDAisadcpslqsRLLVSDTSrpgwinfrellrvaspehnclrtrsgdsmAIYFTSGTTGTPK--MVEHSQ-C 244
Cdd:cd05934 73 ------HSGA----------QLVVVDPA-----------------------------SILYTSGTTGPPKgvVITHANlT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 245 SYGLGFvasgRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVheLPQVDAQTILNTLCRFPITTICCVPTLF 323
Cdd:cd05934 108 FAGYYS----ARRFGLGEDDVYLTVLPLFHINAqAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAML 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 R-LLVQEDLTRYKFQCLRhcLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQI 402
Cdd:cd05934 182 SyLLAQPPSPDDRAHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 403 VDEEGNVLPPGKEGNIAIRikPTRPFCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIG 482
Cdd:cd05934 260 VDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 483 PVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTV 562
Cdd:cd05934 338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFAFCEGQL----AYFKVPRYIRFVDDLPKTP 412
|
490
....*....|
gi 88196780 563 SGKILRSKLR 572
Cdd:cd05934 413 TEKVAKAQLR 422
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
53-572 |
1.20e-69 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 236.58 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 53 NFAHDVLDVwsQLEKTGHRPpnpAFWWVNGSGTEV-KWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTI 131
Cdd:PRK00174 67 NVSYNCLDR--HLKTRGDKV---AIIWEGDDPGDSrKITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 132 VACMRTGV---VMIPGISQltqKDLKYRLQAARVKSIITSD---------ALAPHVDAISADCPSLQSRLLVSDTSRP-G 198
Cdd:PRK00174 141 LACARIGAvhsVVFGGFSA---EALADRIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVRRTGGDvD 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 199 WINFR-----ELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTG 273
Cdd:PRK00174 218 WVEGRdlwwhELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLVYAAMTMKYVFDYKDGDVYWCTADVG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 274 WVKA-AWTLFSAWANGACVFVHE----LPQVDaqtilntlcRF-------PITTICCVPTLFRLLVQ---EDLTRYKFQC 338
Cdd:PRK00174 298 WVTGhSYIVYGPLANGATTLMFEgvpnYPDPG---------RFwevidkhKVTIFYTAPTAIRALMKegdEHPKKYDLSS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 339 LRhcLAG--GEALNSDVrdkWK---NQTGLE---IHEGYGQSET--VLICGnFRGST-IKSGSMGKASPPYDVQIVDEEG 407
Cdd:PRK00174 369 LR--LLGsvGEPINPEA---WEwyyKVVGGErcpIVDTWWQTETggIMITP-LPGATpLKPGSATRPLPGIQPAVVDEEG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 408 NVLPPGKEGNIAIrikpTRPF--CLFNCYLDnPE---KTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIG 482
Cdd:PRK00174 443 NPLEGGEGGNLVI----KDPWpgMMRTIYGD-HErfvKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLG 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 483 PVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTV 562
Cdd:PRK00174 518 TAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGPIAKPDVIQFAPGLPKTR 595
|
570
....*....|
gi 88196780 563 SGKILRSKLR 572
Cdd:PRK00174 596 SGKIMRRILR 605
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
83-573 |
6.24e-65 |
|
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: 220.26 E-value: 6.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 83 SGTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARV 162
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 163 KSIIT-SDALAPHVDAISADCPSLQ--------SRLLVSDTSRPGWINfreLLRVASPEhncLRTRSGDSMAIYFTSGTT 233
Cdd:cd05926 88 KLVLTpKGELGPASRAASKLGLAILelaldvgvLIRAPSAESLSNLLA---DKKNAKSE---GVPLPDDLALILHTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 234 GTPKMVEHSQcsygLGFVASGR---RLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHelPQVDAQTILNTLC 309
Cdd:cd05926 162 GRPKGVPLTH----RNLAASATnitNTYKLTPDDRTLVVMPLFHVHGlVASLLSTLAAGGSVVLP--PRFSASTFWPDVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 310 RFPITTICCVPTLFRLLVQ--EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV--LICGNFRGST 385
Cdd:cd05926 236 DYNATWYTAVPTIHQILLNrpEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPLPPGP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 386 IKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAAS-EQGDFYITGDRAHMDEDGYF 464
Cdd:cd05926 316 RKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGPN-----VTRGYLNNPEANAEAaFKDGWFRTGDLGYLDADGYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 465 WFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshdpEALTRELQEHVKTVTA 544
Cdd:cd05926 390 FLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-----SVTEEELRAFCRKHLA 464
|
490 500
....*....|....*....|....*....
gi 88196780 545 PYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd05926 465 AFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
86-574 |
2.12e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 219.80 E-value: 2.12e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALAPHVDAISADCPSLQSRLLVSDTSRP---GWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK----- 237
Cdd:PRK08316 113 LVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKgamlt 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 238 ----MVEHSQCSYGLGFVASGRRLMAL-----TESDIFWNTTDtgWVKAAWTLfsawangacvfvheLPQVDAQTILNTL 308
Cdd:PRK08316 193 hralIAEYVSCIVAGDMSADDIPLHALplyhcAQLDVFLGPYL--YVGATNVI--------------LDAPDPELILRTI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 309 CRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAG-----GEALNsDVRDKWknqTGLEIHEGYGQSE-----TVLI 377
Cdd:PRK08316 257 EAERITSFFAPPTVWiSLLRHPDFDTRDLSSLRKGYYGasimpVEVLK-ELRERL---PGLRFYNCYGQTEiaplaTVLG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 378 CGNFRGstiKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAH 457
Cdd:PRK08316 333 PEEHLR---RPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR-SPQ----LMLGYWDDPEKTAEAFRGGWFHSGDLGV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 458 MDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP-AYVSHDpealtrELQ 536
Cdd:PRK08316 405 MDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAgATVTED------ELI 478
|
490 500 510
....*....|....*....|....*....|....*...
gi 88196780 537 EHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK08316 479 AHCRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
88-571 |
3.86e-62 |
|
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: 211.62 E-value: 3.86e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgIsqltqkDLKYrlQAARVKSIIt 167
Cdd:cd05930 12 SLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVP-L------DPSY--PAERLAYIL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 SDAlaphvdaisadcpslQSRLLVSDtsrpgwinfrellrvaspehnclrtrsGDSMA-IYFTSGTTGTPK--MVEHSqc 244
Cdd:cd05930 81 EDS---------------GAKLVLTD---------------------------PDDLAyVIYTSGSTGKPKgvMVEHR-- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 245 syGLG-FVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFVHELPQVDAQTILNTLCRFPITTICCVPTL 322
Cdd:cd05930 117 --GLVnLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATlVVLPEEVRKDPEALADLLAEEGITVLHLTPSL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 323 FRLLVQEdLTRYKFQCLRHCLAGGEALNSDVRDKW-KNQTGLEIHEGYGQSETVLICGNFRgstIKSGSMGKASPP---- 397
Cdd:cd05930 195 LRLLLQE-LELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDATYYR---VPPDDEEDGRVPigrp 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 398 ---YDVQIVDEEGNVLPPGKEGNIAIrikpTRPfCLFNCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFV 467
Cdd:cd05930 271 ipnTRVYVLDENLRPVPPGVPGELYI----GGA-GLARGYLNRPELTAERfvpnpfGPGErMYRTGDLVRWLPDGNLEFL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 468 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVTAPYK 547
Cdd:cd05930 346 GRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE-----GGELDEEELRAHLAERLPDYM 420
|
490 500
....*....|....*....|....
gi 88196780 548 YPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd05930 421 VPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-571 |
8.73e-62 |
|
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: 210.03 E-value: 8.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:cd05935 3 TYLELLEVVKKLASFLS-NKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAphvdaisadcpslqsrllvsdtsrpgwinfrellrvaspehnclrtrsgDSMAIYFTSGTTGTPKMVEHSQCSYgLG 249
Cdd:cd05935 82 ELD-------------------------------------------------DLALIPYTSGTTGLPKGCMHTHFSA-AA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 250 FVASGRRLMALTESDIFWNTTD----TGWVKaawTLFSAWANGACVFVheLPQVDAQTILNTLCRFPITTICCVPT-LFR 324
Cdd:cd05935 112 NALQSAVWTGLTPSDVILACLPlfhvTGFVG---SLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTmLVD 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 325 LLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVD 404
Cdd:cd05935 187 LLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 405 -EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD----FYITGDRAHMDEDGYFWFVGRNDDVINSSSY 479
Cdd:cd05935 267 iETGRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEESFIEIkgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSGF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 480 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShdpEALTRELQEHVKTVTAPYKYPRKVAFISELP 559
Cdd:cd05935 342 KVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRG---KVTEEDIIEWAREQMAAYKYPREVEFVDELP 418
|
490
....*....|..
gi 88196780 560 KTVSGKILRSKL 571
Cdd:cd05935 419 RSASGKILWRLL 430
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
60-572 |
1.56e-61 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 211.85 E-value: 1.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 60 DVWSQL-EKTGHrppNPAFWWVNGSGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTG 138
Cdd:PRK08008 11 QMWDDLaDVYGH---KTALIFESSGGVVRRYSYLELNEEINRTANLFY-SLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 139 VVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRP---GWINFRELLRVASPEHNC 215
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPaddGVSSFTQLKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 216 LRTRSGDSMA-IYFTSGTTGTPKMVEHSQCSYGL-GFVASGRrlMALTESDIFWNTTDTGWV----KAAWTLFSAwanGA 289
Cdd:PRK08008 167 APPLSTDDTAeILFTSGTTSRPKGVVITHYNLRFaGYYSAWQ--CALRDDDVYLTVMPAFHIdcqcTAAMAAFSA---GA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 290 CVFVHElpQVDAQTILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAggeALN-SDV-RDKWKNQTGLEIH 366
Cdd:PRK08008 242 TFVLLE--KYSARAFWGQVCKYRATITECIPMMIRtLMVQPPSANDRQHCLREVMF---YLNlSDQeKDAFEERFGVRLL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 367 EGYGQSETVL-ICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRpfCLFNCYLDNPEKTAASE 445
Cdd:PRK08008 317 TSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGK--TIFKEYYLDPKATAKVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 446 QGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyV 524
Cdd:PRK08008 395 EADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG-E 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 88196780 525 SHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK08008 474 TLSEEEFFAFCEQNM----AKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
88-573 |
4.43e-61 |
|
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: 208.68 E-value: 4.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYrlqaarvksIIT 167
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY---------VIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 SDAlaphvdaisadcPSLqsrllvsdtsrpgwinfreLLRVAspehnclrtrsgdsmAIYFTSGTTGTPKMVEHSQCSyg 247
Cdd:cd05941 82 DSE------------PSL-------------------VLDPA---------------LILYTSGTTGRPKGVVLTHAN-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 lgfVASGRRlmALTESdifWNTTDT-------------GWVKAawTLFSAWANGACVFvheLPQVDAQTILNTLCRFPIT 314
Cdd:cd05941 114 ---LAANVR--ALVDA---WRWTEDdvllhvlplhhvhGLVNA--LLCPLFAGASVEF---LPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 315 TICCVPTLFRLLVQ---------EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGN-FRGS 384
Cdd:cd05941 181 VFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNpLDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 385 TIkSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDG 462
Cdd:cd05941 261 RR-PGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEYWNKPEATKEEFTDDgWFKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 463 YFWFVGR-NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEaltrELQEHVKT 541
Cdd:cd05941 335 YYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE----ELKEWAKQ 410
|
490 500 510
....*....|....*....|....*....|..
gi 88196780 542 VTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd05941 411 RLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
43-571 |
4.69e-59 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 206.43 E-value: 4.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 43 LGKRPVPEYfnfahdvLDVWSQLektghRPPNPAFWWVngsGTEVkwTFEELGKQSRKAANILEGAcGLKPGDRLMLVLP 122
Cdd:PRK06178 30 HGERPLTEY-------LRAWARE-----RPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 123 RLPEWWLTIVACMRTGVVMIPgISQLTQK-DLKYRLQAARVKSIITSDALAPHVDAISADC-----------------PS 184
Cdd:PRK06178 92 NCPQFHIVFFGILKLGAVHVP-VSPLFREhELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaePT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 185 LQSRLLVSDTSR--PGWINFRELLRvASPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQ-------CSYGLGFVASG 254
Cdd:PRK06178 171 LPLPDSLRAPRLaaAGAIDLLPALR-ACTAPVPLPPPALDALAaLNYTGGTTGMPKGCEHTQrdmvytaAAAYAVAVVGG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 255 RRLMALTESDIFW-NTTDTGwvkaawTLFSAWANGACVFvheLPQVDAQTILNTLCRFPIT-TICCVPTLFRLLVQEDLT 332
Cdd:PRK06178 250 EDSVFLSFLPEFWiAGENFG------LLFPLFSGATLVL---LARWDAVAFMAAVERYRVTrTVMLVDNAVELMDHPRFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 333 RYKFQCLRH--CLAGGEALNSDVRDKWKNQTGLEIHEG-YGQSETvLICGNF-RGstIKSGSM---------GKASPPYD 399
Cdd:PRK06178 321 EYDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTET-HTCDTFtAG--FQDDDFdllsqpvfvGLPVPGTE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 400 VQIVDEE-GNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSS 478
Cdd:PRK06178 398 FKICDFEtGELLPLGAEGEIVVR-TPS----LLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 479 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvSHDPEALTRELQEHVktvtAPYKYPrKVAFISEL 558
Cdd:PRK06178 473 MSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGA-DLTAAALQAWCRENM----AVYKVP-EIRIVDAL 546
|
570
....*....|...
gi 88196780 559 PKTVSGKILRSKL 571
Cdd:PRK06178 547 PMTATGKVRKQDL 559
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
82-577 |
8.32e-59 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 203.98 E-value: 8.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 82 GSGTEvkWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAAR 161
Cdd:PRK08276 7 PSGEV--VTYGELEARSNRLAHGLR-ALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 162 VKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRsGDSMAiyFTSGTTGTPKMVEH 241
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETA-GADML--YSSGTTGRPKGIKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 242 SQcSYGLGFVASGRRLMALTesdiFWNTTDTGWV--------KAAWTLFSAWAN--GACVFVheLPQVDAQTILNTLCRF 311
Cdd:PRK08276 161 PL-PGLDPDEAPGMMLALLG----FGMYGGPDSVylspaplyHTAPLRFGMSALalGGTVVV--MEKFDAEEALALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 312 PITTICCVPTLF-RLLV--QEDLTRYKFQCLRHCLAGGEALNSDVR----DKWknqtGLEIHEGYGQSEtvlicGNfrGS 384
Cdd:PRK08276 234 RVTHSQLVPTMFvRMLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKramiDWW----GPIIHEYYASSE-----GG--GV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 385 TI--------KSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAIRiKPTRPFClfncYLDNPEKTAASEQG-DFYITGDR 455
Cdd:PRK08276 303 TVitsedwlaHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPFE----YHNDPEKTAAARNPhGWVTVGDV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 456 AHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSPAYVSHDPEALTREL 535
Cdd:PRK08276 377 GYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPADGADAGDALAAEL 454
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 88196780 536 QEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 577
Cdd:PRK08276 455 IAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWE 496
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
61-572 |
1.37e-58 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 205.23 E-value: 1.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 61 VWSQLEKTGHRPpnpAFWWVnGSGTevkwTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVV 140
Cdd:PRK05605 38 YDNAVARFGDRP---ALDFF-GATT----TYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 141 MIPGISQLTQKDLKYRLQ--AARVksIITSDALAPH---------------VDAISAdCPSLQS---RLLVSD--TSR-- 196
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEdhGARV--AIVWDKVAPTverlrrttpletivsVNMIAA-MPLLQRlalRLPIPAlrKARaa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 197 -----PGWINFRELLRVASPEH----NCLRTRSGDSMAIYFTSGTTGTPKMVEhsqcsyglgfvasgrrlmaLTESDIFW 267
Cdd:PRK05605 186 ltgpaPGTVPWETLVDAAIGGDgsdvSHPRPTPDDVALILYTSGTTGKPKGAQ-------------------LTHRNLFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 268 NTTD-TGWVK----------AAWTLFSAWANGAC----VFVHE----LPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ 328
Cdd:PRK05605 247 NAAQgKAWVPglgdgpervlAALPMFHAYGLTLCltlaVSIGGelvlLPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 329 E------DLTRykfqcLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQ 401
Cdd:PRK05605 327 AaeergvDLSG-----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 402 IVDEE--GNVLPPGKEGNIAIRiKPTRpfclFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSY 479
Cdd:PRK05605 402 IVDPEdpDETMPDGEEGELLVR-GPQV----FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 480 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEAltreLQEHVKTVTAPYKYPRKVAFISELP 559
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEG----LRAYCREHLTRYKVPRRFYHVDELP 551
|
570
....*....|...
gi 88196780 560 KTVSGKILRSKLR 572
Cdd:PRK05605 552 RDQLGKVRRREVR 564
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
86-574 |
3.47e-58 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 203.45 E-value: 3.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALAAA-GVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALAPHVDAISADCPSLQSRLLV----SDTSRPGWiNFRELLRVASPEhNCLRTRSGDSMAIYFTSGTTGTPKMV-- 239
Cdd:PRK06155 123 VVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGW-STAPLPPLDAPA-PAAAVQPGDTAAILYTSGTTGPSKGVcc 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 240 EHSQcSYGLGFVASgrRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVheLPQVDAQTILNTLCRFPITTI--- 316
Cdd:PRK06155 201 PHAQ-FYWWGRNSA--EDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATVTyll 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 317 -CCVPTLfrlLVQEDLTRYKFQCLRHCLAGGEAlnSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGSTiKSGSMGKAS 395
Cdd:PRK06155 276 gAMVSIL---LSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 396 PPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrPFCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVIN 475
Cdd:PRK06155 350 PGFEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 476 SSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRelqeHVKTVTAPYKYPRKVAFI 555
Cdd:PRK06155 428 RRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPVALVR----HCEPRLAYFAVPRYVEFV 502
|
490
....*....|....*....
gi 88196780 556 SELPKTVSGKILRSKLRNQ 574
Cdd:PRK06155 503 AALPKTENGKVQKFVLREQ 521
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
89-574 |
4.56e-58 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 202.03 E-value: 4.56e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 89 WTFEELGKQSRKAANILeGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITS 168
Cdd:PRK07514 29 YTYGDLDAASARLANLL-VALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 169 DALAPHVDAISADCPSlqSRLLVSDTSRPGwiNFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK--MVEHsqcsy 246
Cdd:PRK07514 108 PANFAWLSKIAAAAGA--PHVETLDADGTG--SLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLSH----- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 247 glGFVASGrrlmALTESDiFWnttdtgwvkaAWT----------------LFSA----WANGACVFVheLPQVDAQTILN 306
Cdd:PRK07514 179 --GNLLSN----ALTLVD-YW----------RFTpddvlihalpifhthgLFVAtnvaLLAGASMIF--LPKFDPDAVLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 307 TLCRfpITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGN-FRGS 384
Cdd:PRK07514 240 LMPR--ATVMMGVPTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNpYDGE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 385 TIkSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDG 462
Cdd:PRK07514 318 RR-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-GPN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDERG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 463 YFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRELQEHVktv 542
Cdd:PRK07514 392 YVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL--- 467
|
490 500 510
....*....|....*....|....*....|..
gi 88196780 543 tAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK07514 468 -ARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
90-575 |
1.47e-57 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 202.21 E-value: 1.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALA------------PHV------DAISADCPSLQS------RLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMA 225
Cdd:PRK08974 130 NFAhtlekvvfktpvKHViltrmgDQLSTAKGTLVNfvvkyiKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 226 -IYFTSGTTGTPK--MVEHS-------QCSYGLG-FVASGRRLM--ALTESDIFWNTTDtgwvkaawtlfsawangaCVF 292
Cdd:PRK08974 210 fLQYTGGTTGVAKgaMLTHRnmlanleQAKAAYGpLLHPGKELVvtALPLYHIFALTVN------------------CLL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 293 VHEL---------PQvDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTG 362
Cdd:PRK08974 272 FIELggqnllitnPR-DIPGFVKELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLTG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 363 LEIHEGYGQSE-TVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKT 441
Cdd:PRK08974 351 QYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK-GPQ----VMLGYWQRPEAT 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 442 AASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlsp 521
Cdd:PRK08974 426 DEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFV---- 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 88196780 522 ayVSHDPeALTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK08974 502 --VKKDP-SLTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
56-571 |
1.12e-56 |
|
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: 198.61 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 56 HDVLDVWSqLEKTGHRPPNPAFwwVNGS-GTEVkwTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVAC 134
Cdd:cd05904 4 DLPLDSVS-FLFASAHPSRPAL--IDAAtGRAL--TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 135 MRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVdaisadcPSLQSRLLVSDTSRPGWINFRELLrVASPEHN 214
Cdd:cd05904 78 LSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKL-------ASLALPVVLLDSAEFDSLSFSDLL-FEADEAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 215 CLRTRSG--DSMAIYFTSGTTGTPK--MVEHSqcsyglGFVASgrrlMALTESDIFWNTTDTGWVKAAWTLF-------- 282
Cdd:cd05904 150 PPVVVIKqdDVAALLYSSGTTGRSKgvMLTHR------NLIAM----VAQFVAGEGSNSDSEDVFLCVLPMFhiyglssf 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 283 --SAWANGACVFVheLPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLT-RYKFQCLRHCLAGGEALNSDVRDKWK- 358
Cdd:cd05904 220 alGLLRLGATVVV--MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRa 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 359 NQTGLEIHEGYGQSET---VLICGNFRGSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPtrpfCLFNCY 434
Cdd:cd05904 298 KFPNVDLGQGYGMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 435 LDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 512
Cdd:cd05904 373 LNNPEATAATidKEG-WLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 88196780 513 VKAFIVLSPAyvSHDPEAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd05904 452 PMAFVVRKPG--SSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
90-572 |
2.12e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 197.54 E-value: 2.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDAISADCPslqsrLLVSDTSR-PGWINFRELLRVASP---EHNClrtrsgdSMAIYFTSGTTGTPKMV-----E 240
Cdd:PRK13390 105 ALDGLAAKVGADLP-----LRLSFGGEiDGFGSFEAALAGAGPrltEQPC-------GAVMLYSSGTTGFPKGIqpdlpG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 241 HSQCSYGLGFVASGRRLMALTESDIFWNTTdtgwvkaawTLFSAWANGACVFVHEL-------PQVDAQTILNTLCRFPI 313
Cdd:PRK13390 173 RDVDAPGDPIVAIARAFYDISESDIYYSSA---------PIYHAAPLRWCSMVHALggtvvlaKRFDAQATLGHVERYRI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 314 TTICCVPTLF-RLLVQED--LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSE----TVLICGNFRGsti 386
Cdd:PRK13390 244 TVTQMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFIDSPDWLA--- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 387 KSGSMGKaSPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTRPFClfncYLDNPEKTAASEQ--GDFYIT-GDRAHMDEDGY 463
Cdd:PRK13390 321 HPGSVGR-SVLGDLHICDDDGNELPAGRIGTVYFE-RDRLPFR----YLNDPEKTAAAQHpaHPFWTTvGDLGSVDEDGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 464 FWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshDP-EALTRELQEHVKTV 542
Cdd:PRK13390 395 LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGI---RGsDELARELIDYTRSR 471
|
490 500 510
....*....|....*....|....*....|
gi 88196780 543 TAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK13390 472 IAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
90-573 |
5.17e-56 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 197.94 E-value: 5.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK07059 50 TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDAISADCP-------SLQSRL----------------LVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMA- 225
Cdd:PRK07059 129 NFATTVQQVLAKTAvkhvvvaSMGDLLgfkghivnfvvrrvkkMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVAf 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 226 IYFTSGTTGtpkmvehsqcsyglgfVASGrrlMALTESDIFWNTTDTGwvkaAWtLFSAWANGA----CVFVHELP--QV 299
Cdd:PRK07059 209 LQYTGGTTG----------------VSKG---ATLLHRNIVANVLQME----AW-LQPAFEKKPrpdqLNFVCALPlyHI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 300 DAQT---------------ILN---------TLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGEALNSDVR 354
Cdd:PRK07059 265 FALTvcgllgmrtggrnilIPNprdipgfikELKKYQVHIFPAVNTLYNaLLNNPDFDKLDFSKLIVANGGGMAVQRPVA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 355 DKWKNQTGLEIHEGYGQSET--VLICgNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFN 432
Cdd:PRK07059 345 ERWLEMTGCPITEGYGLSETspVATC-NPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-GPQ----VMA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 433 CYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGE 511
Cdd:PRK07059 419 GYWNRPDETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGE 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196780 512 VVKAFIvlspayVSHDPeALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PRK07059 499 AVKLFV------VKKDP-ALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
50-573 |
9.83e-56 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 197.02 E-value: 9.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 50 EYFNFAHDVLDvwSQLEKTGHRPPNPAFwwvngsGTEVkwTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWL 129
Cdd:PRK08751 22 EQFRTVAEVFA--TSVAKFADRPAYHSF------GKTI--TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 130 TIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQS---------------------- 187
Cdd:PRK08751 92 ATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVittglgdmlgfpkaalvnfvvk 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 188 --RLLVSDTSRPGWINFRELLRVASpEHNC--LRTRSGDSMAIYFTSGTTGTPKmvehsqcsyglGFVASGRRLMALTES 263
Cdd:PRK08751 172 yvKKLVPEYRINGAIRFREALALGR-KHSMptLQIEPDDIAFLQYTGGTTGVAK-----------GAMLTHRNLVANMQQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 264 DIFWNTTdTGWVKAA----------WTLFSAWAN-------GACVFVHELPQvDAQTILNTLCRFPITTICCVPTLFR-L 325
Cdd:PRK08751 240 AHQWLAG-TGKLEEGcevvitalplYHIFALTANglvfmkiGGCNHLISNPR-DMPGFVKELKKTRFTAFTGVNTLFNgL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 326 LVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVD 404
Cdd:PRK08751 318 LNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 405 EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGP 483
Cdd:PRK08751 398 DAGTVLAIGEIGELCIK-GPQ----VMKGYWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNVYP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 484 VEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlspayVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVS 563
Cdd:PRK08751 473 NEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVI------VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNV 546
|
570
....*....|
gi 88196780 564 GKILRSKLRN 573
Cdd:PRK08751 547 GKILRRELRD 556
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
71-574 |
2.04e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 195.77 E-value: 2.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 71 RPPNPAFWWVnGSGTevkwTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQ 150
Cdd:PRK07786 30 QPDAPALRFL-GNTT----TWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 151 KDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTS 230
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 231 GTTGTPK--MVEHSQCSyglGFVASGRRLMAL-TESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQVDAQTILNT 307
Cdd:PRK07786 184 GTTGRPKgaVLTHANLT---GQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 308 LCRFPITTICCVPTLFRLLVQEDLTRYKFQCLRhCLAGGEALNSD--VRDKWKNQTGLEIHEGYGQSE----TVLICGNf 381
Cdd:PRK07786 261 LEAEKVTGIFLVPAQWQAVCAEQQARPRDLALR-VLSWGAAPASDtlLRQMAATFPEAQILAAFGQTEmspvTCMLLGE- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 382 rGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDED 461
Cdd:PRK07786 339 -DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEATAEAFAGGWFHSGDLVRQDEE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 462 GYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRELQEHVkt 541
Cdd:PRK07786 413 GYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRL-- 490
|
490 500 510
....*....|....*....|....*....|...
gi 88196780 542 vtAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK07786 491 --ARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
53-568 |
5.11e-55 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 196.71 E-value: 5.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 53 NFAHDVLDVWsqLEKtghRPPNPAFWWVNG-SGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTI 131
Cdd:PRK10524 53 NLCHNAVDRH--LAK---RPEQLALIAVSTeTDEERTYTFRQLHDEVNRMAAMLR-SLGVQRGDRVLIYMPMIAEAAFAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 132 VACMRTGV---VMIPGISQltqKDLKYRLQAARVKSIITSDALA---------PHVDAISADCPSLQSRLLVSDtsrpgw 199
Cdd:PRK10524 127 LACARIGAihsVVFGGFAS---HSLAARIDDAKPVLIVSADAGSrggkvvpykPLLDEAIALAQHKPRHVLLVD------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 200 infRELL---RVASPEHN--CLRTRSGDSMA------------IYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTE 262
Cdd:PRK10524 198 ---RGLApmaRVAGRDVDyaTLRAQHLGARVpvewlesnepsyILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 263 SDIFWNTTDTGWVKA-AWTLFSAWANGACVFVHE-LP-QVDAqTILNTLC-RFPITTICCVPTLFRLLVQED---LTRYK 335
Cdd:PRK10524 275 GETFFCASDIGWVVGhSYIVYAPLLAGMATIMYEgLPtRPDA-GIWWRIVeKYKVNRMFSAPTAIRVLKKQDpalLRKHD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 336 FQCLRHC-LAG-----------GEALNSDVRDK-WKNQTG---LEIHEGYGQSETvlicgnfrgstiKSGSMGKASPPYD 399
Cdd:PRK10524 354 LSSLRALfLAGepldeptaswiSEALGVPVIDNyWQTETGwpiLAIARGVEDRPT------------RLGSPGVPMYGYN 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 400 VQIVDEE-GNVLPPGKEGNIAIRiKPTRPFCLFNCYLDNPE--KTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVIN 475
Cdd:PRK10524 422 VKLLNEVtGEPCGPNEKGVLVIE-GPLPPGCMQTVWGDDDRfvKTYWSLFGRqVYSTFDWGIRDADGYYFILGRTDDVIN 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 476 SSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPE---ALTRELQEHVKTVTAPYKYPRKV 552
Cdd:PRK10524 501 VAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREarlALEKEIMALVDSQLGAVARPARV 580
|
570
....*....|....*.
gi 88196780 553 AFISELPKTVSGKILR 568
Cdd:PRK10524 581 WFVSALPKTRSGKLLR 596
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
71-578 |
1.24e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 190.29 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 71 RPPNPAFWwVNGSGTEVkwTFEELGKQSRKAANILEGAcGLKPGDRLMLVL---PRLPE--WwltivACMRTGVVMIPGI 145
Cdd:PRK13391 10 TPDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLEvcW-----AAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 146 SQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLV-SDTSRPGWINFRELLRvASPEHNCLRTRSGDSM 224
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVA-GLPATPIADESLGTDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 225 aiYFTSGTTGTPKMVE----HSQCSYGLGFVASGRRLMALTESDIF------WNTTDTGWVKAAWTLfsawanGACVFVH 294
Cdd:PRK13391 160 --LYSSGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGFRSDMVYlspaplYHSAPQRAVMLVIRL------GGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 295 ElpQVDAQTILNTLCRFPITTICCVPTLF-RLLV--QEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQ 371
Cdd:PRK13391 232 E--HFDAEQYLALIEEYGVTHTQLVPTMFsRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 372 SETVLICG-NFRGSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAIriKPTRPFClfncYLDNPEKTAAS--EQGD 448
Cdd:PRK13391 310 TEGLGFTAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWF--EGGRPFE----YLNDPAKTAEArhPDGT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 449 FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDP 528
Cdd:PRK13391 383 WSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDG-VDPGP 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 88196780 529 EaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 578
Cdd:PRK13391 462 A-LAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
88-573 |
4.26e-53 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 188.25 E-value: 4.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILeGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIIT 167
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKL-AALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 SDALAphvDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASpehnclrtrsgdsmaIYFTSGTTGTPKMVehsQCSYG 247
Cdd:PRK03640 106 DDDFE---AKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVAT---------------IMYTSGTTGKPKGV---IQTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 LGFV-ASGRRL-MALTESDifwnttdtGWVkAAWTLF-----SAWAN----GACVFVHElpQVDAQTILNTLCRFPITTI 316
Cdd:PRK03640 165 NHWWsAVGSALnLGLTEDD--------CWL-AAVPIFhisglSILMRsviyGMRVVLVE--KFDAEKINKLLQTGGVTII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 317 CCVPT-LFRLLVQEDLTRY--KFQCLrhcLAGGEALNSDVRDKWKnQTGLEIHEGYGQSETV-LICG-NFRGSTIKSGSM 391
Cdd:PRK03640 234 SVVSTmLQRLLERLGEGTYpsSFRCM---LLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETAsQIVTlSPEDALTKLGSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 392 GKASPPYDVQIVDEeGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRND 471
Cdd:PRK03640 310 GKPLFPCELKIEKD-GVVVPPFEEGEIVVK-GPN----VTKGYLNREDATRETFQDGWFKTGDIGYLDEEGFLYVLDRRS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 472 DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayvSHDPEAltrELQEHVKTVTAPYKYPRK 551
Cdd:PRK03640 384 DLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS----GEVTEE---ELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|..
gi 88196780 552 VAFISELPKTVSGKILRSKLRN 573
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQ 478
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-574 |
5.27e-53 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 188.15 E-value: 5.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 84 GTEVKWTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVK 163
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 164 SIITSDALAPHVDAISAdcpslqsrllVSDTSRPGWINFRELLRVASPEhNCLRTRSGDSMAIYFTSGTTGTPKmvehsq 243
Cdd:PRK06839 103 VLFVEKTFQNMALSMQK----------VSYVQRVISITSLKEIEDRKID-NFVEKNESASFIICYTSGTTGKPK------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 csyglGFVasgrrlmaLTESDIFWN------TTDTGWVKAAWTL-------------FSAWANGACVFVHElpQVDAQTI 304
Cdd:PRK06839 166 -----GAV--------LTQENMFWNalnntfAIDLTMHDRSIVLlplfhiggiglfaFPTLFAGGVIIVPR--KFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 305 LNTLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQtGLEIHEGYGQSET-----VLIC 378
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETsptvfMLSE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 379 GNFRGstiKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHM 458
Cdd:PRK06839 310 EDARR---KVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRPDATEETIQDGWLCTGDLARV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 459 DEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVshdpeALTRELQEH 538
Cdd:PRK06839 382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSV-----LIEKDVIEH 456
|
490 500 510
....*....|....*....|....*....|....*.
gi 88196780 539 VKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK06839 457 CRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
90-575 |
5.90e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 189.86 E-value: 5.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQ-KLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDAISADC----------------------PSLQSR-----LLVSDTSRPGWINFRELLRVASPEHNClrTRSGD 222
Cdd:PRK06710 130 LVFPRVTNVQSATkiehvivtriadflpfpknllyPFVQKKqsnlvVKVSESETIHLWNSVEKEVNTGVEVPC--DPEND 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 223 SMAIYFTSGTTGTPKmvehsqcsyglGFVASGRRLMALTESDIFW--NTTD-TGWVKAAWTLFSAWANGACVFVHEL--- 296
Cdd:PRK06710 208 LALLQYTGGTTGFPK-----------GVMLTHKNLVSNTLMGVQWlyNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMqgy 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 297 -----PQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTR-YKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYG 370
Cdd:PRK06710 277 kmvliPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKeYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 371 QSETVLIC-GNFRGSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD 448
Cdd:PRK06710 357 LTESSPVThSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK-GPQ----IMKGYWNKPEETAAVLQDG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 449 FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvSHDP 528
Cdd:PRK06710 432 WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVL-----KEGT 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 88196780 529 EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK06710 507 ECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-572 |
4.79e-52 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 186.90 E-value: 4.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDA------------LAPHV------DAISADCPSLQSRLLVSDTSRPGWINFRELLRVA---SPEHNCLRT---RSG 221
Cdd:PRK12583 122 ICADAfktsdyhamlqeLLPGLaegqpgALACERLPELRGVVSLAPAPPPGFLAWHELQARGetvSREALAERQaslDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 222 DSMAIYFTSGTTGTPK--MVEHSQCSYGLGFVAsgrRLMALTESDI------FWNTTdtGWVKAAwtlFSAWANGACVfV 293
Cdd:PRK12583 202 DPINIQYTSGTTGFPKgaTLSHHNILNNGYFVA---ESLGLTEHDRlcvpvpLYHCF--GMVLAN---LGCMTVGACL-V 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 294 HELPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGL-EIHEGYGQ 371
Cdd:PRK12583 273 YPNEAFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 372 SET---VLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAirikpTRPFCLFNCYLDNPEKTAASEQGD 448
Cdd:PRK12583 353 TETspvSLQTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMKGYWNNPEATAESIDED 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 449 FYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshD 527
Cdd:PRK12583 428 GWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHP-----G 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 88196780 528 PEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK12583 503 HAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
87-572 |
1.74e-51 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 186.70 E-value: 1.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 87 VKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVM-I------PGISQLtqkdlkyrLQA 159
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLH-SLGVGPGDVVAFLLPNLPETHFALWGGEAAGIANpInpllepEQIAEL--------LRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 160 ARVKSIIT------SDaLAPHVDAISADCPSLQSRLLVsDTSR--PGW----------------INF-RELLRVASPEHN 214
Cdd:PRK07529 128 AGAKVLVTlgpfpgTD-IWQKVAEVLAALPELRTVVEV-DLARylPGPkrlavplirrkahariLDFdAELARQPGDRLF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 215 CLRTRSGDSMAIYF-TSGTTGTPKMVEHSqcsYGlGFVA---SGRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWANGA 289
Cdd:PRK07529 206 SGRPIGPDDVAAYFhTGGTTGMPKLAQHT---HG-NEVAnawLGALLLGLGPGDTVFCGLPLFHVNALLvTGLAPLARGA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 290 CVfVHELPQ--------------VDaqtilntlcRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRD 355
Cdd:PRK07529 282 HV-VLATPQgyrgpgvianfwkiVE---------RYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 356 KWKNQTGLEIHEGYGQSE-TVLICGNFRGSTIKSGSMGKASPPYDVQIV--DEEGNVL---PPGKEGNIAIRiKPTrpfc 429
Cdd:PRK07529 352 RFEAATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GPN---- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 430 LFNCYLdNPEKTAASE-QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPI 508
Cdd:PRK07529 427 VFSGYL-EAAHNKGLWlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAH 505
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196780 509 RGEVVKAFIVLSP-AYVSHDpealtrELQEHVKTVTA-PYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK07529 506 AGELPVAYVQLKPgASATEA------ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
91-576 |
1.95e-51 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 184.13 E-value: 1.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 91 FEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQ--AARVkSIITS 168
Cdd:PRK12406 14 FDELAQRAARAAGGLA-ALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEdsGARV-LIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 169 DALAPHVDAISADC--------PSLQSRLLVSD---TSRPGWINFRELLrVASPEHNCLRTRSGDSMaIYfTSGTTGTPK 237
Cdd:PRK12406 92 DLLHGLASALPAGVtvlsvptpPEIAAAYRISPallTPPAGAIDWEGWL-AQQEPYDGPPVPQPQSM-IY-TSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 238 MV-------EHSQcSYGL------GFVASGRRLMA--LTESdifwnttdtgwVKAAWTLFSAWANGACVFvheLPQVDAQ 302
Cdd:PRK12406 169 GVrraaptpEQAA-AAEQmraliyGLKPGIRALLTgpLYHS-----------APNAYGLRAGRLGGVLVL---QPRFDPE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 303 TILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKF--QCLRHCLAGGEALNSDVR----DKWknqtGLEIHEGYGQSETV 375
Cdd:PRK12406 234 ELLQLIERHRITHMHMVPTMFiRLLKLPEEVRAKYdvSSLRHVIHAAAPCPADVKramiEWW----GPVIYEYYGSTESG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 376 LIcgNFRGST---IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFClfncYLDNPEKTAASEQGDFYIT 452
Cdd:PRK12406 310 AV--TFATSEdalSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFT----YHNKPEKRAEIDRGGFITS 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 453 GDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALT 532
Cdd:PRK12406 384 GDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLDEADIR 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 88196780 533 RELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK12406 463 AQLKARL----AGYKVPKHIEIMAELPREDSGKIFKRRLRDPYW 502
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
75-575 |
2.21e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 185.35 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 75 PAFwwvngSGTEVKWTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLK 154
Cdd:PRK05677 41 PAF-----SNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 155 YRLQAARVKSIIT-------SDALAPHVD---AISADCPSLQS---RLLVSDTSR-----------PGWINFRELL---- 206
Cdd:PRK05677 116 HQFNDSGAKALVClanmahlAEKVLPKTGvkhVIVTEVADMLPplkRLLINAVVKhvkkmvpayhlPQAVKFNDALakga 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 207 RVASPEHNClrtRSGDSMAIYFTSGTTGTPK--MVEHSQcsyglgFVASGRRLMALTESDIfwnttDTGW--VKAAWTLF 282
Cdd:PRK05677 196 GQPVTEANP---QADDVAVLQYTGGTTGVAKgaMLTHRN------LVANMLQCRALMGSNL-----NEGCeiLIAPLPLY 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 283 SAWA-NGACVFV-----HEL----PQvDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNS 351
Cdd:PRK05677 262 HIYAfTFHCMAMmlignHNIlisnPR-DLPAMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 352 DVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGStIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcL 430
Cdd:PRK05677 341 ATAERWKEVTGCAICEGYGMTETSpVVSVNPSQA-IQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GPQ----V 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 431 FNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIR 509
Cdd:PRK05677 415 MKGYWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKS 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 88196780 510 GEVVKAFIVLSPAyvshdpEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK05677 495 GEAIKVFVVVKPG------ETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
88-572 |
5.39e-51 |
|
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: 180.62 E-value: 5.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILeGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKsiit 167
Cdd:cd05912 1 SYTFAELFEEVSRLAEHL-AALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 sdalaphVDAIsadcpslqsrllvsdtsrpgwinfrellrvaspehnclrtrsgdsMAIYFTSGTTGTPKMVEHS----- 242
Cdd:cd05912 76 -------LDDI---------------------------------------------ATIMYTSGTTGKPKGVQQTfgnhw 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 243 ----QCSYGLGFVASGRRLMALTesdIFWnttdtgwVKAAWTLFSAWANGACVFVHElpQVDAQTILNTLCRFPITTICC 318
Cdd:cd05912 104 wsaiGSALNLGLTEDDNWLCALP---LFH-------ISGLSILMRSVIYGMTVYLVD--KFDAEQVLHLINSGKVTIISV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 319 VPTLFRLLVQEDLTRY--KFQCLrhcLAGGEALNSDVRDKWKnQTGLEIHEGYGQSETV--LICGNFRGSTIKSGSMGKA 394
Cdd:cd05912 172 VPTMLQRLLEILGEGYpnNLRCI---LLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 395 SPPYDVQIVDEEGnvlPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVI 474
Cdd:cd05912 248 LFPVELKIEDDGQ---PPYEVGEILLK-GPN----VTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 475 NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDpealtrELQEHVKTVTAPYKYPRKVAF 554
Cdd:cd05912 320 ISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEE------ELIAYCSEKLAKYKVPKKIYF 392
|
490
....*....|....*...
gi 88196780 555 ISELPKTVSGKILRSKLR 572
Cdd:cd05912 393 VDELPRTASGKLLRHELK 410
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-577 |
6.55e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 183.26 E-value: 6.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 71 RPPNPAFWWVNGSgtevkWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQ 150
Cdd:PRK06188 25 YPDRPALVLGDTR-----LTYGQLADRISRYIQAFE-ALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 151 KDLKYRLQAARVKSIITSDAlaPHVD---AISADCPSLQSRLLVSDTsrPGWINFRELLRVASPEHNCLRTRSGDSMAIY 227
Cdd:PRK06188 99 DDHAYVLEDAGISTLIVDPA--PFVEralALLARVPSLKHVLTLGPV--PDGVDLLAAAAKFGPAPLVAAALPPDIAGLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 228 FTSGTTGTPKMVEHSQcsyglgfvasgRRLMALTEsdifWNTTDTGWVKAAWTLFSA---WANGACV--------FVHEL 296
Cdd:PRK06188 175 YTGGTTGKPKGVMGTH-----------RSIATMAQ----IQLAEWEWPADPRFLMCTplsHAGGAFFlptllrggTVIVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 297 PQVDAQTILNTLCRFPITTICCVPT-LFRLLVQEDLTRYKFQCLRHCLAGGEALNSDvrdkwKNQTGLEI-----HEGYG 370
Cdd:PRK06188 240 AKFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPV-----RLAEAIERfgpifAQYYG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 371 QSE-----TVLICGNFRGSTIK-SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptRPFcLFNCYLDNPEKTAAS 444
Cdd:PRK06188 315 QTEapmviTYLRKRDHDPDDPKrLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR----GPL-VMDGYWNRPEETAEA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 445 EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyV 524
Cdd:PRK06188 390 FRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-A 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 88196780 525 SHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 577
Cdd:PRK06188 469 AVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWE 517
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
65-572 |
1.06e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 182.55 E-value: 1.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 65 LEKTGHRPPN-PAFWWvngsGTEVkWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIP 143
Cdd:PRK07470 13 LRQAARRFPDrIALVW----GDRS-WTWREIDARVDALAAALA-ARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 144 GISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLqsRLLVSDTSRPGWINFRELLR--------VASPEHNc 215
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDL--THVVAIGGARAGLDYEALVArhlgarvaNAAVDHD- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 216 lrtrsgDSMAIYFTSGTTGTPK--MVEHSQcsygLGFVASGRRlmalteSDIFWNTT--DTGWVKAAWTlfsawaNGACV 291
Cdd:PRK07470 164 ------DPCWFFFTSGTTGRPKaaVLTHGQ----MAFVITNHL------ADLMPGTTeqDASLVVAPLS------HGAGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 292 fvHELPQV--DAQTILNTLCRFPI------------TTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDK 356
Cdd:PRK07470 222 --HQLCQVarGAATVLLPSERFDPaevwalverhrvTNLFTVPTILKMLVEhPAVDRYDHSSLRYVIYAGAPMYRADQKR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 357 WKNQTGLEIHEGYGQSE-----TVL-ICGNFR--GSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrpf 428
Cdd:PRK07470 300 ALAKLGKVLVQYFGLGEvtgniTVLpPALHDAedGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPA---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 429 cLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPI 508
Cdd:PRK07470 376 -VFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPV 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 88196780 509 RGEVVKAFIVLS-PAYVSHDpealtrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK07470 455 WGEVGVAVCVARdGAPVDEA------ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-572 |
1.17e-50 |
|
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: 177.86 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 222 DSMAIYFTSGTTGTPK--MVEHsqcsYGL---GFVAsGRRlMALTESDI----------FwnttdtGWVKAawTLFSAWA 286
Cdd:cd05917 3 DVINIQFTSGTTGSPKgaTLTH----HNIvnnGYFI-GER-LGLTEQDRlcipvplfhcF------GSVLG--VLACLTH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 287 NGACVFVHelPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGL-E 364
Cdd:cd05917 69 GATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 365 IHEGYGQSETVLICGN-FRGSTI--KSGSMGKASPPYDVQIVDEEGNVLPP-GKEGNIAIRikptrPFCLFNCYLDNPEK 440
Cdd:cd05917 147 VTIAYGMTETSPVSTQtRTDDSIekRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 441 TAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 519
Cdd:cd05917 222 TAEAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 88196780 520 SPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05917 302 KE-----GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-502 |
1.70e-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: 179.38 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqkdLKYRLQAARVKSIITsD 169
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVP---------LDPAYPAERLAFILE-D 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDAISADCPSLQSRLLVSDTSRPGWINFREllRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK--MVEHSQCSYg 247
Cdd:TIGR01733 71 AGARLLLTDSALASRLAGLVLPVILLDPLELAALD--DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKgvVVTHRSLVN- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 lgFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVheLPQVDAQTILNTLCRF----PITTICCVPTLF 323
Cdd:TIGR01733 148 --LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVV--PPEDEERDDAALLAALiaehPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 RLLVQEDLTRykFQCLRHCLAGGEALNSDVRDKWKNQTG-LEIHEGYGQSETVLICGNFRGSTIKSGSM-----GKASPP 397
Cdd:TIGR01733 224 ALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDPDDAPREspvpiGRPLAN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 398 YDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAA---------SEQGDFYITGDRAHMDEDGYFWFVG 468
Cdd:TIGR01733 302 TRLYVLDDDLRPVPVGVVGELYIGGP-----GVARGYLNRPELTAErfvpdpfagGDGARLYRTGDLVRYLPDGNLEFLG 376
|
410 420 430
....*....|....*....|....*....|....
gi 88196780 469 RNDDVINSSSYRIGPVEVESALAEHPAVlESAVV 502
Cdd:TIGR01733 377 RIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
110-572 |
6.88e-50 |
|
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: 178.79 E-value: 6.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 110 GLKPGDRLMLVLPRLPEW-WLT---IVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSL 185
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELSfavAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 186 QSRLLVSdtsrpGWINFRELLRVASPEHNclrtrsgDSMAIYFTSGTTGTPK--MVEHSQCSYGLGFVASgrrLMALTES 263
Cdd:cd05922 94 GTVLDAD-----GIRAARASAPAHEVSHE-------DLALLLYTSGSTGSPKlvRLSHQNLLANARSIAE---YLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 264 DIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQVDAQTIlnTLCR-FPITTICCVPTLFRLLVQEDLTRYKFQCLRHC 342
Cdd:cd05922 159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFW--EDLReHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 343 L-AGG---EALNSDVRDKWKnqtGLEIHEGYGQSETvlicgnFRGSTI--------KSGSMGKASPPYDVQIVDEEGNVL 410
Cdd:cd05922 237 TqAGGrlpQETIARLRELLP---GAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 411 PPGKEGNIAirikPTRPFCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESAL 490
Cdd:cd05922 308 PPGEPGEIV----HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 491 AEHPAVLESAVVSSPDPIrGEVVKAFIVLSPAYvshDPEALTRELQEhvktVTAPYKYPRKVAFISELPKTVSGKILRSK 570
Cdd:cd05922 384 RSIGLIIEAAAVGLPDPL-GEKLALFVTAPDKI---DPKDVLRSLAE----RLPPYKVPATVRVVDELPLTASGKVDYAA 455
|
..
gi 88196780 571 LR 572
Cdd:cd05922 456 LR 457
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
86-571 |
1.66e-48 |
|
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: 175.59 E-value: 1.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:cd05920 38 DRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALAPhvdaisadcpsLQSRLLvsdtsrpgwinFRELLRvASPEHNCLRtrsgdsmaiyFTSGTTGTPKMVEHSQCS 245
Cdd:cd05920 117 IVPDRHAG-----------FDHRAL-----------ARELAE-SIPEVALFL----------LSGGTTGTPKLIPRTHND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 246 YGLGFVASGRrLMALTESDIFW--NTTDTGWVKAAWTLFSAWANGACVFVHelPQVDAQTILNTLCRFPITTICCVPTLF 323
Cdd:cd05920 164 YAYNVRASAE-VCGLDQDTVYLavLPAAHNFPLACPGVLGTLLAGGRVVLA--PDPSPDAAFPLIEREGVTVTALVPALV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 RLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRGS-TIKSGSMGKASPPYD-V 400
Cdd:cd05920 241 SLWLDAaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDPdEVIIHTQGRPMSPDDeI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 401 QIVDEEGNVLPPGKEGNIAIRIKPTrpfclFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFVGRNDDVINSSS 478
Cdd:cd05920 321 RVVDEEGNPVPPGEEGELLTRGPYT-----IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPDGYLVVEGRIKDQINRGG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 479 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShdpealTRELQEHVKTV-TAPYKYPRKVAFISE 557
Cdd:cd05920 395 EKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPS------AAQLRRFLRERgLAAYKLPDRIEFVDS 468
|
490
....*....|....
gi 88196780 558 LPKTVSGKILRSKL 571
Cdd:cd05920 469 LPLTAVGKIDKKAL 482
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-573 |
1.91e-48 |
|
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: 176.28 E-value: 1.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 81 NGSGTEVKWTFEELGKQSRKAANILEGAcGLKPGDR---LMLVLPRLPEWWLTiVACMrtGVVMIPGISQLTQKDLKYRL 157
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDRvatLAWNTHRHLELYYA-VPGM--GAVLHTINPRLFPEQIAYII 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 158 QAARVKSIITSDALAPHVDAISADCPSLQSRLLVSD------TSRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSG 231
Cdd:cd12119 94 NHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDdaampePAGVGVLAYEELLAAESPEYDWPDFDENTAAAICYTSG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 232 TTGTPKMVEHSQCS---YGLGFVASGrrLMALTESDIFWNTTDTGWVkAAWTL-FSAWANGACvFVHELPQVDAQTILNT 307
Cdd:cd12119 174 TTGNPKGVVYSHRSlvlHAMAALLTD--GLGLSESDVVLPVVPMFHV-NAWGLpYAAAMVGAK-LVLPGPYLDPASLAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 308 LCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKnQTGLEIHEGYGQSET--VLICGNFRGS 384
Cdd:cd12119 250 IEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFE-ERGVRVIHAWGMTETspLGTVARPPSE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 385 TIKSGSMGKAS-------PPYDVQ--IVDEEGNVLP-PGKE-GNIAIRikptRPFcLFNCYLDNPEKTAASEQGDFYITG 453
Cdd:cd12119 329 HSNLSEDEQLAlrakqgrPVPGVElrIVDDDGRELPwDGKAvGELQVR----GPW-VTKSYYKNDEESEALTEDGWLRTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 454 DRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP-AYVSHDpealt 532
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEgATVTAE----- 478
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 88196780 533 rELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd12119 479 -ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
56-574 |
8.12e-48 |
|
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: 174.95 E-value: 8.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 56 HDVLDVWSQlektgHRPPNPAFwwVNGsgtEVKWTFEELGKQS-RKAANILEGacGLKPGDRLMLVLPRLPEWWLTIVAC 134
Cdd:COG1021 28 GDLLRRRAE-----RHPDRIAV--VDG---ERRLSYAELDRRAdRLAAGLLAL--GLRPGDRVVVQLPNVAEFVIVFFAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 135 MRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD-----ALAPHVDAISADCPSLQSRLLVSDTSrpGWINFRELLrvA 209
Cdd:COG1021 96 FRAGAIPVFALPAHRRAEISHFAEQSEAVAYIIPDrhrgfDYRALARELQAEVPSLRHVLVVGDAG--EFTSLDALL--A 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 210 SPEHNCLRTRSGDSMAIYFTS-GTTGTPKMVEHSQCSYGLGFVASGRrLMALTESDIFWnttdtgwvkAA---------- 278
Cdd:COG1021 172 APADLSEPRPDPDDVAFFQLSgGTTGLPKLIPRTHDDYLYSVRASAE-ICGLDADTVYL---------AAlpaahnfpls 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 279 -WTLFSAWANGACVFVHELPqvDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDK 356
Cdd:COG1021 242 sPGVLGVLYAGGTVVLAPDP--SPDTAFPLIERERVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 357 WKNQTGLEIHEGYGQSETvLICGnfrgsT-------IKSGSMGKASPPYD-VQIVDEEGNVLPPGKEGNIAIRIKPTrpf 428
Cdd:COG1021 320 VRPALGCTLQQVFGMAEG-LVNY-----TrlddpeeVILTTQGRPISPDDeVRIVDEDGNPVPPGEVGELLTRGPYT--- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 429 clFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPD 506
Cdd:COG1021 391 --IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPD 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 507 PIRGEVVKAFIVLspayvshDPEALT-RELQEHVKTV-TAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:COG1021 468 EYLGERSCAFVVP-------RGEPLTlAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
90-575 |
1.97e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 173.96 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILeGACGLKPGDRlMLVLPRLPEWW-LTIVACMRTGVVMI---PGIS--QLtqKDLkyrlqAAR-- 161
Cdd:PRK07788 76 TYAELDEQSNALARGL-LALGVRAGDG-VAVLARNHRGFvLALYAAGKVGARIIllnTGFSgpQL--AEV-----AAReg 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 162 VKSIITSDALAPHVDAISADCPSLQSRLLVSD---TSRPGWINFRELlrVASPEHNCLRTRSGDSMAIYFTSGTTGTPKM 238
Cdd:PRK07788 147 VKALVYDDEFTDLLSALPPDLGRLRAWGGNPDddePSGSTDETLDDL--IAGSSTAPLPKPPKPGGIVILTSGTTGTPKG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 239 VEHSQCSyGLGFVAS-------GRRLMALTESDIFWNTtdtGWvkAAWTLfsAWANGACVFVHElpQVDAQTILNTLCRF 311
Cdd:PRK07788 225 APRPEPS-PLAPLAGllsrvpfRAGETTLLPAPMFHAT---GW--AHLTL--AMALGSTVVLRR--RFDPEATLEDIAKH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 312 PITTICCVPTLFRLLV---QEDLTRYKFQCLRHCLAGGEALNSDVrdkwknqtGLEIHEGYGQsetvLICgNFRGST--- 385
Cdd:PRK07788 295 KATALVVVPVMLSRILdlgPEVLAKYDTSSLKIIFVSGSALSPEL--------ATRALEAFGP----VLY-NLYGSTeva 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 386 -----------IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIairikptrpFC----LFNCYLDNPEKtaasEQGDFY 450
Cdd:PRK07788 362 fatiatpedlaEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRI---------FVgngfPFEGYTDGRDK----QIIDGL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 451 I-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpE 529
Cdd:PRK07788 429 LsSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG------A 502
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 88196780 530 ALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK07788 503 ALDEDaIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
86-572 |
8.89e-47 |
|
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: 170.99 E-value: 8.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALAPHVDAISADcpslqsrllVSDTSRPGWINFRELLRVASPEHNCLrtrsgdSMAIYfTSGTTGTPK--MVEHSQ 243
Cdd:cd17651 97 LTHPALAGELAVELVA---------VTLLDQPGAAAGADAEPDPALDADDL------AYVIY-TSGSTGRPKgvVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 CsygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFVHELPQVDAQTILNTLCRFPITtICCVPTL 322
Cdd:cd17651 161 L---ANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATlVLPPEEVRTDPPALAAWLDEQRIS-RVFLPTV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 323 FRLLVQEDLTRYKFQ--CLRHCLAGGEAL--NSDVRDKWKNQTGLEIHEGYGQSET-VLICGNFRGSTIKSG---SMGKA 394
Cdd:cd17651 237 ALRALAEHGRPLGVRlaALRYLLTGGEQLvlTEDLREFCAGLPGLRLHNHYGPTEThVVTALSLPGDPAAWPappPIGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 395 SPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAA-------SEQGDFYITGDRAHMDEDGYFWFV 467
Cdd:cd17651 317 IDNTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAErfvpdpfVPGARMYRTGDLARWLPDGELEFL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 468 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRELQEHVktvtAPYK 547
Cdd:cd17651 392 GRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-APVDAAELRAALATHL----PEYM 466
|
490 500
....*....|....*....|....*
gi 88196780 548 YPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd17651 467 VPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
63-571 |
1.71e-46 |
|
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: 170.15 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 63 SQLEKTGHRPpnpAFWWvngsgTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMI 142
Cdd:cd17646 6 EQAARTPDAP---AVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 143 PGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRLLVSDTSRPGwinfrellRVASPEHnclrtrsgd 222
Cdd:cd17646 77 PLDPGYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPL--------VPPRPDN--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 223 smAIY--FTSGTTGTPK--MVEHS---------QCSYGLGfvASGRRLMAltesdifwntTDTGWVKAAWTLFSAWANGA 289
Cdd:cd17646 140 --LAYviYTSGSTGRPKgvMVTHAgivnrllwmQDEYPLG--PGDRVLQK----------TPLSFDVSVWELFWPLVAGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 290 CVFVHElP--QVDAQTILNTLCRFPITTICCVPTLFRLLVQEdLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHE 367
Cdd:cd17646 206 RLVVAR-PggHRDPAYLAALIREHGVTTCHFVPSMLRVFLAE-PAAGSCASLRRVFCSGEALPPELAARFLALPGAELHN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 368 GYGQSETVL------ICGNFRGSTIksgSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIR-IKPTRPfclfncYLDNPEK 440
Cdd:cd17646 284 LYGPTEAAIdvthwpVRGPAETPSV---PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGgVQLARG------YLGRPAL 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 441 TAAS------EQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVV 513
Cdd:cd17646 355 TAERfvpdpfGPGSrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARL 434
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 88196780 514 KAFIVLSPAYVSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17646 435 VGYVVPAAGAAGPDTAALRAHLAERL----PEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
86-565 |
3.04e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 170.45 E-value: 3.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALAPHVDAISADCPSLQSRLLVSDTS----RPGWINFRELLRVASPEHNcLRTRSGDSMAIYFTSGTTGTPK--MV 239
Cdd:PRK07798 105 VYEREFAPRVAEVLPRLPKLRTLVVVEDGSgndlLPGAVDYEDALAAGSPERD-FGERSPDDLYLLYTGGTTGMPKgvMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 240 EHSQCsyglgFVAS--GRRLM----ALTESDIFWNTTDTG---WVKAA--------WTLFSAWANGACVFVHELPQVDAQ 302
Cdd:PRK07798 184 RQEDI-----FRVLlgGRDFAtgepIEDEEELAKRAAAGPgmrRFPAPplmhgagqWAAFAALFSGQTVVLLPDVRFDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 303 TILNTLCRFPITTICCVPTLF-RLLVQE--DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSETvlic 378
Cdd:PRK07798 259 EVWRTIEREKVNVITIVGDAMaRPLLDAleARGPYDLSSLFAIASGGALFSPSVKEALLELlPNVVLTDSIGSSET---- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 379 GNFRGSTIKSGSMGKASPPY----DVQIVDEEGNVLPPG--------KEGNIAIRikptrpfclfncYLDNPEKTAAS-- 444
Cdd:PRK07798 335 GFGGSGTVAKGAVHTGGPRFtigpRTVVLDEDGNPVEPGsgeigwiaRRGHIPLG------------YYKDPEKTAETfp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 445 -EQGDFY-ITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPA 522
Cdd:PRK07798 403 tIDGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG 482
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 88196780 523 yVSHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 565
Cdd:PRK07798 483 -ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-578 |
1.13e-45 |
|
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: 173.50 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqLtqkD-------LKYRLQ 158
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLR-ALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVP----L---DpaypaerLAYMLE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 159 AARVKSIITSDALAPHVdaisadcPSLQSRLLVSDTSRPGwinfrellrvASPEHNCLRTRSGDSMA-IYFTSGTTGTPK 237
Cdd:COG1020 571 DAGARLVLTQSALAARL-------PELGVPVLALDALALA----------AEPATNPPVPVTPDDLAyVIYTSGSTGRPK 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 238 --MVEHSqcsyGLG-FVASGRRLMALTESDIF-WNTT---DTgwvkAAWTLFSAWANGAC-VFVHELPQVDAQTILNTLC 309
Cdd:COG1020 634 gvMVEHR----ALVnLLAWMQRRYGLGPGDRVlQFASlsfDA----SVWEIFGALLSGATlVLAPPEARRDPAALAELLA 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 310 RFPITTICCVPTLFRLLVQEDLTRykFQCLRHCLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSETVlICGNFRgsTIKS 388
Cdd:COG1020 706 RHRVTVLNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETT-VDSTYY--EVTP 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 389 GSMGKASPPY-------DVQIVDEEGNVLPPGKEGNIAI------RikptrpfclfnCYLDNPEKTAA-------SEQGD 448
Cdd:COG1020 781 PDADGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELYIggaglaR-----------GYLNRPELTAErfvadpfGFPGA 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 449 -FYITGDRAHMDEDGYFWFVGRNDD-V-INssSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvs 525
Cdd:COG1020 850 rLYRTGDLARWLPDGNLEFLGRADDqVkIR--GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA---- 923
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 88196780 526 hDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 578
Cdd:COG1020 924 -GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA 975
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
89-578 |
3.92e-45 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 167.62 E-value: 3.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 89 WTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSII-- 166
Cdd:PRK06087 50 YTYSALDHAASRLANWLL-AKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFap 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 167 TSDALAPHVD---AISADCPSLQSRLLVsDTSRPGW--INFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPK--MV 239
Cdd:PRK06087 129 TLFKQTRPVDlilPLQNQLPQLQQIVGV-DKLAPATssLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKgvML 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 240 EHSQcsyglgFVASGRRLMA---LTESDIFWnttdtgwvkaawtlFSAWANGACVFVHELPQ---VDAQTILntLCRF-P 312
Cdd:PRK06087 208 THNN------ILASERAYCArlnLTWQDVFM--------------MPAPLGHATGFLHGVTApflIGARSVL--LDIFtP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 313 ITTI-------C-CV----PTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSD-VRDKWknQTGLEIHEGYGQSETV-LIC 378
Cdd:PRK06087 266 DACLalleqqrCtCMlgatPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKvARECQ--QRGIKLLSVYGSTESSpHAV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 379 GNFRGSTIKSGSM-GKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAAS--EQGDFYiTGDR 455
Cdd:PRK06087 344 VNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGEEASR-GPN----VFMGYLDEPELTARAldEEGWYY-SGDL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 456 AHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTREL 535
Cdd:PRK06087 418 CRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEEVVAFF 497
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 88196780 536 QEhvKTVtAPYKYPRKVAFISELPKTVSGKILRSKLRnQEWGR 578
Cdd:PRK06087 498 SR--KRV-AKYKYPEHIVVIDKLPRTASGKIQKFLLR-KDIMR 536
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
88-574 |
4.62e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 166.52 E-value: 4.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEGAcGLKPGDRLMlVLPRLPEWWLTI-VACMRTGVVMIPgisqltqkdLKYRLQAarvksii 166
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRR-GCVDGERLA-VLARNSVWLVALhFACARVGAIYVP---------LNWRLSA------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 167 tsdalaPHVDAISADCpslQSRLLVSDTS----RPGWINFrELLRVASPEHNCLRTRSGDSMA---IYFTSGTTGTPKMV 239
Cdd:PRK09088 84 ------SELDALLQDA---EPRLLLGDDAvaagRTDVEDL-AAFIASADALEPADTPSIPPERvslILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 240 ---EHSQCSYGLGFVASGR---RLMALTESDIFwnttdtGWVKAAWTLFSAWANGACVFVHelPQVDAQTILNTLC--RF 311
Cdd:PRK09088 154 mlsERNLQQTAHNFGVLGRvdaHSSFLCDAPMF------HIIGLITSVRPVLAVGGSILVS--NGFEPKRTLGRLGdpAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 312 PITTICCVPTLFRLLvqEDLTRYKFQCLRHCLA----GGEALNSDVRdKWKNQtGLEIHEGYGQSE--TVL----ICGNF 381
Cdd:PRK09088 226 GITHYFCVPQMAQAF--RAQPGFDAAALRHLTAlftgGAPHAAEDIL-GWLDD-GIPMVDGFGMSEagTVFgmsvDCDVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 382 RGstiKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDE 460
Cdd:PRK09088 302 RA---KAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 461 DGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShDPEaltrELQEHVK 540
Cdd:PRK09088 374 DGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPL-DLE----RIRSHLS 448
|
490 500 510
....*....|....*....|....*....|....
gi 88196780 541 TVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK09088 449 TRLAKYKVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
86-571 |
6.47e-45 |
|
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: 165.84 E-value: 6.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALAPHVDAisadcpsLQSRLLVSDTSRPGwinfrellrvasPEHNCLRTRSGDSMA-IYFTSGTTGTPK--MVEHs 242
Cdd:cd12117 99 LTDRSLAGRAGG-------LEVAVVIDEALDAG------------PAGNPAVPVSPDDLAyVMYTSGSTGRPKgvAVTH- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 243 qcsYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHElPQV--DAQTILNTLCRFPITTICCVP 320
Cdd:cd12117 159 ---RGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAP-KGTllDPDALGALIAEEGVTVLWLTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 321 TLFRLLVQEDLTRykFQCLRHCLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSE-TVLIC------GNFRGSTIksgSMG 392
Cdd:cd12117 235 ALFNQLADEDPEC--FAGLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTEnTTFTTshvvteLDEVAGSI---PIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 393 KASPPYDVQIVDEEGNVLPPGKEGNIairikptrpfCLFNC-----YLDNPEKTAAS-------EQGDFYITGDRAHMDE 460
Cdd:cd12117 310 RPIANTRVYVLDEDGRPVPPGVPGEL----------YVGGDglalgYLNRPALTAERfvadpfgPGERLYRTGDLARWLP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 461 DGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVsspdPIRGEVVKAFIVlspAYVSHDPEALTRELQEHVK 540
Cdd:cd12117 380 DGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVV----VREDAGGDKRLV---AYVVAEGALDAAELRAFLR 452
|
490 500 510
....*....|....*....|....*....|.
gi 88196780 541 TVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd12117 453 ERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
110-574 |
1.08e-44 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 168.67 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 110 GLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITS----DALAPHVDAISADcpsl 185
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSdalrDRFQPSRVAEAAE---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 186 qsrlLVSDTSRPGWINFRELlrvaspehnclrtrSGDSMAI-YFTSGTTGTPKMVEHSQCSYgLGFV-ASGRRLMALTES 263
Cdd:PRK06060 127 ----LMSEAARVAPGGYEPM--------------GGDALAYaTYTSGTTGPPKAAIHRHADP-LTFVdAMCRKALRLTPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 264 DIFWNTTDTGWvkaAWTL-FSAW---ANGACVFVHELPqVDAQTILNTLCRFPITTICCVPTLFRLLVqEDLTRYKFQCL 339
Cdd:PRK06060 188 DTGLCSARMYF---AYGLgNSVWfplATGGSAVINSAP-VTPEAAAILSARFGPSVLYGVPNFFARVI-DSCSPDSFRSL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 340 RHCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSEtvlICGNFRGSTI---KSGSMGKASPPYDVQIVDEEGNVLPPGKE 415
Cdd:PRK06060 263 RCVVSAGEALELGLAERLMEFfGGIPILDGIGSTE---VGQTFVSNRVdewRLGTLGRVLPPYEIRVVAPDGTTAGPGVE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 416 GNIAIRiKPTrpfcLFNCYLDNPEKTAasEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPA 495
Cdd:PRK06060 340 GDLWVR-GPA----IAKGYWNRPDSPV--ANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEA 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196780 496 VLESAVVSSPDPIRGEVVKAFIVlsPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK06060 413 VAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
90-572 |
1.72e-44 |
|
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: 163.71 E-value: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILeGACGLKPGDRlmlVLPRLPEWWLTIV---ACMRTGVVMIPGISQLTQKDLKYRLQAARVKSII 166
Cdd:cd05903 3 TYSELDTRADRLAAGL-AALGVGPGDV---VAFQLPNWWEFAVlylACLRIGAVTNPILPFFREHELAFILRRAKAKVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 167 TSDAlaphvdaisadcpslqsrllvsdtsrpgwinFRELLRVASPehnclrtrsGDSMAIYFTSGTTGTPKMVEHSQCSy 246
Cdd:cd05903 79 VPER-------------------------------FRQFDPAAMP---------DAVALLLFTSGTTGEPKGVMHSHNT- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 247 glgFVASGRRL---MALTESDIFWNTTD----TGWVKAAWTLFSAwanGACVFVHEL--PQVDAQTILNTLCRFpitTIC 317
Cdd:cd05903 118 ---LSASIRQYaerLGLGPGDVFLVASPmahqTGFVYGFTLPLLL---GAPVVLQDIwdPDKALALMREHGVTF---MMG 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 318 CVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLICGNFRG--STIKSGSMGKAS 395
Cdd:cd05903 189 ATPFLTDLLNAVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPapEDRRLYTDGRPL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 396 PPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVIN 475
Cdd:cd05903 269 PGVEIKVVDDTGATLAPGVEGELLSR-GPS----VFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIII 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 476 SSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTRELQEHvktVTAPYKYPRKVAFI 555
Cdd:cd05903 344 RGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG-ALLTFDELVAYLDRQ---GVAKQYWPERLVHV 419
|
490
....*....|....*..
gi 88196780 556 SELPKTVSGKILRSKLR 572
Cdd:cd05903 420 DDLPRTPSGKVQKFRLR 436
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
71-571 |
2.71e-44 |
|
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: 163.19 E-value: 2.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 71 RPPNPAFWWvngsgTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltq 150
Cdd:cd05945 4 NPDRPAVVE-----GGRTLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 151 kdLKYRLQAARVKSIItsDALAPhvDAISADcpslqsrllvsdtsrpgwinfrellrvaspehnclrtrsGDSMA-IYFT 229
Cdd:cd05945 71 --LDASSPAERIREIL--DAAKP--ALLIAD---------------------------------------GDDNAyIIFT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 230 SGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVF-VHELPQVDAQTILNTL 308
Cdd:cd05945 106 SGSTGRPKGVQISHDNL-VSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVpVPRDATADPKQLFRFL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 309 CRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSETVLICGNFR---- 382
Cdd:cd05945 185 AEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEvtpe 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 383 -GSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAAS----EQGDFYITGDRAH 457
Cdd:cd05945 265 vLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGP-----SVSKGYLNNPEKTAAAffpdEGQRAYRTGDLVR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 458 MDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvsHDPEALTRELQE 537
Cdd:cd05945 340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP----GAEAGLTKAIKA 415
|
490 500 510
....*....|....*....|....*....|....
gi 88196780 538 HVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd05945 416 ELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
157-572 |
3.50e-44 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 164.93 E-value: 3.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 157 LQAARVKSIITSDALAPHVDAISADCPslQSRLLVSDTSRPGWINFRELlrVASPEHNCLRTRSGDSMAIYFTSGTTGTP 236
Cdd:PRK13382 136 VTREGVDTVIYDEEFSATVDRALADCP--QATRIVAWTDEDHDLTVEVL--IAAHAGQRPEPTGRKGRVILLTSGTTGTP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 237 KMVEHSqcsyGLGFVASGRRLMalteSDIFWNTTDTGWVKAAwtLFSAWANGACVFVHELP-------QVDAQTILNTLC 309
Cdd:PRK13382 212 KGARRS----GPGGIGTLKAIL----DRTPWRAEEPTVIVAP--MFHAWGFSQLVLAASLActivtrrRFDPEATLDLID 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 310 RFPITTICCVPTLFRL---LVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLIC-GNFRGST 385
Cdd:PRK13382 282 RHRATGLAVVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIAtATPADLR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 386 IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYldNPEKTAASEQGdFYITGDRAHMDEDGYFW 465
Cdd:PRK13382 362 AAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRND-----TQFDGY--TSGSTKDFHDG-FMASGDVGYLDENGRLF 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 466 FVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVTAP 545
Cdd:PRK13382 434 VVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPETLKQHVRDNLAN 508
|
410 420
....*....|....*....|....*..
gi 88196780 546 YKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK13382 509 YKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
77-572 |
6.83e-44 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 165.84 E-value: 6.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 77 FWWVNGSGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYR 156
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLK-DVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 157 LQAARVKSIITSDA---------LAPHVDA---------ISAD-CPSLQSRLLVSDTSRPgWINFRELL---RVASPEHN 214
Cdd:PLN02654 188 IVDCKPKVVITCNAvkrgpktinLKDIVDAaldesakngVSVGiCLTYENQLAMKREDTK-WQEGRDVWwqdVVPNYPTK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 215 C--LRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKA-AWTLFSAWANGACV 291
Cdd:PLN02654 267 CevEWVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 292 FVHE-LPQV-DAQTILNTLCRFPITTICCVPTLFRLLVQED---LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTG---L 363
Cdd:PLN02654 347 LVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSAWRWFFNVVGdsrC 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 364 EIHEGYGQSETvlicGNFRGSTI------KSGSmgKASPPYDVQ--IVDEEGNVLPPGKEGNIAIriKPTRPFCLFNCYL 435
Cdd:PLN02654 427 PISDTWWQTET----GGFMITPLpgawpqKPGS--ATFPFFGVQpvIVDEKGKEIEGECSGYLCV--KKSWPGAFRTLYG 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 436 DNP--EKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVV 513
Cdd:PLN02654 499 DHEryETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGI 578
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 88196780 514 KAFIVLSPAyVSHDPEaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PLN02654 579 YAFVTLVEG-VPYSEE-LRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
86-573 |
4.13e-43 |
|
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: 160.93 E-value: 4.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqkdLKYRLQAARVKSI 165
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNA---------LNTRLDAEEIAFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITsdalapHVDAisadcpslqsRLLVSDTSrpgwINFRELLRVASPEHNCLRTRSG-DSMAIYFTSGTTGTPKMVEHSQc 244
Cdd:cd12118 97 LR------HSEA----------KVLFVDRE----FEYEDLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHH- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 245 syglgfvaSGRRLMALtESDIFWNT-TDTGWVkaaWTL--FSA------WANGACVFVHE-LPQVDAQTILNTLCRFPIT 314
Cdd:cd12118 156 --------RGAYLNAL-ANILEWEMkQHPVYL---WTLpmFHCngwcfpWTVAAVGGTNVcLRKVDAKAIYDLIEKHKVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 315 TICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKwKNQTGLEIHEGYGQSET---VLICG-----NFRGST 385
Cdd:cd12118 224 HFCGAPTVLNMLANaPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVCAwkpewDELPTE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 386 IKSGSMGKASPPY----DVQIVDEEGNVLPP--GKE-GNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHM 458
Cdd:cd12118 303 ERARLKARQGVRYvgleEVDVLDPETMKPVPrdGKTiGEIVFRGN-----IVMKGYLKNPEATAEAFRGGWFHSGDLAVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 459 DEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshdpEALTRELQEH 538
Cdd:cd12118 378 HPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA-----KVTEEEIIAF 452
|
490 500 510
....*....|....*....|....*....|....*
gi 88196780 539 VKTVTAPYKYPRKVAFiSELPKTVSGKILRSKLRN 573
Cdd:cd12118 453 CREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
45-573 |
6.48e-43 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 161.91 E-value: 6.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 45 KRP--VPEYFNFA--HDVLDVWSQ-LEKTGHRPpnpAFwwvngSGTEVKWTFEELGKQSRKAANILEGACGLKPGDRLML 119
Cdd:PRK12492 9 KRPagVPSTIDLAayKSVVEVFERsCKKFADRP---AF-----SNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 120 VLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADC--------------PSL 185
Cdd:PRK12492 81 QMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTgieylieakmgdllPAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 186 QSRL----------LVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMAIY-FTSGTTGTPK--MVEHSQCSYGLGFVa 252
Cdd:PRK12492 161 KGWLvntvvdkvkkMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLDDIAVLqYTGGTTGLAKgaMLTHGNLVANMLQV- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 253 sgRRLMALTESDIFWNTTDTGWVKAA----WTLFSAWANGACVFV---HELPQVDAQTI---LNTLCRFPITTICCVPTL 322
Cdd:PRK12492 240 --RACLSQLGPDGQPLMKEGQEVMIAplplYHIYAFTANCMCMMVsgnHNVLITNPRDIpgfIKELGKWRFSALLGLNTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 323 F-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDV 400
Cdd:PRK12492 318 FvALMDHPGFKDLDFSALKLTNSGGTALVKATAERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTAL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 401 QIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSY 479
Cdd:PRK12492 398 KVIDDDGNELPLGERGELCIK-GPQ----VMKGYWQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGF 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 480 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlspayVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELP 559
Cdd:PRK12492 473 NVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFV------VARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLP 546
|
570
....*....|....
gi 88196780 560 KTVSGKILRSKLRN 573
Cdd:PRK12492 547 MTPVGKILRRELRD 560
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
103-572 |
1.31e-42 |
|
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: 159.08 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 103 NILEGACGLKPGDRLMLVLPRLPEWWLTIVAcmrTGVVMIPGISqltqkdlkyrlqaarvKSIITSDALAPHVDAISAdC 182
Cdd:cd05929 31 ARAAAAEGVWIADGVYIYLINSILTVFAAAA---AWKCGACPAY----------------KSSRAPRAEACAIIEIKA-A 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 183 PSLQSRLLVSDTSrPGWINFrELLRVASPEHNCLRTRSGDSMaiYFTSGTTGTPKMVEHS------------QCSYGLGF 250
Cdd:cd05929 91 ALVCGLFTGGGAL-DGLEDY-EAAEGGSPETPIEDEAAGWKM--LYSGGTTGRPKGIKRGlpggppdndtlmAAALGFGP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 251 VASGRRLMalteSDIFWNTTDTGWVkaawtlFSAWANGACVFVheLPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQE 329
Cdd:cd05929 167 GADSVYLS----PAPLYHAAPFRWS------MTALFMGGTLVL--MEKFDPEEFLRLIERYRVTFAQFVPTMFvRLLKLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 330 DLTRYKFQ--CLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVlicgnfrGSTIKS--------GSMGKASPPyD 399
Cdd:cd05929 235 EAVRNAYDlsSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQ-------GLTIINgeewlthpGSVGRAVLG-K 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 400 VQIVDEEGNVLPPGKEGNIAIRIKPTrpfclFNcYLDNPEKTAASEQGDFYIT-GDRAHMDEDGYFWFVGRNDDVINSSS 478
Cdd:cd05929 307 VHILDEDGNEVPPGEIGEVYFANGPG-----FE-YTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 479 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISEL 558
Cdd:cd05929 381 VNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEFVAEL 458
|
490
....*....|....
gi 88196780 559 PKTVSGKILRSKLR 572
Cdd:cd05929 459 PRDDTGKLYRRLLR 472
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
70-574 |
1.98e-42 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 160.22 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 70 HRPPNPAFWWVN-GSGTEVKWTFEELGKQSRKAANILEgACGLKPGDrlmLVLPRLPEWW-LTIV--ACMRTGVVMIPGI 145
Cdd:PRK13295 36 SCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLA-RLGVGRGD---VVSCQLPNWWeFTVLylACSRIGAVLNPLM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 146 SQLTQKDLKYRLQAARVKSIITSDAL-----APHVDAISADCPSLQSRLLV---SDTS------RPGWinfrELLRVASP 211
Cdd:PRK13295 112 PIFRERELSFMLKHAESKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVggdGADSfealliTPAW----EQEPDAPA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 212 EHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLmALTESD-IFWNTT---DTGW---------VKAA 278
Cdd:PRK13295 188 ILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDvILMASPmahQTGFmyglmmpvmLGAT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 279 WTLFSAWANGACVfvhELPQVDAQTIlntlcrfpitTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWK 358
Cdd:PRK13295 267 AVLQDIWDPARAA---ELIRTEGVTF----------TMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERAR 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 359 NQTGLEIHEGYGQSETVLICGNFRGSTIK--SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptRPFcLFNCYLD 436
Cdd:PRK13295 334 AALGAKIVSAWGMTENGAVTLTKLDDPDEraSTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVR----GCS-NFGGYLK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 437 NPEKTAASEQGdFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAF 516
Cdd:PRK13295 409 RPQLNGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAF 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 88196780 517 IVLSPAYvSHDPEALTRELQEHvkTVTAPYkYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK13295 488 VVPRPGQ-SLDFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
320-568 |
3.17e-42 |
|
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: 154.74 E-value: 3.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 320 PTLFRLLVQEDLTRYKFQCLRHcLAGGEAlnSDVRDKWKNQTGLEIHEGYGQSETV-LICgnFRGSTIKSGSMGKASPPY 398
Cdd:cd17637 97 PILSNLLDAAEKSGVDLSSLRH-VLGLDA--PETIQRFEETTGATFWSLYGQTETSgLVT--LSPYRERPGSAGRPGPLV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 399 DVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRN--DDVINS 476
Cdd:cd17637 172 RVRIVDDNDRPVPAGETGEIVVR-GPL----VFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIKP 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 477 SSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALT-RELQEHVKTVTAPYKYPRKVAFI 555
Cdd:cd17637 247 GGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG------ATLTaDELIEFVGSRIARYKKPRYVVFV 320
|
250
....*....|...
gi 88196780 556 SELPKTVSGKILR 568
Cdd:cd17637 321 EALPKTADGSIDR 333
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
70-571 |
4.06e-42 |
|
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: 158.44 E-value: 4.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 70 HRPPNPAFWWVNGSGTEVKWTfEELGKQSRKAANILEGacGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLT 149
Cdd:cd05923 12 SRAPDACAIADPARGLRLTYS-ELRARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 150 QKDLKYRLQAARVKSIITSDAlAPHVDAISadcpSLQSRLL-VSDTSRPGwinfreLLRVASPEHNCLRTRSGDSMAIYF 228
Cdd:cd05923 89 AAELAELIERGEMTAAVIAVD-AQVMDAIF----QSGVRVLaLSDLVGLG------EPESAGPLIEDPPREPEQPAFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 229 TSGTTGTPK---------------MVEHSQCSYGLGFVASGrrLMALTESDIFWnttdtgwvkaAWTLFSAWANGACVFV 293
Cdd:cd05923 158 TSGTTGLPKgavipqraaesrvlfMSTQAGLRHGRHNVVLG--LMPLYHVIGFF----------AVLVAALALDGTYVVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 294 HELpqvDAQTILNTLCRFPITTICCVPTLFRLLV-QEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQS 372
Cdd:cd05923 226 EEF---DPADALKLIEQERVTSLFATPTHLDALAaAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 373 ETVlicgnfrGSTI----KSGSMGKASPPYDVQIVDEEGNV---LPPGKEGNIAIRIKPTRPFclfNCYLDNPEKTAASE 445
Cdd:cd05923 303 EAM-------NSLYmrdaRTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 446 QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVS 525
Cdd:cd05923 373 QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLS 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 88196780 526 HDpealtrELQEHVKTVT-APYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd05923 453 AD------ELDQFCRASElADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
90-574 |
1.34e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 156.97 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALaphvDAIsadcPSLQSRLLVSDTSRPgwinfRELLRVASPEHNCLR---TRSGDSMAIYFTSGTTGTPKMVEHSqcsY 246
Cdd:PRK06145 108 EF----DAI----VALETPKIVIDAAAQ-----ADSRRLAQGGLEIPPqaaVAPTDLVRLMYTSGTTDRPKGVMHS---Y 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 247 G------------LGFVASGRRLMALTESDIfwNTTDTGWVKAAWtlfsawaNGACVFVHElpQVDAQTILNTLCRFPIT 314
Cdd:PRK06145 172 GnlhwksidhviaLGLTASERLLVVGPLYHV--GAFDLPGIAVLW-------VGGTLRIHR--EFDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 315 TICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEAL-NSDVRDKWKNQTGLEIHEGYGQSETvliCGnfrGSTI------ 386
Cdd:PRK06145 241 CAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEKTpESRIRDFTRVFTRARYIDAYGLTET---CS---GDTLmeagre 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 387 --KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIR-IKPTRPfclfncYLDNPEKTAASEQGDFYITGDRAHMDEDGY 463
Cdd:PRK06145 315 ieKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRgPKVTKG------YWKDPEKTAEAFYGDWFRSGDVGYLDEEGF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 464 FWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALT-RELQEHVKTV 542
Cdd:PRK06145 389 LYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG------ATLTlEALDRHCRQR 462
|
490 500 510
....*....|....*....|....*....|..
gi 88196780 543 TAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK06145 463 LASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
87-574 |
2.79e-41 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 156.89 E-value: 2.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 87 VKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMipgisqLT------QKDLKYRLQAA 160
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLL-ALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL------VTinpayrLSELEYALNQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 161 RVKSIITSDA------------LAPHVDAI------SADCPSLQSRLLVSDTSRPGWINFRELL-RVASPEHNCLRTRSG 221
Cdd:PRK08315 115 GCKALIAADGfkdsdyvamlyeLAPELATCepgqlqSARLPELRRVIFLGDEKHPGMLNFDELLaLGRAVDDAELAARQA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 222 -----DSMAIYFTSGTTGTPK--MVEHsqcsYGLG----FVAsgrRLMALTESD---I-------FwnttdtGWVKAawT 280
Cdd:PRK08315 195 tldpdDPINIQYTSGTTGFPKgaTLTH----RNILnngyFIG---EAMKLTEEDrlcIpvplyhcF------GMVLG--N 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 281 LfSAWANGACVfVHELPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKN 359
Cdd:PRK08315 260 L-ACVTHGATM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLRTGIMAGSPCPIEVMKRVID 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 360 QTGL-EIHEGYGQSETVlicgnfRGSTIKS---------GSMGKASPPYDVQIVDEE-GNVLPPGKEGNIAirikpTRPF 428
Cdd:PRK08315 338 KMHMsEVTIAYGMTETS------PVSTQTRtddplekrvTTVGRALPHLEVKIVDPEtGETVPRGEQGELC-----TRGY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 429 CLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVI-----NsssyrIGPVEVESALAEHPAVLESAVV 502
Cdd:PRK08315 407 SVMKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIirggeN-----IYPREIEEFLYTHPKIQDVQVV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196780 503 SSPDPIRGEVVKAFIVLspayvsHDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK08315 482 GVPDEKYGEEVCAWIIL------RPGATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-572 |
6.53e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 151.86 E-value: 6.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 221 GDSMAIYF-TSGTTGTPKMVEHSQCsyglGFVAS---GRRLMALTESDIFWNTTDTGWVKAAW-TLFSAWANGACVFV-- 293
Cdd:cd05944 1 SDDVAAYFhTGGTTGTPKLAQHTHS----NEVYNawmLALNSLFDPDDVLLCGLPLFHVNGSVvTLLTPLASGAHVVLag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 294 ---HELPQVdAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRyKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYG 370
Cdd:cd05944 77 pagYRNPGL-FDNFWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEGYG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 371 QSE-TVLICGNFRGSTIKSGSMGKASPPYDVQIV--DEEGNVL---PPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAAS 444
Cdd:cd05944 155 LTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLrdcAPDEVGEICVA-GPG----VFGGYLYTEGNKNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 445 EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP-AY 523
Cdd:cd05944 230 VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPgAV 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 88196780 524 VShdPEALTRELQEHVKTVTApykYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05944 310 VE--EEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
89-571 |
1.58e-40 |
|
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: 153.22 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 89 WTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITS 168
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 169 DALAphvDAISADCPSLQsrllvsdtsrpgwinfRELLRVASPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQCSYg 247
Cdd:cd12116 92 DALP---DRLPAGLPVLL----------------LALAAAAAAPAAPRTPVSPDDLAyVIYTSGSTGRPKGVVVSHRNL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 LGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLF-SAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLL 326
Cdd:cd12116 152 VNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLlPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRML 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 327 VQEDltrykFQCLR--HCLAGGEALNSDVRDKWKNQTGlEIHEGYGQSETVL------ICGNFRGSTIksgsmGKASPPY 398
Cdd:cd12116 232 LDAG-----WQGRAglTALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI-----GRPLANT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 399 DVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAAS--------EQGDFYITGDRAHMDEDGYFWFVGRN 470
Cdd:cd12116 301 QVYVLDAALRPVPPGVPGELYIGGD-----GVAQGYLGRPALTAERfvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 471 DDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLspayvsHDPEAL-TRELQEHVKTVTAPYKYP 549
Cdd:cd12116 376 DGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL------KAGAAPdAAALRAHLRATLPAYMVP 448
|
490 500
....*....|....*....|..
gi 88196780 550 RKVAFISELPKTVSGKILRSKL 571
Cdd:cd12116 449 SAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
226-575 |
6.96e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 151.68 E-value: 6.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 226 IYFTSGTTGTPKmvehsqcsyglGFVASgRRLMAltesdifwntTDTGWVKAAWtlfsAWaNGACVFVHELP--QVDAqT 303
Cdd:PRK07787 133 IVYTSGTTGPPK-----------GVVLS-RRAIA----------ADLDALAEAW----QW-TADDVLVHGLPlfHVHG-L 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 304 ILNTL-----------------------CRFPITTICCVPTLF-RLLVQEDLTRyKFQCLRHCLAGGEALNSDVRDKWKN 359
Cdd:PRK07787 185 VLGVLgplrignrfvhtgrptpeayaqaLSEGGTLYFGVPTVWsRIAADPEAAR-ALRGARLLVSGSAALPVPVFDRLAA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 360 QTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKE--GNIAIRiKPTrpfcLFNCYLDN 437
Cdd:PRK07787 264 LTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVR-GPT----LFDGYLNR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 438 PEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRND-DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 515
Cdd:PRK07787 339 PDATAAAFTADgWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVA 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 516 FIvlspayVSHDPEALTrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK07787 419 YV------VGADDVAAD-ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
70-538 |
7.33e-40 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 153.72 E-value: 7.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 70 HRPPNPAFWWVNGsGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgISQ-L 148
Cdd:COG1022 23 RFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLL-ALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP-IYPtS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 149 TQKDLKYRLQAARVKSIITSD-ALAPHVDAISADCPSLQsRLLVSD----TSRPGWINFRELLR----VASPE--HNCLR 217
Cdd:COG1022 100 SAEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVLDprglRDDPRLLSLDELLAlgreVADPAelEARRA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 218 TRSGDSMA-IYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIF------WnttdtgWVKA-AWTLFsAWANGA 289
Cdd:COG1022 179 AVKPDDLAtIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRTlsflplA------HVFErTVSYY-ALAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 290 CVFVHElpqvDAQTILNTLCRFPITTICCVPTLF-----RLLVQ-EDLTRYK---FQ----------------------- 337
Cdd:COG1022 251 TVAFAE----SPDTLAEDLREVKPTFMLAVPRVWekvyaGIQAKaEEAGGLKrklFRwalavgrryararlagkspslll 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 338 ---------------------CLRHCLAGGEALNSDVrDKWKNQTGLEIHEGYGQSET-VLICGNfRGSTIKSGSMGKAS 395
Cdd:COG1022 327 rlkhaladklvfsklrealggRLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETsPVITVN-RPGDNRIGTVGPPL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 396 PPYDVQIvDEEGNVLppgkegniairIK-PtrpfCLFNCYLDNPEKTAAS--EQGDFYiTGDRAHMDEDGYFWFVGRNDD 472
Cdd:COG1022 405 PGVEVKI-AEDGEIL-----------VRgP----NVMKGYYKNPEATAEAfdADGWLH-TGDIGELDEDGFLRITGRKKD 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 473 VI-NSSSYRIGPVEVESALAEHPAVLESAVVsspdpirGE---VVKAFIVLspayvshDPEALTRELQEH 538
Cdd:COG1022 468 LIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpFLAALIVP-------DFEALGEWAEEN 523
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
228-573 |
1.48e-39 |
|
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: 147.09 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 228 FTSGTTGTPKMVEHSQ----------CSYgLGFVASGRRLMALTESDIfwnttdTG---WVKAAWTlfsawanGACVFVH 294
Cdd:cd17630 7 LTSGSTGTPKAVVHTAanllasaaglHSR-LGFGGGDSWLLSLPLYHV------GGlaiLVRSLLA-------GAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 295 ELPQVDAQTILntlcRFPITTICCVPTLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQtGLEIHEGYGQSET 374
Cdd:cd17630 73 ERNQALAEDLA----PPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 375 V-LICGNFRGSTiKSGSMGKASPPYDVQIVDEegnvlppgkeGNIAIRikptrPFCLFNCYLDNPEKTAASEQGDFYiTG 453
Cdd:cd17630 148 AsQVATKRPDGF-GRGGVGVLLPGRELRIVED----------GEIWVG-----GASLAMGYLRGQLVPEFNEDGWFT-TK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 454 DRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvshDPEALTR 533
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGPADPA 283
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 88196780 534 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd17630 284 ELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
65-574 |
2.93e-39 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 150.90 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 65 LEKTGHRPPNPAFwwVNGSGTEVkWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPG 144
Cdd:PLN02246 30 FERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLH-KLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 145 ISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLqsrLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSM 224
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDGVT---VVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 225 AIYFTSGTTGTPK--MVEHSqcsyglGFVASGRRLMALTESDIFWNTTDTgwVKAAWTLFSAWA----------NGACVF 292
Cdd:PLN02246 183 ALPYSSGTTGLPKgvMLTHK------GLVTSVAQQVDGENPNLYFHSDDV--ILCVLPMFHIYSlnsvllcglrVGAAIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 293 VheLPQVDAQTILNTLCRFPITTICCVPTLFRLLVQED-LTRYKFQCLRHCLAG----GEALNSDVRDKWKNQTgleIHE 367
Cdd:PLN02246 255 I--MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGaaplGKELEDAFRAKLPNAV---LGQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 368 GYGQSE--TVL-ICGNFRGS--TIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKT 441
Cdd:PLN02246 330 GYGMTEagPVLaMCLAFAKEpfPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQ-----IMKGYLNDPEAT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 442 AASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLS 520
Cdd:PLN02246 405 ANTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRS 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 88196780 521 PAY-VSHDpealtrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN02246 485 NGSeITED------EIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
90-571 |
4.70e-39 |
|
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: 148.61 E-value: 4.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqKDLKYrlQAARVKSIITsd 169
Cdd:cd17643 14 TYGELDARANRLARTLRAE-GVGPGDRVALALPRSAELIVALLAILKAGGAYVP-------IDPAY--PVERIAFILA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 alaphvDAisadcpslQSRLLVSDTSRPGWInfrellrvaspehnclrtrsgdsmaIYfTSGTTGTPK--MVEHSQCsyg 247
Cdd:cd17643 82 ------DS--------GPSLLLTDPDDLAYV-------------------------IY-TSGSTGRPKgvVVSHANV--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 LGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGA-CVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLL 326
Cdd:cd17643 119 LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGrLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 327 VQEDLTRYKFQ-CLRHCLAGGEALNSDVRDKWKNQTGL---EIHEGYGQSET-VLIcgNFR-----------GSTIksgs 390
Cdd:cd17643 199 VEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETtVHV--TFRpldaadlpaaaASPI---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 391 mGKASPPYDVQIVDEEGNVLPPGKEGNIAI-RIKPTRPfclfncYLDNPEKTA-------ASEQGD-FYITGDRAHMDED 461
Cdd:cd17643 273 -GRPLPGLRVYVLDADGRPVPPGVVGELYVsGAGVARG------YLGRPELTAerfvanpFGGPGSrMYRTGDLARRLPD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 462 GYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdPEALTRELQEHVKT 541
Cdd:cd17643 346 GELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AAADIAELRALLKE 420
|
490 500 510
....*....|....*....|....*....|
gi 88196780 542 VTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17643 421 LLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
112-566 |
1.81e-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: 147.86 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 112 KPGDRLMLVLPRLPEWWLTIVACMRTGVVmiPGISQLTQ--KDLKYRLQAARVKSIITSDAL-----APHVDAISADC-- 182
Cdd:cd05909 29 KEGENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAglRELRACIKLAGIKTVLTSKQFieklkLHHLFDVEYDAri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 183 ---PSLQSRLLVSD--------TSRPGWINFRELLRVASPEhnclrtrsgDSMAIYFTSGTTGTPKMVEHSQCSYgLGFV 251
Cdd:cd05909 107 vylEDLRAKISKADkckaflagKFPPKWLLRIFGVAPVQPD---------DPAVILFTSGSEGLPKGVVLSHKNL-LANV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 252 ASGRRLMALTESDIFWNTTDT----GWVKAAWTLFSAwanGACVFVHELPqVDAQTILNTLCRFPITTICCVPTLFRLLV 327
Cdd:cd05909 177 EQITAIFDPNPEDVVFGALPFfhsfGLTGCLWLPLLS---GIKVVFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 328 QEdLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNFRGSTIKSGSMGKASPPYDVQIVDEE 406
Cdd:cd05909 253 RA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 407 GNV-LPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRnddviNSSSYRIG--- 482
Cdd:cd05909 332 THEeVPIGEGGLLLVR-GPN----VMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGR-----LSRFAKIAgem 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 483 -PVE-VESALAEH-PAVLESAVVSSPDPIRGEVVKAFivlspayvsHDPEALTR-ELQEHVKTVTAPYKY-PRKVAFISE 557
Cdd:cd05909 402 vSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL---------TTTTDTDPsSLNDILKNAGISNLAkPSYIHQVEE 472
|
....*....
gi 88196780 558 LPKTVSGKI 566
Cdd:cd05909 473 IPLLGTGKP 481
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
222-568 |
2.31e-38 |
|
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: 144.33 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 222 DSMAIYFTSGTTGTPKMV-----------EHSQcSYGLGFVASGRRLMALTESDIFwnttdtgwvKAAWTLFSAWANGAC 290
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVllanktffavpDILQ-KEGLNWVVGDVTYLPLPATHIG---------GLWWILTCLIHGGLC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 291 VFVHELPQVdaQTILNTLCRFPITTICCVPTLFRLLVQE--DLTRYKFQcLRHCLAGGE-ALNSDVRD-KWKNQTGLEIH 366
Cdd:cd17635 72 VTGGENTTY--KSLFKILTTNAVTTTCLVPTLLSKLVSElkSANATVPS-LRLIGYGGSrAIAADVRFiEATGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 367 egYGQSET-VLICGNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIriKPTRpfcLFNCYLDNPEKTAASE 445
Cdd:cd17635 149 --YGLSETgTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWI--KSPA---NMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 446 QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayvS 525
Cdd:cd17635 222 IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----A 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 88196780 526 HDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:cd17635 298 ELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
89-574 |
1.03e-37 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 146.66 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 89 WTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITS 168
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 169 DALAPHVDAISADCpslqsrLLVSDTSRPGWINFRELLRVASpehnclrtRSGDSM-----------AIYFTSGTTGTPK 237
Cdd:PLN02330 135 DTNYGKVKGLGLPV------IVLGEEKIEGAVNWKELLEAAD--------RAGDTSdneeilqtdlcALPFSSGTTGISK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 238 --MVEHSQ-----CS--YGLGFVASGRrLMALTESDIFWNTTDTGwvkaawTLFSAWANGACVFVheLPQVDAQTILNTL 308
Cdd:PLN02330 201 gvMLTHRNlvanlCSslFSVGPEMIGQ-VVTLGLIPFFHIYGITG------ICCATLRNKGKVVV--MSRFELRTFLNAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 309 CRFPITTICCVPTLFRLLVQE------DLTRYKfqcLRHCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSETVLICGNF 381
Cdd:PLN02330 272 ITQEVSFAPIVPPIILNLVKNpiveefDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITLTH 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 382 ----RGSTI-KSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYI-TGD 454
Cdd:PLN02330 349 gdpeKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRTIDEDGWLhTGD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 455 RAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALtre 534
Cdd:PLN02330 424 IGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDIL--- 500
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 88196780 535 lqEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN02330 501 --NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
222-568 |
1.19e-37 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 141.87 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 222 DSMAIYFTSGTTGTPK--MVEHSQCsygLGFVASGRRLMALTESD------IFWNTTdtGWvKAAWtlFSAWANGACVfv 293
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQT---LRAAAAWADCADLTEDDryliinPFFHTF--GY-KAGI--VACLLTGATV-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 294 heLPQV--DAQTILNTLCRFPITTICCVPTLFR-LLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLE-IHEGY 369
Cdd:cd17638 71 --VPVAvfDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 370 GQSE--TVLICGNFRGSTIKSGSMGKASPPYDVQIVDEeGNVLppgkegniairikpTRPFCLFNCYLDNPEKTAASEQG 447
Cdd:cd17638 149 GLTEagVATMCRPGDDAETVATTCGRACPGFEVRIADD-GEVL--------------VRGYNVMQGYLDDPEATAEAIDA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 448 DFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSH 526
Cdd:cd17638 214 DGWLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTL 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 88196780 527 DPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:cd17638 293 TEEDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-571 |
2.20e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 148.95 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALI-ARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALL 4652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALAPHVD-AISADCpslqsrlLVSDTSRPgWINFrellrvasPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQ 243
Cdd:PRK12316 4653 LTQSHLLQRLPiPDGLAS-------LALDRDED-WEGF--------PAHDPAVRLHPDNLAyVIYTSGSTGRPKGVAVSH 4716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 CSYgLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLF 323
Cdd:PRK12316 4717 GSL-VNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYL 4795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDK-WKNQTGLEIHEGYGQSETVL--ICGNFRGSTIKSGS---MGKASPP 397
Cdd:PRK12316 4796 QQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVtvLLWKARDGDACGAAympIGTPLGN 4875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 398 YDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAA-------SEQGD-FYITGDRAHMDEDGYFWFVGR 469
Cdd:PRK12316 4876 RSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAErfvpdpfGAPGGrLYRTGDLARYRADGVIDYLGR 4950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 470 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLSPAYVSHDPEA---LTRELQEHVKTVTAPY 546
Cdd:PRK12316 4951 VDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLV-GYVVPQDPALADADEAqaeLRDELKAALRERLPEY 5029
|
490 500
....*....|....*....|....*
gi 88196780 547 KYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
88-572 |
8.90e-37 |
|
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: 142.51 E-value: 8.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqkdlkyrlqaarvksiit 167
Cdd:cd17649 12 SLSYAELDARANRLAHRLR-ALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP------------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 sdaLAPhvdaisaDCPSLQSRLLVSDtSRPGWinfrellrvaspehncLRTRSGDSMA-IYFTSGTTGTPKMVEHSQCSY 246
Cdd:cd17649 67 ---LDP-------EYPAERLRYMLED-SGAGL----------------LLTHHPRQLAyVIYTSGSTGTPKGVAVSHGPL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 247 GLGFVASGRRLmALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQ-VDAQTILNTLCRFPITTICCVPTLFRL 325
Cdd:cd17649 120 AAHCQATAERY-GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELwASADELAEMVRELGVTVLDLPPAYLQQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 326 LVQE--DLTRYKFQCLRHCLAGGEALNSDVRDKWKnQTGLEIHEGYGQSETV---LICGNFRGSTIKSGSM--GKASPPY 398
Cdd:cd17649 199 LAEEadRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTEATvtpLVWKCEAGAARAGASMpiGRPLGGR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 399 DVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFVGRN 470
Cdd:cd17649 278 SAYILDADLNPVPVGVTGELYIGGE-----GLARGYLGRPELTAerfvpdpfGAPGSRLYRTGDLARWRDDGVIEYLGRV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 471 DDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLSpayvshDPEALTrELQEHVKTVTA----PY 546
Cdd:cd17649 353 DHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLR------AAAAQP-ELRAQLRTALRaslpDY 424
|
490 500
....*....|....*....|....*.
gi 88196780 547 KYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd17649 425 MVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
85-572 |
9.98e-37 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 143.82 E-value: 9.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 85 TEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIP--------------GISQLT- 149
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALK-KYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPtndiynereldhslNISKPTi 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 150 --------QKDLKYRLQAARVKSIITSDAlaphvdaiSADCPSLQSrlLVSDTSRPGWINFRELlRVASPEHNclrtRSG 221
Cdd:cd17642 120 vfcskkglQKVLNVQKKLKIIKTIIILDS--------KEDYKGYQC--LYTFITQNLPPGFNEY-DFKPPSFD----RDE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 222 DSMAIYFTSGTTGTPKMVEHSQCSYGLGFVAS-----GRRLMALTE--SDIFWNttdtgwvkAAWTLFSAWANGACVF-V 293
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHArdpifGNQIIPDTAilTVIPFH--------HGFGMFTTLGYLICGFrV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 294 HELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLT-RYKFQCLRHCLAGGEALNSDVRDKWKNQTGLE-IHEGYGQ 371
Cdd:cd17642 257 VLMYKFEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVdKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 372 SET---VLICGNfrgSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQG 447
Cdd:cd17642 337 TETtsaILITPE---GDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK-GPM----IMKGYVNNPEATKALIDK 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 448 DFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvSH 526
Cdd:cd17642 409 DGWLhSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL-----EA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 88196780 527 DPEALTRELQEHVKTVTAPYKYPR-KVAFISELPKTVSGKILRSKLR 572
Cdd:cd17642 484 GKTMTEKEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
107-574 |
2.38e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 142.57 E-value: 2.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 107 GACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDA-----LAPHVDAISAD 181
Cdd:PRK06164 53 AAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAAVPPD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 182 C-PSLQSRLLVSDTSR--PGWINFRELLRVASP---EHNCLRTRSGDSMA---IYFTSGTTGTPKMVEHSQ--------- 243
Cdd:PRK06164 133 AlPPLRAIAVVDDAADatPAPAPGARVQLFALPdpaPPAAAGERAADPDAgalLFTTSGTTSGPKLVLHRQatllrhara 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 CSYGLGFVASGRRLMALTESDIFWNTTdtgwvkaawtLFSAWANGACVfvHELPQVDAQTILNTLCRFPITTICCVPTLF 323
Cdd:PRK06164 213 IARAYGYDPGAVLLAALPFCGVFGFST----------LLGALAGGAPL--VCEPVFDAARTARALRRHRVTHTFGNDEML 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 RLLVQEDLTRYKFQCLRHC-----LAGGEALNSDVRDKWKNQTGLeihegYGQSETVLICGNFRGSTIKS----GSMGKA 394
Cdd:PRK06164 281 RRILDTAGERADFPSARLFgfasfAPALGELAALARARGVPLTGL-----YGSSEVQALVALQPATDPVSvrieGGGRPA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 395 SPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDD 472
Cdd:PRK06164 356 SPEARVRARDpQDGALLPDGESGEIEIR-APS----LMRGYLDNPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGD 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 473 VINSSSYRIGPVEVESALAEHPAVLESAVVSSpdPIRGE-VVKAFIVLSPAyVSHDPEALTRELQEHVktvtAPYKYPRK 551
Cdd:PRK06164 431 SLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDG-ASPDEAGLMAACREAL----AGFKVPAR 503
|
490 500
....*....|....*....|....*.
gi 88196780 552 VAFISELPKTVSG---KILRSKLRNQ 574
Cdd:PRK06164 504 VQVVEAFPVTESAngaKIQKHRLREM 529
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-568 |
2.89e-36 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 137.92 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 226 IYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALT-ESDIFWNTT--DTGWVKAAwtLFSAWANGAcvfVHELPQVDAQ 302
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSW-IESFVCNEDLFNISgEDAILAPGPlsHSLFLYGA--ISALYLGGT---FIGQRKFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 303 TILNTLCRFPITTICCVPTLFRLLVQEDLTRYKFQCLrhcLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSETVLICGNF 381
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 382 RGSTIKSGSMGKASPPYDVQIVDEEGnvlppGKEGNIAIRiKPTRpfclFNCYLDNPEktaaSEQGDFYITGDRAHMDED 461
Cdd:cd17633 156 NQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVK-SEMV----FSGYVRGGF----SNPDGWMSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 462 GYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayvshdpEALTRELQEHVKT 541
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--------KLTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*..
gi 88196780 542 VTAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-565 |
1.08e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 137.51 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 219 RSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGfVASGRRLMALTESDIFW------NTTDTGWVKAA--------WTLFSA 284
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQEDIFRM-LMGGADFGTGEFTPSEDahkaaaAAAGTVMFPAPplmhgtgsWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 285 WANGACVFVHElPQVDAQTILNTLCRFPITTICCVPTLF-RLLVQE--DLTRYKFQCLRHCLAGGEALNSDVRDKW-KNQ 360
Cdd:cd05924 80 LLGGQTVVLPD-DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlrDAGPYDLSSLFAISSGGALLSPEVKQGLlELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 361 TGLEIHEGYGQSET-VLICGNFRGSTIKSGSMGKASPpyDVQIVDEEGNVLPPGKE--GNIAIR-IKPtrpfclfNCYLD 436
Cdd:cd05924 159 PNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGgvGWIARRgHIP-------LGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 437 NPEKTAAS--EQGD--FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 512
Cdd:cd05924 230 DEAKTAETfpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 88196780 513 VKAFIVLSPAyvsHDPEAltRELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 565
Cdd:cd05924 310 VVAVVQLREG---AGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
368-564 |
5.03e-35 |
|
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: 134.74 E-value: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 368 GYGQSETV-LICGNFRGSTIKsGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQ 446
Cdd:cd17636 142 GYGQTEVMgLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEVNARRTR 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 447 GDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP-AYVS 525
Cdd:cd17636 216 GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPgASVT 295
|
170 180 190
....*....|....*....|....*....|....*....
gi 88196780 526 HDpealtrELQEHVKTVTAPYKYPRKVAFISELPKTVSG 564
Cdd:cd17636 296 EA------ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
228-573 |
9.81e-35 |
|
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: 136.90 E-value: 9.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 228 FTSGTTGTPK--MVEHSqcSYGLGFVASGRRLMALTESDIFWnttdtgwvKAAWT-------LFSAWANGACVFV---HE 295
Cdd:cd05918 113 FTSGSTGKPKgvVIEHR--ALSTSALAHGRALGLTSESRVLQ--------FASYTfdvsileIFTTLAAGGCLCIpseED 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 296 LPQvdaqTILNTLCRFPITTICCVPTLFRLLVQEDLTrykfqCLRHCLAGGEALNSDVRDKWKNQTGLeiHEGYGQSE-T 374
Cdd:cd05918 183 RLN----DLAGFINRLRVTWAFLTPSVARLLDPEDVP-----SLRTLVLGGEALTQSDVDTWADRVRL--INAYGPAEcT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 375 VLICGNFRGSTIKSGSMGkasPPYDVQ--IVDEEGN--VLPPGKEGNIAIrikpTRPfCLFNCYLDNPEKTAAS------ 444
Cdd:cd05918 252 IAATVSPVVPSTDPRNIG---RPLGATcwVVDPDNHdrLVPIGAVGELLI----EGP-ILARGYLNDPEKTAAAfiedpa 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 445 --------EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK-- 514
Cdd:cd05918 324 wlkqegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPql 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196780 515 -AFIVLSP------------AYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd05918 404 vAFVVLDGsssgsgdgdslfLEPSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
84-538 |
1.03e-34 |
|
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: 136.57 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 84 GTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVK 163
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLI-ALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 164 SIITSDAlaphvdaisadcpslqsrllvSDTSrpgwinfrellrvaspehnclrtrsgdsmAIYFTSGTTGTPKMVEHSQ 243
Cdd:cd05907 80 ALFVEDP---------------------DDLA-----------------------------TIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 CSYgLGFVASGRRLMALTESD----------IFWNTTDtgwvkaawtLFSAWANGACVFVHElpqvDAQTILNTLCRFPI 313
Cdd:cd05907 110 RNI-LSNALALAERLPATEGDrhlsflplahVFERRAG---------LYVPLLAGARIYFAS----SAETLLDDLSEVRP 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 314 TTICCVPTLFR----LLVQEDLTRYK--------FQCLRHCLAGGEALNSDVrDKWKNQTGLEIHEGYGQSETV-LICGN 380
Cdd:cd05907 176 TVFLAVPRVWEkvyaAIKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAEL-LHFFRALGIPVYEGYGLTETSaVVTLN 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 381 fRGSTIKSGSMGKASPPYDVQIvDEEGNVLppgkegniairikpTRPFCLFNCYLDNPEKTAASEQGD-FYITGDRAHMD 459
Cdd:cd05907 255 -PPGDNRIGTVGKPLPGVEVRI-ADDGEIL--------------VRGPNVMLGYYKNPEATAEALDADgWLHTGDLGEID 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 460 EDGYFWFVGRNDDVI-NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPirgeVVKAFIVLspayvshDPEALTRELQEH 538
Cdd:cd05907 319 EDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP-------DPEALEAWAEEH 387
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
90-571 |
6.43e-34 |
|
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: 133.98 E-value: 6.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILeGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqKDLKYrlQAARVKSIITsD 169
Cdd:cd12115 26 TYAELNRRANRLAARL-RAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVP-------LDPAY--PPERLRFILE-D 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVdaisadcpslqsrllvsdtsrpgwinfrellrvaspehnclRTRSGDSMAIYFTSGTTGTPKMV--EHSQCSYG 247
Cdd:cd12115 95 AQARLV-----------------------------------------LTDPDDLAYVIYTSGSTGRPKGVaiEHRNAAAF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 LGFVA---SGRRLMALTESdifwntTDTGWVKAAWTLFSAWANGACVFVHE-------LPQVDAQTILNTlcrfpittic 317
Cdd:cd12115 134 LQWAAaafSAEELAGVLAS------TSICFDLSVFELFGPLATGGKVVLADnvlalpdLPAAAEVTLINT---------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 318 cVPTLFRLLVQEDLTRYKFQCLrhCLAGgEALNSD-VRDKWKNQTGLEIHEGYGQSE-----TVLIcgnFRGSTIKSGSM 391
Cdd:cd12115 198 -VPSAAAELLRHDALPASVRVV--NLAG-EPLPRDlVQRLYARLQVERVVNLYGPSEdttysTVAP---VPPGASGEVSI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 392 GKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYF 464
Cdd:cd12115 271 GRPLANTQAYVLDRALQPVPLGVPGELYIGGAG-----VARGYLGRPGLTAERflpdpfGPGArLYRTGDLVRWRPDGLL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 465 WFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVShdpeaLTRELQEHVKTVTA 544
Cdd:cd12115 346 EFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLP 420
|
490 500
....*....|....*....|....*..
gi 88196780 545 PYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd12115 421 AYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
108-574 |
7.30e-34 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 135.40 E-value: 7.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 108 ACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITsDALAPH-VDAISADCPSLQ 186
Cdd:PRK05852 62 RSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLI-DADGPHdRAEPTTRWWPLT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 187 SRLlVSDTSRPGWINFRELLRVASPEHNC---LRTRSGDSMaIYFTSGTTGTPKMVE----------HSQCS-YGLGFVA 252
Cdd:PRK05852 141 VNV-GGDSGPSGGTLSVHLDAATEPTPATstpEGLRPDDAM-IMFTGGTTGLPKMVPwthaniassvRAIITgYRLSPRD 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 253 SGRRLMALTESDifwnttdtGWVKAawtLFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQEDLT 332
Cdd:PRK05852 219 ATVAVMPLYHGH--------GLIAA---LLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAAT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 333 ------RYKFQCLRHCLAggeALNSDVRDKWKNQTGLEIHEGYGQSET--------VLICGNFRGSTIKSGSMGKASPPy 398
Cdd:PRK05852 288 epsgrkPAALRFIRSCSA---PLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTENPVVSTGLVGRSTGA- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 399 DVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSS 478
Cdd:PRK05852 364 QIRIVGSDGLPLPAGAVGEVWLR-GTT----VVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 479 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV-LSPAYVSHDpealtrELQEHVKTVTAPYKYPRKVAFISE 557
Cdd:PRK05852 439 EKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVpRESAPPTAE------ELVQFCRERLAAFEIPASFQEASG 512
|
490
....*....|....*..
gi 88196780 558 LPKTVSGKILRSKLRNQ 574
Cdd:PRK05852 513 LPHTAKGSLDRRAVAEQ 529
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
90-571 |
7.46e-34 |
|
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: 134.76 E-value: 7.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:cd17655 24 TYRELNERANQLARTLR-EKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPhvdaisadcPSLQSRLLVSDTSRPGWINFRELLRVASpehnclrtRSGDSMAIYFTSGTTGTPK--MVEHSQCSYg 247
Cdd:cd17655 103 HLQP---------PIAFIGLIDLLDEDTIYHEESENLEPVS--------KSDDLAYVIYTSGSTGKPKgvMIEHRGVVN- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 lgFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQV-DAQTILNTLCRFPITTICCVPTLFRLL 326
Cdd:cd17655 165 --LVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVlDGQALTQYIRQNRITIIDLTPAHLKLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 327 VQEDLTryKFQCLRHCLAGGEALNSDVRDKWKNQTGL--EIHEGYGQSETVLIC--GNFRGSTIKSGS--MGKASPPYDV 400
Cdd:cd17655 243 DAADDS--EGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPTETTVDAsiYQYEPETDQQVSvpIGKPLGNTRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 401 QIVDEEGNVLPPGKEGNIAI------RikptrpfclfnCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFV 467
Cdd:cd17655 321 YILDQYGRPQPVGVAGELYIggegvaR-----------GYLNRPELTAEKfvddpfVPGErMYRTGDLARWLPDGNIEFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 468 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAfivlspAYVSHDPEALTRELQEHVKTVTAPYK 547
Cdd:cd17655 390 GRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDE-QGQNYLC------AYIVSEKELPVAQLREFLARELPDYM 462
|
490 500
....*....|....*....|....
gi 88196780 548 YPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17655 463 IPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
110-572 |
2.15e-33 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 134.20 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 110 GLKPGDRLMLVLPR---LPEWWLTIVACMRTGVVMIPGISQLTQKdlkyrlqaARVKSiiTSDALAPHVDAISADCPSLQ 186
Cdd:PLN02574 88 GVRQGDVVLLLLPNsvyFPVIFLAVLSLGGIVTTMNPSSSLGEIK--------KRVVD--CSVGLAFTSPENVEKLSPLG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 187 -SRLLVS-----DTSRPGWINFRELLRvASPEHnCLR--TRSGDSMAIYFTSGTTGTPKmvehsqcsyglGFVASGRRLM 258
Cdd:PLN02574 158 vPVIGVPenydfDSKRIEFPKFYELIK-EDFDF-VPKpvIKQDDVAAIMYSSGTTGASK-----------GVVLTHRNLI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 259 ALTE-------SDIFWNTTDTGWVkAAWTLFSAWanGACVFVHEL----------PQVDAQTILNTLCRFPITTICCVPT 321
Cdd:PLN02574 225 AMVElfvrfeaSQYEYPGSDNVYL-AALPMFHIY--GLSLFVVGLlslgstivvmRRFDASDMVKVIDRFKVTHFPVVPP 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 322 LFRLLVQ--EDLTRYKFQCLRHCLAGGEALNSD-VRDKWKNQTGLEIHEGYGQSETVLIcgNFRGSTIKS----GSMGKA 394
Cdd:PLN02574 302 ILMALTKkaKGVCGEVLKSLKQVSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAV--GTRGFNTEKlskySSVGLL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 395 SPPYDVQIVD-EEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFVGRNDD 472
Cdd:PLN02574 380 APNMQAKVVDwSTGCLLPPGNCGELWIQ-GPG----VMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 473 VINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALTRE-LQEHVKTVTAPYKYPRK 551
Cdd:PLN02574 455 IIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVINYVAKQVAPYKKVRK 528
|
490 500
....*....|....*....|.
gi 88196780 552 VAFISELPKTVSGKILRSKLR 572
Cdd:PLN02574 529 VVFVQSIPKSPAGKILRRELK 549
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
80-571 |
8.37e-32 |
|
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: 128.54 E-value: 8.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 80 VNGSGTevkWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEwwlTIVACM---RTGVVMIPgisqltqkdLKYR 156
Cdd:cd12114 7 ICGDGT---LTYGELAERARRVAGALK-AAGVRPGDLVAVTLPKGPE---QVVAVLgilAAGAAYVP---------VDID 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 157 LQAARVKSIItSDAlapHVDAISADCPSLQSRLLVSDTSRPgwinfRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTP 236
Cdd:cd12114 71 QPAARREAIL-ADA---GARLVLTDGPDAQLDVAVFDVLIL-----DLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 237 K--MVEHSQCsygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFVHELPQVDAQTILNTLCRFPI 313
Cdd:cd12114 142 KgvMISHRAA---LNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATlVLPDEARRRDPAHWAELIERHGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 314 TTICCVPTLFRLLVQEDLTRYKFQC-LRHCLAGGEALNSDVRDKWKNQT-GLEIHEGYGQSETVlICGNFRgsTIKSGSM 391
Cdd:cd12114 219 TLWNSVPALLEMLLDVLEAAQALLPsLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEAS-IWSIYH--PIDEVPP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 392 GKASPPYDV-------QIVDEEGNVLPPGKEGNIAI--RikptrpfCLFNCYLDNPEKTAAS-----EQGDFYITGDRAH 457
Cdd:cd12114 296 DWRSIPYGRplanqryRVLDPRGRDCPDWVPGELWIggR-------GVALGYLGDPELTAARfvthpDGERLYRTGDLGR 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 458 MDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVLSPAYVSHDPEALTRELQE 537
Cdd:cd12114 369 YRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDALRAFLAQ 447
|
490 500 510
....*....|....*....|....*....|....
gi 88196780 538 HVktvtAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd12114 448 TL----PAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
86-574 |
9.44e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 129.30 E-value: 9.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEwwltIVACmRTGVVMIPGI-----SQLTQKDLKYRLQAA 160
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPA----MVEA-HFGVPMAGAVlntlnTRLDAASIAFMLRHG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 161 RVKSIITSDALAPHVDAISADCPSLqsRLLVSD--------TSRPGWINFRELLRVASPEHNCLRTRSG-DSMAIYFTSG 231
Cdd:PRK08162 115 EAKVLIVDTEFAEVAREALALLPGP--KPLVIDvddpeypgGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNYTSG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 232 TTGTPK-MVEHSQCSYglgfvasgrrLMALTesdifwNTTDTGWVKAA---WTL--FS------AWANGACVFVHE-LPQ 298
Cdd:PRK08162 193 TTGNPKgVVYHHRGAY----------LNALS------NILAWGMPKHPvylWTLpmFHcngwcfPWTVAARAGTNVcLRK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 299 VDAQTILNTLCRFPITTICCVPTLFRLLVQ-EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNqTGLEIHEGYGQSET--- 374
Cdd:PRK08162 257 VDPKLIFDLIREHGVTHYCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAKMEE-IGFDLTHVYGLTETygp 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 375 VLICGNFRG-----STIKSGSMGKASPPYDVQivdEEGNVLPP---------GKE-GNIAIR----IKPtrpfclfncYL 435
Cdd:PRK08162 336 ATVCAWQPEwdalpLDERAQLKARQGVRYPLQ---EGVTVLDPdtmqpvpadGETiGEIMFRgnivMKG---------YL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 436 DNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 515
Cdd:PRK08162 404 KNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCA 483
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 88196780 516 FIVLSPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILRSKLRNQ 574
Cdd:PRK08162 484 FVELKD-----GASATEEEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
90-573 |
9.75e-32 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 127.43 E-value: 9.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqkdLKYRLQAARVKSIITSd 169
Cdd:cd17653 24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP---------LDAKLPSARIQAILRT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 alaphvdaisadcpsLQSRLLVSDTSrpgwinfrellrvasPEhnclrtrsgDSMAIYFTSGTTGTPK--MVEHSQCSYG 247
Cdd:cd17653 93 ---------------SGATLLLTTDS---------------PD---------DLAYIIFTSGSTGIPKgvMVPHRGVLNY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 LGFVAS------GRRlMALTESDIFWnttdtgwvKAAWTLFSAWANGACVFVHElPQVDAQTILNTLCRFPITticcvPT 321
Cdd:cd17653 134 VSQPPArldvgpGSR-VAQVLSIAFD--------ACIGEIFSTLCNGGTLVLAD-PSDPFAHVARTVDALMST-----PS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 322 LFRLLVQEDltrykFQCLRHCLAGGEALNSDVRDKWKNqtGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQ 401
Cdd:cd17653 199 ILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 402 IVDEEGNVLPPGKEGNIAIR-IKPTRPfclfncYLDNPEKTAASEQGD-------FYITGDRAHMDEDGYFWFVGRNDDV 473
Cdd:cd17653 272 ILDADLQPVPEGVVGEICISgVQVARG------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGREDNQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 474 INSSSYRIGPVEVESALAEHPAVLESAVVSSpdpIRGEVVkAFIVlsPAYVshDPEALTRELQEHVktvtAPYKYPRKVA 553
Cdd:cd17653 346 VKVRGFRINLEEIEEVVLQSQPEVTQAAAIV---VNGRLV-AFVT--PETV--DVDGLRSELAKHL----PSYAVPDRII 413
|
490 500
....*....|....*....|
gi 88196780 554 FISELPKTVSGKILRSKLRN 573
Cdd:cd17653 414 ALDSFPLTANGKVDRKALRE 433
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
86-572 |
1.88e-31 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 128.18 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLK-YRLQ------ 158
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRRQ-GIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNaYASQiepall 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 159 -AARVKSIITSDALaphVDAISADCPSLQSRLLVSDTSRPG---WINFRELLRVASPEhnclrtrSGDSMAIYFTSG-TT 233
Cdd:PRK10946 125 iADRQHALFSDDDF---LNTLVAEHSSLRVVLLLNDDGEHSlddAINHPAEDFTATPS-------PADEVAFFQLSGgST 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 234 GTPKMV--EHSQCSYGL-------GFVASGRRLMALTESDIFWNTTdtgwvKAAWTLFsaWANGACVFVHElPQVdaqti 304
Cdd:PRK10946 195 GTPKLIprTHNDYYYSVrrsveicGFTPQTRYLCALPAAHNYPMSS-----PGALGVF--LAGGTVVLAPD-PSA----- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 305 lnTLCrFP------ITTICCVP---TLFRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSE-- 373
Cdd:PRK10946 262 --TLC-FPliekhqVNVTALVPpavSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEgl 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 374 ---TVLICGNFRGSTIKSGSMgkaSPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTrpfclFNCYLDNPEKTAAS--EQGd 448
Cdd:PRK10946 339 vnyTRLDDSDERIFTTQGRPM---SPDDEVWVADADGNPLPQGEVGRLMTRGPYT-----FRGYYKSPQHNASAfdANG- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 449 FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYvshDP 528
Cdd:PRK10946 410 FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPL---KA 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 88196780 529 EALTRELQEHvktVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK10946 487 VQLRRFLREQ---GIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
101-574 |
1.99e-31 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 128.38 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 101 AANILEGacGLKPGDRLMLVLPRlPEW---WLTIVACMrtGVVMIPgisqltqkdLKYR--LQAAR-----VK-SIITSD 169
Cdd:PLN02860 46 AAGLLRL--GLRNGDVVAIAALN-SDLyleWLLAVACA--GGIVAP---------LNYRwsFEEAKsamllVRpVMLVTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPH--VDAISADCPSLQSRLLVSDTSRPGWINFRELLRvasPEHncLRTRSG------------DSMAIYFTSGTTGT 235
Cdd:PLN02860 112 ETCSSwyEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLT---TEM--LKQRALgtteldyawapdDAVLICFTSGTTGR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 236 PKMVEHSQCSY---GLGFVAsgrrLMALTESDIFWNTT---DTGWVKAAWTLFSAwanGAC-VFvheLPQVDAQTILNTL 308
Cdd:PLN02860 187 PKGVTISHSALivqSLAKIA----IVGYGEDDVYLHTAplcHIGGLSSALAMLMV---GAChVL---LPKFDAKAALQAI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 309 CRFPITTICCVPTLFRLLV---QEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSETvliCGNFRGS 384
Cdd:PLN02860 257 KQHNVTSMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLfPNAKLFSAYGMTEA---CSSLTFM 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 385 TIKSGSMgkASPPYDVQIVDEEGNVLPPGKEG--------NIAIRIKP----------TRPFCLFNCYLDNPEKTAASEQ 446
Cdd:PLN02860 334 TLHDPTL--ESPKQTLQTVNQTKSSSVHQPQGvcvgkpapHVELKIGLdessrvgrilTRGPHVMLGYWGQNSETASVLS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 447 GDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVS 525
Cdd:PLN02860 412 NDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIW 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 526 HDPEALTR---------ELQEHVKTVT-APYKYPRK-VAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN02860 492 SDNEKENAkknltlsseTLRHHCREKNlSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
88-571 |
3.41e-31 |
|
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: 126.13 E-value: 3.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEGaCGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIIT 167
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 SdalaphvdaisadcpslqsrllvsdtsrpgwinfrellrvaspehnclrtrSGDSMAIYFTSGTTGTPK--MVEHSQCs 245
Cdd:cd17645 102 N---------------------------------------------------PDDLAYVIYTSGSTGLPKgvMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 246 ygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVfvHELPQVDAQTI--LNTLCRFPITTICCVPTLf 323
Cdd:cd17645 130 --VNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAAL--HVVPSERRLDLdaLNDYFNQEGITISFLPTG- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 rllVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKnqtgleIHEGYGQSETVLICGNFR-GSTIKSGSMGKASPPYDVQI 402
Cdd:cd17645 205 ---AAEQFMQLDNQSLRVLLTGGDKLKKIERKGYK------LVNNYGPTENTVVATSFEiDKPYANIPIGKPIDNTRVYI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 403 VDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAASEQGD-------FYITGDRAHMDEDGYFWFVGRNDDVIN 475
Cdd:cd17645 276 LDEALQLQPIGVAGELCIAGEG-----LARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLGRLDQQVK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 476 SSSYRIGPVEVESALAEHPAVLESAVVSSPDpirGEVVKAFIvlspAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFI 555
Cdd:cd17645 351 IRGYRIEPGEIEPFLMNHPLIELAAVLAKED---ADGRKYLV----AYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHL 423
|
490
....*....|....*.
gi 88196780 556 SELPKTVSGKILRSKL 571
Cdd:cd17645 424 KALPLTANGKVDRKAL 439
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
80-574 |
4.36e-31 |
|
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: 127.40 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 80 VNGSGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPR----LPEWWltivACMRTGVVMIPgisqlTQKDLKY 155
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLR-QLGLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAP-----LTVPPTY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 156 RLQAARVKS------------IITSDALAPHVDAISADCPSLQSRLLVSDtsrpgwinfrELLRVASPEHncLRTRSGDS 223
Cdd:cd05906 101 DEPNARLRKlrhiwqllgspvVLTDAELVAEFAGLETLSGLPGIRVLSIE----------ELLDTAADHD--LPQSRPDD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 224 MA-IYFTSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFWNttdtgWVKaawtLFSAwanGACVFVHELP----- 297
Cdd:cd05906 169 LAlLMLTSGSTGFPKAVPLTHRNI-LARSAGKIQHNGLTPQDVFLN-----WVP----LDHV---GGLVELHLRAvylgc 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 298 -QVDAQT---------ILNTLCRFPITtICCVPTLFRLLVQEDLTR-----YKFQCLRHCLAGGEALNSDVRDKWKN--- 359
Cdd:cd05906 236 qQVHVPTeeiladplrWLDLIDRYRVT-ITWAPNFAFALLNDLLEEiedgtWDLSSLRYLVNAGEAVVAKTIRRLLRlle 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 360 QTGLE---IHEGYGQSET---VLICGNFRGSTIKSG----SMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfC 429
Cdd:cd05906 315 PYGLPpdaIRPAFGMTETcsgVIYSRSFPTYDHSQAlefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP-----V 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 430 LFNCYLDNPEKTAASEQGD-FYITGDRAHMDeDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLES--AVVSSPD 506
Cdd:cd05906 390 VTKGYYNNPEANAEAFTEDgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRD 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196780 507 PIRGEVVKAfIVLSPAYVSHDP-EALTRELQEHVK---TVTAPYKYP-RKvafiSELPKTVSGKILRSKLRNQ 574
Cdd:cd05906 469 PGAETEELA-IFFVPEYDLQDAlSETLRAIRSVVSrevGVSPAYLIPlPK----EEIPKTSLGKIQRSKLKAA 536
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
90-571 |
1.04e-30 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 124.67 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqkdlkyrlqaarvksiitsd 169
Cdd:cd17652 14 TYAELNARANRLARLLA-ARGVGPERLVALALPRSAELVVAILAVLKAGAAYLP-------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 alaphvdaISADCPSLQSRLLVSDtSRPGwinfrellrvaspehnCLRTRSGDSMAIYFTSGTTGTPK--MVEHSqcsyG 247
Cdd:cd17652 67 --------LDPAYPAERIAYMLAD-ARPA----------------LLLTTPDNLAYVIYTSGSTGRPKgvVVTHR----G 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 L-GFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFVHELPQVDAQTILNTLCRFPITTICCVPTLFRL 325
Cdd:cd17652 118 LaNLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATlVLAPAEELLPGEPLADLLREHRITHVTLPPAALAA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 326 LVQEDLTRykfqcLRHCLAGGEALNSDVRDKWKNqtGLEIHEGYGQSETVLicgnfrGSTIKSGSMGKASPP-------Y 398
Cdd:cd17652 198 LPPDDLPD-----LRTLVVAGEACPAELVDRWAP--GRRMINAYGPTETTV------CATMAGPLPGGGVPPigrpvpgT 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 399 DVQIVDEEGNVLPPGKEGNIAIR-IKPTRPfclfncYLDNPEKTAASEQGD--------FYITGDRAHMDEDGYFWFVGR 469
Cdd:cd17652 265 RVYVLDARLRPVPPGVPGELYIAgAGLARG------YLNRPGLTAERFVADpfgapgsrMYRTGDLARWRADGQLEFLGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 470 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVTAPYKYP 549
Cdd:cd17652 339 ADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVP 413
|
490 500
....*....|....*....|..
gi 88196780 550 RKVAFISELPKTVSGKILRSKL 571
Cdd:cd17652 414 AAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
90-571 |
1.32e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 128.36 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSd 169
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ- 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 alaphvdaisadcPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMA-IYFTSGTTGTPK--MVEHSQCSy 246
Cdd:PRK12467 617 -------------SHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAyVIYTSGSTGQPKgvAISHGALA- 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 247 glGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVfvHELPQ---VDAQTILNTLCRFPITTICCVPTLF 323
Cdd:PRK12467 683 --NYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVPSHL 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 RLLVQEDLTRykfQCLR-HCLA-GGEALNSDVRDKWKN-QTGLEIHEGYGQSETVLICGNFR----GSTIKSGSMGKASP 396
Cdd:PRK12467 759 QALLQASRVA---LPRPqRALVcGGEALQVDLLARVRAlGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLA 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 397 PYDVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFVG 468
Cdd:PRK12467 836 NLGLYILDHYLNPVPVGVVGELYIGGAG-----LARGYHRRPALTAerfvpdpfGADGGRLYRTGDLARYRADGVIEYLG 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 469 RNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKY 548
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMV 989
|
490 500
....*....|....*....|...
gi 88196780 549 PRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK12467 990 PAHLLLLDSLPLTPNGKLDRKAL 1012
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
90-571 |
2.47e-30 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 127.08 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK10252 485 SYREMREQVVALANLLR-ERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDAISADCPSLQSRLLVSDTSRPgwinfrelLRVASPEHnclrtrsgdSMAIYFTSGTTGTPK--MVEHSqcsyg 247
Cdd:PRK10252 564 DQLPRFADVPDLTSLCYNAPLAPQGAAP--------LQLSQPHH---------TAYIIFTSGSTGRPKgvMVGQT----- 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 lgfvASGRRLM------ALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHElPQV--DAQTILNTLCRFPITTICCV 319
Cdd:PRK10252 622 ----AIVNRLLwmqnhyPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAE-PEAhrDPLAMQQFFAEYGVTTTHFV 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 320 PTLFRLLVQE---DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVL------ICG----NFRGSTI 386
Cdd:PRK10252 697 PSMLAAFVASltpEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdvswypAFGeelaAVRGSSV 776
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 387 KSGsmgkaSPPYDVQ--IVDEEGNVLPPGKEGNIAIR-IKptrpfcLFNCYLDNPEKTA-------ASEQGDFYITGDRA 456
Cdd:PRK10252 777 PIG-----YPVWNTGlrILDARMRPVPPGVAGDLYLTgIQ------LAQGYLGRPDLTAsrfiadpFAPGERMYRTGDVA 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 457 HMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHP----AVLESAVVSSPDPIRGEVVKafIVlspAY-VSHDPEAL 531
Cdd:PRK10252 846 RWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQ--LV---GYlVSQSGLPL 920
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 88196780 532 TRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK10252 921 DTSaLQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
165-576 |
5.47e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 123.98 E-value: 5.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 165 IITSDALAPHVDAIsaDCPSLqsRLLVSDTsrPGWinfRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVehsQC 244
Cdd:PRK13388 103 LVTDAEHRPLLDGL--DLPGV--RVLDVDT--PAY---AELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAV---RC 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 245 SYG----LGFVASGRRlmALTESDIFWNTT---DTGWVKAAWTlfSAWANGACVFVHelPQVDAQTILNTLCRFPITTIC 317
Cdd:PRK13388 171 SHGrlafAGRALTERF--GLTRDDVCYVSMplfHSNAVMAGWA--PAVASGAAVALP--AKFSASGFLDDVRRYGATYFN 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 318 CV-PTLFRLLVQEDLTRYKFQCLRHCLaGGEALNSDvRDKWKNQTGLEIHEGYGQSETVLICgnFRGSTIKSGSMGKASP 396
Cdd:PRK13388 245 YVgKPLAYILATPERPDDADNPLRVAF-GNEASPRD-IAEFSRRFGCQVEDGYGSSEGAVIV--VREPGTPPGSIGRGAP 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 397 pyDVQIV-------------DEEGNVLPPGKegniAI-RIKPTRPFCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDG 462
Cdd:PRK13388 321 --GVAIYnpetltecavarfDAHGALLNADE----AIgELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 463 YFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyVSHDPEALTREL--QEHVK 540
Cdd:PRK13388 395 WIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAAFLaaQPDLG 473
|
410 420 430
....*....|....*....|....*....|....*.
gi 88196780 541 TVTApykyPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK13388 474 TKAW----PRYVRIAADLPSTATNKVLKRELIAQGW 505
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
99-573 |
1.47e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 123.21 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 99 RKAANILegACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAI 178
Cdd:PLN03102 51 RLAASLI--SLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 179 SADCPSLQSRL-----LVSDTSRPGWINFRE-----LLRVASPEHNCLRT-----RSGDSMAIYFTSGTTGTPKmvehsq 243
Cdd:PLN03102 129 LHLLSSEDSNLnlpviFIHEIDFPKRPSSEEldyecLIQRGEPTPSLVARmfriqDEHDPISLNYTSGTTADPK------ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 csyglGFVASGRRLMALTESDIFwnttdtGWVKAA-----WTL-----------FSAWANGACVFVheLPQVDAQTILNT 307
Cdd:PLN03102 203 -----GVVISHRGAYLSTLSAII------GWEMGTcpvylWTLpmfhcngwtftWGTAARGGTSVC--MRHVTAPEIYKN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 308 LCRFPITTICCVPTLFRLLVQEDLTRYKFQCLR-HCLAGGEALNSDVRDKWKnQTGLEIHEGYGQSET---VLIC----- 378
Cdd:PLN03102 270 IEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPvHVLTGGSPPPAALVKKVQ-RLGFQVMHAYGLTEAtgpVLFCewqde 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 379 ------GNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKE-GNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYI 451
Cdd:PLN03102 349 wnrlpeNQQMELKARQGVSILGLADVDVKNKETQESVPRDGKTmGEIVIKGS-----SIMKGYLKNPKATSEAFKHGWLN 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 452 TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL--SPAYVSHDPE 529
Cdd:PLN03102 424 TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLekGETTKEDRVD 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 88196780 530 ALT---RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PLN03102 504 KLVtreRDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRD 550
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
84-555 |
1.87e-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: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 84 GTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVK 163
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALR-ALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 164 SIITS-----DALAPHVDAisadcpSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKM 238
Cdd:cd05932 81 ALFVGklddwKAMAPGVPE------GLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 239 VEHSQCSYGLGfVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACV--FVHELpqvdaQTILNTLCRFPITTI 316
Cdd:cd05932 155 VMLTFGSFAWA-AQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLvaFAESL-----DTFVEDVQRARPTLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 317 CCVP---TLFRLLVQEDLTRYKFQCL--------------------RHC--LAGGEALNSDVRDKWKNQTGLEIHEGYGQ 371
Cdd:cd05932 229 FSVPrlwTKFQQGVQDKIPQQKLNLLlkipvvnslvkrkvlkglglDQCrlAGCGSAPVPPALLEWYRSLGLNILEAYGM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 372 SEtvlicgNFRGSTI------KSGSMGKASPPYDVQIvDEEGNVLppgkegniairikpTRPFCLFNCYLDNPEKTAASE 445
Cdd:cd05932 309 TE------NFAYSHLnypgrdKIGTVGNAGPGVEVRI-SEDGEIL--------------VRSPALMMGYYKDPEATAEAF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 446 QGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYR-IGPVEVESALAEHPAVLESAVVSS--PDPIRGEVVKAFIVlsP 521
Cdd:cd05932 368 TADgFLRTGDKGELDADGNLTITGRVKDIFKTSKGKyVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEAR--L 445
|
490 500 510
....*....|....*....|....*....|....
gi 88196780 522 AYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFI 555
Cdd:cd05932 446 RADAFARAELEASLRAHLARVNSTLDSHEQLAGI 479
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
215-566 |
1.54e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 121.18 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 215 CLRTRSGDSMA-IYFTSGTTGTPKmvehsqcsyglGFVASGRRLMALTE--SDIFwNTTDTGWVKAAWTLFSA------- 284
Cdd:PRK08633 775 YGPTFKPDDTAtIIFSSGSEGEPK-----------GVMLSHHNILSNIEqiSDVF-NLRNDDVILSSLPFFHSfgltvtl 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 285 W---ANGACVFVHELPqVDAQTILNTLCRFPITTICCVPTLFRLLvqedlTRYK------FQCLRHCLAGGEALNSDVRD 355
Cdd:PRK08633 843 WlplLEGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLY-----LRNKklhplmFASLRLVVAGAEKLKPEVAD 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 356 KWKNQTGLEIHEGYGQSET----------VLICGNFRGSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAIRiKP 424
Cdd:PRK08633 917 AFEEKFGIRILEGYGATETspvasvnlpdVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-GP 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 425 TrpfcLFNCYLDNPEKTAA----SEQGDFYITGDRAHMDEDGYFWFVGRnddviNSSSYRIG----PV-EVESALAE--H 493
Cdd:PRK08633 996 Q----VMKGYLGDPEKTAEvikdIDGIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemvPLgAVEEELAKalG 1066
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196780 494 PAVLESAVVSSPDPIRGEVVkafIVLspayvsHDPEAL-TRELQEHVKTVTAP--YKyPRKVAFISELPKTVSGKI 566
Cdd:PRK08633 1067 GEEVVFAVTAVPDEKKGEKL---VVL------HTCGAEdVEELKRAIKESGLPnlWK-PSRYFKVEALPLLGSGKL 1132
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
125-576 |
1.92e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 119.40 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 125 PEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPslqsrllVSDTSRPGWINFRE 204
Cdd:PRK07867 65 PEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGVR-------VINVDSPAWADELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 205 LLRVASPEHNclRTRSGDSMAIYFTSGTTGTPKMVehsQCSYGLgFVASGRRLMA---LTESDIFWNTT---DTGWVKAA 278
Cdd:PRK07867 138 AHRDAEPPFR--VADPDDLFMLIFTSGTSGDPKAV---RCTHRK-VASAGVMLAQrfgLGPDDVCYVSMplfHSNAVMAG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 279 WTLfsAWANGACVFVHelPQVDAQTILNTLCRFPITTICCV--PtLFRLLVQEDLTRYKFQCLRhCLAGGEALNSDVrDK 356
Cdd:PRK07867 212 WAV--ALAAGASIALR--RKFSASGFLPDVRRYGATYANYVgkP-LSYVLATPERPDDADNPLR-IVYGNEGAPGDI-AR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 357 WKNQTGLEIHEGYGQSETVLICGnfRGSTIKSGSMGKASPpyDVQIVD-EEGNVLPPGK-------EGNIAI--RIKPTR 426
Cdd:PRK07867 285 FARRFGCVVVDGFGSTEGGVAIT--RTPDTPPGALGPLPP--GVAIVDpDTGTECPPAEdadgrllNADEAIgeLVNTAG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 427 PfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPD 506
Cdd:PRK07867 361 P-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPD 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 507 PIRGEVVKAFIVLSPAyVSHDPEALTRELqeHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK07867 440 PVVGDQVMAALVLAPG-AKFDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
90-571 |
4.87e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 120.45 E-value: 4.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK12316 2030 SYAELDSRANRLAHRLR-ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALaphvdaiSADCPSLQSrLLVSDTSRPGWINfrellrvASPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQCSYGL 248
Cdd:PRK12316 2109 HL-------LERLPLPAG-VARLPLDRDAEWA-------DYPDTAPAVQLAGENLAyVIYTSGSTGLPKGVAVSHGALVA 2173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 249 GFVASGRRlMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQ 328
Cdd:PRK12316 2174 HCQAAGER-YELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAE 2252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 329 EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLE-IHEGYGQSETVLI-----CGNFRGSTIKSGSMGKASPPYDVQI 402
Cdd:PRK12316 2253 HAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTpllwkCRPQDPCGAAYVPIGRALGNRRAYI 2332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 403 VDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFVGRNDDVI 474
Cdd:PRK12316 2333 LDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQV 2407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 475 NSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIvlspayVSHDP-EALTRELQEHVKTVTAPYKYPRKVA 553
Cdd:PRK12316 2408 KIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYV------VPDDAaEDLLAELRAWLAARLPAYMVPAHWV 2480
|
490
....*....|....*...
gi 88196780 554 FISELPKTVSGKILRSKL 571
Cdd:PRK12316 2481 VLERLPLNPNGKLDRKAL 2498
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
220-573 |
1.03e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 117.92 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 220 SGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHE---- 295
Cdd:PTZ00237 253 SSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEggii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 296 LPQVDAQTILNTLCRFPITTICCVPTLFRLLVQED------LTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGY 369
Cdd:PTZ00237 333 KNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRGY 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 370 GQSE---TVLICgnFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIkPTRPfCLFNCYLDNPE--KTAAS 444
Cdd:PTZ00237 413 GQTEigiTYLYC--YGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPP-SFATTFYKNDEkfKQLFS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 445 EQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYV 524
Cdd:PTZ00237 489 KFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQDQS 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 88196780 525 SH--DPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PTZ00237 569 NQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
90-574 |
1.23e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 116.42 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILeGACGLKPgDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK07638 28 TYKDWFESVCKVANWL-NEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNADMIVTER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDaiSADCPSLQSRLLVSDTSRpgwiNFRELLRVASPEHnclrtrsgDSMAIYFTSGTTGTPKMVEHSQCSYGLG 249
Cdd:PRK07638 106 YKLNDLP--DEEGRVIEIDEWKRMIEK----YLPTYAPIENVQN--------APFYMGFTSGSTGKPKAFLRAQQSWLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 250 FvasgrrlmALTESDIFWNTTDTgwVKAAWTLFSA---WANGACVF----VHELPQVDAQTILNTLCRFPITTICCVPTL 322
Cdd:PRK07638 172 F--------DCNVHDFHMKREDS--VLIAGTLVHSlflYGAISTLYvgqtVHLMRKFIPNQVLDKLETENISVMYTVPTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 323 FRLLVQEDltRYKFQCLRhCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSETVLICG-NFRGSTIKSGSMGKASPPYDV 400
Cdd:PRK07638 242 LESLYKEN--RVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFYGASELSFVTAlVDEESERRPNSVGRPFHNVQV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 401 QIVDEEGNVLPPGKEGNIAIRiKPTRpfclFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYR 480
Cdd:PRK07638 319 RICNEAGEEVQKGEIGTVYVK-SPQF----FMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 481 IGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlspayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPK 560
Cdd:PRK07638 394 IFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPY 464
|
490
....*....|....
gi 88196780 561 TVSGKILRSKLRNQ 574
Cdd:PRK07638 465 TNSGKIARMEAKSW 478
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
485-565 |
5.74e-27 |
|
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: 103.78 E-value: 5.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 485 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSG 564
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 88196780 565 K 565
Cdd:pfam13193 76 K 76
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
86-568 |
9.13e-27 |
|
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: 113.69 E-value: 9.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDalaphvdaisadcpslqsrllvsdtsrpgwinfrellrvasPEhnclrtrsgDSMAIYFTSGTTGTPK--MVEHSQ 243
Cdd:cd05914 84 FVSD-----------------------------------------ED---------DVALINYTSGTTGNSKgvMLTYRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 CsygLGFVASGRRLMALTESDIFWNTTDTGWV-KAAWTLFSAWANGA-CVFVHELPQvdAQTILNTLCRFPITTICCVPT 321
Cdd:cd05914 114 I---VSNVDGVKEVVLLGKGDKILSILPLHHIyPLTFTLLLPLLNGAhVVFLDKIPS--AKIIALAFAQVTPTLGVPVPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 322 LFR------LLVQEDLTRYKFQC------------------------LRHCLAGGEALNSDVRDKWKnQTGLEIHEGYGQ 371
Cdd:cd05914 189 VIEkifkmdIIPKLTLKKFKFKLakkinnrkirklafkkvheafggnIKEFVIGGAKINPDVEEFLR-TIGFPYTIGYGM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 372 SETV-LICGNfRGSTIKSGSMGKASPPYDVQIVDEEgnvlPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAA--SEQGD 448
Cdd:cd05914 268 TETApIISYS-PPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPN-----VMKGYYKNPEATAEafDKDGW 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 449 FYiTGDRAHMDEDGYFWFVGRNDDVINSSSYR-IGPVEVESALAEHPAVLESAVVsspdpIRGEVVKAFIVLSPAY---- 523
Cdd:cd05914 338 FH-TGDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFldvk 411
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 88196780 524 ---VSHDPEALTRELQEHVKTVTAPYKYPRKVAFI-SELPKTVSGKILR 568
Cdd:cd05914 412 alkQRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
179-572 |
1.13e-26 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 114.17 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 179 SADCPSLQSRLlvsdtsRPGWINFRELLRVASPEHNCLRTRSG-DSMAIYFTSGTTGTPK-MVEHSQCSYglgfvasgrr 256
Cdd:PLN02479 158 TCDPKSLQYAL------GKGAIEYEKFLETGDPEFAWKPPADEwQSIALGYTSGTTASPKgVVLHHRGAY---------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 257 LMALTESdIFWNTTD-------------TGWVkAAWTLFSAWANGACvfvheLPQVDAQTILNTLCRFPITTICCVPTLF 323
Cdd:PLN02479 222 LMALSNA-LIWGMNEgavylwtlpmfhcNGWC-FTWTLAALCGTNIC-----LRQVTAKAIYSAIANYGVTHFCAAPVVL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 324 RLLVQ--EDLTRYKFQCLRHCLAGGEALNSDVRDKWkNQTGLEIHEGYGQSETvlicgnFRGSTIKSGSMGKASPPYDVQ 401
Cdd:PLN02479 295 NTIVNapKSETILPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHTYGLSET------YGPSTVCAWKPEWDSLPPEEQ 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 402 ------------------IVDEEGNVLPP--GKE-GNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDE 460
Cdd:PLN02479 368 arlnarqgvryiglegldVVDTKTMKPVPadGKTmGEIVMRGN-----MVMKGYLKNPKANEEAFANGWFHSGDLGVKHP 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 461 DGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRELQEHVK 540
Cdd:PLN02479 443 DGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCR 522
|
410 420 430
....*....|....*....|....*....|..
gi 88196780 541 TVTAPYKYPRKVAFiSELPKTVSGKILRSKLR 572
Cdd:PLN02479 523 ERLPAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
65-571 |
1.35e-26 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 113.95 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 65 LEKTGHRPPNPAFWWVNGSgTEVKWTfEELGKQSRKAANILEGAcgLKPGDRLMLVLPRLPEWWLTIVACMRTGV--VMI 142
Cdd:PRK05857 21 FEQARQQPEAIALRRCDGT-SALRYR-ELVAEVGGLAADLRAQS--VSRGSRVLVISDNGPETYLSVLACAKLGAiaVMA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 143 PG---------ISQLTQKDLKYRLQAARVKSIITSDALAPhVDAISADCPSLQSRLLVS-DTSRPGwinfrellrvASPE 212
Cdd:PRK05857 97 DGnlpiaaierFCQITDPAAALVAPGSKMASSAVPEALHS-IPVIAVDIAAVTRESEHSlDAASLA----------GNAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 213 HNclrtrSGDSMAIYFTSGTTGTPKMVehsqcsyglgfVASGRRLMA----LTESDIFWNTtdtgWVKAA---------- 278
Cdd:PRK05857 166 QG-----SEDPLAMIFTSGTTGEPKAV-----------LLANRTFFAvpdiLQKEGLNWVT----WVVGEttysplpath 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 279 -----WTLFSAWANGACVFVHElpqvDAQTILNTLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGG-EALNS 351
Cdd:PRK05857 226 igglwWILTCLMHGGLCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSElKSANATVPSLRLVGYGGsRAIAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 352 DVRdkWKNQTGLEIHEGYGQSET-----VLICGNFRGSTIKSGSMGKASPPYDVQIVDEEG------NVLPPGKEGNIAI 420
Cdd:PRK05857 302 DVR--FIEATGVRTAQVYGLSETgctalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 421 RikptRPFCLFNcYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESA 500
Cdd:PRK05857 380 K----SPANMLG-YWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAA 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196780 501 VVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK05857 455 CYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-571 |
2.56e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.05 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSI 165
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALA-PHVDAISADCPSLQSRLLvsdtsrpgwinfrellrvasPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVEHSQ 243
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLDLDRGDENY--------------------AEANPAIRTMPENLAyVIYTSGSTGKPKGVGIRH 3218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 244 CSYGLGFVASGRrLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQVDAQTILNTLCRFP-ITTICCVPTL 322
Cdd:PRK12316 3219 SALSNHLCWMQQ-AYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEgVDVLHAYPSM 3297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 323 FRLLVQEDLTRyKFQCLRHCLAGGEALNSDVRDKWknQTGLEIHEGYGQSETVLICGNFRGSTIKSGS--MGKASPPYDV 400
Cdd:PRK12316 3298 LQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRAC 3374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 401 QIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAA-------SEQGDFYITGDRAHMDEDGYFWFVGRNDDV 473
Cdd:PRK12316 3375 YILDGSLEPVPVGALGELYLGGEG-----LARGYHNRPGLTAErfvpdpfVPGERLYRTGDLARYRADGVIEYIGRVDHQ 3449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 474 INSSSYRIGPVEVESALAEHPAVLESAVVSspdpIRGEVVKAFIVLSpayvshDPE-ALTRELQEHVKTVTAPYKYPRKV 552
Cdd:PRK12316 3450 VKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPE------DEAgDLREALKAHLKASLPEYMVPAHL 3519
|
490
....*....|....*....
gi 88196780 553 AFISELPKTVSGKILRSKL 571
Cdd:PRK12316 3520 LFLERMPLTPNGKLDRKAL 3538
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
84-574 |
1.64e-25 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 110.61 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 84 GTEVKWTFEELGKQSRKAANILEGAcGLKPGDRLMLV---LPRLPEWWLTIvacMRTGVVMIPGISQLTQKDLKYRLQAA 160
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWYGI---MGIGAICHTVNPRLFPEQIAWIINHA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 161 RVKSIITSDALAPHVDAISADCPSLQSRLLVSD------TSRPGWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTG 234
Cdd:PRK06018 111 EDRVVITDLTFVPILEKIADKLPSVERYVVLTDaahmpqTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTTG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 235 TPKMVEHSQCSYGL-GFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVfVHELPQVDAQTILNTLCRFPI 313
Cdd:PRK06018 191 DPKGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKL-VMPGAKLDGASVYELLDTEKV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 314 TTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQtGLEIHEGYGQSETVLIcGNFrgSTIK---SG 389
Cdd:PRK06018 270 TFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTEMSPL-GTL--AALKppfSK 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 390 SMGKAS---------PPYDVQ--IVDEEGNVLPpgKEGNIAIRIKPTRPfCLFNCYLdNPEKTAASEQGdFYITGDRAHM 458
Cdd:PRK06018 346 LPGDARldvlqkqgyPPFGVEmkITDDAGKELP--WDGKTFGRLKVRGP-AVAAAYY-RVDGEILDDDG-FFDTGDVATI 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 459 DEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayvshDPEALTRELQEH 538
Cdd:PRK06018 421 DAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP-----GETATREEILKY 495
|
490 500 510
....*....|....*....|....*....|....*.
gi 88196780 539 VKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK06018 496 MDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
90-571 |
4.09e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 111.02 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK12467 1601 TYGELNRRANRLAHRLI-ALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPHVDAISAdcpslqSRLLVSDTSRpGWINfrellrvASPEHNCLRTRSGDSMA--IYfTSGTTGTPKMVEHSQCSYG 247
Cdd:PRK12467 1680 HLQARLPLPDG------LRSLVLDQED-DWLE-------GYSDSNPAVNLAPQNLAyvIY-TSGSTGRPKGAGNRHGALV 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 LGFVASGRRLmALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFV-----HELPqvdAQTIlNTLCRFPITTICCVPTL 322
Cdd:PRK12467 1745 NRLCATQEAY-QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIappgaHRDP---EQLI-QLIERQQVTTLHFVPSM 1819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 323 FRLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTG-LEIHEGYGQSETVlICGNFRGSTIKSGSMGKASP---PY 398
Cdd:PRK12467 1820 LQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETA-VDVTHWTCRRKDLEGRDSVPigqPI 1898
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 399 D---VQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFV 467
Cdd:PRK12467 1899 AnlsTYILDASLNPVPIGVAGELYLGGVG-----LARGYLNRPALTAerfvadpfGTVGSRLYRTGDLARYRADGVIEYL 1973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 468 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIV-LSPAYVSHD--PEALTRELQEHVKTVTA 544
Cdd:PRK12467 1974 GRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDeaQVALRAILKNHLKASLP 2052
|
490 500
....*....|....*....|....*..
gi 88196780 545 PYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK12467 2053 EYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-571 |
9.78e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 110.05 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 33 EVVATWEAislgkrpVPEYFNFAHDVLDVW-SQLEKTghrPPNPAFwwVNGsgtEVKWTFEELGKQSRKAANILEgACGL 111
Cdd:PRK12316 495 QLVEGWNA-------TAAEYPLQRGVHRLFeEQVERT---PEAPAL--AFG---EETLDYAELNRRANRLAHALI-ERGV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 112 KPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDaisadcpsLQSRLLV 191
Cdd:PRK12316 559 GPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLP--------LAAGVQV 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 192 SDTSRPG-WINfrellrvASPEHNCLRTRSGDSMA-IYFTSGTTGTPKMV--EHS---------QCSYGLGfvASGRRLM 258
Cdd:PRK12316 631 LDLDRPAaWLE-------GYSEENPGTELNPENLAyVIYTSGSTGKPKGAgnRHRalsnrlcwmQQAYGLG--VGDTVLQ 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 259 ALTES-DIfwnttdtgwvkAAWTLFSAWANGACVfvHELPQ---VDAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRy 334
Cdd:PRK12316 702 KTPFSfDV-----------SVWEFFWPLMSGARL--VVAAPgdhRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA- 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 335 kfQC--LRHCLAGGEALNSDVRDKW---KNQTGLEIHegYGQSETV--LICGNFRGSTIKSGSMGKASPPYDVQIVDEEG 407
Cdd:PRK12316 768 --SCtsLRRIVCSGEALPADAQEQVfakLPQAGLYNL--YGPTEAAidVTHWTCVEEGGDSVPIGRPIANLACYILDANL 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 408 NVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTA----ASEQGD---FYITGDRAHMDEDGYFWFVGRNDDVINSSSYR 480
Cdd:PRK12316 844 EPVPVGVLGELYLAGRG-----LARGYHGRPGLTAerfvPSPFVAgerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 918
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 481 IGPVEVESALAEHPAVLESAVVSspdpIRGEVVKAFIVLSpayvshDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELP 559
Cdd:PRK12316 919 IELGEIEARLLEHPWVREAAVLA----VDGKQLVGYVVLE------SEGGDWREaLKAHLAASLPEYMVPAQWLALERLP 988
|
570
....*....|..
gi 88196780 560 KTVSGKILRSKL 571
Cdd:PRK12316 989 LTPNGKLDRKAL 1000
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
88-574 |
7.37e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 105.56 E-value: 7.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILeGACGLKPGDR------------------------LMLVLPRL-PEWWLTIVACMRTGVVMI 142
Cdd:PRK07008 39 RYTYRDCERRAKQLAQAL-AALGVEPGDRvgtlawngyrhleayygvsgsgavCHTINPRLfPEQIAYIVNHAEDRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 143 pgisqltqkDLKYrlqaarvksiitsdalAPHVDAISADCPSLQSRLLVSDTSR-PG----WINFRELLRVASPEHN--C 215
Cdd:PRK07008 118 ---------DLTF----------------LPLVDALAPQCPNVKGWVAMTDAAHlPAgstpLLCYETLVGAQDGDYDwpR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 216 LRTRSGDSMAiyFTSGTTGTPKMVEHSQCSYGL-GFVASGRRLMALTESDIFWNTTDTGWVKAaWTL-FSAWANGaCVFV 293
Cdd:PRK07008 173 FDENQASSLC--YTSGTTGNPKGALYSHRSTVLhAYGAALPDAMGLSARDAVLPVVPMFHVNA-WGLpYSAPLTG-AKLV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 294 HELPQVDAQTILNTLCRFPITTICCVPTLFRLLVQE-DLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQS 372
Cdd:PRK07008 249 LPGPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 373 E-----TVLICGNFRGSTIKSGSM------GKASPPYDVQIVDEEGNVLP-PGKE-GNIAIRikptRPFCLfncylDNPE 439
Cdd:PRK07008 329 EmsplgTLCKLKWKHSQLPLDEQRkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR----GPWVI-----DRYF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 440 KTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 518
Cdd:PRK07008 400 RGDASPLVDgWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 88196780 519 LSPAYvshdpeALTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK07008 480 KRPGA------EVTReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-576 |
2.52e-23 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 105.64 E-value: 2.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 72 PPNPAFWWVNGSgtevkWTFEELGKQSRKAANILEGaCGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQK 151
Cdd:PRK05691 1145 PERIALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAE 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 152 DLKYRLQAARVKSIITSDAL---APHVDAISADCpsLQSRLLVSDTSRPGWINFrellrvaspehnclrtrSGDSMA-IY 227
Cdd:PRK05691 1219 RLAYMLADSGVELLLTQSHLlerLPQAEGVSAIA--LDSLHLDSWPSQAPGLHL-----------------HGDNLAyVI 1279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 228 FTSGTTGTPKMVehsqcsyGLGFVASGRRLM------ALTESDIFWNTTDTGWVKAAWTLFSAWANGaCVFVHELP--QV 299
Cdd:PRK05691 1280 YTSGSTGQPKGV-------GNTHAALAERLQwmqatyALDDSDVLMQKAPISFDVSVWECFWPLITG-CRLVLAGPgeHR 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 300 DAQTILNTLCRFPITTICCVPTLFRLLVQEDLTRykfQC--LRHCLAGGEALNSDVRDKWKNQ-TGLEIHEGYGQSETVL 376
Cdd:PRK05691 1352 DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA---ACtsLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAI 1428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 377 ICGNFRGStiksGSMGKASP---PYD---VQIVDEEGNVLPPGKEGNIAIRikptrPFCLFNCYLDNPEKTAA------- 443
Cdd:PRK05691 1429 NVTHWQCQ----AEDGERSPigrPLGnvlCRVLDAELNLLPPGVAGELCIG-----GAGLARGYLGRPALTAErfvpdpl 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 444 SEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVsspdpIRGEVVKAFIVlspA 522
Cdd:PRK05691 1500 GEDGArLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLV---G 1571
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 88196780 523 YVSHD--PEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK05691 1572 YYTGEagQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVW 1627
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
90-538 |
3.23e-23 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 103.44 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMI---PGISQltqKDLKYRLQAARVKSII 166
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPGMGI---KNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 167 TSdALApHVDAI--SADCPSLQSRLLVSDTSRPGWINFRELLRVASP-EHNCLRTRSGDSMAIYFTSGTTGTPKMV--EH 241
Cdd:PRK09274 119 GI-PKA-HLARRlfGWGKPSVRRLVTVGGRLLWGGTTLATLLRDGAAaPFPMADLAPDDMAAILFTSGSTGTPKGVvyTH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 242 SQcsyglgFVAsgrRLMALTES-DIFWNTTDTgwvkAAWTLFS--AWANGACVFVHEL----P-QVDAQTILNTLCRFPI 313
Cdd:PRK09274 197 GM------FEA---QIEALREDyGIEPGEIDL----PTFPLFAlfGPALGMTSVIPDMdptrPaTVDPAKLFAAIERYGV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 314 TTICCVPTLFRLLVQEDLTR-YKFQCLRHCLAGG------------EALNSDVrdkwknqtglEIHEGYGQSETVLICG- 379
Cdd:PRK09274 264 TNLFGSPALLERLGRYGEANgIKLPSLRRVISAGapvpiavierfrAMLPPDA----------EILTPYGATEALPISSi 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 380 ----NFRGSTIKSGSM-----GKASPPYDVQIVD---------EEGNVLPPGKEGNIAIRiKP--TRpfclfnCYLDNPE 439
Cdd:PRK09274 334 esreILFATRAATDNGagicvGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA-GPmvTR------SYYNRPE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 440 KTAAS----EQGDFY-ITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPirGEVVK 514
Cdd:PRK09274 407 ATRLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP--GAQRP 484
|
490 500
....*....|....*....|....
gi 88196780 515 AFIVLSPAYVSHDPEALTRELQEH 538
Cdd:PRK09274 485 VLCVELEPGVACSKSALYQELRAL 508
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
121-574 |
3.89e-23 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 102.97 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 121 LPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALA------PHVDAISADCPSLQSRLLVSDT 194
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 195 S-----RPGWINFRELLRVASPEH----NCLRTRSGDS---MAIYFTSGTTGTPKMVEHSQCSyGLGFVASGRRLMALTE 262
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAQGsvggNEYSPVYAPVesvTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 263 SDIFWNTTDTGWVKAAWTLFSAWANGACVFVHElpqvdAQTILNTLCRF----PITTICCVPTLFR--------LLVQED 330
Cdd:PLN03051 160 GDVVCWPTNLGWMMGPWLLYSAFLNGATLALYG-----GAPLGRGFGKFvqdaGVTVLGLVPSIVKawrhtgafAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 331 LTRYKFQCLRhclagGEALNSD-------VRDKWKNQT----GLEIHEGYGQSETVLICGNfrgSTIKSGSMGKAsppyd 399
Cdd:PLN03051 235 WSKLRVFAST-----GEASAVDdvlwlssVRGYYKPVIeycgGTELASGYISSTLLQPQAP---GAFSTASLGTR----- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 400 VQIVDEEGNVLPPGKE--GNIAIRIkptrPFCLFNCYLDNPEKTAASEQG--DFYITGD--RAHMDE-----DGYFWFVG 468
Cdd:PLN03051 302 FVLLNDNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmpMYGSKGMplRRHGDImkrtpGGYFCVQG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 469 RNDDVINSSSYRIGPVEVESALAE-HPAVLESAVVSSPDPIRGE----VVKAFIVLSPAYVSHDPEALTRELQEHVKTVT 543
Cdd:PLN03051 378 RADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTNL 457
|
490 500 510
....*....|....*....|....*....|.
gi 88196780 544 APYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN03051 458 NPLFKVSRVKIVPELPRNASNKLLRRVLRDQ 488
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
207-571 |
6.90e-23 |
|
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: 101.78 E-value: 6.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 207 RVASPEHNCLRTRSGDSMA-IYFTSGTTGTPKMVE-HSQCSygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSA 284
Cdd:cd17654 103 LSFTPEHRHFNIRTDECLAyVIHTSGTTGTPKIVAvPHKCI--LPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 285 WANGAC---------VFVHELPQVDAQtilntlcRFPITTICCVPTLFRLLVQEDLTRY---KFQCLRHCLAGGEALNSD 352
Cdd:cd17654 181 LSSGATllivptsvkVLPSKLADILFK-------RHRITVLQATPTLFRRFGSQSIKSTvlsATSSLRVLALGGEPFPSL 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 353 VRDKWKNQTGLEIH--EGYGQSETVLICGNFRGSTIKSG-SMGKASPPYDVQIVDEEGNvlppGKEGNIAIRIKPTRpfC 429
Cdd:cd17654 254 VILSSWRGKGNRTRifNIYGITEVSCWALAYKVPEEDSPvQLGSPLLGTVIEVRDQNGS----EGTGQVFLGGLNRV--C 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 430 LFNCYLDNPEktaaseqGDFYITGDRAHMdEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDpir 509
Cdd:cd17654 328 ILDDEVTVPK-------GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ--- 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 88196780 510 gEVVKAFIVlspayvshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17654 397 -QRLIAFIV--------GESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
86-571 |
1.77e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 102.93 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEgACGLKPgDRLM-LVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKS 164
Cdd:PRK12467 3118 DQQLSYAELNRRANRLAHRLI-AIGVGP-DVLVgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKL 3195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 165 IITSDALAPHVDAISADcpslqSRLLVSDTSRPGWinfrellrvasPEHNCLRTRSGDSMA-IYFTSGTTGTPK--MVEH 241
Cdd:PRK12467 3196 LLTQAHLLEQLPAPAGD-----TALTLDRLDLNGY-----------SENNPSTRVMGENLAyVIYTSGSTGKPKgvGVRH 3259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 242 S---------QCSYGLGfvASGRRLMALTES-DIfwnttdtgwvkAAWTLFSAWANGACVFVHELPQVDAQTILNTLCRF 311
Cdd:PRK12467 3260 GalanhlcwiAEAYELD--ANDRVLLFMSFSfDG-----------AQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAH 3326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 312 PITTICCVPTLFRLLVQeDLTRYKFQCLRHCLAGGEALNSD----VRDKWKNQTgleIHEGYGQSETVLI-----CGNFR 382
Cdd:PRK12467 3327 RISIACFPPAYLQQFAE-DAGGADCASLDIYVFGGEAVPPAafeqVKRKLKPRG---LTNGYGPTEAVVTvtlwkCGGDA 3402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 383 GSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTA--------ASEQGDFYITGD 454
Cdd:PRK12467 3403 VCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRPSLTAerfvadpfSGSGGRLYRTGD 3477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 455 RAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIVLspayvsHDP-EALTR 533
Cdd:PRK12467 3478 LARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVP------ADPqGDWRE 3550
|
490 500 510
....*....|....*....|....*....|....*...
gi 88196780 534 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK12467 3551 TLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
226-571 |
2.04e-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: 100.59 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 226 IYFTSGTTGTPK--MVEH-SQCSYGLGFVasgrRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGAC-VFVHELPQVDA 301
Cdd:cd17644 111 VIYTSGSTGKPKgvMIEHqSLVNLSHGLI----KEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATlVLRPEEMRSSL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 302 QTILNTLCRFPITTICCVPTLFRLLVQEDL--TRYKFQCLRHCLAGGEALNSDVRDKWKNQTG--LEIHEGYGQSE---T 374
Cdd:cd17644 187 EDFVQYIQQWQLTVLSLPPAYWHLLVLELLlsTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEatiA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 375 VLIC--GNFRGSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptrPFCLFNCYLDNPEKTA---------A 443
Cdd:cd17644 267 ATVCrlTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIG-----GVGLARGYLNRPELTAekfishpfnS 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 444 SEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlsPAY 523
Cdd:cd17644 342 SESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV--PHY 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 88196780 524 vshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17644 420 ---EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
226-571 |
3.15e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 100.46 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 226 IYFTSGTTGTPKMVEHS-QCSYGLGF---------VASGRRLMALTEsdiFWNTTDTGWVKAAWTLfsawanGACVFVHE 295
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRApQLRSAVGVwvtildrtrLRTGSRISVAMP---MFHGLGLGMLMLTIAL------GGTVLTHR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 296 lpQVDAQTILNTLCRFPITTICCVP-TLFRLLVQEDLTRYK--FQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQS 372
Cdd:PRK13383 250 --HFDAEAALAQASLHRADAFTAVPvVLARILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGST 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 373 EtVLICGNFRGSTIKSG--SMGKASPPYDVQIVDEEGNVLPPGKEGNIAI--RIKPTRpfclfncYLDNPEKTAASEQGD 448
Cdd:PRK13383 328 E-VGIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVggELAGTR-------YTDGGGKAVVDGMTS 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 449 fyiTGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvsHDP 528
Cdd:PRK13383 400 ---TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG---SGV 473
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 88196780 529 EAltRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK13383 474 DA--AQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-573 |
7.67e-22 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 99.47 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTI--VACMrtGVVMIPGISQLTQKDLKYRLQAARVKSIIT 167
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLEVLfaVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 SDALAPHVDAISADCPSLQSRLLV--SDTSRPGwINFRELLRVASPEhNCLRTRSG----------DSMAIYFTSGTTGT 235
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIgpSDADSAA-AHMPEGIKVYSYE-ALLDGRSTvydwpeldetTAAAICYSTGTTGA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 236 PKMVEHSQCSYGLgfvasgrRLMALTESDIFWNTTDTGWVKA-------AWTL-FSAWANGA-CVFV-HEL-PQVDAQTI 304
Cdd:PRK05620 196 PKGVVYSHRSLYL-------QSLSLRTTDSLAVTHGESFLCCvpiyhvlSWGVpLAAFMSGTpLVFPgPDLsAPTLAKII 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 305 LNTLCRfpitTICCVPTLF-RLLVQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLIcgnfrG 383
Cdd:PRK05620 269 ATAMPR----VAHGVPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPV-----G 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 384 STIK--SGSMGKASPPYDV-----------QIVDeEGNVLPPG--KEGNIAIRiKPTrpfcLFNCYLDNPEKT---AASE 445
Cdd:PRK05620 340 TVARppSGVSGEARWAYRVsqgrfpasleyRIVN-DGQVMESTdrNEGEIQVR-GNW----VTASYYHSPTEEgggAAST 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 446 QGDFYI--------------TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGE 511
Cdd:PRK05620 414 FRGEDVedandrftadgwlrTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGE 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196780 512 VVKAFIVLSPAYvshDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PRK05620 494 RPLAVTVLAPGI---EPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
89-506 |
1.60e-21 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 98.41 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 89 WTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVV--MIPgiSQLTQKDLKYRLQAARVKSII 166
Cdd:PRK08279 63 ISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVvaLLN--TQQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 167 TSDALAPHVDAISADcPSLQSRLLVSD----TSRPGWINFRELLRvASPEHNcLRTRSGDSM---AIY-FTSGTTGTPK- 237
Cdd:PRK08279 140 VGEELVEAFEEARAD-LARPPRLWVAGgdtlDDPEGYEDLAAAAA-GAPTTN-PASRSGVTAkdtAFYiYTSGTTGLPKa 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 238 -MVEHS--QCSYGlGFVAsgrrLMALTESDIFWNTT----DTGWVkAAWTlfSAWANGACVFVHELPQV-----DAQtil 305
Cdd:PRK08279 217 aVMSHMrwLKAMG-GFGG----LLRLTPDDVLYCCLplyhNTGGT-VAWS--SVLAAGATLALRRKFSAsrfwdDVR--- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 306 ntlcRFPITTICCVPTLFRLLVQ----EDLTRYKfqcLRhcLAGGEALNSDVRDKWKNQTGLE-IHEGYGQSE--TVLIc 378
Cdd:PRK08279 286 ----RYRATAFQYIGELCRYLLNqppkPTDRDHR---LR--LMIGNGLRPDIWDEFQQRFGIPrILEFYAASEgnVGFI- 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 379 gNFRGstiKSGSMGKaSPP----------YDVQ----IVDEEGNVLP--PGKEGNIAIRIKPTRPfclFNCYLDnPEKTA 442
Cdd:PRK08279 356 -NVFN---FDGTVGR-VPLwlahpyaivkYDVDtgepVRDADGRCIKvkPGEVGLLIGRITDRGP---FDGYTD-PEASE 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 88196780 443 AS------EQGDFYI-TGDRAHMDEDGYFWFVGRNDDvinssSYR-----IGPVEVESALAEHPAVLESAV--VSSPD 506
Cdd:PRK08279 427 KKilrdvfKKGDAWFnTGDLMRDDGFGHAQFVDRLGD-----TFRwkgenVATTEVENALSGFPGVEEAVVygVEVPG 499
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
86-573 |
1.77e-21 |
|
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: 97.43 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYrlqaarvksI 165
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLY---------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSdalaphvdaisadcpSLQSRLLVSDTSrpgwinfrellrvaspehnclrtrsgDSMA-IYFTSGTTGTPK--MVEHS 242
Cdd:cd17640 73 LNH---------------SESVALVVENDS--------------------------DDLAtIIYTSGTTGNPKgvMLTHA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 243 QCSYGLGFVAS------GRRLMALTESdifWNTTDtgwvKAAWTLFSAWAnGACVFVhelpqvDAQTILNTLCRFPITTI 316
Cdd:cd17640 112 NLLHQIRSLSDivppqpGDRFLSILPI---WHSYE----RSAEYFIFACG-CSQAYT------SIRTLKDDLKRVKPHYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 317 CCVPTLFRLL---VQEDLTRYKF------------QCLRHCLAGGEALNSDVrDKWKNQTGLEIHEGYGQSET--VLICG 379
Cdd:cd17640 178 VSVPRLWESLysgIQKQVSKSSPikqflflfflsgGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETspVVSAR 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 380 NFRGSTIksGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAASEQGD-FYITGDRAH 457
Cdd:cd17640 257 RLKCNVR--GSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQ-----VMKGYYKNPEATSKVLDSDgWFNTGDLGW 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 458 MDEDGYFWFVGRNDDVIN-SSSYRIGPVEVESALAEHPaVLESAVVSSPDPIRgevVKAFIVlsPayvshDPEALTRELQ 536
Cdd:cd17640 330 LTCGGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSP-FIEQIMVVGQDQKR---LGALIV--P-----NFEELEKWAK 398
|
490 500 510
....*....|....*....|....*....|....*..
gi 88196780 537 EhvktvtapykypRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd17640 399 E------------SGVKLANDRSQLLASKKVLKLYKN 423
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
177-572 |
2.65e-21 |
|
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: 97.50 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 177 AISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLR-TRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASG- 254
Cdd:cd05915 108 PLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGLPKGVVYSHRALVLHSLAASl 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 255 RRLMALTESDIFWNTTD----TGWVkAAWTLFSAwaNGACVFVHELPqvDAQTILNTLCRFPITTICCVPTLFRLLVQ-E 329
Cdd:cd05915 188 VDGTALSEKDVVLPVVPmfhvNAWC-LPYAATLV--GAKQVLPGPRL--DPASLVELFDGEGVTFTAGVPTVWLALADyL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 330 DLTRYKFQCLRHCLAGGEAlNSDVRDKWKNQTGLEIHEGYGQSEtVLICGNF-----RGSTIKSGSMGKASPPYDVQIVD 404
Cdd:cd05915 263 ESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTE-TSPVVVQnfvksHLESLSEEEKLTLKAKTGLPIPL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 405 EEGNVLPPGK----EGNIAIRIKPTRPFCLFNCYLDNPEKTAASE-QGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSY 479
Cdd:cd05915 341 VRLRVADEEGrpvpKDGKALGEVQLKGPWITGGYYGNEEATRSALtPDGFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 480 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALTRELQEHVKTVTAPYKY-PRKVAFISEL 558
Cdd:cd05915 421 WISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGE------KPTPEELNEHLLKAGFAKWQlPDAYVFAEEI 494
|
410
....*....|....
gi 88196780 559 PKTVSGKILRSKLR 572
Cdd:cd05915 495 PRTSAGKFLKRALR 508
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
88-571 |
4.14e-21 |
|
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: 96.39 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIIT 167
Cdd:cd17656 13 KLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 ----SDALAPHVDAISADCPSLQSrllvSDTSRPGWINfrellrvaspehnclrtRSGDSMAIYFTSGTTGTPK--MVEH 241
Cdd:cd17656 92 qrhlKSKLSFNKSTILLEDPSISQ----EDTSNIDYIN-----------------NSDDLLYIIYTSGTTGKPKgvQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 242 SQCsygLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVF-VHELPQVDAQTILNTLCRFPITTICCVP 320
Cdd:cd17656 151 KNM---VNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIEVVFLPV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 321 TLFRLLVQE-DLTRYKFQCLRHCLAGGEAL--NSDVRDKWKNQtGLEIHEGYGQSETVLICgnfrGSTIKSGSMGKASPP 397
Cdd:cd17656 228 AFLKFIFSErEFINRFPTCVKHIITAGEQLviTNEFKEMLHEH-NVHLHNHYGPSETHVVT----TYTINPEAEIPELPP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 398 Y-------DVQIVDEEGNVLPPGKEGNIAIrikptRPFCLFNCYLDNPEKTAASEQGD-------FYITGDRAHMDEDGY 463
Cdd:cd17656 303 IgkpisntWIYILDQEQQLQPQGIVGELYI-----SGASVARGYLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 464 FWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayvshDPEALTRELQEHVKTVT 543
Cdd:cd17656 378 IEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-------EQELNISQLREYLAKQL 450
|
490 500
....*....|....*....|....*...
gi 88196780 544 APYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17656 451 PEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
86-566 |
2.20e-20 |
|
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: 94.00 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 86 EVKWTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRlPEWWLT-IVACMRTGVVMIPgisqltqkdlkyrlqaarvks 164
Cdd:cd17648 10 DKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIaILAVWKAGAAYVP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 165 iitsdalaphvdaISADCPSLQSRLLVSDTSRPGWInfrellrvaspehnclrTRSGDSMAIYFTSGTTGTPK--MVEHS 242
Cdd:cd17648 68 -------------IDPSYPDERIQFILEDTGARVVI-----------------TNSTDLAYAIYTSGTTGKPKgvLVEHG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 243 qcsyglGFVASGRRLMALtesdIFWNTTDTgwvkAAWTLFSAWangacVFVHELPQ-VDAQTILNTLCRFPITTICCVPT 321
Cdd:cd17648 118 ------SVVNLRTSLSER----YFGRDNGD----EAVLFFSNY-----VFDFFVEQmTLALLNGQKLVVPPDEMRFDPDR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 322 LFRLLVQEDLT----------RYKFQCLRH---CLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVL--ICGNFRGSTI 386
Cdd:cd17648 179 FYAYINREKVTylsgtpsvlqQYDLARLPHlkrVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVtnHKRFFPGDQR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 387 KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRikptrPFCLFNCYLDNPEKTA--------ASEQ-------GDFYI 451
Cdd:cd17648 259 FDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLG-----GDGVARGYLNRPELTAerflpnpfQTEQerargrnARLYK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 452 TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDP-IRGEVVKAFIVlspAYVSHDPEA 530
Cdd:cd17648 334 TGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsQAQSRIQKYLV---GYYLPEPGH 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 88196780 531 LTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKI 566
Cdd:cd17648 411 VPEsDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
41-567 |
1.09e-19 |
|
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: 92.72 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 41 ISLGKRPVPEYF-----NFAHDVLdvwsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANILEgACGLKPGD 115
Cdd:cd05943 54 VSGRIMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALR-ALGVKPGD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 116 RLMLVLPRLPEwwlTIVACMRT--------------GVvmiPGISQltqkdlkyRLQAARVKSIITSDA---------LA 172
Cdd:cd05943 125 RVAGYLPNIPE---AVVAMLATasigaiwsscspdfGV---PGVLD--------RFGQIEPKVLFAVDAytyngkrhdVR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 173 PHVDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEhNCLRTRSG-----------DSMAIYFTSGTTGTPKMVEH 241
Cdd:cd05943 191 EKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKIAKALTLE-DFLATGAAgelefeplpfdHPLYILYSSGTTGLPKCIVH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 242 SqcsyglgfvASGRRLMALTE---------SD-IFWNTTdTGWVKAAWtLFSAWANGA-CVFVHELPQVDAQTILNTLC- 309
Cdd:cd05943 270 G---------AGGTLLQHLKEhilhcdlrpGDrLFYYTT-CGWMMWNW-LVSGLAVGAtIVLYDGSPFYPDTNALWDLAd 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 310 RFPITTICCVPTLFRLLVQEDL---TRYKFQCLRHCLAGGEALNSD----VRDKWKNqtGLEIHEGYGQSEtvlICGNF- 381
Cdd:cd05943 339 EEGITVFGTSAKYLDALEKAGLkpaETHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGGTD---IISCFv 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 382 RGSTIKSGSMGKASPPY---DVQIVDEEGNVLPpGKEGNIAIrikpTRPFCLFNCYLDNPEKTAASEQGDF------YIT 452
Cdd:cd05943 414 GGNPLLPVYRGEIQCRGlgmAVEAFDEEGKPVW-GEKGELVC----TKPFPSMPVGFWNDPDGSRYRAAYFakypgvWAH 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 453 GDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyvshdpEALT 532
Cdd:cd05943 489 GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG------VELD 562
|
570 580 590
....*....|....*....|....*....|....*....
gi 88196780 533 RELQEHVKTVTA----PYKYPRKVAFISELPKTVSGKIL 567
Cdd:cd05943 563 DELRKRIRSTIRsalsPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
88-574 |
1.63e-19 |
|
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: 91.26 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVmipgisqltqkdlkyrlqAARVKSIIT 167
Cdd:cd05940 3 ALTYAELDAMANRYARWLK-SLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV------------------AALINYNLR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 SDALApHVdaisadcpslqsrllvsdtsrpgwinfrelLRVASPEHnCLRTRSgdsMAIYfTSGTTGTPK--MVEHSQCS 245
Cdd:cd05940 64 GESLA-HC------------------------------LNVSSAKH-LVVDAA---LYIY-TSGTTGLPKaaIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 246 YGLGFVASGRRLMAlteSDIFWNTTD--------TGWVK---AAWTL-----FSA---W----ANGACVFVHelpqvdaq 302
Cdd:cd05940 108 RGGAFFAGSGGALP---SDVLYTCLPlyhstaliVGWSAclaSGATLvirkkFSAsnfWddirKYQATIFQY-------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 303 tiLNTLCRFpittICCVPTlfrllvQEDLTRYKFQClrhclAGGEALNSDVRDKWKNQTGL-EIHEGYGQSETVLICGNF 381
Cdd:cd05940 177 --IGELCRY----LLNQPP------KPTERKHKVRM-----IFGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGFINF 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 382 RGstiKSGSMGKASPP-----------YDVQ----IVDEEGNV--LPPGKEGNIAIRIKPTRPFclfNCYLDNPEKTA-- 442
Cdd:cd05940 240 FG---KPGAIGRNPSLlrkvaplalvkYDLEsgepIRDAEGRCikVPRGEPGLLISRINPLEPF---DGYTDPAATEKki 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 443 ---ASEQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV--VSSPDpIRGEVVKAF 516
Cdd:cd05940 314 lrdVFKKGDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAA 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 88196780 517 IVLSPAYvSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:cd05940 393 IVLQPNE-EFDLSALAAHLEKNL----PGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
69-572 |
3.56e-19 |
|
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: 91.15 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 69 GHRPPNPAFWWVN-GSGTEVKWTFEELGKQSRKAANILEGACglKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgISQ 147
Cdd:cd05931 4 AARPDRPAYTFLDdEGGREETLTYAELDRRARAIAARLQAVG--KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVP-LPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 148 LTQKDLKYRLQA----ARVKSIITSDALAPHVDAISADCPSLqsrllvsdtsRPGWINFRELLRVASPEHNCLRTRSGDS 223
Cdd:cd05931 81 PTPGRHAERLAAiladAGPRVVLTTAAALAAVRAFAASRPAA----------GTPRLLVVDLLPDTSAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 224 MA-IYFTSGTTGTPK--MVEHsqcsyglgfvasgRRLMA---LTESDIFWNTTDTGwvkAAW-----------TLFSAWA 286
Cdd:cd05931 151 IAyLQYTSGSTGTPKgvVVTH-------------RNLLAnvrQIRRAYGLDPGDVV---VSWlplyhdmgligGLLTPLY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 287 NGA-CVFVHELPQVdAQTI--LNTLCRFPITtICCVPTL-FRLLVQ----EDLTRYKFQCLRHCLAGGEALNSDVRDKWK 358
Cdd:cd05931 215 SGGpSVLMSPAAFL-RRPLrwLRLISRYRAT-ISAAPNFaYDLCVRrvrdEDLEGLDLSSWRVALNGAEPVRPATLRRFA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 359 N---QTGLE---IHEGYGQSETVLI--------------------CGNFRGSTIKSG------SMGKASPPYDVQIVDEE 406
Cdd:cd05931 293 EafaPFGFRpeaFRPSYGLAEATLFvsggppgtgpvvlrvdrdalAGRAVAVAADDPaarelvSCGRPLPDQEVRIVDPE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 407 GN-VLPPGKEGNIAIRIKPTRPfclfnCYLDNPEKTAASEQ-------GDFYITGDRAHMDeDGYFWFVGRNDDVINSSS 478
Cdd:cd05931 373 TGrELPDGEVGEIWVRGPSVAS-----GYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGRLKDLIIVRG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 479 YRIGPVEVESALAEHPAVLES---AVVSSPDPIRGEVVkAFIVLSPAYVSHDPEALTRELQEHVKT---VTapykyPRKV 552
Cdd:cd05931 447 RNHYPQDIEATAEEAHPALRPgcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA-----PADV 520
|
570 580
....*....|....*....|..
gi 88196780 553 AFIS--ELPKTVSGKILRSKLR 572
Cdd:cd05931 521 VLVRpgSIPRTSSGKIQRRACR 542
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
90-571 |
4.44e-19 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 90.22 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgisqltqkdLKYRLQAARVKSIITsD 169
Cdd:cd17650 14 TYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVP---------IDPDYPAERLQYMLE-D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALAPhvdaisadcpslqsrLLVSDTSRPGWInfrellrvaspehnclrtrsgdsmaIYfTSGTTGTPK--MVEHSQCS-- 245
Cdd:cd17650 83 SGAK---------------LLLTQPEDLAYV-------------------------IY-TSGTTGKPKgvMVEHRNVAha 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 246 -------YGLGFVASGRRLMALTESDIFwnttdtgwvkAAWTLFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICC 318
Cdd:cd17650 122 ahawrreYELDSFPVRLLQMASFSFDVF----------AGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMES 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 319 VPTLFRLLVQE-DLTRYKFQCLRHCLAGGEAlnsdVRDKWKNQ------TGLEIHEGYGQSETVLICGNFRGS-----TI 386
Cdd:cd17650 192 TPALIRPVMAYvYRNGLDLSAMRLLIVGSDG----CKAQDFKTlaarfgQGMRIINSYGVTEATIDSTYYEEGrdplgDS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 387 KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAI------RikptrpfclfnCYLDNPEKTAA-------SEQGDFYITG 453
Cdd:cd17650 268 ANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIggagvaR-----------GYLNRPELTAErfvenpfAPGERMYRTG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 454 DRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEvvkAFIVlspAYVSHDPEALTR 533
Cdd:cd17650 337 DLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGE---ARLC---AYVVAAATLNTA 409
|
490 500 510
....*....|....*....|....*....|....*...
gi 88196780 534 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17650 410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
90-574 |
2.07e-18 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 88.98 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEW---WLTIVACmrtG--VVMIPgiSQLTQKDLKYRLQAARVKS 164
Cdd:PLN03052 210 TLSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAviiYLAIILA---GcvVVSIA--DSFAPSEIATRLKISKAKA 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 165 IITSD-----------------ALAPHVDAISADCPSLQSRLLVSDTSrpgWINFRELLR-VASPEHNCLRTRSGDS-MA 225
Cdd:PLN03052 284 IFTQDvivrggksiplysrvveAKAPKAIVLPADGKSVRVKLREGDMS---WDDFLARANgLRRPDEYKAVEQPVEAfTN 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 226 IYFTSGTTGTPKMVEHSQCSyGLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLFSAWANGACV-------------- 291
Cdd:PLN03052 361 ILFSSGTTGEPKAIPWTQLT-PLRAAADAWAHLDIRKGDIVCWPTNLGWMMGPWLVYASLLNGATLalyngsplgrgfak 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 292 FVHelpqvDAQ-TILNTlcrfpitticcVPTLFRLL----VQEDLTRYKFQCLRhclAGGEALNSD------VRDKWKnq 360
Cdd:PLN03052 440 FVQ-----DAKvTMLGT-----------VPSIVKTWkntnCMAGLDWSSIRCFG---STGEASSVDdylwlmSRAGYK-- 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 361 tglEIHEGYGQSEtvlICGNF-RGSTIKSGSMGKASPP---YDVQIVDEEGNVLPPGKEGniairikpTRPFCLFNCYLD 436
Cdd:PLN03052 499 ---PIIEYCGGTE---LGGGFvTGSLLQPQAFAAFSTPamgCKLFILDDSGNPYPDDAPC--------TGELALFPLMFG 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 437 NPEKTAASEQGDFYITGD--------RAHMDE-----DGYFWFVGRNDDVINSSSYRIGPVEVESAL-AEHPAVLESAVV 502
Cdd:PLN03052 565 ASSTLLNADHYKVYFKGMpvfngkilRRHGDIfertsGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAI 644
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196780 503 SSPDPIRG--EVVKAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN03052 645 GVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
157-571 |
3.25e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.07 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 157 LQAARVKSIITSDAlAPhVDAISADCPSLQSRLL--VSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMA-IYFTSGTT 233
Cdd:PRK05691 3804 LPAQRLQRIIELSR-TP-VLVCSAACREQARALLdeLGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAyVIYTSGST 3881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 234 GTPK--MVEH--------SQCSYglgfvasgrrlMALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVheLPQV---D 300
Cdd:PRK05691 3882 GLPKgvMVEQrgmlnnqlSKVPY-----------LALSEADVIAQTASQSFDISVWQFLAAPLFGARVEI--VPNAiahD 3948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 301 AQTILNTLCRFPITTICCVPTLFRLLVQEDltRYKFQCLRHCLAGGEALNSDVRDKWKN---QTGLEihEGYGQSETVLI 377
Cdd:PRK05691 3949 PQGLLAHVQAQGITVLESVPSLIQGMLAED--RQALDGLRWMLPTGEAMPPELARQWLQrypQIGLV--NAYGPAECSDD 4024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 378 CGNFR-------GSTIKSGSmgkaspPYD---VQIVDEEGNVLPPGKEGNIairikptrpfCLFNC-----YLDNPEKTA 442
Cdd:PRK05691 4025 VAFFRvdlastrGSYLPIGS------PTDnnrLYLLDEALELVPLGAVGEL----------CVAGTgvgrgYVGDPLRTA 4088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 443 AS-------EQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVK 514
Cdd:PRK05691 4089 LAfvphpfgAPGErLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLV 4167
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 88196780 515 AFIVlsPAYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK05691 4168 GYLV--PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
407-572 |
4.30e-18 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 86.97 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 407 GNVLP-------PGKEGNIAIRIKPtrpfcLFNCYLdnPEKTAASEqgdFYITGDRAHMDEDGYFWFVGRNDDVINSSSY 479
Cdd:PRK07445 286 GQVLPhaqitipANQTGNITIQAQS-----LALGYY--PQILDSQG---IFETDDLGYLDAQGYLHILGRNSQKIITGGE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 480 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFivlspaYVSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELP 559
Cdd:PRK07445 356 NVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAI------YVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLP 429
|
170
....*....|...
gi 88196780 560 KTVSGKILRSKLR 572
Cdd:PRK07445 430 RNPQGKINRQQLQ 442
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
392-571 |
1.71e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 85.33 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 392 GKASPPYDVQIVDEEGNVLPPGKEGNIAIrIKPtrpfCLFNCYLDNPEKTAA---SEQGD-FYITGDRAHMDeDGYFWFV 467
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SGP----SVSKGYLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 468 GRNDDVINSSSYRIGPVEVESALAEHPAVlESAVVSspdPI-RGEVVK---AFIVLSPAYVSHDpEALTRELQEHVKTVT 543
Cdd:PRK04813 395 GRIDFQIKLNGYRIELEEIEQNLRQSSYV-ESAVVV---PYnKDHKVQyliAYVVPKEEDFERE-FELTKAIKKELKERL 469
|
170 180
....*....|....*....|....*...
gi 88196780 544 APYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK04813 470 MEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
90-571 |
2.36e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 86.38 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSD 169
Cdd:PRK05691 2215 SYAELDARANRLARALRER-GVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDR 2293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 170 ALaphVDAIsADCPSLQSRLLVSDTSrPGWINFR--ELLRVASPEHNclrtrsgdSMAIYfTSGTTGTPKMVEHSQCSYG 247
Cdd:PRK05691 2294 AL---FEAL-GELPAGVARWCLEDDA-AALAAYSdaPLPFLSLPQHQ--------AYLIY-TSGSTGKPKGVVVSHGEIA 2359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 248 LGFVASGRRLmALTESDIFWNTTDTGWVKAAWTLFSAWANGACVFVHELPQVDAQTILNTLCRFPITTICCVPTLFRLLV 327
Cdd:PRK05691 2360 MHCQAVIERF-GMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLA 2438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 328 QEDLTRYKFQCLRHCLAGGEALNSD----VRDKWKNQtglEIHEGYGQSETVLI-CGNFRGSTIKSGS----MGKASPPY 398
Cdd:PRK05691 2439 QWLAGQGEQLPVRMCITGGEALTGEhlqrIRQAFAPQ---LFFNAYGPTETVVMpLACLAPEQLEEGAasvpIGRVVGAR 2515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 399 DVQIVDEEGNVLPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFVGRN 470
Cdd:PRK05691 2516 VAYILDADLALVPQGATGELYVGGAG-----LAQGYHDRPGLTAerfvadpfAADGGRLYRTGDLVRLRADGLVEYVGRI 2590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 471 DDVINSSSYRIGPVEVESALAEHPAVLEsAVVSSPDPIRGEVVKAFIVLSPAYVSHDPEALTRE-LQEHVKTVTAPYKYP 549
Cdd:PRK05691 2591 DHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAVAGQDDEAQAALREaLKAHLKQQLPDYMVP 2669
|
490 500
....*....|....*....|..
gi 88196780 550 RKVAFISELPKTVSGKILRSKL 571
Cdd:PRK05691 2670 AHLILLDSLPLTANGKLDRRAL 2691
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
90-574 |
1.01e-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: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEW---WLTI------VACMRTgvvmipgisQLTQKDLKYRLQAA 160
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLGLaklgcpVAFLNT---------NIRSKSLLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 161 RVKSIITSDALaphVDAISADCPSLQSR-----LLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSM---AIY-FTSG 231
Cdd:cd05938 78 GAKVLVVAPEL---QEAVEEVLPALRADgvsvwYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHVTIkspALYiYTSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 232 TTGTPK--MVEHSQCSYGLGFVasgrRLMALTESDIFWNTTD-----------TGWVKAAWTL-----FSA---WANgac 290
Cdd:cd05938 155 TTGLPKaaRISHLRVLQCSGFL----SLCGVTADDVIYITLPlyhssgfllgiGGCIELGATCvlkpkFSAsqfWDD--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 291 vfvhelpqvdaqtilntlCR-FPITTICCVPTLFRLLV----QEDLTRYKFQclrhcLAGGEALNSDVRDKWKNQTG-LE 364
Cdd:cd05938 228 ------------------CRkHNVTVIQYIGELLRYLCnqpqSPNDRDHKVR-----LAIGNGLRADVWREFLRRFGpIR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 365 IHEGYGQSEtvlicGN--FRGSTIKSGSMGKAS-------P----PYDVQ----IVDEEGNVLP--PGKEGNIAIRIKPT 425
Cdd:cd05938 285 IREFYGSTE-----GNigFFNYTGKIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 426 RPfclFNCYLDNPEKTAAS------EQGDFYI-TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLE 498
Cdd:cd05938 360 SP---FLGYAGDKEQTEKKllrdvfKKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQE 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 88196780 499 SAV--VSSPDpIRGEVVKAFIVLSPayvshdPEALT-RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:cd05938 437 VNVygVTVPG-HEGRIGMAAVKLKP------GHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
452-568 |
1.26e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 82.39 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 452 TGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfivlspAYVSH---DP 528
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVISHeeiDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 88196780 529 EALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:PRK08308 369 VQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSR 404
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
88-574 |
3.41e-15 |
|
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: 78.24 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIIT 167
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 168 sDALAPHVDAISADCPSLQSRllvsdtsrpgwiNFRELLrvaspehnclrtrsgdsMAIYfTSGTTGTPK--MVEHSQcs 245
Cdd:cd05939 82 -NLLDPLLTQSSTEPPSQDDV------------NFRDKL-----------------FYIY-TSGTTGLPKaaVIVHSR-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 246 YgLGFVASGRRLMALTESDIFWNT-----TDTGWVKAAwtlfSAWANGACVFVHElpQVDAQTILNTLCRFPITTICCVP 320
Cdd:cd05939 129 Y-YRIAAGAYYAFGMRPEDVVYDClplyhSAGGIMGVG----QALLHGSTVVIRK--KFSASNFWDDCVKYNCTIVQYIG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 321 TLFRLLVQEDLTRYKFQ-CLRhcLAGGEALNSDVrdkWKNQTG----LEIHEGYGQSETVLICGNFRGSTIKSGSMGKAS 395
Cdd:cd05939 202 EICRYLLAQPPSEEEQKhNVR--LAVGNGLRPQI---WEQFVRrfgiPQIGEFYGATEGNSSLVNIDNHVGACGFNSRIL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 396 PP-YDVQIV-----------DEEGNVLP--PGKEGNIAIRIKPTRPFCLFNCYLD---NPEKTAAS--EQGD-FYITGDR 455
Cdd:cd05939 277 PSvYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNegaTNKKIARDvfKKGDsAFLSGDV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 456 AHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV--VSSPDpIRGEVVKAFIVLSPAYVshDPEALTR 533
Cdd:cd05939 357 LVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIVDPERKV--DLDRFSA 433
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 88196780 534 ELQEhvktVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:cd05939 434 VLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
110-566 |
3.54e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 79.24 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 110 GLKPGDRLMLVLPRLPEWWLTIVACMRTGVV--MI---PGIsqltqKDLKYRLQAARVKSIITSDA------LAPHVDAI 178
Cdd:PRK06814 678 NTPPGENVGVMLPNANGAAVTFFALQSAGRVpaMInfsAGI-----ANILSACKAAQVKTVLTSRAfiekarLGPLIEAL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 179 SAdcpslQSRLLVSDTSRPG---WINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKmvehsqcsyglGFVASGR 255
Cdd:PRK06814 753 EF-----GIRIIYLEDVRAQiglADKIKGLLAGRFPLVYFCNRDPDDPAVILFTSGSEGTPK-----------GVVLSHR 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 256 RLMA----------LTESDIFWNttdtgwvkaAWTLFSAWA----------NGACVFVHELP-----------QVDAqTI 304
Cdd:PRK06814 817 NLLAnraqvaaridFSPEDKVFN---------ALPVFHSFGltgglvlpllSGVKVFLYPSPlhyriipeliyDTNA-TI 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 305 LntlcrFPITTIccvptlfrllvqedLT-------RYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET--V 375
Cdd:PRK06814 887 L-----FGTDTF--------------LNgyaryahPYDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETapV 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 376 LICgnfrgST---IKSGSMGKASPPYD-----VQIVDEEGNVLPPGKegNIAIRikptrpfclfncYL--DNPEKTAASE 445
Cdd:PRK06814 948 IAL-----NTpmhNKAGTVGRLLPGIEyrlepVPGIDEGGRLFVRGP--NVMLG------------YLraENPGVLEPPA 1008
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 446 QGdFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVvkafIVLspayVS 525
Cdd:PRK06814 1009 DG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVSIPDARKGER----IIL----LT 1079
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 88196780 526 HDPEALTRELQEHVKTVTAPYKY-PRKVAFISELPKTVSGKI 566
Cdd:PRK06814 1080 TASDATRAAFLAHAKAAGASELMvPAEIITIDEIPLLGTGKI 1121
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
343-572 |
1.13e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.85 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 343 LAGGEALNSDVRDKWKnQTGLEIHEGYGQSETvliCGnfrgstiksGSMGKASPPYDVQIVDEEGNVLPPGkegniairi 422
Cdd:PRK07824 157 LVGGGPAPAPVLDAAA-AAGINVVRTYGMSET---SG---------GCVYDGVPLDGVRVRVEDGRIALGG--------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 423 kPTrpfcLFNCYLDNPEKTAASEQGDFyITGDRAHMDeDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 502
Cdd:PRK07824 215 -PT----LAKGYRNPVDPDPFAEPGWF-RTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 503 SSPDPIRGEVVKAFIVLSPAyvshdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK07824 288 GLPDDRLGQRVVAAVVGDGG-----PAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
90-565 |
2.90e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 72.82 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEGACglKPGDRLMLVLPRLpewwlTIVACMRTGVVM---IPGISQLTQ--KDLKYRLQAARVKS 164
Cdd:PRK08043 233 SYRKLLKKTLFVGRILEKYS--VEGERIGLMLPNA-----TISAAVIFGASLrrrIPAMMNYTAgvKGLTSAITAAEIKT 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 165 IITSDA---------LAPHVDAIS-------ADCPSLQSRLlvsdtsrpgWInFRELLrvaSPEHNCLRTRSGDSMAIYF 228
Cdd:PRK08043 306 IFTSRQfldkgklwhLPEQLTQVRwvyledlKDDVTTADKL---------WI-FAHLL---MPRLAQVKQQPEDAALILF 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 229 TSGTTGTPKMVEHSQCSYgLGFVASGRRLMALTESDIFwnttdtgwvKAAWTLFSAWA----------NGACVFVHELPQ 298
Cdd:PRK08043 373 TSGSEGHPKGVVHSHKSL-LANVEQIKTIADFTPNDRF---------MSALPLFHSFGltvglftpllTGAEVFLYPSPL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 299 -----------------VDAQTILNTLCRF--PitticcvptlfrllvqedltrYKFQCLRHCLAGGEALNSDVRDKWKN 359
Cdd:PRK08043 443 hyrivpelvydrnctvlFGTSTFLGNYARFanP---------------------YDFARLRYVVAGAEKLQESTKQLWQD 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 360 QTGLEIHEGYGQSE---TVLIcgNFRGSTiKSGSMGKASPPYDVQIVdeegNVlpPGKE--GNIAIRiKPTrpfcLFNCY 434
Cdd:PRK08043 502 KFGLRILEGYGVTEcapVVSI--NVPMAA-KPGTVGRILPGMDARLL----SV--PGIEqgGRLQLK-GPN----IMNGY 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 435 L--DNPEK----TAASEQGD----FYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVES-ALAEHPAVLESAVVS 503
Cdd:PRK08043 568 LrvEKPGVlevpTAENARGEmergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIK 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196780 504 SpDPIRGEVVKAFivlspayvSHDPEaLTRE-LQEHVKTVTAP-YKYPRKVAFISELPKTVSGK 565
Cdd:PRK08043 648 S-DASKGEALVLF--------TTDSE-LTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGK 701
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
88-525 |
4.59e-13 |
|
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: 71.69 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEW-WLTIVACMRTGVVMipGISQ-LTQKDLKYRLQAARVKSI 165
Cdd:cd17641 11 EFTWADYADRVRAFALGLL-ALGVGRGDVVAILGDNRPEWvWAELAAQAIGALSL--GIYQdSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSD-----ALAPHVDAIsadcPSLQsRLLVSDT------SRPGWINF---RELLRVASPEH-----NCLRTRSGDSMAI 226
Cdd:cd17641 88 IAEDeeqvdKLLEIADRI----PSVR-YVIYCDPrgmrkyDDPRLISFedvVALGRALDRRDpglyeREVAAGKGEDVAV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 227 Y-FTSGTTGTPK--------MVEHS-----------------------------------QCSYGLGFVASGRRLMA-LT 261
Cdd:cd17641 163 LcTTSGTTGKPKlamlshgnFLGHCaaylaadplgpgdeyvsvlplpwigeqmysvgqalVCGFIVNFPEEPETMMEdLR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 262 E-----------------SDIFWNTTDTGWVKAAwtlfsawangacVFVHELPQVDAQTILNTLCRFPITTICCVPTLFR 324
Cdd:cd17641 243 EigptfvllpprvwegiaADVRARMMDATPFKRF------------MFELGMKLGLRALDRGKRGRPVSLWLRLASWLAD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 325 LLVQEDL-TRYKFQCLRHCLAGGEALNSDVRDKWKnQTGLEIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIv 403
Cdd:cd17641 311 ALLFRPLrDRLGFSRLRSAATGGAALGPDTFRFFH-AIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 404 DEEGNVLppgkegniairikpTRPFCLFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFVGRNDDVINSS-SYRI 481
Cdd:cd17641 389 DEVGEIL--------------VRSPGVFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRF 454
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 88196780 482 GPVEVESALAEHPAVLESAVVSSPDPIrgevVKAFIVLSPAYVS 525
Cdd:cd17641 455 SPQFIENKLKFSPYIAEAVVLGAGRPY----LTAFICIDYAIVG 494
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-567 |
2.15e-12 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 69.82 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 53 NFAHDVLdvwsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEwwlTIV 132
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNIPE---TVV 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 133 ACMRT-----------------GVVmipgisqltqkDlkyRLQAARVKSIITSDA---------LAPHVDAISADCPSLQ 186
Cdd:PRK03584 155 AMLATaslgaiwsscspdfgvqGVL-----------D---RFGQIEPKVLIAVDGyryggkafdRRAKVAELRAALPSLE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 187 SRLLVS-------DTSRPGWINFRELLR-VASPEHNCLRTRSGDSMAIYFTSGTTGTPKMVEHSQCSYGLGFVASGRRLM 258
Cdd:PRK03584 221 HVVVVPylgpaaaAAALPGALLWEDFLApAEAAELEFEPVPFDHPLWILYSSGTTGLPKCIVHGHGGILLEHLKELGLHC 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 259 ALTESD-IFWNTTdTGWVKAAWtLFSAWANGACVFVHE----LPQVDAqtilntlcrfpitticcvptLFRLLVQEDLT- 332
Cdd:PRK03584 301 DLGPGDrFFWYTT-CGWMMWNW-LVSGLLVGATLVLYDgspfYPDPNV--------------------LWDLAAEEGVTv 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 333 --------------------RYKFQCLRHCLAGGEALNSD----VRDKWKnqtgleihegygqsETVL---------ICG 379
Cdd:PRK03584 359 fgtsakyldacekaglvpgeTHDLSALRTIGSTGSPLPPEgfdwVYEHVK--------------ADVWlasisggtdICS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 380 NFRGST----IKSGSMGKASPPYDVQIVDEEGN-VLppGKEGNIAIrikpTRPFCLFNCYLDNpektaaSEQGDFYIT-- 452
Cdd:PRK03584 425 CFVGGNpllpVYRGEIQCRGLGMAVEAWDEDGRpVV--GEVGELVC----TKPFPSMPLGFWN------DPDGSRYRDay 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 453 ----------GDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPA 522
Cdd:PRK03584 493 fdtfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEG 572
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 88196780 523 YVSHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:PRK03584 573 VTLDD--ALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
90-502 |
3.94e-12 |
|
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: 68.64 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 90 TFEELGKQSRKAANILEgACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMI---PGISQltqKDLKYRLQAARVKSII 166
Cdd:cd05910 4 SFRELDERSDRIAQGLT-AYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVlidPGMGR---KNLKQCLQEAEPDAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 167 TSdalaphvdaisadcpslqsrllvsdtsrpgwinfrellrvaspehnclrTRSGDSMAIYFTSGTTGTPKMVEHSQCSY 246
Cdd:cd05910 80 GI-------------------------------------------------PKADEPAAILFTSGSTGTPKGVVYRHGTF 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 247 GlGFVASGRRLMALTESDIFWnttdtgwvkAAWTLFSAW--ANGACVFVHEL-----PQVDAQTILNTLCRFPITTICCV 319
Cdd:cd05910 111 A-AQIDALRQLYGIRPGEVDL---------ATFPLFALFgpALGLTSVIPDMdptrpARADPQKLVGAIRQYGVSIVFGS 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 320 PTLFRLLvqedlTRY------KFQCLRHCLAGGEALNSDVRDKWKN--QTGLEIHEGYGQSETVLICG----NFRGSTIK 387
Cdd:cd05910 181 PALLERV-----ARYcaqhgiTLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSSigsrELLATTTA 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 388 SGS------MGKASPPYDVQIV--DEEG-------NVLPPGKEGNIAIRIKPTRPfclfnCYLDNPEKTAASE-----QG 447
Cdd:cd05910 256 ATSggagtcVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTP-----TYVNRPVATALAKiddnsEG 330
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 88196780 448 DFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 502
Cdd:cd05910 331 FWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
390-574 |
4.58e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 68.48 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 390 SMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPFclfncYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGR 469
Cdd:PRK07768 361 TLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG-----YLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 470 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVLSPAYVSHDPEALTRELQEHVKTVTAPYKY- 548
Cdd:PRK07768 436 VKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVr 514
|
170 180
....*....|....*....|....*...
gi 88196780 549 PRKVAFIS--ELPKTVSGKILRSKLRNQ 574
Cdd:PRK07768 515 PRNVVVLGpgSIPKTPSGKLRRANAAEL 542
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
89-576 |
7.82e-11 |
|
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: 64.38 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 89 WTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVmipgisqltqkdlkyrlqAARVKSIITS 168
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA------------------PAFINYNLSG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 169 DALApHVDAISadcpslQSRLLVSDTSRPgwinfrellrvaspehnclrtrsgdSMAIYfTSGTTGTPKMVehsqcsygl 248
Cdd:cd05937 68 DPLI-HCLKLS------GSRFVIVDPDDP-------------------------AILIY-TSGTTGLPKAA--------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 249 gFVASGRRLMALTESDIFWNTTDTGWVKAAWTLF--SAWANGACVFVHE------LPQVDAQTILNTLCRFPITTICCVP 320
Cdd:cd05937 106 -AISWRRTLVTSNLLSHDLNLKNGDRTYTCMPLYhgTAAFLGACNCLMSggtlalSRKFSASQFWKDVRDSGATIIQYVG 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 321 TLFRLLVQEDLTRYKfQCLRHCLAGGEALNSDVRDKWKNQTGL-EIHEGYGQSETVLICGNFRGSTIKSGSMGKASPPYD 399
Cdd:cd05937 185 ELCRYLLSTPPSPYD-RDHKVRVAWGNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 400 ---------VQIVDEEGNVL-----------PPGKEGNIAIRIkPTRPFCLFNCYLDNPEKTAAS------EQGD-FYIT 452
Cdd:cd05937 264 wkfenqvvlVKMDPETDDPIrdpktgfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKlvrdvfRKGDiYFRT 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 453 GDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDP-IRGEVVKAFIVLSPAyvSHDPEAL 531
Cdd:cd05937 343 GDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEES--SAVPTEF 420
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 88196780 532 TR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:cd05937 421 TKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDEGV 466
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
392-573 |
5.67e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 61.94 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 392 GKASPPYDVQIVDEEGNVLPPGKEGNIAIRiKPTrpfcLFNCYLDNPEKTAASEQGDFYITGDRAHMdEDGYFWFVGRND 471
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GPS----LMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 472 DVINSSSYRIGPVEVESALAEHPAVL--ESAVVSSPDPIRGEVVkafiVLSPAYVShDPE---ALTRELQEHVKTVTApy 546
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV----LLVQCRIS-DEErrgQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*....
gi 88196780 547 kYPRKVAFIS--ELPKTVSGKILRSKLRN 573
Cdd:PRK09192 535 -VEAAVELVPphSLPRTSSGKLSRAKAKK 562
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
390-574 |
2.04e-09 |
|
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: 60.19 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 390 SMGKASPPYDVQIVDEEGNVLPPGKEGNIAIRIKPTRPfclfnCYLDNPEKTAA--SEQGdFYITGDRAHMdEDGYFWFV 467
Cdd:cd05908 315 EVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP-----GYYNNPEATAKvfTDDG-WLKTGDLGFI-RNGRLVIT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 468 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS---SPDPIRGEVVKAFIVLSPAyvSHDPEALTRELQEHVKTVTA 544
Cdd:cd05908 388 GREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRKS--EDDFYPLGKKIKKHLNKRGG 465
|
170 180 190
....*....|....*....|....*....|
gi 88196780 545 pyKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:cd05908 466 --WQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
79-534 |
5.95e-09 |
|
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: 58.60 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 79 WVNGSGTEVKW---TFEELGKQSRKAANILEGAcGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgIS---QLTQKD 152
Cdd:cd05921 13 WLAEREGNGGWrrvTYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAP-VSpaySLMSQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 153 ---LKYRLQAARVKSIITSDAlAPHVDAISA----DCPSLQSRLLVSD---TSRPGWINFRELLRVASpehncLRTRSG- 221
Cdd:cd05921 91 lakLKHLFELLKPGLVFAQDA-APFARALAAifplGTPLVVSRNAVAGrgaISFAELAATPPTAAVDA-----AFAAVGp 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 222 DSMAIY-FTSGTTGTPKMVEHSQcsyglGFVASGRRLMALTESD-----------IFWNTTDTGWVKAAWTLFsawaNGA 289
Cdd:cd05921 165 DTVAKFlFTSGSTGLPKAVINTQ-----RMLCANQAMLEQTYPFfgeeppvlvdwLPWNHTFGGNHNFNLVLY----NGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 290 CVFVHE---LPQVDAQTILNtLCRFPITTICCVPTLFRLLVQ-----EDLTRYKFQCLRHCLAGGEALNSDVRDKWKN-- 359
Cdd:cd05921 236 TLYIDDgkpMPGGFEETLRN-LREISPTVYFNVPAGWEMLVAalekdEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAla 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 360 --QTGLEI--HEGYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVdeegnvlPPGkeGNIAIRIK-PTrpfcLFNCY 434
Cdd:cd05921 315 vaTVGERIpmMAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKLV-------PSG--GKYEVRVKgPN----VTPGY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 435 LDNPEKTAAS--EQGdFYITGDRAHM----DEDGYFWFVGR--NDDVINSSSY-RIGPVEVESALAEHPAVLEsAVVSSP 505
Cdd:cd05921 382 WRQPELTAQAfdEEG-FYCLGDAAKLadpdDPAKGLVFDGRvaEDFKLASGTWvSVGPLRARAVAACAPLVHD-AVVAGE 459
|
490 500 510
....*....|....*....|....*....|....*..
gi 88196780 506 DpirGEVVKAFIVLSPAYV--------SHDPEALTRE 534
Cdd:cd05921 460 D---RAEVGALVFPDLLACrrlvglqeASDAEVLRHA 493
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
92-493 |
8.68e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 54.82 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 92 EELGKQS----RKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGvvMIPGISQLTQ--KDLKYRLQAARVKSI 165
Cdd:PRK06334 41 EQLGKLSynqvRKAVIALATKVSKYPDQHIGIMMPASAGAYIAYFATLLSG--KIPVMINWSQglREVTACANLVGVTHV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 166 ITSDALAPHVDAISADCPSLQSRLLVSDTSRPGwINFRELLRVA----SPEHNCLR------TRSGDSMAIYFTSGTTGT 235
Cdd:PRK06334 119 LTSKQLMQHLAQTHGEDAEYPFSLIYMEEVRKE-LSFWEKCRIGiymsIPFEWLMRwfgvsdKDPEDVAVILFTSGTEKL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 236 PKMVEHSQCSyglgfvasgrrLMALTESDI-FWNTTDTGWVKAAWTLFSAWANGACVFVHELPQV---------DAQTIL 305
Cdd:PRK06334 198 PKGVPLTHAN-----------LLANQRACLkFFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVpvvfaynplYPKKIV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 306 NTLCRFPITTICCVPTLFRLLvqedLTRYKFQ-----CLRHCLAGGEALNSDVRDK-WKNQTGLEIHEGYGQSE-TVLIC 378
Cdd:PRK06334 267 EMIDEAKVTFLGSTPVFFDYI----LKTAKKQesclpSLRFVVIGGDAFKDSLYQEaLKTFPHIQLRQGYGTTEcSPVIT 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 379 GNFRGSTIKSGSMGKASPPYDVQIVDEEGNV-LPPGKEGNIAIRIKPtrpfcLFNCYLDNPEKTAASEQG--DFYITGDR 455
Cdd:PRK06334 343 INTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTS-----LFSGYLGEDFGQGFVELGgeTWYVTGDL 417
|
410 420 430
....*....|....*....|....*....|....*...
gi 88196780 456 AHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEH 493
Cdd:PRK06334 418 GYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
229-543 |
1.14e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 54.38 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 229 TSGTTGTPKMVEHSQ-------CSYGLGFVASGrrlmaLTESDIFWNTTDTGWVKAAWTLFS-AWANGACVFVHELPQVD 300
Cdd:COG1541 91 SSGTTGKPTVVGYTRkdldrwaELFARSLRAAG-----VRPGDRVQNAFGYGLFTGGLGLHYgAERLGATVIPAGGGNTE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 301 AQtiLNTLCRFPITTICCVPTLFRLLVQE------DLTRYKfqcLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSET 374
Cdd:COG1541 166 RQ--LRLMQDFGPTVLVGTPSYLLYLAEVaeeegiDPRDLS---LKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 375 -VLI---CGNFRGSTIKSGSMgkasppYdVQIVDEE-GNVLPPGKEGNIA-----------IRikptrpfclfncyldnp 438
Cdd:COG1541 241 gPGVayeCEAQDGLHIWEDHF------L-VEIIDPEtGEPVPEGEEGELVvttltkeamplIR----------------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 439 ektaaseqgdfYITGDRAHMDED----G------YFWFvGRNDDVInssSYR---IGPVEVESALAEHPAVLESAVVSSP 505
Cdd:COG1541 297 -----------YRTGDLTRLLPEpcpcGrthpriGRIL-GRADDML---IIRgvnVFPSQIEEVLLRIPEVGPEYQIVVD 361
|
330 340 350
....*....|....*....|....*....|....*...
gi 88196780 506 DPIRGEVVKAFIVLSPAYvshDPEALTRELQEHVKTVT 543
Cdd:COG1541 362 REGGLDELTVRVELAPGA---SLEALAEAIAAALKAVL 396
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
110-461 |
1.18e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 54.67 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 110 GLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIP---GISQLTQKDLKYRLQAARVK-SIITSDALAPHVDAISAdcPSL 185
Cdd:PRK12582 101 GLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPvspAYSLMSHDHAKLKHLFDLVKpRVVFAQSGAPFARALAA--LDL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 186 QSRLLVSDTSRP---GWINFRELLRVA-SPEHNCLRTRSG-DSMAIY-FTSGTTGTPKMVEHSQcsyglGFVASGRRLMA 259
Cdd:PRK12582 179 LDVTVVHVTGPGegiASIAFADLAATPpTAAVAAAIAAITpDTVAKYlFTSGSTGMPKAVINTQ-----RMMCANIAMQE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 260 LTESD------------IFWNTTDTGWVkaawtLFSA--WaNGACVFVHE---LPQVDAQTILNtLCRFPITTICCVPTL 322
Cdd:PRK12582 254 QLRPRepdppppvsldwMPWNHTMGGNA-----NFNGllW-GGGTLYIDDgkpLPGMFEETIRN-LREISPTVYGNVPAG 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 323 FRLLVQ-----EDLTRYKFQCLRHCLAGGEALNSDVRDKWK----NQTG--LEIHEGYGQSETVLICGNFRGSTIKSGSM 391
Cdd:PRK12582 327 YAMLAEamekdDALRRSFFKNLRLMAYGGATLSDDLYERMQalavRTTGhrIPFYTGYGATETAPTTTGTHWDTERVGLI 406
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 88196780 392 GKASPPYDVQIVdeegnvlPPGKEgnIAIRIKPTrpfCLFNCYLDNPEKTAAS--EQGdFYITGDRAH-MDED 461
Cdd:PRK12582 407 GLPLPGVELKLA-------PVGDK--YEVRVKGP---NVTPGYHKDPELTAAAfdEEG-FYRLGDAARfVDPD 466
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
88-492 |
1.97e-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: 53.90 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 88 KWTFEELGKQSRKAANILegacglkpgdrLMLVLPRL----------PEWWLTIVACMRTGVVMIpGI-SQLTQKDLKYR 156
Cdd:cd05933 8 TLTYKEYYEACRQAAKAF-----------LKLGLERFhgvgilgfnsPEWFIAAVGAIFAGGIAV-GIyTTNSPEACQYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 157 LQAARVKSIITSDA--LA---------PHVDAIsadcpsLQSRLLVSDtSRPGWINFRELLRVA--SPEHNCL----RTR 219
Cdd:cd05933 76 AETSEANILVVENQkqLQkilqiqdklPHLKAI------IQYKEPLKE-KEPNLYSWDEFMELGrsIPDEQLDaiisSQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 220 SGDSMAIYFTSGTTGTPK--MVEHSQCSY-GLGFVASGRRLMA----------LTESDIFWNTTDTgWVKAAWtlfsawa 286
Cdd:cd05933 149 PNQCCTLIYTSGTTGMPKgvMLSHDNITWtAKAASQHMDLRPAtvgqesvvsyLPLSHIAAQILDI-WLPIKV------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 287 nGACVFvheLPQVDA--QTILNTLCRFPITTICCVPTLF----------------------------------RLLVQED 330
Cdd:cd05933 221 -GGQVY---FAQPDAlkGTLVKTLREVRPTAFMGVPRVWekiqekmkavgaksgtlkrkiaswakgvgletnlKLMGGES 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 331 LTRYKFQCLRH-----------------CLAGGEALNSDVRDKWknqTGLEI--HEGYGQSE-----TVLICGNFRgsti 386
Cdd:cd05933 297 PSPLFYRLAKKlvfkkvrkalgldrcqkFFTGAAPISRETLEFF---LSLNIpiMELYGMSEtsgphTISNPQAYR---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 387 kSGSMGKASPPYDVQIVDEEGNvlppgKEGNIAIRIKPtrpfcLFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFW 465
Cdd:cd05933 370 -LLSCGKALPGCKTKIHNPDAD-----GIGEICFWGRH-----VFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLY 438
|
490 500
....*....|....*....|....*...
gi 88196780 466 FVGRNDD-VINSSSYRIGPVEVESALAE 492
Cdd:cd05933 439 ITGRIKElIITAGGENVPPVPIEDAVKK 466
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
383-574 |
2.71e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 50.15 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 383 GSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKE-GNIAIRIKptrpfCLFNCYLDNpektAASEQGDFYITGDRAHMDED 461
Cdd:PRK05851 339 SGARRHAVLGNPIPGMEVRISPGDGAAGVAGREiGEIEIRGA-----SMMSGYLGQ----APIDPDDWFPTGDLGYLVDG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 462 GYFwFVGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGevVKAFIVLSPAYVSHDPEALTRELQEHVKT 541
Cdd:PRK05851 410 GLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVAS 486
|
170 180 190
....*....|....*....|....*....|....*
gi 88196780 542 VTApyKYPRKVAFIS--ELPKTVSGKILRSKLRNQ 574
Cdd:PRK05851 487 ECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKRS 519
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
125-531 |
3.31e-06 |
|
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: 49.91 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 125 PEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAphvdaisadcpslqsrlLVSdtsrpgWINFRE 204
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAGVK-----------------VYS------LEEFEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 205 LLRVASPEHNcLRTRSgDSMAIYFTSGTTGTPKMVEHSQ---CSYGLGFVASGRRLMALTESDifwnttdtgwvkaawTL 281
Cdd:cd05927 100 LGKKNKVPPP-PPKPE-DLATICYTSGTTGNPKGVMLTHgniVSNVAGVFKILEILNKINPTD---------------VY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 282 FS---------------AWANGACVFVHelpQVDAQTILNTLCRFPITTICCVPTLF-RLL------VQED--LTR---- 333
Cdd:cd05927 163 ISylplahifervvealFLYHGAKIGFY---SGDIRLLLDDIKALKPTVFPGVPRVLnRIYdkifnkVQAKgpLKRklfn 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 334 ----YKFQCLRH---------------------------CLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETV-LICGNF 381
Cdd:cd05927 240 falnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTaGATLTL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 382 RGSTIKsGSMGKASPPYDVQIVD-EEGN--VLPPGKEGNIAIRikptrPFCLFNCYLDNPEKTA-ASEQGDFYITGDRAH 457
Cdd:cd05927 320 PGDTSV-GHVGGPLPCAEVKLVDvPEMNydAKDPNPRGEVCIR-----GPNVFSGYYKDPEKTAeALDEDGWLHTGDIGE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196780 458 MDEDGYFWFVGRNDDVINSS--SYrIGPVEVESALAEHPAVLESAVvsspdpiRGEVVKAFIVlspAYVSHDPEAL 531
Cdd:cd05927 394 WLPNGTLKIIDRKKNIFKLSqgEY-VAPEKIENIYARSPFVAQIFV-------YGDSLKSFLV---AIVVPDPDVL 458
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
67-247 |
1.74e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 48.24 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 67 KTGHRPPNPAFWWVNGSGTE-VKWTFEELGKQSRKAANILEGACGlkPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGI 145
Cdd:PRK05691 18 RAAQTPDRLALRFLADDPGEgVVLSYRDLDLRARTIAAALQARAS--FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 146 SQLTQKdlkyRLQAARVKSIItSDALAPHVDAISADCPSLQSRLLVSDTSRPGWINFRELLRVASPEHNCLRTRSGDSMA 225
Cdd:PRK05691 96 PPESAR----RHHQERLLSII-ADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQPDDIAF 170
|
170 180
....*....|....*....|..
gi 88196780 226 IYFTSGTTGTPKMVehsQCSYG 247
Cdd:PRK05691 171 LQYTSGSTALPKGV---QVSHG 189
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
450-571 |
6.32e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 45.59 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 450 YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLES------------AVVS--SPDPIRGEVVKA 515
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPDDESF 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88196780 516 FIVLSPAYVSHDPEA--------LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
229-416 |
1.46e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 44.54 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 229 TSGTTGTPKMVEHSQ--CSYGLGFVASGRRLMALTESDIFWNTTDTGWVKAAWTLF-SAWANGACVFvhelP----QVDA 301
Cdd:cd05913 86 SSGTTGKPTVVGYTKndLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHyGAERLGALVI----PagggNTER 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 302 QtiLNTLCRFPITTICCVPTLFRLL---VQEDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETVLIC 378
Cdd:cd05913 162 Q--LQLIKDFGPTVLCCTPSYALYLaeeAEEEGIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPG 239
|
170 180 190
....*....|....*....|....*....|....*....
gi 88196780 379 GNFrgSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEG 416
Cdd:cd05913 240 VAF--ECEEKDGLHIWEDHFIPEIIDpETGEPVPPGEVG 276
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
80-173 |
3.00e-04 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 43.49 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 80 VNGSGTEVK-WTFEELGKQSRKAANILEGACGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQ 158
Cdd:cd05905 5 LDSKGKEATtLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLG 84
|
90
....*....|....*
gi 88196780 159 AARVKSIITSDALAP 173
Cdd:cd05905 85 TCKVRVALTVEACLK 99
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
81-454 |
1.53e-03 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 41.40 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 81 NGSGTEVKWTFEELGKQSRK-AANILEgaCGLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPgIS---QLTQKD---L 153
Cdd:PRK08180 62 GADGGWRRLTYAEALERVRAiAQALLD--RGLSAERPLMILSGNSIEHALLALAAMYAGVPYAP-VSpaySLVSQDfgkL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 154 KYRLQAARVKSIITSDAlAPHVDAISADCPSlqSRLLVSDTSRPG---WINFRELLRVASPE-----HNCLRtrsGDSMA 225
Cdd:PRK08180 139 RHVLELLTPGLVFADDG-AAFARALAAVVPA--DVEVVAVRGAVPgraATPFAALLATPPTAavdaaHAAVG---PDTIA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 226 IY-FTSGTTGTPKMVEHSQ---CSyglgfvasgrRLMALTESDIF-------------WNTTDTGWVKAAWTLFsawaNG 288
Cdd:PRK08180 213 KFlFTSGSTGLPKAVINTHrmlCA----------NQQMLAQTFPFlaeeppvlvdwlpWNHTFGGNHNLGIVLY----NG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 289 ACVFVHE---LPQVDAQTILNtLCRFPITTICCVPTLFRLLVQ-----EDLTRYKFQCLRHCLAGGEALNSDVRDKWKNQ 360
Cdd:PRK08180 279 GTLYIDDgkpTPGGFDETLRN-LREISPTVYFNVPKGWEMLVPalerdAALRRRFFSRLKLLFYAGAALSQDVWDRLDRV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 361 TGLEIHE------GYGQSETVLICGNFRGSTIKSGSMGKASPPYDVQIVDEegnvlppgkEGNIAIRIK-PTrpfcLFNC 433
Cdd:PRK08180 358 AEATCGErirmmtGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPV---------GGKLEVRVKgPN----VTPG 424
|
410 420
....*....|....*....|...
gi 88196780 434 YLDNPEKTAAS--EQGdFYITGD 454
Cdd:PRK08180 425 YWRAPELTAEAfdEEG-YYRSGD 446
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
110-239 |
1.75e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 41.37 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 110 GLKPGDRLMLVLPRLPEWWLTIVACMRTGVVMIPGISQLTQKDLKYRLQAARVKSIITSDALAPHVDAISADCPSLQSRL 189
Cdd:PLN02861 98 GVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILSCLPKCSSNLKTI 177
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 88196780 190 L----VSDTSRP-------GWINFRELLRVASPEHNCLRTRSGDSMAIYFTSGTTGTPKMV 239
Cdd:PLN02861 178 VsfgdVSSEQKEeaeelgvSCFSWEEFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKGV 238
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
339-576 |
1.91e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 40.95 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 339 LRHCLAGGEALNSDVRDKWKNQTGLEIHEGYGQSETvliCGnfrGSTI-------KSGSMGKASPPYDVQI--VDEEG-N 408
Cdd:PLN02430 385 LRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LG---PTTLgfpdemcMLGTVGAPAVYNELRLeeVPEMGyD 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 409 VLPPGKEGNIAIRIKptrpfCLFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVE-VE 487
Cdd:PLN02430 459 PLGEPPRGEICVRGK-----CLFSGYYKNPELTEEVMKDGWFHTGDIGEILPNGVLKIIDRKKNLIKLSQGEYVALEyLE 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 488 SALAEHPAVLESAVVsspdpirGEVVKAFIVlspAYVSHDPEALTR--ELQEHVKTVTAPYKYPR-KVAFISELPKTVSg 564
Cdd:PLN02430 534 NVYGQNPIVEDIWVY-------GDSFKSMLV---AVVVPNEENTNKwaKDNGFTGSFEELCSLPElKEHILSELKSTAE- 602
|
250
....*....|..
gi 88196780 565 kilRSKLRNQEW 576
Cdd:PLN02430 603 ---KNKLRGFEY 611
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
450-571 |
3.92e-03 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 40.43 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 450 YITGDRAHMDEDGYFWFVGRNDDVINSSSYRIGPVEVESALAEHPAVLE----------------SAVVSSPDPirgEVV 513
Cdd:TIGR03443 680 YRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREnvtlvrrdkdeeptlvSYIVPQDKS---DEL 756
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 88196780 514 KAFIVLSPAYVSHDP--------EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:TIGR03443 757 EEFKSEVDDEESSDPvvkglikyRKLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPAL 822
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
468-574 |
4.42e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 39.75 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88196780 468 GRNDDVINSssyriGPVeVESALAEHPAVLESAVVSSPDPIRGEVVKAFivlspayVSHDPEALTRELQEHVKTVTAPyK 547
Cdd:PRK09188 233 GTGDRIDNE-----APA-IQAALKSDPAVSDVAIALFSLPAKGVGLYAF-------VEAELPADEKSLRARLAGAKPP-K 298
|
90 100 110
....*....|....*....|....*....|.
gi 88196780 548 YPRKVAFISELPKTVSGK----ILRSKLRNQ 574
Cdd:PRK09188 299 PPEHIQPVAALPRDADGTvrddILRLIAMNQ 329
|
|
| |
