|
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: 1029.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 48 VPEYFNFAHDVLDVWSQLEKTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDW 127
Cdd:cd05928 1 VPEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 128 WLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLR 207
Cdd:cd05928 81 WLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 208 AASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFWNTTDTGWVKAAW-TLFSAWS 286
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 287 NGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELH 366
Cdd:cd05928 241 QGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 367 EGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFCFFNCYLDNPEKTAASEQ 446
Cdd:cd05928 321 EGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 447 GDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASH 526
Cdd:cd05928 401 GDFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSH 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 26341010 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: 585.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 48 VPEYFNFAHDVLDVWsqLEKTGHRPpnpAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDW 127
Cdd:COG0365 4 VGGRLNIAYNCLDRH--AEGRGDKV---ALIWEGEDGEERTLTYAELRREVNRFANALRAL-GVKKGDRVAIYLPNIPEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 128 WLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA---------LAPQVDAISADCPSLQTKLLV----SDT 194
Cdd:COG0365 78 VIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADGglrggkvidLKEKVDEALEELPSLEHVIVVgrtgADV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 195 SRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFWNTTDTGW 274
Cdd:COG0365 158 PMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGW 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 275 VKAAW-TLFSAWSNGACIFVHE--LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQED---LTRYKFQCLRHCLTGGEA 348
Cdd:COG0365 238 ATGHSyIVYGPLLNGATVVLYEgrPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGdepLKKYDLSSLRLLGSAGEP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 349 LNPDVRDKWKSQTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptRP 427
Cdd:COG0365 318 LNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIK----GP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 428 F-CFFNCYLDNPEKTAASEQGDF---YITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS 503
Cdd:COG0365 394 WpGMFRGYWNDPERYRETYFGRFpgwYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVG 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26341010 504 SPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 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: 568.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 89 WTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DalapqvdaisadcpslqtkllvSDTSrpgwinfrellraaspehncvrtrsgdsvAIYFTSGTTGAPKMVEHSqSSYGL 248
Cdd:cd05972 80 A----------------------EDPA-----------------------------LIYFTSGTTGLPKGVLHT-HSYPL 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 249 GFVAGGRRWMALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLV 327
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 328 QEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEG 407
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 408 NVLPPGKEGNIAVRIKPTRPFCFfncYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVE 487
Cdd:cd05972 268 RELPPGEEGDIAIKLPPPGLFLG---YVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 488 SALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYE--PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*
gi 26341010 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: 556.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 48 VPEYFNFAHDVLDVWSQLEktghrPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDW 127
Cdd:cd05970 12 VPENFNFAYDVVDAMAKEY-----PDKLALVWCDDAGEERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYEF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 128 WLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT--SDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFREL 205
Cdd:cd05970 86 WYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 206 LRAASPE----HNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSsYGLGFVAGGRRWMALTESDIFWNTTDTGWVKAAW-T 280
Cdd:cd05970 166 IKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFT-YPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 281 LFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQ 360
Cdd:cd05970 245 IYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 361 TGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFCFFNCYLDNPEK 440
Cdd:cd05970 325 TGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDAEK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 441 TAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLS 520
Cdd:cd05970 405 TAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLA 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 26341010 521 PAYAShdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:cd05970 485 KGYEP--SEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
76-577 |
3.08e-129 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 390.02 E-value: 3.08e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 76 AFWWVnGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKY 155
Cdd:PRK04319 62 ALRYL-DASRKEKYTYKELKELSNKFANVLKEL-GVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 156 RLQAARAKSIVTSDALAPQVdaISADCPSLQTKLLVSDTSR--PGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTT 233
Cdd:PRK04319 140 RLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLDFNALMEQASDEFDIEWTDREDGAILHYTSGST 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 234 GAPKMVEHSQSSYGLGFVAGgrRW-MALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHElPRVDAKTILNTLCRF 311
Cdd:PRK04319 218 GKPKGVLHVHNAMLQHYQTG--KYvLDLHEDDVYWCTADPGWVTGtSYGIFAPWLNGATNVIDG-GRFSPERWYRILEDY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 312 PITTLCCVPTLFRLLV---QEDLTRYKFQCLRHCLTGGEALNPDVRdKW-KSQTGLELHEGYGQSET--VVICgNSRNST 385
Cdd:PRK04319 295 KVTVWYTAPTAIRMLMgagDDLVKKYDLSSLRHILSVGEPLNPEVV-RWgMKVFGLPIHDNWWMTETggIMIA-NYPAMD 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 386 IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAvrIKPTRPfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFW 465
Cdd:PRK04319 373 IKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLA--IKKGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFW 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 466 FLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKTVTAP 545
Cdd:PRK04319 450 FQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE--ELKEEIRGFVKKGLGA 527
|
490 500 510
....*....|....*....|....*....|..
gi 26341010 546 YKYPRKVAFISELPKTVSGKILRSKLRNQEWG 577
Cdd:PRK04319 528 HAAPREIEFKDKLPKTRSGKIMRRVLKAWELG 559
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-575 |
4.10e-126 |
|
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: 377.29 E-value: 4.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAksivtsd 169
Cdd:cd05974 2 SFAEMSARSSRVANFLRS-IGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDAISADCPSLqtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvaIYFTSGTTGAPKMVEHSQSSYGLG 249
Cdd:cd05974 74 VYAAVDENTHADDPML----------------------------------------LYFTSGTTSKPKLVEHTHRSYPVG 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 250 FVAGgRRWMALTESDIFWNTTDTGWVKAAWT-LFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ 328
Cdd:cd05974 114 HLST-MYWIGLKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 329 EDLTRYKFQcLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGN 408
Cdd:cd05974 193 QDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 409 vlpPGKEGNIAVRIKPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVES 488
Cdd:cd05974 272 ---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 489 ALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALtrELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILR 568
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLRAGYEPSPETAL--EIFRFSRERLAPYKRIRRLEF-AELPKTISGKIRR 425
|
....*..
gi 26341010 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 |
8.05e-120 |
|
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: 361.43 E-value: 8.05e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 89 WTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSL-GVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DalapqvdaisadcpslqtkllvsdtsrpgwinfrELLRAASPEhncvrtrsgDSVAIYFTSGTTGAPKMVEHSQSSYGL 248
Cdd:cd05969 80 E----------------------------------ELYERTDPE---------DPTLLHYTSGTTGTPKGVLHVHDAMIF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 249 GFVAGgrRW-MALTESDIFWNTTDTGWVK-AAWTLFSAWSNGACIFVHElPRVDAKTILNTLCRFPITTLCCVPTLFRLL 326
Cdd:cd05969 117 YYFTG--KYvLDLHPDDIYWCTADPGWVTgTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRML 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 327 VQED---LTRYKFQCLRHCLTGGEALNPDVRdKWKSQT-GLELHEGYGQSET--VVICgNSRNSTIKSGSMGKASPPYDV 400
Cdd:cd05969 194 MKEGdelARKYDLSSLRFIHSVGEPLNPEAI-RWGMEVfGVPIHDTWWQTETgsIMIA-NYPCMPIKPGSMGKPLPGVKA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 401 QIVDEEGNVLPPGKEGNIAvrIKPTRPfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYR 480
Cdd:cd05969 272 AVVDENGNELPPGTKGILA--LKPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 481 IGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPK 560
Cdd:cd05969 349 VGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD--ELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
|
490
....*....|....*
gi 26341010 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 |
2.98e-119 |
|
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: 360.28 E-value: 2.98e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 56 HDVLDVWSQlektgHRPPNPAFwwVNGSGTevkWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACM 135
Cdd:COG0318 2 ADLLRRAAA-----RHPDRPAL--VFGGRR---LTYAELDARARRLAAALRA-LGVGPGDRVALLLPNSPEFVVAFLAAL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 136 RTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTsdalapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehnc 215
Cdd:COG0318 71 RAGAVVVPLNPRLTAEELAYILEDSGARALVT------------------------------------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 216 vrtrsgdsVAIYFTSGTTGAPKMVEHSQSSYgLGFVAGGRRWMALTESDIFWNTT----DTGWVkaaWTLFSAWSNGACI 291
Cdd:COG0318 103 --------ALILYTSGTTGRPKGVMLTHRNL-LANAAAIAAALGLTPGDVVLVALplfhVFGLT---VGLLAPLLAGATL 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 292 FVheLPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYG 370
Cdd:COG0318 171 VL--LPRFDPERVLELIERERVTVLFGVPTMLaRLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 371 QSET-VVICGNSRNS-TIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptrPFCFFNCYLDNPEKTAASEQGD 448
Cdd:COG0318 249 LTETsPVVTVNPEDPgERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDG 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 449 FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDP 528
Cdd:COG0318 324 WLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDA 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 26341010 529 EALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 578
Cdd:COG0318 403 EELRAFLRERL----ARYKVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
84-572 |
2.00e-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: 329.39 E-value: 2.00e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:cd05971 2 GTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 164 SIVTsdalapqvDAisADCPSLqtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvaIYFTSGTTGAPKMVEHSQ 243
Cdd:cd05971 81 ALVT--------DG--SDDPAL----------------------------------------IIYTSGTTGPPKGALHAH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 244 SSYgLGFVAGGRRW--MALTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVP 320
Cdd:cd05971 111 RVL-LGHLPGVQFPfnLFPRDGDLYWTPADWAWIGGLLdVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 321 TLFRLLVQEDLTRYKFQC-LRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRN-STIKSGSMGKASPPY 398
Cdd:cd05971 190 TALKMMRQQGEQLKHAQVkLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIGNCSAlFPIKPGSMGKPIPGH 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 399 DVQIVDEEGNVLPPGKEGNIAVRiKPTrPFCFFNcYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSS 478
Cdd:cd05971 270 RVAIVDDNGTPLPPGEVGEIAVE-LPD-PVAFLG-YWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDVITSSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 479 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISEL 558
Cdd:cd05971 347 YRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGET--PSDALAREIQELVKTRLAAHEYPREIEFVNEL 424
|
490
....*....|....
gi 26341010 559 PKTVSGKILRSKLR 572
Cdd:cd05971 425 PRTATGKIRRRELR 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
50-572 |
1.45e-106 |
|
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: 329.71 E-value: 1.45e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 50 EYFNFAHDVLDvwsQLEKTghRPPNPAFWWVNGSgtevkWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWL 129
Cdd:cd05959 1 EKYNAATLVDL---NLNEG--RGDKTAFIDDAGS-----LTYAELEAEARRVAGALRAL-GVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 130 ISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQV-DAISADCPSLQTkLLVSDTSRP--GWINFRELL 206
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLaAALTKSEHTLVV-LIVSGGAGPeaGALLLAELV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 207 RAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFWNTTdtgwvkaawTLFSAWS 286
Cdd:cd05959 149 AAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGIREDDVCFSAA---------KLFFAYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 287 NG-ACIF--------VHELPRVDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDK 356
Cdd:cd05959 220 LGnSLTFplsvgattVLMPERPTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGER 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 357 WKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFcffncYLD 436
Cdd:cd05959 300 WKARFGLDILDGIGSTEMLHIFLSNRPGRVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATM-----YWN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 437 NPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAF 516
Cdd:cd05959 375 NRDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAF 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 26341010 517 IVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05959 455 VVLRPGYE--DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
222-567 |
4.43e-104 |
|
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: 317.30 E-value: 4.43e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPKMVEHSQSSYgLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHelPRVDA 301
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNL-LAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 302 KTILNTLCRFPITTLCCVPTLFRLLVQEDL-TRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET--VVIC 378
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPEsAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETggTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 379 GNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIkPTRpfcfFNCYLDNPEKTAASEQGDFYITGDRAHM 458
Cdd:cd04433 158 GPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRG-PSV----MKGYWNNPEATAAVDEDGWYRTGDLGRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 459 DEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEH 538
Cdd:cd04433 233 DEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPG-ADLDAE----ELRAH 307
|
330 340
....*....|....*....|....*....
gi 26341010 539 VKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
61-572 |
2.05e-101 |
|
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: 314.89 E-value: 2.05e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 61 VWSQLEKT-GHRPPNPAFWWvngsgTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGV 139
Cdd:cd05936 1 LADLLEEAaRRFPDKTALIF-----MGRKLTYRELDALAEAFAAGLQNL-GVQPGDRVALMLPNCPQFPIAYFGALKAGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 140 VMIPGVSQLTAKDLKYRLQaaraksivtsdalapqvdaisaDCpslQTKLLVSDTSrpgwinFRELLRAASPEHNCVRTR 219
Cdd:cd05936 75 VVVPLNPLYTPRELEHILN----------------------DS---GAKALIVAVS------FTDLLAAGAPLGERVALT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 220 SGDSVAIYFTSGTTGAPKMVEHSQSSYgLGFVAGGRRWM--ALTESDIFwnttdtgwVKA-------AWT--LFSAWSNG 288
Cdd:cd05936 124 PEDVAVLQYTSGTTGVPKGAMLTHRNL-VANALQIKAWLedLLEGDDVV--------LAAlplfhvfGLTvaLLLPLALG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 289 ACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHE 367
Cdd:cd05936 195 ATIVL--IPRFRPIGVLKEIRKHRVTIFPGVPTMYiALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 368 GYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTAASEQ 446
Cdd:cd05936 273 GYGLTETSpVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-GPQV----MKGYWNRPEETAEAFV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 447 GDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayasH 526
Cdd:cd05936 348 DGWLRTGDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL------K 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 26341010 527 DPEALT-RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05936 422 EGASLTeEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
90-573 |
2.64e-98 |
|
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: 305.98 E-value: 2.64e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSd 169
Cdd:cd05973 2 TFGELRALSARFANALQEL-GVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 alAPQVDAISADcpslqtkLLVsdtsrpgwinfrellraaspehncvrtrsgdsvaIYFTSGTTGAPKMVEHSQSsYGLG 249
Cdd:cd05973 80 --AANRHKLDSD-------PFV----------------------------------MMFTSGTTGLPKGVPVPLR-ALAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 250 FVAGGRRWMALTESDIFWNTTDTGWvkaAWTLFSAWSNG-----ACIFVHELPRVDakTILNTLCRFPITTLCCVPTLFR 324
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGW---AYGLYYAITGPlalghPTILLEGGFSVE--STWRVIERLGVTNLAGSPTAYR 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 325 LLVQ---EDLTRYKFQcLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRN--STIKSGSMGKASPPYD 399
Cdd:cd05973 191 LLMAagaEVPARPKGR-LRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHAleHPVHAGSAGRAMPGWR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 400 VQIVDEEGNVLPPGKEGNIAVRIKPTrPFCFFNCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSY 479
Cdd:cd05973 270 VAVLDDDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 480 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyasHDP-EALTRELQEHVKTVTAPYKYPRKVAFISEL 558
Cdd:cd05973 346 RIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGG---HEGtPALADELQLHVKKRLSAHAYPRTIHFVDEL 422
|
490
....*....|....*
gi 26341010 559 PKTVSGKILRSKLRN 573
Cdd:cd05973 423 PKTPSGKIQRFLLRR 437
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
86-572 |
2.33e-95 |
|
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: 298.24 E-value: 2.33e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 VTSDALapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrTRSGDSVAIYFTSGTTGAPKMVEHSQSS 245
Cdd:cd05958 88 LCAHAL----------------------------------------------TASDDICILAFTSGTTGAPKATMHFHRD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 246 YGLGFVAGGRRWMALTESDIFwnttdTGWVKAAWT------LFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCV 319
Cdd:cd05958 122 PLASADRYAVNVLRLREDDRF-----VGSPPLAFTfglggvLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 320 PTLFRLLV------QEDLTrykfqCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGK 393
Cdd:cd05958 195 PTAYRAMLahpdaaGPDLS-----SLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARPGATGK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 394 ASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcffNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDV 473
Cdd:cd05958 270 PVPGYEAKVVDDEGNPVPDGTIGRLAVR-GPT------GCRYLADKRQRTYVQGGWNITGDTYSRDPDGYFRHQGRSDDM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 474 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAShdPEALTRELQEHVKTVTAPYKYPRKVA 553
Cdd:cd05958 343 IVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIP--GPVLARELQDHAKAHIAPYKYPRAIE 420
|
490
....*....|....*....
gi 26341010 554 FISELPKTVSGKILRSKLR 572
Cdd:cd05958 421 FVTELPRTATGKLQRFALR 439
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
85-576 |
2.49e-92 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 293.25 E-value: 2.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 85 TEVKWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVlprlpDW----WLISV-ACMRTGVVMIPGVSQLTAKDLKYRLQA 159
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVF-----DWnsheYLEAYfAVPKIGAVLHPINIRLKPEEIAYILND 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 160 ARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPG----WINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGA 235
Cdd:PRK06187 102 AEDRVVLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 236 PKMVEHSQSSYGLGfVAGGRRWMALTESDIFWNTTDTGWVkAAWTL-FSAWSNGACIFVHElpRVDAKTILNTLCRFPIT 314
Cdd:PRK06187 182 PKGVVLSHRNLFLH-SLAVCAWLKLSRDDVYLVIVPMFHV-HAWGLpYLALMAGAKQVIPR--RFDPENLLDLIETERVT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 315 TLCCVPTLFRLLVQEDLTR-YKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGN-----SRNSTIK 387
Cdd:PRK06187 258 FFFAVPTIWQMLLKAPRAYfVDFSSLRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSpVVSVLppedqLPGQWTK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 388 SGSMGKASPPYDVQIVDEEGNVLPP-GKE-GNIAVRiKPtrpfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFW 465
Cdd:PRK06187 338 RRSAGRPLPGVEARIVDDDGDELPPdGGEvGEIIVR-GP----WLMQGYWNRPEATAETIDGGWLHTGDVGYIDEDGYLY 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 466 FLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAP 545
Cdd:PRK06187 413 ITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG-ATLDAK----ELRAFLRGRLAK 487
|
490 500 510
....*....|....*....|....*....|.
gi 26341010 546 YKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK06187 488 FKLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
90-572 |
4.54e-82 |
|
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: 265.93 E-value: 4.54e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:TIGR02262 32 SYGELEAQVRRLAAALRRL-GVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDAISADCPSLQTKLLVSDtSRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLG 249
Cdd:TIGR02262 111 ALLPVIKAALGKSPHLEHRVVVGR-PEAGEVQLAELLATESEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 250 FVAGGRRWMALTESDIfwnttdtgwVKAAWTLFSAWSNGACIF-----------VHELPRVDAktILNTLCRFPITTLCC 318
Cdd:TIGR02262 190 AELYARNTLGIREDDV---------CFSAAKLFFAYGLGNALTfpmsvgattvlMGERPTPDA--VFDRLRRHQPTIFYG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 319 VPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPP 397
Cdd:TIGR02262 259 VPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVDIVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 398 YDVQIVDEEGNVLPPGKEGNIAVRiKPTRPFCFFNcyldNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSS 477
Cdd:TIGR02262 339 YRLRLVGDGGQDVADGEPGELLIS-GPSSATMYWN----NRAKSRDTFQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 478 SYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYashdpEALTRELQEHVKTVTAPYKYPRKVAFISE 557
Cdd:TIGR02262 414 GIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ-----TALETELKEHVKDRLAPYKYPRWIVFVDD 488
|
490
....*....|....*
gi 26341010 558 LPKTVSGKILRSKLR 572
Cdd:TIGR02262 489 LPKTATGKIQRFKLR 503
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
90-572 |
6.79e-80 |
|
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: 258.16 E-value: 6.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:cd05919 12 TYGQLHDGANRLGSALRNL-GVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 AlapqvdaisaDCPSLQtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvaiyFTSGTTGAPKMVEHSQSSYgLG 249
Cdd:cd05919 91 D----------DIAYLL-----------------------------------------YSSGTTGPPKGVMHAHRDP-LL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 250 FV-AGGRRWMALTESDIFWNTTDTGWvkaAW----TLFSAWSNGACIFVHELPRvDAKTILNTLCRFPITTLCCVPTLF- 323
Cdd:cd05919 119 FAdAMAREALGLTPGDRVFSSAKMFF---GYglgnSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYa 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 324 RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIV 403
Cdd:cd05919 195 NLLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 404 DEEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGP 483
Cdd:cd05919 275 DEEGHTIPPGEEGDLLVR-GPSA----AVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 484 VEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHdpEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVS 563
Cdd:cd05919 350 VEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTAT 427
|
....*....
gi 26341010 564 GKILRSKLR 572
Cdd:cd05919 428 GKLQRFKLR 436
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
53-573 |
4.24e-79 |
|
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: 260.96 E-value: 4.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 53 NFAHDVLDVWsqLEKTGHRPpnpAFWWV-NGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLIS 131
Cdd:cd05966 53 NISYNCLDRH--LKERGDKV---AIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 132 VACMRTGV---VMIPGVSqltAKDLKYRLQAARAKSIVTSDA---------LAPQVDAISADCPSLQTKLLVSDTSRPGW 199
Cdd:cd05966 127 LACARIGAvhsVVFAGFS---AESLADRINDAQCKLVITADGgyrggkvipLKEIVDEALEKCPSVEKVLVVKRTGGEVP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 200 IN------FRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGfVAGGRRWM-ALTESDIFWNTTDT 272
Cdd:cd05966 204 MTegrdlwWHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGGYLLY-AATTFKYVfDYHPDDIYWCTADI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 273 GWVKA-AWTLFSAWSNGACIFVHE----LPrvDAKTILNTLCRFPITTLCCVPTLFRLLVQ---EDLTRYKFQCLRHCLT 344
Cdd:cd05966 283 GWITGhSYIVYGPLANGATTVMFEgtptYP--DPGRYWDIVEKHKVTIFYTAPTAIRALMKfgdEWVKKHDLSSLRVLGS 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 345 GGEALNPDVrdkWK---SQTGLE---LHEGYGQSET--VVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEG 416
Cdd:cd05966 361 VGEPINPEA---WMwyyEVIGKErcpIVDTWWQTETggIMITPLPGATPLKPGSATRPFFGIEPAILDEEGNEVEGEVEG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 417 NIAvrIKPTRPFCFFNCYLDNP--EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHP 494
Cdd:cd05966 438 YLV--IKRPWPGMARTIYGDHEryEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHP 515
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26341010 495 AVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd05966 516 AVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
53-567 |
4.81e-79 |
|
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: 260.20 E-value: 4.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 53 NFAHDVLDvwSQLEKTGHRPpnpAFWWVNGSGTEVK-WTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLIS 131
Cdd:cd17634 53 NLAANALD--RHLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTLLDL-GVKKGDRVAIYMPMIPEAAVAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 132 VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA---------LAPQVD-AISADCPSLQTKLLVSDTSRP---- 197
Cdd:cd17634 127 LACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvpLKKNVDdALNPNVTSVEHVIVLKRTGSDidwq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 198 --GWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFWNTTDTGWV 275
Cdd:cd17634 207 egRDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWV 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 276 KA-AWTLFSAWSNGACIFVHELPRV--DAKTILNTLCRFPITTLCCVPTLFRLLVQED---LTRYKFQCLRHCLTGGEAL 349
Cdd:cd17634 287 TGhSYLLYGPLACGATTLLYEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRALMAAGddaIEGTDRSSLRILGSVGEPI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 350 NPDV-RDKWK--SQTGLELHEGYGQSETV-VICGNSRNST-IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIK- 423
Cdd:cd17634 367 NPEAyEWYWKkiGKEKCPVVDTWWQTETGgFMITPLPGAIeLKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPw 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 424 PTRPFCFFNcylDNPE--KTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV 501
Cdd:cd17634 447 PGQTRTLFG---DHERfeQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26341010 502 VSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:cd17634 524 VGIPHAIKGQAPYAYVVLNHGVE--PSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKIM 587
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
69-568 |
4.75e-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: 253.30 E-value: 4.75e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 69 GHRPPNPAFWWVNGSgtevkWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQL 148
Cdd:cd17631 6 RRHPDRTALVFGGRS-----LTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 149 TAKDLKYRLQAARAKsivtsdalapqvdaisadcpslqtkLLVSDTSRpgwinfrellraaspehncvrtrsgdsvaIYF 228
Cdd:cd17631 80 TPPEVAYILADSGAK-------------------------VLFDDLAL-----------------------------LMY 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 229 TSGTTGAPKMVEHSQssyglgfvaggRRWMALTES---DIFWNTTDTGWVKA---------AWTLFSAWSNGACIFvheL 296
Cdd:cd17631 106 TSGTTGRPKGAMLTH-----------RNLLWNAVNalaALDLGPDDVLLVVAplfhigglgVFTLPTLLRGGTVVI---L 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 297 PRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSqTGLELHEGYGQSETV 375
Cdd:cd17631 172 RKFDPETVLDLIERHRVTSFFLVPTMIQALLQhPRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETS 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 376 -VICGNSRNSTI-KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTAASEQGDFYITG 453
Cdd:cd17631 251 pGVTFLSPEDHRrKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GPHV----MAGYWNRPEATAAAFRDGWFHTG 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 454 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayaSHDPEALtr 533
Cdd:cd17631 326 DLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRP---GAELDED-- 400
|
490 500 510
....*....|....*....|....*....|....*
gi 26341010 534 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:cd17631 401 ELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
47-573 |
2.34e-77 |
|
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: 256.47 E-value: 2.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 47 PVPEYF-----NFAHDVLDVWSQlektGHRPPNPAFWWVNGS-GTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLV 120
Cdd:cd05967 39 PFTRWFvggrlNTCYNALDRHVE----AGRGDQIALIYDSPVtGTERTYTYAELLDEVSRLAGVLRKL-GVVKGDRVIIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 121 LPRLPDWWLISVACMRTGV---VMIPGVSqltAKDLKYRLQAARAKSIVTSDA---------LAPQVD-AIS------AD 181
Cdd:cd05967 114 MPMIPEAAIAMLACARIGAihsVVFGGFA---AKELASRIDDAKPKLIVTASCgiepgkvvpYKPLLDkALElsghkpHH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 182 CPSLQTKLLVSDTSRPG-WINFRELLRAASPeHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMAL 260
Cdd:cd05967 191 VLVLNRPQVPADLTKPGrDLDWSELLAKAEP-VDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 261 TESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHELPRV---DAKTILNTLCRFPITTLCCVPTLFRLLVQED-----L 331
Cdd:cd05967 270 KPGDVWWAASDVGWVVGhSYIVYGPLLHGATTVLYEGKPVgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDpdgkyI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 332 TRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET-VVICGNSRN---STIKSGSMGKASPPYDVQIVDEEG 407
Cdd:cd05967 350 KKYDLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDHWWQTETgWPITANPVGlepLPIKAGSPGKPVPGYQVQVLDEDG 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 408 NVLPPGKEGNIAVRIkPTRPFCFFNCYLDNP--EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVE 485
Cdd:cd05967 430 EPVGPNELGNIVIKL-PLPPGCLLTLWKNDErfKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGE 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 486 VESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYaSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 565
Cdd:cd05967 509 MEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGV-KITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGK 587
|
....*...
gi 26341010 566 ILRSKLRN 573
Cdd:cd05967 588 ILRRTLRK 595
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
65-477 |
7.78e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 249.54 E-value: 7.78e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 65 LEKTGHRPPN-PAFwwvnGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIP 143
Cdd:pfam00501 1 LERQAARTPDkTAL----EVGEGRRLTYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 144 GVSQLTAKDLKYRLQAARAKSIVTSDAL-APQVDAISADCPSLQTKLLVS-DTSRPGWINFRELLRAASPEHNCVRTRSG 221
Cdd:pfam00501 76 LNPRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVLDrDPVLKEEPLPEEAKPADVPPPPPPPPDPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPKMVEHSQSSY---GLGFVAGGRRWMALTESDIFWNTT----DTGWVkaaWTLFSAWSNGACI-FV 293
Cdd:pfam00501 156 DLAYIIYTSGTTGKPKGVMLTHRNLvanVLSIKRVRPRGFGLGPDDRVLSTLplfhDFGLS---LGLLGPLLAGATVvLP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 294 HELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQS 372
Cdd:pfam00501 233 PGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEaGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 373 ETVVICGNSRN---STIKSGSMGKASPPYDVQIVDEE-GNVLPPGKEGNIAVRikptRPfCFFNCYLDNPEKTAAS-EQG 447
Cdd:pfam00501 313 ETTGVVTTPLPldeDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAfDED 387
|
410 420 430
....*....|....*....|....*....|
gi 26341010 448 DFYITGDRAHMDEDGYFWFLGRNDDVINSS 477
Cdd:pfam00501 388 GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
84-572 |
8.58e-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: 255.25 E-value: 8.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGV---VMIPGVSqltAKDLKYRLQAA 160
Cdd:TIGR02188 84 GEVRKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGAihsVVFGGFS---AEALADRINDA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 161 RAKSIVTSD---------ALAPQVDAISADCPSLQTKLLV---SDTSRPGWIN-----FRELLRAASPEHNCVRTRSGDS 223
Cdd:TIGR02188 160 GAKLVITADeglrggkviPLKAIVDEALEKCPVSVEHVLVvrrTGNPVVPWVEgrdvwWHDLMAKASAYCEPEPMDSEDP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 224 VAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHE-LPRV-D 300
Cdd:TIGR02188 240 LFILYTSGSTGKPKGVLHTTGGYLLYAAMTMKYVFDIKDGDIFWCTADVGWITGhSYIVYGPLANGATTVMFEgVPTYpD 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 301 AKTILNTLCRFPITTLCCVPTLFRLLVQ---EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLE---LHEGYGQSET 374
Cdd:TIGR02188 320 PGRFWEIIEKHKVTIFYTAPTAIRALMRlgdEWVKKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKErcpIVDTWWQTET 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 375 VVICGNSRNSTI--KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVrIKPTRPFCFFNCYLDnPE---KTAASEQGDF 449
Cdd:TIGR02188 400 GGIMITPLPGATptKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGYLV-IKQPWPGMLRTIYGD-HErfvDTYFSPFPGY 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 450 YITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpe 529
Cdd:TIGR02188 478 YFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDD-- 555
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 26341010 530 ALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:TIGR02188 556 ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLR 598
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
90-574 |
1.26e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 251.75 E-value: 1.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK07656 32 TYAELNARVRRAAAALAAL-GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDAISADCPSLQTKLLVSDT----SRPGWINFRELLRAASPEHNcVRTRSGDSVA-IYFTSGTTGAPK--MVEHS 242
Cdd:PRK07656 111 LFLGVDYSATTRLPALEHVVICETEeddpHTEKMKTFTDFLAAGDPAER-APEVDPDDVAdILFTSGTTGRPKgaMLTHR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 243 Q--SSYG-----LGFVAGGRRWMALTESDIFwnttdtGWvKAAWTlfSAWSNGACIFVHelPRVDAKTILNTLCRFPITT 315
Cdd:PRK07656 190 QllSNAAdwaeyLGLTEGDRYLAANPFFHVF------GY-KAGVN--APLMRGATILPL--PVFDPDEVFRLIETERITV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 316 LCCVPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNP----DVRDKWKSQTGLElheGYGQSE---TVVICGNSRNSTIK 387
Cdd:PRK07656 259 LPGPPTMYNsLLQHPDRSAEDLSSLRLAVTGAASMPValleRFESELGVDIVLT---GYGLSEasgVTTFNRLDDDRKTV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 388 SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptrpfcFFNC---YLDNPEKTAASEQGDFYI-TGDRAHMDEDGY 463
Cdd:PRK07656 336 AGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR--------GPNVmkgYYDDPEATAAAIDADGWLhTGDLGRLDEEGY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 464 FWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVT 543
Cdd:PRK07656 408 LYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG-AELTEE----ELIAYCREHL 482
|
490 500 510
....*....|....*....|....*....|.
gi 26341010 544 APYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK07656 483 AKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
61-578 |
3.25e-76 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 251.42 E-value: 3.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 61 VWSQLEKTGHRPPN-PAFWWVngsGTEVkwTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGV 139
Cdd:PRK08314 12 LFHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 140 VMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQV------------------DAISADCP-----SLQTKLLVSDTSR 196
Cdd:PRK08314 87 VVVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysDYLPAEPEiavpaWLRAEPPLQALAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 197 PGWINFRELLRA--ASPEHNcvrTRSGDSVAIYFTSGTTGAPKMVEHSQSSYgLGFVAGGRRWMALTESDIFWNTTD--- 271
Cdd:PRK08314 167 GGVVAWKEALAAglAPPPHT---AGPDDLAVLPYTSGTTGVPKGCMHTHRTV-MANAVGSVLWSNSTPESVVLAVLPlfh 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 272 -TGWVKAawtLFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPT-LFRLLVQEDLTRYKFQCLRhCLTGGEAL 349
Cdd:PRK08314 243 vTGMVHS---MNAPIYAGATVVL--MPRWDREAAARLIERYRVTHWTNIPTmVVDFLASPGLAERDLSSLR-YIGGGGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 350 NPD-VRDKWKSQTGLELHEGYGQSETVV-ICGNSRNSTiKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTr 426
Cdd:PRK08314 317 MPEaVAERLKELTGLDYVEGYGLTETMAqTHSNPPDRP-KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVH-GPQ- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 427 pfcFFNCYLDNPEKTAAS----EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 502
Cdd:PRK08314 394 ---VFKGYWNRPEATAEAfieiDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVI 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26341010 503 SSPDPIRGEVVKAFIVLSPAYASHDPEAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 578
Cdd:PRK08314 471 ATPDPRRGETVKAVVVLRPEARGKTTEE---EIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQEQEKAR 543
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
88-572 |
6.01e-74 |
|
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: 241.81 E-value: 6.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd05934 3 RWTYAELLRESARIAAALAA-LGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 sdalapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgDSVAIYFTSGTTGAPKMVEHSQSSYg 247
Cdd:cd05934 82 ------------------------------------------------------DPASILYTSGTTGPPKGVVITHANL- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 248 LGFVAGGRRWMALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLFR-L 325
Cdd:cd05934 107 TFAGYYSARRFGLGEDDVYLTVLPLFHINAqAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSyL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 326 LVQEDLTRYKFQCLRhcLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDE 405
Cdd:cd05934 185 LAQPPSPDDRAHRLR--AAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 406 EGNVLPPGKEGNIAVRikPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVE 485
Cdd:cd05934 263 DGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 486 VESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGK 565
Cdd:cd05934 341 VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFAFCEGQL----AYFKVPRYIRFVDDLPKTPTEK 415
|
....*..
gi 26341010 566 ILRSKLR 572
Cdd:cd05934 416 VAKAQLR 422
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
85-567 |
1.55e-71 |
|
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: 237.50 E-value: 1.55e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 85 TEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKS 164
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 165 IVTSDALAPQVDAISADCPSlQTKLLVSDTSRPGWINFRELLRAAS--PEHN---CVRTRSGDSVAIYFTSGTTGAPK-- 237
Cdd:cd05911 86 IFTDPDGLEKVKEAAKELGP-KDKIIVLDDKPDGVLSIEDLLSPTLgeEDEDlppPLKDGKDDTAAILYSSGTTGLPKgv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 238 ---------MVEHSQSSYGLGFVAGGRRWMALTesdIFWNTTDTgwvkaaWTLFSAWsNGACIFVHelPRVDAKTILNTL 308
Cdd:cd05911 165 clshrnliaNLSQVQTFLYGNDGSNDVILGFLP---LYHIYGLF------TTLASLL-NGATVIIM--PKFDSELFLDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 309 CRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGL-ELHEGYGQSETVVICGNSRNSTI 386
Cdd:cd05911 233 EKYKITFLYLVPPIAAALAKsPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNaTIKQGYGMTETGGILTVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 387 KSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAVRIkptrPFCFfNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGY 463
Cdd:cd05911 313 KPGSVGRLLPNVEAKIVDDDGKdSLGPNEPGEICVRG----PQVM-KGYYNNPEATKETfdEDG-WLHTGDIGYFDEDGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 464 FWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEHVKTVT 543
Cdd:cd05911 387 LYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKP-----GEKLTEKEVKDYVAKKV 461
|
490 500
....*....|....*....|....*
gi 26341010 544 APYKYPRK-VAFISELPKTVSGKIL 567
Cdd:cd05911 462 ASYKQLRGgVVFVDEIPKSASGKIL 486
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
47-572 |
3.01e-70 |
|
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: 237.39 E-value: 3.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 47 PVPEYF-----NFAHDVLDVWsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVL 121
Cdd:cd05968 50 PWAAWFvggrmNIVEQLLDKW-----LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGLRAL-GVGKGDRVGIYL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 122 PRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA---------LAPQVDAISADCPSLQTKLLVS 192
Cdd:cd05968 124 PMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGftrrgrevnLKEEADKACAQCPTVEKVVVVR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 193 DTSRP-GWINFREL---LRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESD-IFW 267
Cdd:cd05968 204 HLGNDfTPAKGRDLsydEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQFDLKPGDlLTW 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 268 nTTDTGWVKAAWTLFSAWSNGACIFVHE----LPrvDAKTILNTLCRFPITTLCCVPTLFRLLV---QEDLTRYKFQCLR 340
Cdd:cd05968 284 -FTDLGWMMGPWLIFGGLILGATMVLYDgapdHP--KADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 341 HCLTGGEALNPD-----VRDKWKSQT-------GLELHEGygqsetvvICGNSRNSTIKSGSMGKASPPYDVQIVDEEGN 408
Cdd:cd05968 361 VLGSTGEPWNPEpwnwlFETVGKGRNpiinysgGTEISGG--------ILGNVLIKPIKPSSFNGPVPGMKADVLDESGK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 409 VLPPgKEGNIAVRiKP----TRPFC-----FFNCYLDNPEktaaseqgDFYITGDRAHMDEDGYFWFLGRNDDVINSSSY 479
Cdd:cd05968 433 PARP-EVGELVLL-APwpgmTRGFWrdedrYLETYWSRFD--------NVWVHGDFAYYDEEGYFYILGRSDDTINVAGK 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 480 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshDPEALTRELQEHVKTVTAPYKYPRKVAFISELP 559
Cdd:cd05968 503 RVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERVADELGKPLSPERILFVKDLP 580
|
570
....*....|...
gi 26341010 560 KTVSGKILRSKLR 572
Cdd:cd05968 581 KTRNAKVMRRVIR 593
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
53-572 |
2.42e-69 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 235.42 E-value: 2.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 53 NFAHDVLDVwsQLEKTGHRPpnpAFWWVNGSGTEV-KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLIS 131
Cdd:PRK00174 67 NVSYNCLDR--HLKTRGDKV---AIIWEGDDPGDSrKITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 132 VACMRTGV---VMIPGVSqltAKDLKYRLQAARAKSIVTSD---------ALAPQVDAISADCPSLQTKLLVSDTSRP-G 198
Cdd:PRK00174 141 LACARIGAvhsVVFGGFS---AEALADRIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVRRTGGDvD 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 199 WINFR-----ELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLgfvaggrrWMALT--------ESDI 265
Cdd:PRK00174 218 WVEGRdlwwhELVAGASDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTGGYLV--------YAAMTmkyvfdykDGDV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 266 FWNTTDTGWVKA-AWTLFSAWSNGACIFVHE-LPRV-DAKTILNTLCRFPITTLCCVPTLFRLLVQ---EDLTRYKFQCL 339
Cdd:PRK00174 290 YWCTADVGWVTGhSYIVYGPLANGATTLMFEgVPNYpDPGRFWEVIDKHKVTIFYTAPTAIRALMKegdEHPKKYDLSSL 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 340 RhcLTG--GEALNPDVRdKWksqtgleLHEGYGQSETVVIcgnsrnST-------------------IKSGSMGKASPPY 398
Cdd:PRK00174 370 R--LLGsvGEPINPEAW-EW-------YYKVVGGERCPIV------DTwwqtetggimitplpgatpLKPGSATRPLPGI 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 399 DVQIVDEEGNVLPPGKEGNIAVrikpTRPFcffncyldnP-------------EKTAASEQGDFYITGDRAHMDEDGYFW 465
Cdd:PRK00174 434 QPAVVDEEGNPLEGGEGGNLVI----KDPW---------PgmmrtiygdherfVKTYFSTFKGMYFTGDGARRDEDGYYW 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 466 FLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDpeALTRELQEHVKTVTAP 545
Cdd:PRK00174 501 ITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGP 578
|
570 580
....*....|....*....|....*..
gi 26341010 546 YKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK00174 579 IAKPDVIQFAPGLPKTRSGKIMRRILR 605
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
86-574 |
1.13e-67 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 228.28 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLvLPRLPDWWLIS-VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKS 164
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDL-GLKKGDRVAA-LGHNSDAYALLwLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 165 IVTSDALAPQVDAISADCPSLQTKLLVSDTSRP---GWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEH 241
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVLGGREapgGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 242 SQSS----YGLGFVAGGrrwmaLTESDIFWNttdtgwvkaAWTLF-SAWSN---GACIFV----HELPRVDAKTILNTLC 309
Cdd:PRK08316 192 THRAliaeYVSCIVAGD-----MSADDIPLH---------ALPLYhCAQLDvflGPYLYVgatnVILDAPDPELILRTIE 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 310 RFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTG-----GEALNpDVRDKWksqTGLELHEGYGQSE-----TVVic 378
Cdd:PRK08316 258 AERITSFFAPPTVWiSLLRHPDFDTRDLSSLRKGYYGasimpVEVLK-ELRERL---PGLRFYNCYGQTEiaplaTVL-- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 379 gNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikpTRPFCffNCYLDNPEKTAASEQGDFYITGDRAHM 458
Cdd:PRK08316 332 -GPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR---SPQLM--LGYWDDPEKTAEAFRGGWFHSGDLGVM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 459 DEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEH 538
Cdd:PRK08316 406 DEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG-ATVTED----ELIAH 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 26341010 539 VKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK08316 481 CRARLAGFKVPKRVIFVDELPRNPSGKILKRELRER 516
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
82-577 |
1.49e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 219.39 E-value: 1.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 82 GSGTEvkWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAAR 161
Cdd:PRK08276 7 PSGEV--VTYGELEARSNRLAHGLRAL-GLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 162 AKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDsvaIYFTSGTTGAPKMVEH 241
Cdd:PRK08276 84 AKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGAD---MLYSSGTTGRPKGIKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 242 SQSSYGLGFVAGGRRWMALtesdiFWNTTDTGWV--------KAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPI 313
Cdd:PRK08276 161 PLPGLDPDEAPGMMLALLG-----FGMYGGPDSVylspaplyHTAPLRFGMSALALGGTVVVMEKFDAEEALALIERYRV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 314 TTLCCVPTLF-RLLV--QEDLTRYKFQCLRHCLTGGEALNPDVR----DKWksqtGLELHEGYGQSE----TVVicgNSR 382
Cdd:PRK08276 236 THSQLVPTMFvRMLKlpEEVRARYDVSSLRVAIHAAAPCPVEVKramiDWW----GPIIHEYYASSEgggvTVI---TSE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 383 NSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAVRiKPTRPFCffncYLDNPEKTAASEQG-DFYITGDRAHMDED 461
Cdd:PRK08276 309 DWLAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE-MDGYPFE----YHNDPEKTAAARNPhGWVTVGDVGYLDED 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 462 GYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSPAYASHDPEALTRELQEHVKT 541
Cdd:PRK08276 383 GYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPADGADAGDALAAELIAWLRG 460
|
490 500 510
....*....|....*....|....*....|....*.
gi 26341010 542 VTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 577
Cdd:PRK08276 461 RLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWE 496
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
90-571 |
5.25e-64 |
|
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: 216.19 E-value: 5.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:cd05935 3 TYLELLEVVKKLASFLSN-KGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgDSVA-IYFTSGTTGAPKMVEHSQSSYgL 248
Cdd:cd05935 82 EL--------------------------------------------------DDLAlIPYTSGTTGLPKGCMHTHFSA-A 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 249 GFVAGGRRWMALTESDIFWNTTD----TGWVKaawTLFSAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPT-LF 323
Cdd:cd05935 111 ANALQSAVWTGLTPSDVILACLPlfhvTGFVG---SLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTmLV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 324 RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIV 403
Cdd:cd05935 186 DLLATPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 404 D-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGD----FYITGDRAHMDEDGYFWFLGRNDDVINSSS 478
Cdd:cd05935 266 DiETGRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEESFIEIkgrrFFRTGDLGYMDEEGYFFFVDRVKRMINVSG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 479 YRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAY-ASHDPEaltrELQEHVKTVTAPYKYPRKVAFISE 557
Cdd:cd05935 341 FKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrGKVTEE----DIIEWAREQMAAYKYPREVEFVDE 416
|
490
....*....|....
gi 26341010 558 LPKTVSGKILRSKL 571
Cdd:cd05935 417 LPRSASGKILWRLL 430
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
61-572 |
6.97e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 219.49 E-value: 6.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 61 VWSQLEKTGHRPpnpAFWWVnGSGTevkwTFEELGKQSRKAANVLEgVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVV 140
Cdd:PRK05605 38 YDNAVARFGDRP---ALDFF-GATT----TYAELGKQVRRAAAGLR-ALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 141 MIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPsLQTKLLVSDTSR------------------------ 196
Cdd:PRK05605 109 VVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVERLRRTTP-LETIVSVNMIAAmpllqrlalrlpipalrkaraalt 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 197 ---PGWINFRELLRAASPEH----NCVRTRSGDSVAIYFTSGTTGAPK--MVEHSQSSYGLgfvAGGRRWM-ALTESDif 266
Cdd:PRK05605 188 gpaPGTVPWETLVDAAIGGDgsdvSHPRPTPDDVALILYTSGTTGKPKgaQLTHRNLFANA---AQGKAWVpGLGDGP-- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 267 wnttDTgwVKAAWTLFSAW----------SNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE------D 330
Cdd:PRK05605 263 ----ER--VLAALPMFHAYgltlcltlavSIGGELVL--LPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 331 LTRykfqcLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEE--G 407
Cdd:PRK05605 335 LSG-----VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSpIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEdpD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 408 NVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVE 487
Cdd:PRK05605 410 ETMPDGEEGELLVR-GPQV----FKGYWNRPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 488 SALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEAltreLQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:PRK05605 485 EVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPG-AALDPEG----LRAYCREHLTRYKVPRRFYHVDELPRDQLGKVR 559
|
....*
gi 26341010 568 RSKLR 572
Cdd:PRK05605 560 RREVR 564
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
43-571 |
6.99e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 219.53 E-value: 6.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 43 LGRQPVPEYfnfahdvLDVWSQLektghRPPNPAFWWVngsGTEVkwTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLP 122
Cdd:PRK06178 30 HGERPLTEY-------LRAWARE-----RPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 123 RLPDWWLISVACMRTGVVMIPgVSQLT-AKDLKYRLQAARAKSIVTSDALAPQVDAISADC-----------------PS 184
Cdd:PRK06178 92 NCPQFHIVFFGILKLGAVHVP-VSPLFrEHELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaePT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 185 LQTKLLVSDTSR--PGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQ-------SSYGLGFVAGGR 255
Cdd:PRK06178 171 LPLPDSLRAPRLaaAGAIDLLPALRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQrdmvytaAAAYAVAVVGGE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 256 RWMALTESDIFW-NTTDTGwvkaawTLFSAWSNGACIFvheLPRVDAKTILNTLCRFPIT-TLCCVPTLFRLLVQEDLTR 333
Cdd:PRK06178 251 DSVFLSFLPEFWiAGENFG------LLFPLFSGATLVL---LARWDAVAFMAAVERYRVTrTVMLVDNAVELMDHPRFAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 334 YKFQCLRH--CLTGGEALNPDVRDKWKSQTGLELHEG-YGQSETvvicgNSRNsTIKSGS-------------MGKASPP 397
Cdd:PRK06178 322 YDLSSLRQvrVVSFVKKLNPDYRQRWRALTGSVLAEAaWGMTET-----HTCD-TFTAGFqdddfdllsqpvfVGLPVPG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 398 YDVQIVDEE-GNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINS 476
Cdd:PRK06178 396 TEFKICDFEtGELLPLGAEGEIVVR-TPS----LLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 477 SSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPrKVAFIS 556
Cdd:PRK06178 471 NGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPG-ADLTAAALQAWCRENM----AVYKVP-EIRIVD 544
|
570
....*....|....*
gi 26341010 557 ELPKTVSGKILRSKL 571
Cdd:PRK06178 545 ALPMTATGKVRKQDL 559
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
88-573 |
1.76e-62 |
|
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: 212.15 E-value: 1.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYrlqaaraksiVT 167
Cdd:cd05941 11 SITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEY----------VI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SDAlapqvdaisadCPSLqtkllvsdtsrpgwinfreLLRAAspehncvrtrsgdsvAIYFTSGTTGAPKMVEHSQSSyg 247
Cdd:cd05941 81 TDS-----------EPSL-------------------VLDPA---------------LILYTSGTTGRPKGVVLTHAN-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 248 LGFVAggrrwMALTESdifWNTTDT-------------GWVKAawTLFSAWSNGACIFvheLPRVDAKTILNTLCRFPIT 314
Cdd:cd05941 114 LAANV-----RALVDA---WRWTEDdvllhvlplhhvhGLVNA--LLCPLFAGASVEF---LPKFDPKEVAISRLMPSIT 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 315 TLCCVPTLFRLLVQ---------EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNST 385
Cdd:cd05941 181 VFMGVPTIYTRLLQyyeahftdpQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALSNPLDGE 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 386 IKSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGY 463
Cdd:cd05941 261 RRPGTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEYWNKPEATKEEFTDDgWFKTGDLGVVDEDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 464 FWFLGR-NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEaltrELQEHVKTV 542
Cdd:cd05941 336 YWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLE----ELKEWAKQR 411
|
490 500 510
....*....|....*....|....*....|.
gi 26341010 543 TAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd05941 412 LAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
89-574 |
1.93e-62 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 213.97 E-value: 1.93e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 89 WTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:PRK07514 29 YTYGDLDAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DALAPQVDAISADCPSLQTKLLvsDTSRPGwiNFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPK--MVEHSQ-SS 245
Cdd:PRK07514 108 PANFAWLSKIAAAAGAPHVETL--DADGTG--SLLEAAAAAPDDFETVPRGADDLAAILYTSGTTGRSKgaMLSHGNlLS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 246 YGL------GFVAGGRRWMALTesdIFwnTTDTGWVKAAWTLFSAwsnGACIFvheLPRVDAKTILNTLCRfpITTLCCV 319
Cdd:PRK07514 184 NALtlvdywRFTPDDVLIHALP---IF--HTHGLFVATNVALLAG---ASMIF---LPKFDPDAVLALMPR--ATVMMGV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 320 PTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPY 398
Cdd:PRK07514 251 PTFYtRLLQEPRLTREAAAHMRLFISGSAPLLAETHREFQERTGHAILERYGMTETNMNTSNPYDGERRAGTVGFPLPGV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 399 DVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINS 476
Cdd:PRK07514 331 SLRVTDpETGAELPPGEIGMIEVK-GPN----VFKGYWRMPEKTAEEFRADgFFITGDLGKIDERGYVHIVGRGKDLIIS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 477 SSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFIS 556
Cdd:PRK07514 406 GGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL----ARFKQPKRVFFVD 480
|
490
....*....|....*...
gi 26341010 557 ELPKTVSGKILRSKLRNQ 574
Cdd:PRK07514 481 ELPRNTMGKVQKNLLREQ 498
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
60-572 |
5.43e-62 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 213.01 E-value: 5.43e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 60 DVWSQL-EKTGHrppNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTG 138
Cdd:PRK08008 11 QMWDDLaDVYGH---KTALIFESSGGVVRRYSYLELNEEINRTANLFYS-LGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 139 VVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRP---GWINFRELLRAASPEHNC 215
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALPaddGVSSFTQLKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 216 VRTRSGDSVA-IYFTSGTTGAPKMVEHSQssYGLGFVAGGRRWM-ALTESDIFWNTTDTGWV----KAAWTLFSAwsnGA 289
Cdd:PRK08008 167 APPLSTDDTAeILFTSGTTSRPKGVVITH--YNLRFAGYYSAWQcALRDDDVYLTVMPAFHIdcqcTAAMAAFSA---GA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 290 CIFVHElpRVDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTggeALNPDVRDK--WKSQTGLELH 366
Cdd:PRK08008 242 TFVLLE--KYSARAFWGQVCKYRATITECIPMMIRtLMVQPPSANDRQHCLREVMF---YLNLSDQEKdaFEERFGVRLL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 367 EGYGQSETVV-ICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRpfCFFNCYLDNPEKTAASE 445
Cdd:PRK08008 317 TSYGMTETIVgIIGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGK--TIFKEYYLDPKATAKVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 446 QGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyA 524
Cdd:PRK08008 395 EADGWLhTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEG-E 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 26341010 525 SHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK08008 474 TLSEEEFFAFCEQNM----AKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
83-573 |
2.26e-61 |
|
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: 210.63 E-value: 2.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 83 SGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARA 162
Cdd:cd05926 9 PGSTPALTYADLAELVDDLARQLAAL-GIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 163 KSIVT-SDALAPQVDAISADCPSLQTklLVSDTSRPGWINFRELLRAASPEHNCVRT----RSGDSVAIYFTSGTTGAPK 237
Cdd:cd05926 88 KLVLTpKGELGPASRAASKLGLAILE--LALDVGVLIRAPSAESLSNLLADKKNAKSegvpLPDDLALILHTSGTTGRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 238 MV-----------EHSQSSYglgfvaggrrwmALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACIFVHelPRVDAKTIL 305
Cdd:cd05926 166 GVplthrnlaasaTNITNTY------------KLTPDDRTLVVMPLFHVHGlVASLLSTLAAGGSVVLP--PRFSASTFW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 306 NTLCRFPITTLCCVPTLFRLLVQ--EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV--VICGNS 381
Cdd:cd05926 232 PDVRDYNATWYTAVPTIHQILLNrpEPNPESPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMTSNPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 382 RNSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAVRIKptrpfcffNC---YLDNPEKTAAS-EQGDFYITGDRAH 457
Cdd:cd05926 312 PPGPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLRGP--------NVtrgYLNNPEANAEAaFKDGWFRTGDLGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 458 MDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYashdpEALTRELQE 537
Cdd:cd05926 383 LDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGA-----SVTEEELRA 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 26341010 538 HVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd05926 458 FCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
86-574 |
2.02e-59 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 206.92 E-value: 2.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEgVCGLQPGDRMMLVL---PRLPDWWLisvACMRTGVVMIPGVSQLTAKDLKYRLQAARA 162
Cdd:PRK06155 44 GTRWTYAEAARAAAAAAHALA-AAGVKRGDRVALMCgnrIEFLDVFL---GCAWLGAIAVPINTALRGPQLEHILRNSGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 163 KSIVTSDALAPQVDAISADCPSLQTKLLV----SDTSRPGWiNFRELLRAASPEhNCVRTRSGDSVAIYFTSGTTGAPKM 238
Cdd:PRK06155 120 RLLVVEAALLAALEAADPGDLPLPAVWLLdapaSVSVPAGW-STAPLPPLDAPA-PAAAVQPGDTAAILYTSGTTGPSKG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 239 V--EHSQSsYGLGFVAGgrRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVheLPRVDAKTILNTLCRFPIT-T 315
Cdd:PRK06155 198 VccPHAQF-YWWGRNSA--EDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL--EPRFSASGFWPAVRRHGATvT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 316 LCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEAlnPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTiKSGSMGKAS 395
Cdd:PRK06155 273 YLLGAMVSILLSQPARESDRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPGSMGRLA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 396 PPYDVQIVDEEGNVLPPGKEGNIAVRIKPtrPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVIN 475
Cdd:PRK06155 350 PGFEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDRIKDAIR 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 476 SSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAShDPEALTRelqeHVKTVTAPYKYPRKVAFI 555
Cdd:PRK06155 428 RRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTAL-EPVALVR----HCEPRLAYFAVPRYVEFV 502
|
490
....*....|....*....
gi 26341010 556 SELPKTVSGKILRSKLRNQ 574
Cdd:PRK06155 503 AALPKTENGKVQKFVLREQ 521
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
88-571 |
2.78e-59 |
|
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: 203.91 E-value: 2.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWwLISV-ACMRTGVVMIPgvsqLtakDLKYrlQAARAKSIV 166
Cdd:cd05930 12 SLTYAELDARANRLARYLRER-GVGPGDLVAVLLERSLEM-VVAIlAVLKAGAAYVP----L---DPSY--PAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 167 tSDAlapqvdaisadcpslQTKLLVSDtsrpgwinfrellraaspehncvrtrsGDSVA-IYFTSGTTGAPK--MVEHSq 243
Cdd:cd05930 81 -EDS---------------GAKLVLTD---------------------------PDDLAyVIYTSGSTGKPKgvMVEHR- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 244 ssyGLG-FVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACI-FVHELPRVDAKTILNTLCRFPITTLCCVPT 321
Cdd:cd05930 117 ---GLVnLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLvVLPEEVRKDPEALADLLAEEGITVLHLTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 322 LFRLLVQEdLTRYKFQCLRHCLTGGEALNPDVRDKW-KSQTGLELHEGYGQSETVVIC---------GNSRNSTIksgsm 391
Cdd:cd05930 194 LLRLLLQE-LELAALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVDAtyyrvppddEEDGRVPI----- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 392 GKASPPYDVQIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTAAS------EQGD-FYITGDRAHM 458
Cdd:cd05930 268 GRPIPNTRVYVLDENLRPVPPGVPGELYIggaglaR-----------GYLNRPELTAERfvpnpfGPGErMYRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 459 DEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayASHDPEALTRELQEH 538
Cdd:cd05930 337 LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVV-----PDEGGELDEEELRAH 411
|
490 500 510
....*....|....*....|....*....|...
gi 26341010 539 VKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd05930 412 LAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
56-571 |
5.29e-58 |
|
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: 202.08 E-value: 5.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 56 HDVLDVWSqLEKTGHRPPNPAFwwVNGS-GTEVkwTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVAC 134
Cdd:cd05904 4 DLPLDSVS-FLFASAHPSRPAL--IDAAtGRAL--TYAELERRVRRLAAGLAK-RGGRKGDVVLLLSPNSIEFPVAFLAV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 135 MRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVdaisadcPSLQTKLLVSDTSRPGWINFRELLRAAsPEHN 214
Cdd:cd05904 78 LSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKL-------ASLALPVVLLDSAEFDSLSFSDLLFEA-DEAE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 215 CVRTRSG--DSVAIYFTSGTTGAPK--MVEHSqssyglGFVAGgrrwMALTESDIFWNTTDTGWVKAAWTLF-------- 282
Cdd:cd05904 150 PPVVVIKqdDVAALLYSSGTTGRSKgvMLTHR------NLIAM----VAQFVAGEGSNSDSEDVFLCVLPMFhiyglssf 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 283 --SAWSNGACIFVheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLT-RYKFQCLRHCLTGGEALNPDVRDKWKS 359
Cdd:cd05904 220 alGLLRLGATVVV--MPRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVdKYDLSSLRQIMSGAAPLGKELIEAFRA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 360 Q-TGLELHEGYGQSET---VVICGNSRNSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPtrpfCFFNCY 434
Cdd:cd05904 298 KfPNVDLGQGYGMTEStgvVAMCFAPEKDRAKYGSVGRLVPNVEAKIVDpETGESLPPNQTGELWIR-GP----SIMKGY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 435 LDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 512
Cdd:cd05904 373 LNNPEATAATidKEG-WLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEV 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 26341010 513 VKAFIVLSPayASHDPEAltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd05904 452 PMAFVVRKP--GSSLTED---EIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
90-575 |
2.22e-57 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 201.82 E-value: 2.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIpGVSQL-TAKDLKYRLQAARAKSIVTS 168
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVV-NVNPLyTPRELEHQLNDSGAKAIVIV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DALAPQVDAISADCP-----------SLQT-------------KLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSV 224
Cdd:PRK08974 129 SNFAHTLEKVVFKTPvkhviltrmgdQLSTakgtlvnfvvkyiKRLVPKYHLPDAISFRSALHKGRRMQYVKPELVPEDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 225 A-IYFTSGTTGAPK--MVEHS-------QSSYGLG-FVAGGRRWM--ALTESDIFWNTTDtgwvkaawtlfsawsngaCI 291
Cdd:PRK08974 209 AfLQYTGGTTGVAKgaMLTHRnmlanleQAKAAYGpLLHPGKELVvtALPLYHIFALTVN------------------CL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 292 FVHEL---------PRvDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQT 361
Cdd:PRK08974 271 LFIELggqnllitnPR-DIPGFVKELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERWVKLT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 362 GLELHEGYGQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEK 440
Cdd:PRK08974 350 GQYLLEGYGLTEcSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK-GPQ----VMLGYWQRPEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 441 TAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVls 520
Cdd:PRK08974 425 TDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKIFVV-- 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 26341010 521 payaSHDPeALTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK08974 503 ----KKDP-SLTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
71-574 |
3.12e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 200.77 E-value: 3.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 71 RPPNPAFWWVnGSGTevkwTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTA 150
Cdd:PRK07786 30 QPDAPALRFL-GNTT----TWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 151 KDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTS 230
Cdd:PRK07786 104 PEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 231 GTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCR 310
Cdd:PRK07786 184 GTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDVLEA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 311 FPITTLCCVPTLFRLLVQEDLTRYKFQCLRhCLTGGEALNPD--VRDKWKSQTGLELHEGYGQSE----TVVICGNsrNS 384
Cdd:PRK07786 264 EKVTGIFLVPAQWQAVCAEQQARPRDLALR-VLSWGAAPASDtlLRQMAATFPEAQILAAFGQTEmspvTCMLLGE--DA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 385 TIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYF 464
Cdd:PRK07786 341 IRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEATAEAFAGGWFHSGDLVRQDEEGYV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 465 WFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVktvtA 544
Cdd:PRK07786 416 WVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRL----A 491
|
490 500 510
....*....|....*....|....*....|
gi 26341010 545 PYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK07786 492 RYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
90-573 |
9.13e-57 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 199.86 E-value: 9.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIpGVSQL-TAKDLKYRLQAARAKSIVTS 168
Cdd:PRK07059 50 TYGELDELSRALAAWLQSR-GLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVV-NVNPLyTPRELEHQLKDSGAEAIVVL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DALAPQVDAISADCP-------SL----------------QTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVA 225
Cdd:PRK07059 128 ENFATTVQQVLAKTAvkhvvvaSMgdllgfkghivnfvvrRVKKMVPAWSLPGHVRFNDALAEGARQTFKPVKLGPDDVA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 226 -IYFTSGTTGAPK--MVEHSQSsygLGFVAGGRRWM-----------------ALTESDIFwnttdtgwvkaAWTL--FS 283
Cdd:PRK07059 208 fLQYTGGTTGVSKgaTLLHRNI---VANVLQMEAWLqpafekkprpdqlnfvcALPLYHIF-----------ALTVcgLL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 284 AWSNGACIFVHELPRvDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTG 362
Cdd:PRK07059 274 GMRTGGRNILIPNPR-DIPGFIKELKKYQVHIFPAVNTLYNaLLNNPDFDKLDFSKLIVANGGGMAVQRPVAERWLEMTG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 363 LELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPfcffnCYLDNPEKT 441
Cdd:PRK07059 353 CPITEGYGLSETSpVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMA-----GYWNRPDET 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 442 AASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVls 520
Cdd:PRK07059 428 AKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-- 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 26341010 521 payaSHDPeALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PRK07059 506 ----KKDP-ALTEEdVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELRD 554
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
90-572 |
2.69e-56 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 197.54 E-value: 2.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDA-GLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDAISADCPslqtkLLVSDTSR-PGWINFRELLRAASP---EHNCvrtrsgdSVAIYFTSGTTGAPKMV-----E 240
Cdd:PRK13390 105 ALDGLAAKVGADLP-----LRLSFGGEiDGFGSFEAALAGAGPrltEQPC-------GAVMLYSSGTTGFPKGIqpdlpG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 241 HSQSSYGLGFVAGGRRWMALTESDIFWNTTdtgwvkaawTLFSAWSNGACIFVHEL-------PRVDAKTILNTLCRFPI 313
Cdd:PRK13390 173 RDVDAPGDPIVAIARAFYDISESDIYYSSA---------PIYHAAPLRWCSMVHALggtvvlaKRFDAQATLGHVERYRI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 314 TTLCCVPTLF-RLLVQED--LTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE----TVVicgNSRNSTI 386
Cdd:PRK13390 244 TVTQMVPTMFvRLLKLDAdvRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEahgmTFI---DSPDWLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 387 KSGSMGKaSPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTRPFCffncYLDNPEKTAASEQ--GDFYIT-GDRAHMDEDGY 463
Cdd:PRK13390 321 HPGSVGR-SVLGDLHICDDDGNELPAGRIGTVYFE-RDRLPFR----YLNDPEKTAAAQHpaHPFWTTvGDLGSVDEDGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 464 FWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayASHDP-EALTRELQEHVKTV 542
Cdd:PRK13390 395 LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLV---EGIRGsDELARELIDYTRSR 471
|
490 500 510
....*....|....*....|....*....|
gi 26341010 543 TAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK13390 472 IAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
50-573 |
7.62e-56 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 197.41 E-value: 7.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 50 EYFNFAHDVLDvwSQLEKTGHRPPNPAFwwvngsGTEVkwTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWL 129
Cdd:PRK08751 22 EQFRTVAEVFA--TSVAKFADRPAYHSF------GKTI--TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 130 ISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQT---------------------- 187
Cdd:PRK08751 92 ATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVIADTPVKQVittglgdmlgfpkaalvnfvvk 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 188 --KLLVSDTSRPGWINFRELLrAASPEHNC--VRTRSGDSVAIYFTSGTTGAPK--MVEHsqssyglgfvaggRRWMALT 261
Cdd:PRK08751 172 yvKKLVPEYRINGAIRFREAL-ALGRKHSMptLQIEPDDIAFLQYTGGTTGVAKgaMLTH-------------RNLVANM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 262 ESDIFWNTTdTGWVKAA----------WTLFSAWSN-------GACIFVHELPRvDAKTILNTLCRFPITTLCCVPTLFR 324
Cdd:PRK08751 238 QQAHQWLAG-TGKLEEGcevvitalplYHIFALTANglvfmkiGGCNHLISNPR-DMPGFVKELKKTRFTAFTGVNTLFN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 325 -LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQI 402
Cdd:PRK08751 316 gLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 403 VDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRI 481
Cdd:PRK08751 396 KDDAGTVLAIGEIGELCIK-GPQ----VMKGYWKRPEETAKVMDADGWLhTGDIARMDEQGFVYIVDRKKDMILVSGFNV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 482 GPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayaSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKT 561
Cdd:PRK08751 471 YPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------KKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKT 544
|
570
....*....|..
gi 26341010 562 VSGKILRSKLRN 573
Cdd:PRK08751 545 NVGKILRRELRD 556
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
71-578 |
1.35e-54 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 192.98 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 71 RPPNPAFWwVNGSGTEVkwTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTA 150
Cdd:PRK13391 10 TPDKPAVI-MASTGEVV--TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 151 KDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLV-SDTSRPGWINFRELLrAASPEHNCVRTRSGDsvAIYFT 229
Cdd:PRK13391 86 AEAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAV-AGLPATPIADESLGT--DMLYS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 230 SGTTGAPKMVE----HSQSSYGLGFVAGGRRWMALTESDIF------WNTTDTGWVKaawtlfSAWSNGACIFVHElpRV 299
Cdd:PRK13391 163 SGTTGRPKGIKrplpEQPPDTPLPLTAFLQRLWGFRSDMVYlspaplYHSAPQRAVM------LVIRLGGTVIVME--HF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 300 DAKTILNTLCRFPITTLCCVPTLF-RLLV--QEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVV 376
Cdd:PRK13391 235 DAEQYLALIEEYGVTHTQLVPTMFsRMLKlpEEVRDKYDLSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 377 ICG-NSRNSTIKSGSMGKASPPyDVQIVDEEGNVLPPGKEGNIAvrIKPTRPFCFFNcyldNPEKTAAS--EQGDFYITG 453
Cdd:PRK13391 315 FTAcDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIW--FEGGRPFEYLN----DPAKTAEArhPDGTWSTVG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 454 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSPAYASHDPEALTR 533
Cdd:PRK13391 388 DIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKA--VVQPVDGVDPGPALAA 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 26341010 534 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 578
Cdd:PRK13391 466 ELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYWGN 510
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
53-568 |
1.34e-53 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 192.86 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 53 NFAHDVLDVWsqLEKtghRPPNPAFWWVNG-SGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLIS 131
Cdd:PRK10524 53 NLCHNAVDRH--LAK---RPEQLALIAVSTeTDEERTYTFRQLHDEVNRMAAMLRSL-GVQRGDRVLIYMPMIAEAAFAM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 132 VACMRTGV---VMIPGvsqLTAKDLKYRLQAARAKSIVTSDALA---------PQVDAISADCPSLQTKLLVSD------ 193
Cdd:PRK10524 127 LACARIGAihsVVFGG---FASHSLAARIDDAKPVLIVSADAGSrggkvvpykPLLDEAIALAQHKPRHVLLVDrglapm 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 194 TSRPGwinfREL----LRAASPEHN--CVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFW 267
Cdd:PRK10524 204 ARVAG----RDVdyatLRAQHLGARvpVEWLESNEPSYILYTSGTTGKPKGVQRDTGGYAVALATSMDTIFGGKAGETFF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 268 NTTDTGWVKA-AWTLFSAWSNGACIFVHE-LP-RVDAkTILNTLC-RFPITTLCCVPTLFRLLVQED---LTRYKFQCLR 340
Cdd:PRK10524 280 CASDIGWVVGhSYIVYAPLLAGMATIMYEgLPtRPDA-GIWWRIVeKYKVNRMFSAPTAIRVLKKQDpalLRKHDLSSLR 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 341 HCLTGGEALN-PDVRdkWKSQT-GLELHEGYGQSET----VVICGNSRNSTIKSGSMGKASPPYDVQIVDEE-GNVLPPG 413
Cdd:PRK10524 359 ALFLAGEPLDePTAS--WISEAlGVPVIDNYWQTETgwpiLAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPN 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 414 KEGNIAVRiKPTRPFC----------FFNCYLdnpekTAASEQgdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGP 483
Cdd:PRK10524 437 EKGVLVIE-GPLPPGCmqtvwgdddrFVKTYW-----SLFGRQ--VYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGT 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 484 VEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPE---ALTRELQEHVKTVTAPYKYPRKVAFISELPK 560
Cdd:PRK10524 509 REIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADREarlALEKEIMALVDSQLGAVARPARVWFVSALPK 588
|
....*...
gi 26341010 561 TVSGKILR 568
Cdd:PRK10524 589 TRSGKLLR 596
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
91-576 |
1.38e-53 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 190.29 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 91 FEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT-SD 169
Cdd:PRK12406 14 FDELAQRAARAAGGLAAL-GVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAhAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDAISADC--------PSLQTKLLVSD---TSRPGWINFRELLrAASPEHNCVRTRSGDSVaIYfTSGTTGAPKM 238
Cdd:PRK12406 93 LLHGLASALPAGVtvlsvptpPEIAAAYRISPallTPPAGAIDWEGWL-AQQEPYDGPPVPQPQSM-IY-TSGTTGHPKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 239 V-------EHSQS-----SYGLGFVAGGRrwmALTESDIFWNTTDtgwvkaAWTLFSAWSNGACIFvheLPRVDAKTILN 306
Cdd:PRK12406 170 VrraaptpEQAAAaeqmrALIYGLKPGIR---ALLTGPLYHSAPN------AYGLRAGRLGGVLVL---QPRFDPEELLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 307 TLCRFPITTLCCVPTLF-RLLVQEDLTRYKF--QCLRHCLTGGEALNPDVR----DKWksqtGLELHEGYGQSET-VVIC 378
Cdd:PRK12406 238 LIERHRITHMHMVPTMFiRLLKLPEEVRAKYdvSSLRHVIHAAAPCPADVKramiEWW----GPVIYEYYGSTESgAVTF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 379 GNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFCffncYLDNPEKTAASEQGDFYITGDRAHM 458
Cdd:PRK12406 314 ATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDFT----YHNKPEKRAEIDRGGFITSGDVGYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 459 DEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEH 538
Cdd:PRK12406 390 DADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPG-ATLDEADIRAQLKAR 468
|
490 500 510
....*....|....*....|....*....|....*...
gi 26341010 539 VktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK12406 469 L----AGYKVPKHIEIMAELPREDSGKIFKRRLRDPYW 502
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-572 |
5.87e-53 |
|
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: 184.02 E-value: 5.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPK--MVEHsqssYGL---GFVAGGRrwMALTESDI----------FwnttdtGWVKAawTLFSAWS 286
Cdd:cd05917 3 DVINIQFTSGTTGSPKgaTLTH----HNIvnnGYFIGER--LGLTEQDRlcipvplfhcF------GSVLG--VLACLTH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 287 NGACIFVHelPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGL-E 364
Cdd:cd05917 69 GATMVFPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMkD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 365 LHEGYGQSETVVICGNSR-NSTI--KSGSMGKASPPYDVQIVDEEGNVLPP-GKEGNIAVRikptrPFCFFNCYLDNPEK 440
Cdd:cd05917 147 VTIAYGMTETSPVSTQTRtDDSIekRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 441 TAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 519
Cdd:cd05917 222 TAEAIDGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRL 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 26341010 520 SPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05917 302 KE-----GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
86-572 |
7.09e-53 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 189.21 E-value: 7.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 VTSDA------------LAPQV------DAISADCPSLQTKLLVSDTSRPGWINFRELLRAA---SPEHNCVRT---RSG 221
Cdd:PRK12583 122 ICADAfktsdyhamlqeLLPGLaegqpgALACERLPELRGVVSLAPAPPPGFLAWHELQARGetvSREALAERQaslDRD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPK--MVEHSQSSYGLGFVAggrRWMALTESDI------FWNTTdtGWVKAAwtlFSAWSNGACIfV 293
Cdd:PRK12583 202 DPINIQYTSGTTGFPKgaTLSHHNILNNGYFVA---ESLGLTEHDRlcvpvpLYHCF--GMVLAN---LGCMTVGACL-V 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 294 HELPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGL-ELHEGYGQ 371
Cdd:PRK12583 273 YPNEAFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMaEVQIAYGM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 372 SETV-VICGNSRNSTI--KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAvrikpTRPFCFFNCYLDNPEKTAASEQGD 448
Cdd:PRK12583 353 TETSpVSLQTTAADDLerRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMKGYWNNPEATAESIDED 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 449 FYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshd 527
Cdd:PRK12583 428 GWMhTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHA--- 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 26341010 528 peALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK12583 505 --ASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
110-572 |
5.25e-52 |
|
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: 184.57 E-value: 5.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 110 GLQPGDRMMLVLPRLPDW-WL---ISVACMRTGVVMIPGVSQLTAKDLKYrLQAARAKSIVTSDA-LAPQVDAISADCPS 184
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELsfaVAYAGGRLGLVFVPLNPTLKESVLRY-LVADAGGRIVLADAgAADRLRDALPASPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 185 LQTKLLVSdtsrpGWINFRELLRAASPEHNcvrtrsgDSVAIYFTSGTTGAPK--MVEHSQSSYGLGFVAggrRWMALTE 262
Cdd:cd05922 93 PGTVLDAD-----GIRAARASAPAHEVSHE-------DLALLLYTSGSTGSPKlvRLSHQNLLANARSIA---EYLGITA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 263 SDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTIlnTLCR-FPITTLCCVPTLFRLLVQEDLTRYKFQCLRH 341
Cdd:cd05922 158 DDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFW--EDLReHGATGLAGVPSTYAMLTRLGFDPAKLPSLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 342 CLTGGEALNPDVRDKWKSQ-TGLELHEGYGQSETvvicgnSRNSTI--------KSGSMGKASPPYDVQIVDEEGNVLPP 412
Cdd:cd05922 236 LTQAGGRLPQETIARLRELlPGAQVYVMYGQTEA------TRRMTYlpperileKPGSIGLAIPGGEFEILDDDGTPTPP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 413 GKEGNIAVRikptRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAE 492
Cdd:cd05922 310 GEPGEIVHR----GPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 493 HPAVLESAVVSSPDPIrGEVVKAFIVLSPAYashDPEALTRELQEhvktVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05922 386 IGLIIEAAAVGLPDPL-GEKLALFVTAPDKI---DPKDVLRSLAE----RLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
90-575 |
6.73e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 186.78 E-value: 6.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK06710 51 TFSVFHDKVKRFANYLQKL-GVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDAISADC----------------------PSLQTK-----LLVSDTSRPGWINFRELLRAASPEHNCvrTRSGD 222
Cdd:PRK06710 130 LVFPRVTNVQSATkiehvivtriadflpfpknllyPFVQKKqsnlvVKVSESETIHLWNSVEKEVNTGVEVPC--DPEND 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 223 SVAIYFTSGTTGAPKMVEHSQSSYgLGFVAGGRRWMaltesdifWNTTD-TGWVKAAWTLFSAWSNGACIFVHEL----- 296
Cdd:PRK06710 208 LALLQYTGGTTGFPKGVMLTHKNL-VSNTLMGVQWL--------YNCKEgEEVVLGVLPFFHVYGMTAVMNLSIMqgykm 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 297 ---PRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTR-YKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQS 372
Cdd:PRK06710 279 vliPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKeYDISSIRACISGSAPLPVEVQEKFETVTGGKLVEGYGLT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 373 ETV-VICGNSRNSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFY 450
Cdd:PRK06710 359 ESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK-GPQ----IMKGYWNKPEETAAVLQDGWL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 451 ITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayaSHDPEA 530
Cdd:PRK06710 434 HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVL-----KEGTEC 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 26341010 531 LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK06710 509 SEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
71-577 |
1.48e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 184.80 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 71 RPPNPAFWWVNGSgtevkWTFEELGKQSRKAANVLEGvCGLQPGDR-MMLVLPRlPDWWLISVACMRTGVVMIPGVSQLT 149
Cdd:PRK06188 25 YPDRPALVLGDTR-----LTYGQLADRISRYIQAFEA-LGLGTGDAvALLSLNR-PEVLMAIGAAQLAGLRRTALHPLGS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 150 AKDLKYRLQAARAKS-IVTSDALAPQVDAISADCPSLQTKLLVSDTsrPGWINFRELLRAASPEHNCVRTRSGDSVAIYF 228
Cdd:PRK06188 98 LDDHAYVLEDAGISTlIVDPAPFVERALALLARVPSLKHVLTLGPV--PDGVDLLAAAAKFGPAPLVAAALPPDIAGLAY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 229 TSGTTGAPKMVEHSQSSYGLGFVAggrrwmALTESDI-----FWNTTDTGWVKAAWTLFSAWSNGaciFVHELPRVDAKT 303
Cdd:PRK06188 176 TGGTTGKPKGVMGTHRSIATMAQI------QLAEWEWpadprFLMCTPLSHAGGAFFLPTLLRGG---TVIVLAKFDPAE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 304 ILNTLCRFPITTLCCVPT-LFRLLVQEDLTRYKFQCLRHCLTGGEALNPdVRdkwksqtgleLHEG-----------YGQ 371
Cdd:PRK06188 247 VLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSP-VR----------LAEAierfgpifaqyYGQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 372 SETV-VIC-----GNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptRPFcFFNCYLDNPEKTAASE 445
Cdd:PRK06188 316 TEAPmVITylrkrDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR----GPL-VMDGYWNRPEETAEAF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 446 QGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyAS 525
Cdd:PRK06188 391 RDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPG-AA 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 26341010 526 HDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWG 577
Cdd:PRK06188 470 VDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARYWE 517
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-573 |
2.36e-51 |
|
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: 184.37 E-value: 2.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 81 NGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRmmlvlprlpdwwlISVACMRT--------GVVMIPGV-----SQ 147
Cdd:cd12119 18 THEGEVHRYTYAEVAERARRLANALRRL-GVKPGDR-------------VATLAWNThrhlelyyAVPGMGAVlhtinPR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 148 LTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKLLVSD------TSRPGWINFRELLRAASPEHNCVRTRSG 221
Cdd:cd12119 84 LFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDdaampePAGVGVLAYEELLAAESPEYDWPDFDEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPKMVEHSQSSYGLG-FVAGGRRWMALTESDIFWNTTDTGWVkAAWTL-FSAWSNGACiFVHELPRV 299
Cdd:cd12119 164 TAAAICYTSGTTGNPKGVVYSHRSLVLHaMAALLTDGLGLSESDVVLPVVPMFHV-NAWGLpYAAAMVGAK-LVLPGPYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 300 DAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEALNPDVRDKWKsQTGLELHEGYGQSET--VV 376
Cdd:cd12119 242 DPASLAELIEREGVTFAAGVPTVWQGLLDHlEANGRDLSSLRRVVIGGSAVPRSLIEAFE-ERGVRVIHAWGMTETspLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 377 ICGNSRNSTIKSG---------SMGKASPPYDVQIVDEEGNVLP-PGKE-GNIAVR---IKPTrpfcffncYLDNPEKTA 442
Cdd:cd12119 321 TVARPPSEHSNLSedeqlalraKQGRPVPGVELRIVDDDGRELPwDGKAvGELQVRgpwVTKS--------YYKNDEESE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 443 ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPA 522
Cdd:cd12119 393 ALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEG 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 26341010 523 yASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd12119 473 -ATVTAE----ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
84-574 |
2.76e-51 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 183.52 E-value: 2.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 84 GTEVKWTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 164 SIVTSDALAPQVDAISAdcpslqtkllVSDTSRPGWINFRELLRAASPEhNCVRTRSGDSVAIYFTSGTTGAPKmvehsq 243
Cdd:PRK06839 103 VLFVEKTFQNMALSMQK----------VSYVQRVISITSLKEIEDRKID-NFVEKNESASFIICYTSGTTGKPK------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 244 ssyglGFVaggrrwmaLTESDIFWN------TTDTGWVKAAWTL-------------FSAWSNGACIFVHElpRVDAKTI 304
Cdd:PRK06839 166 -----GAV--------LTQENMFWNalnntfAIDLTMHDRSIVLlplfhiggiglfaFPTLFAGGVIIVPR--KFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 305 LNTLCRFPITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGeALNPDVRDKWKSQTGLELHEGYGQSET--VVICGNS 381
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIHQALINCsKFETTNLQSVRWFYNGG-APCPEELMREFIDRGFLFGQGFGMTETspTVFMLSE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 382 RNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDED 461
Cdd:PRK06839 310 EDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRPDATEETIQDGWLCTGDLARVDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 462 GYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshdpeALTRELQEHVKT 541
Cdd:PRK06839 385 GFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSV-----LIEKDVIEHCRL 459
|
490 500 510
....*....|....*....|....*....|...
gi 26341010 542 VTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK06839 460 FLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
75-575 |
3.51e-51 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 184.58 E-value: 3.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 75 PAFwwvngSGTEVKWTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLK 154
Cdd:PRK05677 41 PAF-----SNLGKTLTYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 155 YRLQAARAKSIVTSDALAPQVDAI-------------SADCPSLQTKLLVSDTSR-----------PGWINFRELL-RAA 209
Cdd:PRK05677 116 HQFNDSGAKALVCLANMAHLAEKVlpktgvkhvivteVADMLPPLKRLLINAVVKhvkkmvpayhlPQAVKFNDALaKGA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 210 SPEHNCVRTRSGDSVAIYFTSGTTGAPK--MVEHSQssyglgFVAGGRRWMALTESDIfwnttDTGW--VKAAWTLFSAW 285
Cdd:PRK05677 196 GQPVTEANPQADDVAVLQYTGGTTGVAKgaMLTHRN------LVANMLQCRALMGSNL-----NEGCeiLIAPLPLYHIY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 286 S-NGACIFV-----HEL----PRvDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVR 354
Cdd:PRK05677 265 AfTFHCMAMmlignHNIlisnPR-DLPAMVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 355 DKWKSQTGLELHEGYGQSETV-VICGNSRNStIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNC 433
Cdd:PRK05677 344 ERWKEVTGCAICEGYGMTETSpVVSVNPSQA-IQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GPQ----VMKG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 434 YLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 512
Cdd:PRK05677 418 YWQRPEATDEILDSDGWLkTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEA 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26341010 513 VKAFIVLSPAyashdpEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK05677 498 IKVFVVVKPG------ETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEE 555
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
87-572 |
1.28e-50 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 184.39 E-value: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 87 VKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMiPGVSQLTAKDLKYRLQAARAKSIV 166
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSL-GVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 167 TsdaLAPQ--------VDAISADCPSLQTKLLVsDTSR--PGW----------------INF-RELLRAASPEHNCVRTR 219
Cdd:PRK07529 135 T---LGPFpgtdiwqkVAEVLAALPELRTVVEV-DLARylPGPkrlavplirrkahariLDFdAELARQPGDRLFSGRPI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 220 SGDSVAIYF-TSGTTGAPKMVEHSQSsyglGFVAGGrrWMAltESDIFWNTTDTgwVKAAWTLF----------SAWSNG 288
Cdd:PRK07529 211 GPDDVAAYFhTGGTTGMPKLAQHTHG----NEVANA--WLG--ALLLGLGPGDT--VFCGLPLFhvnallvtglAPLARG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 289 AcifvHEL---------PRVdAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKS 359
Cdd:PRK07529 281 A----HVVlatpqgyrgPGV-IANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 360 QTGLELHEGYGQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQIV--DEEGNVL---PPGKEGNIAVRiKPTrpfcFFNC 433
Cdd:PRK07529 356 ATGVRIVEGYGLTEaTCVSSVNPPDGERRIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GPN----VFSG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 434 YLdNPEKTAASE-QGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 512
Cdd:PRK07529 431 YL-EAAHNKGLWlEDGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGEL 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26341010 513 VKAFIVLSPAyASHDPEaltrELQEHVKTVTA-PYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK07529 510 PVAYVQLKPG-ASATEA----ELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPALR 565
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
86-565 |
3.72e-50 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 181.24 E-value: 3.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 VTSDALAPQVDAISADCPSLQTKLLVSDTS----RPGWINFRELLRAASPEHNcVRTRSGDSVAIYFTSGTTGAPK--MV 239
Cdd:PRK07798 105 VYEREFAPRVAEVLPRLPKLRTLVVVEDGSgndlLPGAVDYEDALAAGSPERD-FGERSPDDLYLLYTGGTTGMPKgvMW 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 240 EHSQSSYGLGfvaGGRRWM----ALTESDIFWNTTDTG---WVKAA--------WTLFSAWSNGACIFVHELPRVDAKTI 304
Cdd:PRK07798 184 RQEDIFRVLL---GGRDFAtgepIEDEEELAKRAAAGPgmrRFPAPplmhgagqWAAFAALFSGQTVVLLPDVRFDADEV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 305 LNTLCRFPITTLCCVPTLF-RLLVQE--DLTRYKFQCLRHCLTGGEALNPDVRDKWKSQ-TGLELHEGYGQSETvvicGN 380
Cdd:PRK07798 261 WRTIEREKVNVITIVGDAMaRPLLDAleARGPYDLSSLFAIASGGALFSPSVKEALLELlPNVVLTDSIGSSET----GF 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 381 SRNSTIKSGSMGKASPPY----DVQIVDEEGNVLPPG--------KEGNIAVRikptrpfcffncYLDNPEKTAAS---E 445
Cdd:PRK07798 337 GGSGTVAKGAVHTGGPRFtigpRTVVLDEDGNPVEPGsgeigwiaRRGHIPLG------------YYKDPEKTAETfptI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 446 QGDFY-ITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyA 524
Cdd:PRK07798 405 DGVRYaIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-A 483
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 26341010 525 SHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 565
Cdd:PRK07798 484 RPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGK 520
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
88-573 |
7.05e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 179.39 E-value: 7.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAAL-GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SDALApqvDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASpehncvrtrsgdsvaIYFTSGTTGAPKMVehsQSSYG 247
Cdd:PRK03640 106 DDDFE---AKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVAT---------------IMYTSGTTGKPKGV---IQTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 248 LGFvaggrrWMA--------LTESDifwnttdtGWVkAAWTLF--SAWS-------NGACIFVHElpRVDAKTILNTLCR 310
Cdd:PRK03640 165 NHW------WSAvgsalnlgLTEDD--------CWL-AAVPIFhiSGLSilmrsviYGMRVVLVE--KFDAEKINKLLQT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 311 FPITTLCCVPT-LFRLLVQEDLTRY--KFQCLrhcLTGGEALNPDVRDKWKsQTGLELHEGYGQSETV--VICGNSRNST 385
Cdd:PRK03640 228 GGVTIISVVSTmLQRLLERLGEGTYpsSFRCM---LLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETAsqIVTLSPEDAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 386 IKSGSMGKASPPYDVQIVDEeGNVLPPGKEGNIAVR---IKPTrpfcffncYLDNPEKTAASEQGDFYITGDRAHMDEDG 462
Cdd:PRK03640 304 TKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKgpnVTKG--------YLNREDATRETFQDGWFKTGDIGYLDEEG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 463 YFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayaSHDPEAltrELQEHVKTV 542
Cdd:PRK03640 375 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKS----GEVTEE---ELRHFCEEK 447
|
490 500 510
....*....|....*....|....*....|.
gi 26341010 543 TAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PRK03640 448 LAKYKVPKRFYFVEELPRNASGKLLRHELKQ 478
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
56-574 |
1.04e-49 |
|
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: 179.96 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 56 HDVLDVWSQlektgHRPPNPAFwwVNGsgtEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACM 135
Cdd:COG1021 28 GDLLRRRAE-----RHPDRIAV--VDG---ERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 136 RTGVvmIPgVSQLTA---KDLKYRLQAARAKSIVTSD-----ALAPQVDAISADCPSLQTKLLVSDTSrpGWINFRELLr 207
Cdd:COG1021 97 RAGA--IP-VFALPAhrrAEISHFAEQSEAVAYIIPDrhrgfDYRALARELQAEVPSLRHVLVVGDAG--EFTSLDALL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 208 aASPEHNCVRTRSGDSVAIYFTS-GTTGAPKMVEHSQSSYGLGFVAGGRRWmALTESDIFWnttdtgwvkAA-------- 278
Cdd:COG1021 171 -AAPADLSEPRPDPDDVAFFQLSgGTTGLPKLIPRTHDDYLYSVRASAEIC-GLDADTVYL---------AAlpaahnfp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 279 ---WTLFSAWSNGACIFVHELPRVDAktilntlCrFP------ITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEA 348
Cdd:COG1021 240 lssPGVLGVLYAGGTVVLAPDPSPDT-------A-FPliererVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 349 LNPDVRDKWKSQTGLELHEGYGQSETVVIC---GNSRNSTIksGSMGKASPPYD-VQIVDEEGNVLPPGKEGNIAVRIKP 424
Cdd:COG1021 312 LSPELARRVRPALGCTLQQVFGMAEGLVNYtrlDDPEEVIL--TTQGRPISPDDeVRIVDEDGNPVPPGEVGELLTRGPY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 425 TrpfcfFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 502
Cdd:COG1021 390 T-----IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVV 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26341010 503 SSPDPIRGEVVKAFIVLspayashDPEALT-RELQEHVKTV-TAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:COG1021 464 AMPDEYLGERSCAFVVP-------RGEPLTlAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
84-571 |
1.31e-49 |
|
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: 179.01 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:cd17646 19 DEGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 164 SIVTSDALAPQVDAISADCPSLQTKLLVSDTSRPGwinfrellraaspehncVRTRSGDSVAIYFTSGTTGAPK--MVEH 241
Cdd:cd17646 98 VVLTTADLAARLPAGGDVALLGDEALAAPPATPPL-----------------VPPRPDNLAYVIYTSGSTGRPKgvMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 242 SQssyglgfVAGGRRWM----ALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHElP--RVDAKTILNTLCRFPITT 315
Cdd:cd17646 161 AG-------IVNRLLWMqdeyPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVAR-PggHRDPAYLAALIREHGVTT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 316 LCCVPTLFRLLVQEdLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVV------ICGNSRNSTIksg 389
Cdd:cd17646 233 CHFVPSMLRVFLAE-PAAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdvthwpVRGPAETPSV--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 390 SMGKASPPYDVQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTAAS------EQGD-FYITGDRAHMDED 461
Cdd:cd17646 309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGgVQLARG------YLGRPALTAERfvpdpfGPGSrMYRTGDLARWRPD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 462 GYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVkt 541
Cdd:cd17646 383 GALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAALRAHLAERL-- 460
|
490 500 510
....*....|....*....|....*....|
gi 26341010 542 vtAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17646 461 --PEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
90-502 |
6.41e-49 |
|
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: 175.15 E-value: 6.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPdwWLI--SVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSA--ELVvaILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SDALAPQVD--AISADCPSLQTKLLVSDtsrpgwinfrellrAASPEHNCVRTRSGDSVAIYFTSGTTGAPK--MVEHSQ 243
Cdd:TIGR01733 79 DSALASRLAglVLPVILLDPLELAALDD--------------APAPPPPDAPSGPDDLAYVIYTSGSTGRPKgvVVTHRS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 244 SSYglgFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVheLPRVDAKTILNTLCRF----PITTLCCV 319
Cdd:TIGR01733 145 LVN---LLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVV--PPEDEERDDAALLAALiaehPVTVLNLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 320 PTLFRLLVQEDLTRykFQCLRHCLTGGEALNPDVRDKWKSQTG-LELHEGYGQSETVVICGNSR-----NSTIKSGSMGK 393
Cdd:TIGR01733 220 PSLLALLAAALPPA--LASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLvdpddAPRESPVPIGR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 394 ASPPYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAA---------SEQGDFYITGDRAHMDEDGYF 464
Cdd:TIGR01733 298 PLANTRLYVLDDDLRPVPVGVVGELYIGGP-----GVARGYLNRPELTAErfvpdpfagGDGARLYRTGDLVRYLPDGNL 372
|
410 420 430
....*....|....*....|....*....|....*...
gi 26341010 465 WFLGRNDDVINSSSYRIGPVEVESALAEHPAVlESAVV 502
Cdd:TIGR01733 373 EFLGRIDDQVKIRGYRIELGEIEAALLRHPGV-REAVV 409
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
65-572 |
2.12e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 176.39 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 65 LEKTGHRPPN-PAFWWvngsGTEVkWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIP 143
Cdd:PRK07470 13 LRQAARRFPDrIALVW----GDRS-WTWREIDARVDALAAALAAR-GVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 144 GVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLqtKLLVSDTSRPGWINFRELLRA-ASPEHNCVRTRSGD 222
Cdd:PRK07470 87 TNFRQTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDL--THVVAIGGARAGLDYEALVARhLGARVANAAVDHDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 223 SVAIYFTSGTTGAPK--MVEHSQssygLGFVAGGRRwmalteSDIFWNTT--DTGWVKAAWtlfsawSNGACIfvHELPR 298
Cdd:PRK07470 165 PCWFFFTSGTTGRPKaaVLTHGQ----MAFVITNHL------ADLMPGTTeqDASLVVAPL------SHGAGI--HQLCQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 299 V--DAKTILNTLCRFPI------------TTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEalnPDVRDKWK---SQ 360
Cdd:PRK07470 227 VarGAATVLLPSERFDPaevwalverhrvTNLFTVPTILKMLVEhPAVDRYDHSSLRYVIYAGA---PMYRADQKralAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 361 TGLELHEGYGQSE-----TVV-ICGNSRNS--TIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTrpfcfFN 432
Cdd:PRK07470 304 LGKVLVQYFGLGEvtgniTVLpPALHDAEDgpDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAV-----FA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 433 CYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 512
Cdd:PRK07470 379 GYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEV 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 513 VKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK07470 459 GVAVCVARDG-APVDEA----ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVR 513
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
86-578 |
9.51e-48 |
|
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: 179.67 E-value: 9.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWwLISV-ACMRTGVVMIPGVSQLTAKDLKYRLQAARAKS 164
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLRA-LGVGPGDLVGVCLERSLEM-VVALlAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 165 IVTSDALAPQVdaisadcPSLQTKLLVSDTsrpgwinfreLLRAASPEHNCVRTRSGDSVA-IYFTSGTTGAPK--MVEH 241
Cdd:COG1020 577 VLTQSALAARL-------PELGVPVLALDA----------LALAAEPATNPPVPVTPDDLAyVIYTSGSTGRPKgvMVEH 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 242 SqssyGLG-FVAGGRRWMALTESDIF-WNTT---DTgwvkAAWTLFSAWSNGACI-FVHELPRVDAKTILNTLCRFPITT 315
Cdd:COG1020 640 R----ALVnLLAWMQRRYGLGPGDRVlQFASlsfDA----SVWEIFGALLSGATLvLAPPEARRDPAALAELLARHRVTV 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 316 LCCVPTLFRLLVQEDLTRykFQCLRHCLTGGEALNPDVRDKWKSQT-GLELHEGYGQSETVVicgnsrNST---IKSGSM 391
Cdd:COG1020 712 LNLTPSLLRALLDAAPEA--LPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTV------DSTyyeVTPPDA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 392 GKASPPY-------DVQIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTAA-------SEQGD-FY 450
Cdd:COG1020 784 DGGSVPIgrpiantRVYVLDAHLQPVPVGVPGELYIggaglaR-----------GYLNRPELTAErfvadpfGFPGArLY 852
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 451 ITGDRAHMDEDGYFWFLGRNDD-V-INssSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDP 528
Cdd:COG1020 853 RTGDLARWLPDGNLEFLGRADDqVkIR--GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA-----GA 925
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 26341010 529 EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEWGR 578
Cdd:COG1020 926 AAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAA 975
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
88-572 |
1.07e-47 |
|
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: 171.76 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAAraksivt 167
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAAL-GVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDS------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 sdalAPQVDAISAdcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvaIYFTSGTTGAPKMVehsQSSYG 247
Cdd:cd05912 73 ----DVKLDDIAT---------------------------------------------IMYTSGTTGKPKGV---QQTFG 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 248 LGFvaggrrWMALTESDIFWNTTDTGWVkAAWTLF--SAWS-------NGACIFVHElpRVDAKTILNTLCRFPITTLCC 318
Cdd:cd05912 101 NHW------WSAIGSALNLGLTEDDNWL-CALPLFhiSGLSilmrsviYGMTVYLVD--KFDAEQVLHLINSGKVTIISV 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 319 VPTLFRLLVQEDLTRY--KFQCLrhcLTGGEALNPDVRDKWKsQTGLELHEGYGQSETV--VICGNSRNSTIKSGSMGKA 394
Cdd:cd05912 172 VPTMLQRLLEILGEGYpnNLRCI---LLGGGPAPKPLLEQCK-EKGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 395 SPPYDVQIVDEEGnvlPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVI 474
Cdd:cd05912 248 LFPVELKIEDDGQ---PPYEVGEILLK-GPN----VTKGYLNRPDATEESFENGWFKTGDIGYLDEEGFLYVLDRRSDLI 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 475 NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayashdpEALTR-ELQEHVKTVTAPYKYPRKVA 553
Cdd:cd05912 320 ISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSE--------RPISEeELIAYCSEKLAKYKVPKKIY 391
|
490
....*....|....*....
gi 26341010 554 FISELPKTVSGKILRSKLR 572
Cdd:cd05912 392 FVDELPRTASGKLLRHELK 410
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
90-572 |
1.11e-47 |
|
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: 172.18 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRmmlVLPRLPDWW---LISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIV 166
Cdd:cd05903 3 TYSELDTRADRLAAGLAAL-GVGPGDV---VAFQLPNWWefaVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 167 TSDAlapqvdaisadcpslqtkllvsdtsrpgwinFRELLRAASPehncvrtrsGDSVAIYFTSGTTGAPKMVEHSQSSY 246
Cdd:cd05903 79 VPER-------------------------------FRQFDPAAMP---------DAVALLLFTSGTTGEPKGVMHSHNTL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 247 GLGFVAGGRRWMaLTESDIFWNTTD----TGWVKAAWT---------LFSAWSNGACIfvhELPRVDAKTILNTLCRFpI 313
Cdd:cd05903 119 SASIRQYAERLG-LGPGDVFLVASPmahqTGFVYGFTLplllgapvvLQDIWDPDKAL---ALMREHGVTFMMGATPF-L 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 314 TTLCCVPtlfrLLVQEDLTRykfqcLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRN--STIKSGSM 391
Cdd:cd05903 194 TDLLNAV----EEAGEPLSR-----LRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPapEDRRLYTD 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 392 GKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRND 471
Cdd:cd05903 265 GRPLPGVEIKVVDDTGATLAPGVEGELLSR-GPS----VFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 472 DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHvktVTAPYKYPRK 551
Cdd:cd05903 340 DIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSG-ALLTFDELVAYLDRQ---GVAKQYWPER 415
|
490 500
....*....|....*....|.
gi 26341010 552 VAFISELPKTVSGKILRSKLR 572
Cdd:cd05903 416 LVHVDDLPRTPSGKVQKFRLR 436
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
86-572 |
1.67e-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: 173.30 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd17651 18 GRRLTYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 VTSDALAPQVDAISAdcpslqtkllvsdtsrPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSS 245
Cdd:cd17651 97 LTHPALAGELAVELV----------------AVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 246 YgLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACI-FVHELPRVDAKTILNTLCRFPITtLCCVPTLFR 324
Cdd:cd17651 161 L-ANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLvLPPEEVRTDPPALAAWLDEQRIS-RVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 325 LLVQEDLTRYKFQ--CLRHCLTGGEAL--NPDVRDKWKSQTGLELHEGYGQSET-VVICGNSRNSTIKSG---SMGKASP 396
Cdd:cd17651 239 RALAEHGRPLGVRlaALRYLLTGGEQLvlTEDLREFCAGLPGLRLHNHYGPTEThVVTALSLPGDPAAWPappPIGRPID 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 397 PYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAA-------SEQGDFYITGDRAHMDEDGYFWFLGR 469
Cdd:cd17651 319 NTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAErfvpdpfVPGARMYRTGDLARWLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 470 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYP 549
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-APVDAAELRAALATHL----PEYMVP 468
|
490 500
....*....|....*....|...
gi 26341010 550 RKVAFISELPKTVSGKILRSKLR 572
Cdd:cd17651 469 SAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
90-575 |
2.22e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 173.96 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMlVLPRLPDWWLIS-VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:PRK07788 76 TYAELDEQSNALARGLLAL-GVRAGDGVA-VLARNHRGFVLAlYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DALAPQVDAISADCPSLQTKLLVSD---TSRPGWINFRELLRAASPEHNCVRTRSGDSVAIyfTSGTTGAPKMVEHSQSS 245
Cdd:PRK07788 154 DEFTDLLSALPPDLGRLRAWGGNPDddePSGSTDETLDDLIAGSSTAPLPKPPKPGGIVIL--TSGTTGTPKGAPRPEPS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 246 yGLGFVAG-------GRRWMALTESDIFWNTtdtGWvkAAWTLfsAWSNGACIFVHElpRVDAKTILNTLCRFPITTLCC 318
Cdd:PRK07788 232 -PLAPLAGllsrvpfRAGETTLLPAPMFHAT---GW--AHLTL--AMALGSTVVLRR--RFDPEATLEDIAKHKATALVV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 319 VPTLFRLLV---QEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE-TVVICGNSRNSTIKSGSMGKA 394
Cdd:PRK07788 302 VPVMLSRILdlgPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYGSTEvAFATIATPEDLAEAPGTVGRP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 395 SPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTrpfcfFNCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFLGRNDDVI 474
Cdd:PRK07788 382 PKGVTVKILDENGNEVPRGVVGRIFVGNGFP-----FEGYTDGRDKQII---DGLLSSGDVGYFDEDGLLFVDGRDDDMI 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 475 NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAF 554
Cdd:PRK07788 454 VSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPG-AALDED----AIKDYVRDNLARYKVPRDVVF 528
|
490 500
....*....|....*....|.
gi 26341010 555 ISELPKTVSGKILRSKLRNQE 575
Cdd:PRK07788 529 LDELPRNPTGKVLKRELREMD 549
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
89-578 |
1.20e-46 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 171.85 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 89 WTFEELG-KQSRKAANVLEgvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:PRK06087 50 YTYSALDhAASRLANWLLA--KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SDALA-----PQVDAISADCPSLQTKLLVsDTSRPGW--INFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPK--M 238
Cdd:PRK06087 128 PTLFKqtrpvDLILPLQNQLPQLQQIVGV-DKLAPATssLSLSQIIADYEPLTTAITTHGDELAAVLFTSGTEGLPKgvM 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 239 VEH-----SQSSYGLGfvaggrrwMALTESDIFWNTTD----TGWV---------------------KAAWTLFS----A 284
Cdd:PRK06087 207 LTHnnilaSERAYCAR--------LNLTWQDVFMMPAPlghaTGFLhgvtapfligarsvlldiftpDACLALLEqqrcT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 285 WSNGACIFVHELprvdaktilntlcrfpittLCCVptlfrllvQEDltRYKFQCLRHCLTGGEALNPD-VRDKWksQTGL 363
Cdd:PRK06087 279 CMLGATPFIYDL-------------------LNLL--------EKQ--PADLSALRFFLCGGTTIPKKvARECQ--QRGI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 364 ELHEGYGQSETV--VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptRPFCFFNcYLDNPEKT 441
Cdd:PRK06087 328 KLLSVYGSTESSphAVVNLDDPLSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASR----GPNVFMG-YLDEPELT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 442 AAS--EQGDFYiTGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVL 519
Cdd:PRK06087 403 ARAldEEGWYY-SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVL 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 26341010 520 SPAYASHDPEALTRELQEhvKTVtAPYKYPRKVAFISELPKTVSGKILRSKLRnQEWGR 578
Cdd:PRK06087 482 KAPHHSLTLEEVVAFFSR--KRV-AKYKYPEHIVVIDKLPRTASGKIQKFLLR-KDIMR 536
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
86-571 |
3.83e-46 |
|
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: 169.30 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDwwliSVACM----RTGVVMIPGVSQLTAKDLKYRLQAAR 161
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPE----LVVALlavlKAGAAYVPLDPELPAERLAFMLADAG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 162 AKSIVTSDALAPQVDAisadcpsLQTKLLVSDTSRPGwinfrellraasPEHNCVRTRSGDSVA-IYFTSGTTGAPK--M 238
Cdd:cd12117 95 AKVLLTDRSLAGRAGG-------LEVAVVIDEALDAG------------PAGNPAVPVSPDDLAyVMYTSGSTGRPKgvA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 239 VEHsqssYGLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRV-DAKTILNTLCRFPITTLC 317
Cdd:cd12117 156 VTH----RGVVRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 318 CVPTLFRLLVQEDLTRykFQCLRHCLTGGEALNPD-VRDKWKSQTGLELHEGYGQSET-------VVICGNSRNSTIksg 389
Cdd:cd12117 232 LTAALFNQLADEDPEC--FAGLRELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENttfttshVVTELDEVAGSI--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 390 SMGKASPPYDVQIVDEEGNVLPPGKEGNIavrikptrpfcffnC---------YLDNPEKTAAS-------EQGDFYITG 453
Cdd:cd12117 307 PIGRPIANTRVYVLDEDGRPVPPGVPGEL--------------YvggdglalgYLNRPALTAERfvadpfgPGERLYRTG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 454 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVsspdPIRGEVVKAFIVlspAYASHDPEALTR 533
Cdd:cd12117 373 DLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVV----VREDAGGDKRLV---AYVVAEGALDAA 445
|
490 500 510
....*....|....*....|....*....|....*...
gi 26341010 534 ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd12117 446 ELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
86-573 |
3.85e-46 |
|
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: 169.40 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKsi 165
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAK-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 vtsdalapqvdaisadcpslqtkLLVSDTSrpgwINFRELLRAASPEHNCVRTRSG-DSVAIYFTSGTTGAPKMVEHSQS 244
Cdd:cd12118 104 -----------------------VLFVDRE----FEYEDLLAEGDPDFEWIPPADEwDPIALNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 245 SYGLGFVAGGRRWMALTESDIFWNTTD---TGWVkAAWTLFSAWSNGACifvheLPRVDAKTILNTLCRFPITTLCCVPT 321
Cdd:cd12118 157 GAYLNALANILEWEMKQHPVYLWTLPMfhcNGWC-FPWTVAAVGGTNVC-----LRKVDAKAIYDLIEKHKVTHFCGAPT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 322 LFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKwKSQTGLELHEGYGQSET---VVICG-----NSRNSTIKSGSMG 392
Cdd:cd12118 231 VLNMLANaPPSDARPLPHRVHVMTAGAPPPAAVLAK-MEELGFDVTHVYGLTETygpATVCAwkpewDELPTEERARLKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 393 KASPPY----DVQIVDEEGNVLPP--GKE-GNIAVRIKPTrpfcfFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFW 465
Cdd:cd12118 310 RQGVRYvgleEVDVLDPETMKPVPrdGKTiGEIVFRGNIV-----MKGYLKNPEATAEAFRGGWFHSGDLAVIHPDGYIE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 466 FLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYashdpEALTRELQEHVKTVTAP 545
Cdd:cd12118 385 IKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGA-----KVTEEEIIAFCREHLAG 459
|
490 500
....*....|....*....|....*...
gi 26341010 546 YKYPRKVAFiSELPKTVSGKILRSKLRN 573
Cdd:cd12118 460 FMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
86-571 |
9.30e-46 |
|
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: 168.27 E-value: 9.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd05920 38 DRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 VTSDALAPqvdaisADCPSLqtkllvsdtsrpgwinFRELLRaaspehncvrtrSGDSVAIYFTS-GTTGAPKMVEHSQS 244
Cdd:cd05920 117 IVPDRHAG------FDHRAL----------------ARELAE------------SIPEVALFLLSgGTTGTPKLIPRTHN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 245 SYGLGFVAGGRrWMALTESDIFW--NTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLccVPTL 322
Cdd:cd05920 163 DYAYNVRASAE-VCGLDQDTVYLavLPAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPLIEREGVTVTAL--VPAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 323 FRLLVQE-DLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVicgnsrNST-------IKSGSMGKA 394
Cdd:cd05920 240 VSLWLDAaASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLL------NYTrlddpdeVIIHTQGRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 395 SPPYD-VQIVDEEGNVLPPGKEGNIAVRIKPTrpfcfFNCYLDNPEKTAAS--EQGdFYITGDRAHMDEDGYFWFLGRND 471
Cdd:cd05920 314 MSPDDeIRVVDEEGNPVPPGEEGELLTRGPYT-----IRGYYRAPEHNARAftPDG-FYRTGDLVRRTPDGYLVVEGRIK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 472 DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayashDPEALTRELQEHVKTV-TAPYKYPR 550
Cdd:cd05920 388 DQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR------DPPPSAAQLRRFLRERgLAAYKLPD 461
|
490 500
....*....|....*....|.
gi 26341010 551 KVAFISELPKTVSGKILRSKL 571
Cdd:cd05920 462 RIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
70-574 |
3.82e-45 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 167.54 E-value: 3.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 70 HRPPNPAFWWVN-GSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDrmmLVLPRLPDWWLISV---ACMRTGVVMIPGV 145
Cdd:PRK13295 36 SCPDKTAVTAVRlGTGAPRRFTYRELAALVDRVAVGLARL-GVGRGD---VVSCQLPNWWEFTVlylACSRIGAVLNPLM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 146 SQLTAKDLKYRLQAARAKSIVtsdalAPQ----------VDAISADCPSLQTKLLV---SDTS------RPGWinfrELL 206
Cdd:PRK13295 112 PIFRERELSFMLKHAESKVLV-----VPKtfrgfdhaamARRLRPELPALRHVVVVggdGADSfealliTPAW----EQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 207 RAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRwMALTESD-IFWNTT---DTGW-------- 274
Cdd:PRK13295 183 PDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAER-LGLGADDvILMASPmahQTGFmyglmmpv 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 275 -VKAAWTLFSAWSNGACIfvhELPRVDAKTIlntlcrfpitTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDV 353
Cdd:PRK13295 262 mLGATAVLQDIWDPARAA---ELIRTEGVTF----------TMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGAL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 354 RDKWKSQTGLELHEGYGQSET--VVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIkptrpfCF- 430
Cdd:PRK13295 329 VERARAALGAKIVSAWGMTENgaVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRG------CSn 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 431 FNCYLDNPEKTAASEQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRG 510
Cdd:PRK13295 403 FGGYLKRPQLNGTDADG-WFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLG 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26341010 511 EVVKAFIVLSPAyASHDPEALTRELQEHvkTVTAPYkYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK13295 482 ERACAFVVPRPG-QSLDFEEMVEFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
88-574 |
7.46e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 165.75 E-value: 7.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMlVLPRLPDWWLI-SVACMRTGVVMIPgvsqltakdLKYRLQAaraksiv 166
Cdd:PRK09088 22 RWTYAELDALVGRLAAVLRRR-GCVDGERLA-VLARNSVWLVAlHFACARVGAIYVP---------LNWRLSA------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 167 tsdalaPQVDAISADCpslQTKLLVSDTS----RPGWINFrELLRAASPEHNCVRTRSGDSVA---IYFTSGTTGAPKMV 239
Cdd:PRK09088 84 ------SELDALLQDA---EPRLLLGDDAvaagRTDVEDL-AAFIASADALEPADTPSIPPERvslILFTSGTSGQPKGV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 240 ---EHSQSSYGLGFVAGGR---RWMALTESDIFwnttdtGWVKAAWTLFSAWSNGACIFVHelPRVDAKTILNTLC--RF 311
Cdd:PRK09088 154 mlsERNLQQTAHNFGVLGRvdaHSSFLCDAPMF------HIIGLITSVRPVLAVGGSILVS--NGFEPKRTLGRLGdpAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 312 PITTLCCVPTLFRLL-VQEDLTRYKFQCLRHCLTGGeALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTI---K 387
Cdd:PRK09088 226 GITHYFCVPQMAQAFrAQPGFDAAALRHLTALFTGG-APHAAEDILGWLDDGIPMVDGFGMSEAGTVFGMSVDCDViraK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 388 SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWF 466
Cdd:PRK09088 305 AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDADGFFWV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 467 LGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPY 546
Cdd:PRK09088 380 VDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG-APLDLE----RIRSHLSTRLAKY 454
|
490 500
....*....|....*....|....*...
gi 26341010 547 KYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK09088 455 KVPKHLRLVDALPRTASGKLQKARLRDA 482
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
87-574 |
2.79e-44 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 165.37 E-value: 2.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 87 VKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMipgVSQLTA---KDLKYRLQAARAK 163
Cdd:PRK08315 42 LRWTYREFNEEVDALAKGLLAL-GIEKGDRVGIWAPNVPEWVLTQFATAKIGAIL---VTINPAyrlSELEYALNQSGCK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 164 SIVTSDA------------LAPQVDAI------SADCPSLQTKLLVSDTSRPGWINFRELL-RAASPEHNCVRTRSG--- 221
Cdd:PRK08315 118 ALIAADGfkdsdyvamlyeLAPELATCepgqlqSARLPELRRVIFLGDEKHPGMLNFDELLaLGRAVDDAELAARQAtld 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 --DSVAIYFTSGTTGAPK--MVEHsqssYGLG----FVAggrRWMALTESD---I-------FwnttdtGWVKAawTLfS 283
Cdd:PRK08315 198 pdDPINIQYTSGTTGFPKgaTLTH----RNILnngyFIG---EAMKLTEEDrlcIpvplyhcF------GMVLG--NL-A 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 284 AWSNGACIfVHELPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRhclTGGEALNP-------DVRD 355
Cdd:PRK08315 262 CVTHGATM-VYPGEGFDPLATLAAVEEERCTALYGVPTMFiAELDHPDFARFDLSSLR---TGIMAGSPcpievmkRVID 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 356 KwksqtgLELHE---GYGQSETV-VICGNSRNSTI--KSGSMGKASPPYDVQIVDEE-GNVLPPGKEGNIAvrikpTRPF 428
Cdd:PRK08315 338 K------MHMSEvtiAYGMTETSpVSTQTRTDDPLekRVTTVGRALPHLEVKIVDPEtGETVPRGEQGELC-----TRGY 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 429 CFFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVI-----NsssyrIGPVEVESALAEHPAVLESAVV 502
Cdd:PRK08315 407 SVMKGYWNDPEKTAEAIDADGWMhTGDLAVMDEEGYVNIVGRIKDMIirggeN-----IYPREIEEFLYTHPKIQDVQVV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26341010 503 SSPDPIRGEVVKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK08315 482 GVPDEKYGEEVCAWIILRPG-ATLTEE----DVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMREM 548
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
320-568 |
3.53e-44 |
|
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: 160.13 E-value: 3.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 320 PTLFRLLVQEDLTRYKFQCLRHcLTGGEAlnPDVRDKWKSQTGLELHEGYGQSET--VVICGNSRNstiKSGSMGKASPP 397
Cdd:cd17637 97 PILSNLLDAAEKSGVDLSSLRH-VLGLDA--PETIQRFEETTGATFWSLYGQTETsgLVTLSPYRE---RPGSAGRPGPL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 398 YDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRN--DDVIN 475
Cdd:cd17637 171 VRVRIVDDNDRPVPAGETGEIVVR-GPL----VFQGYWNLPELTAYTFRNGWHHTGDLGRFDEDGYLWYAGRKpeKELIK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 476 SSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyashdpEALT-RELQEHVKTVTAPYKYPRKVAF 554
Cdd:cd17637 246 PGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG------ATLTaDELIEFVGSRIARYKKPRYVVF 319
|
250
....*....|....
gi 26341010 555 ISELPKTVSGKILR 568
Cdd:cd17637 320 VEALPKTADGSIDR 333
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
110-574 |
3.74e-44 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 167.13 E-value: 3.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 110 GLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS----DALAPQVDAISADcpsl 185
Cdd:PRK06060 51 GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSdalrDRFQPSRVAEAAE---- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 186 qtklLVSDTSRPGWINFRELlraaspehncvrtrSGDSVAI-YFTSGTTGAPKMVEHSQSSYgLGFV-AGGRRWMALTES 263
Cdd:PRK06060 127 ----LMSEAARVAPGGYEPM--------------GGDALAYaTYTSGTTGPPKAAIHRHADP-LTFVdAMCRKALRLTPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 264 DIFWNTTDTGWvkaAWTL-FSAW---SNGACIFVHELPrVDAKTILNTLCRFPITTLCCVPTLFRLLVqEDLTRYKFQCL 339
Cdd:PRK06060 188 DTGLCSARMYF---AYGLgNSVWfplATGGSAVINSAP-VTPEAAAILSARFGPSVLYGVPNFFARVI-DSCSPDSFRSL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 340 RHCLTGGEALNPDVRDKWKSQ-TGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNI 418
Cdd:PRK06060 263 RCVVSAGEALELGLAERLMEFfGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 419 AVRiKPTrpfcFFNCYLDNPEKTAasEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLE 498
Cdd:PRK06060 343 WVR-GPA----IAKGYWNRPDSPV--ANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26341010 499 SAVVSSPDPIRGEVVKAFIVlsPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK06060 416 AAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALRKQ 489
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
90-572 |
4.80e-44 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 164.55 E-value: 4.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVCGLQPgdRMMLVLPRLPDWWLIS-VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:PRK13382 70 TWRELDERSDALAAALQALPIGEP--RVVGIMCRNHRGFVEAlLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DALAPQVDAISADCPslQTKLLVSDTSRPGWINFrELLRAA----SPEHncvRTRSGDSvaIYFTSGTTGAPKMVEHSQS 244
Cdd:PRK13382 148 EEFSATVDRALADCP--QATRIVAWTDEDHDLTV-EVLIAAhagqRPEP---TGRKGRV--ILLTSGTTGTPKGARRSGP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 245 syglgfvaGGRRWMALTESDIFWNTTDTGWVKAAwtLFSAWSNGACIFVHELP-------RVDAKTILNTLCRFPITTLC 317
Cdd:PRK13382 220 --------GGIGTLKAILDRTPWRAEEPTVIVAP--MFHAWGFSQLVLAASLActivtrrRFDPEATLDLIDRHRATGLA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 318 CVPTLFRL---LVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVIC-GNSRNSTIKSGSMGK 393
Cdd:PRK13382 290 VVPVMFDRimdLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGMIAtATPADLRAAPDTAGR 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 394 ASPPYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYldNPEKTAASEQGdFYITGDRAHMDEDGYFWFLGRNDDV 473
Cdd:PRK13382 370 PAEGTEIRILDQDFREVPTGEVGTIFVRND-----TQFDGY--TSGSTKDFHDG-FMASGDVGYLDENGRLFVVGRDDEM 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 474 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRKVA 553
Cdd:PRK13382 442 IVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKP-----GASATPETLKQHVRDNLANYKVPRDIV 516
|
490
....*....|....*....
gi 26341010 554 FISELPKTVSGKILRSKLR 572
Cdd:PRK13382 517 VLDELPRGATGKILRRELQ 535
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
70-538 |
8.02e-44 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 164.89 E-value: 8.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 70 HRPPNPAFWWVNGsGTEVKWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLT 149
Cdd:COG1022 23 RFPDRVALREKED-GIWQSLTWAEFAERVRALAAGLLA-LGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 150 AKDLKYRLQAARAKSIVTSD-ALAPQVDAISADCPSLQtKLLVSD----TSRPGWINFRELLRAASPEHN------CVRT 218
Cdd:COG1022 101 AEEVAYILNDSGAKVLFVEDqEQLDKLLEVRDELPSLR-HIVVLDprglRDDPRLLSLDELLALGREVADpaeleaRRAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 219 RSGDSVA-IYFTSGTTGAPKMVEHSQSSYgLGFVAGGRRWMALTESDIF------WnttdtgWVKA-AWTLFsAWSNGAC 290
Cdd:COG1022 180 VKPDDLAtIIYTSGTTGRPKGVMLTHRNL-LSNARALLERLPLGPGDRTlsflplA------HVFErTVSYY-ALAAGAT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 291 IFVHElprvDAKTILNTLCRFPITTLCCVPTLF-----RLLVQ-EDLTRYK---FQ------------------------ 337
Cdd:COG1022 252 VAFAE----SPDTLAEDLREVKPTFMLAVPRVWekvyaGIQAKaEEAGGLKrklFRwalavgrryararlagkspslllr 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 338 --------------------CLRHCLTGGEALNPDVrDKWKSQTGLELHEGYGQSET-VVICGNsRNSTIKSGSMGKASP 396
Cdd:COG1022 328 lkhaladklvfsklrealggRLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETsPVITVN-RPGDNRIGTVGPPLP 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 397 PYDVQIvDEEGNVLPPGkeGNIavrikptrpfcfFNCYLDNPEKTAAS--EQGDFYiTGDRAHMDEDGYFWFLGRNDDVI 474
Cdd:COG1022 406 GVEVKI-AEDGEILVRG--PNV------------MKGYYKNPEATAEAfdADGWLH-TGDIGELDEDGFLRITGRKKDLI 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26341010 475 -NSSSYRIGPVEVESALAEHPAVLESAVVsspdpirGE---VVKAFIVLspayashDPEALTRELQEH 538
Cdd:COG1022 470 vTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpFLAALIVP-------DFEALGEWAEEN 523
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
71-571 |
1.10e-43 |
|
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: 161.65 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 71 RPPNPAFWWvngsgTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPgvsqlta 150
Cdd:cd05945 4 NPDRPAVVE-----GGRTLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 151 kdlkyrlqaaraksivtsdalapqVDAISAdcpslqtkllvsdTSRpgwinFRELLRAASPEhnCVRTRSGDSVAIYFTS 230
Cdd:cd05945 71 ------------------------LDASSP-------------AER-----IREILDAAKPA--LLIADGDDNAYIIFTS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 231 GTTGAPKMVEHSQSSYgLGFVAggrrWM----ALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVheLPR---VDAKT 303
Cdd:cd05945 107 GSTGRPKGVQISHDNL-VSFTN----WMlsdfPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVP--VPRdatADPKQ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 304 ILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQT-GLELHEGYGQSETVVICgns 381
Cdd:cd05945 180 LFRFLAEHGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAV--- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 382 rnSTI----------KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAAS----EQG 447
Cdd:cd05945 257 --TYIevtpevldgyDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGP-----SVSKGYLNNPEKTAAAffpdEGQ 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 448 DFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayasHD 527
Cdd:cd05945 330 RAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKP----GA 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 26341010 528 PEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd05945 406 EAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
93-572 |
1.99e-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: 158.69 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 93 ELGKQSRKAANVLEGVCGLQPGDRMMLVLPR----LPDWWLisvacMRTGVVMIPGVSQLTAKDLKYRLQAARA-KSIVT 167
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARaaaaEGVWIA-----DGVYIYLINSILTVFAAAAAWKCGACPAyKSSRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SDALAPQVDAISAdcPSLQTKLLVSDTSRPGWINFrELLRAASPEHNCVRTRSGDsvAIYFTSGTTGAPKMVEHSQSSyG 247
Cdd:cd05929 77 PRAEACAIIEIKA--AALVCGLFTGGGALDGLEDY-EAAEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGIKRGLPG-G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 248 LGFVAGGRRWmalteSDIFWNTTDTGWVKAAwTLF----SAWSNGAcIF----VHELPRVDAKTILNTLCRFPITTLCCV 319
Cdd:cd05929 151 PPDNDTLMAA-----ALGFGPGADSVYLSPA-PLYhaapFRWSMTA-LFmggtLVLMEKFDPEEFLRLIERYRVTFAQFV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 320 PTLF-RLLVQEDLTRYKFQ--CLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKAS 395
Cdd:cd05929 224 PTMFvRLLKLPEAVRNAYDlsSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGQgLTIINGEEWLTHPGSVGRAV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 396 PPyDVQIVDEEGNVLPPGKEGNIAVRIKPTrpfcfFNcYLDNPEKTAASEQGDFYIT-GDRAHMDEDGYFWFLGRNDDVI 474
Cdd:cd05929 304 LG-KVHILDEDGNEVPPGEIGEVYFANGPG-----FE-YTNDPEKTAAARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 475 NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfiVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAF 554
Cdd:cd05929 377 ISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIEF 454
|
490
....*....|....*...
gi 26341010 555 ISELPKTVSGKILRSKLR 572
Cdd:cd05929 455 VAELPRDDTGKLYRRLLR 472
|
|
| 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 26341010 70 HRPPNPAFWWVNGSGTEVKWTfEELGKQSRKAANVLEGvcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLT 149
Cdd:cd05923 12 SRAPDACAIADPARGLRLTYS-ELRARIEAVAARLHAR--GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 150 AKDLKYRLQAARAKSIVTSDAlAPQVDAISAdcpSLQTKLLVSDTSRPGWI-NFRELLRAASPehncvrtRSGDSVAIYF 228
Cdd:cd05923 89 AAELAELIERGEMTAAVIAVD-AQVMDAIFQ---SGVRVLALSDLVGLGEPeSAGPLIEDPPR-------EPEQPAFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 229 TSGTTGAPK---------------MVEHSQSSYGLGFVAGGrrWMALTESDIFWnttdtgwvkaAWTLFSAWSNGACIFV 293
Cdd:cd05923 158 TSGTTGLPKgavipqraaesrvlfMSTQAGLRHGRHNVVLG--LMPLYHVIGFF----------AVLVAALALDGTYVVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 294 HELPRVDAktiLNTLCRFPITTLCCVPTLFRLLV-QEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQS 372
Cdd:cd05923 226 EEFDPADA---LKLIEQERVTSLFATPTHLDALAaAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 373 ETVvicgnsrNSTI----KSGSMGKASPPYDVQIVDEEGNV---LPPGKEGNIAVRIKPTRPFcffNCYLDNPEKTAASE 445
Cdd:cd05923 303 EAM-------NSLYmrdaRTGTEMRPGFFSEVRIVRIGGSPdeaLANGEEGELIVAAAADAAF---TGYLNQPEATAKKL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 446 QGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAS 525
Cdd:cd05923 373 QDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLS 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 26341010 526 HDpealtrELQEHVKTVT-APYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd05923 453 AD------ELDQFCRASElADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
77-572 |
5.92e-42 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 160.45 E-value: 5.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 77 FWWVNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYR 156
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYLKDV-GVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 157 LQAARAKSIVTSDA---------LAPQVDA---------ISAD-CPSLQTKLLVSDTSRPgWINFREL----LRAASPEH 213
Cdd:PLN02654 188 IVDCKPKVVITCNAvkrgpktinLKDIVDAaldesakngVSVGiCLTYENQLAMKREDTK-WQEGRDVwwqdVVPNYPTK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 214 NCVR-TRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFWNTTDTGWVKA-AWTLFSAWSNGACI 291
Cdd:PLN02654 267 CEVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGhSYVTYGPMLNGATV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 292 FVHE-LPRV-DAKTILNTLCRFPITTLCCVPTLFRLLVQED---LTRYKFQCLRHCLTGGEALNPDVrdkWK------SQ 360
Cdd:PLN02654 347 LVFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPSA---WRwffnvvGD 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 361 TGLELHEGYGQSET--VVICGNSRNSTIKSGSmgKASPPYDVQ--IVDEEGNVLPPGKEGNIAvrIKPTRPFCFFNCYLD 436
Cdd:PLN02654 424 SRCPISDTWWQTETggFMITPLPGAWPQKPGS--ATFPFFGVQpvIVDEKGKEIEGECSGYLC--VKKSWPGAFRTLYGD 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 437 NP--EKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK 514
Cdd:PLN02654 500 HEryETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIY 579
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 26341010 515 AFIVLSPAYAShdPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PLN02654 580 AFVTLVEGVPY--SEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILR 635
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
75-573 |
6.18e-42 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 158.83 E-value: 6.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 75 PAFwwvngSGTEVKWTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLK 154
Cdd:PRK12492 41 PAF-----SNLGVTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 155 YRLQAARAKSIVTSDALAPQVDAISADC--------------PSLQ----------TKLLVSDTSRPGWINFRELLRAAS 210
Cdd:PRK12492 116 HQFKDSGARALVYLNMFGKLVQEVLPDTgieylieakmgdllPAAKgwlvntvvdkVKKMVPAYHLPQAVPFKQALRQGR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 211 PEHNCVRTRSGDSVAIY-FTSGTTGAPK--MVEHSQSSYGLGFVaggRRWMALTESDIFWNTTDTGWVKAA----WTLFS 283
Cdd:PRK12492 196 GLSLKPVPVGLDDIAVLqYTGGTTGLAKgaMLTHGNLVANMLQV---RACLSQLGPDGQPLMKEGQEVMIAplplYHIYA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 284 AWSNGACIFV---HEL----PRvDAKTILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRD 355
Cdd:PRK12492 273 FTANCMCMMVsgnHNVlitnPR-DIPGFIKELGKWRFSALLGLNTLFvALMDHPGFKDLDFSALKLTNSGGTALVKATAE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 356 KWKSQTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCY 434
Cdd:PRK12492 352 RWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GPQ----VMKGY 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 435 LDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVV 513
Cdd:PRK12492 427 WQQPEATAEALDAEgWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAV 506
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 514 KAFIVlspayaSHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PRK12492 507 KLFVV------ARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRD 560
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
90-574 |
7.75e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 154.66 E-value: 7.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK06145 29 SYAEFHQRILQAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALapqvDAIsadcPSLQTKLLV------SDTSRPGWINfrellRAASPEHncvRTRSGDSVAIYFTSGTTGAPKMVEHSq 243
Cdd:PRK06145 108 EF----DAI----VALETPKIVidaaaqADSRRLAQGG-----LEIPPQA---AVAPTDLVRLMYTSGTTDRPKGVMHS- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 244 ssYGlgfvaggrrwmaltesDIFWNTTD----TGWVKAAWTLFSA--WSNGACifvhELPRV---------------DAK 302
Cdd:PRK06145 171 --YG----------------NLHWKSIDhviaLGLTASERLLVVGplYHVGAF----DLPGIavlwvggtlrihrefDPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 303 TILNTLCRFPITTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEAlNPD--VRDKWKSQTGLELHEGYGQSETvviCG 379
Cdd:PRK06145 229 AVLAAIERHRLTCAWMAPVMLsRVLTVPDRDRFDLDSLAWCIGGGEK-TPEsrIRDFTRVFTRARYIDAYGLTET---CS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 380 NSR-----NSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTAASEQGDFYITG 453
Cdd:PRK06145 305 GDTlmeagREIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRgPKVTKG------YWKDPEKTAEAFYGDWFRSG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 454 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTR 533
Cdd:PRK06145 379 DVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPG-ATLTLEALDR 457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 26341010 534 elqeHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK06145 458 ----HCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVLRDE 494
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
89-574 |
2.64e-40 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 153.98 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 89 WTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALRSL-GLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DALAPQVDAISADCpslqtkLLVSDTSRPGWINFRELLRAASpehncvrtRSGDSV-----------AIYFTSGTTGAPK 237
Cdd:PLN02330 135 DTNYGKVKGLGLPV------IVLGEEKIEGAVNWKELLEAAD--------RAGDTSdneeilqtdlcALPFSSGTTGISK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 238 --MVEHSQssyglgFVAGGRRWMALTESDIFWNTTDTGWVK------AAWTLFSAWSNGACIFVheLPRVDAKTILNTLC 309
Cdd:PLN02330 201 gvMLTHRN------LVANLCSSLFSVGPEMIGQVVTLGLIPffhiygITGICCATLRNKGKVVV--MSRFELRTFLNALI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 310 RFPITTLCCVPTLFRLLVQE------DLTRYKfqcLRHCLTGGEALNPDVRDKWKSQ-TGLELHEGYGQSETVVIC---G 379
Cdd:PLN02330 273 TQEVSFAPIVPPIILNLVKNpiveefDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEHSCITlthG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 380 N-SRNSTI-KSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAASEQGDFYI-TGDR 455
Cdd:PLN02330 350 DpEKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQ-----CVMQGYYNNKEETDRTIDEDGWLhTGDI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 456 AHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALtrel 535
Cdd:PLN02330 425 GYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDIL---- 500
|
490 500 510
....*....|....*....|....*....|....*....
gi 26341010 536 qEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN02330 501 -NFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
221-572 |
2.83e-40 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 149.94 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 221 GDSVAIYF-TSGTTGAPKMVEHSQSsyglGFVAGGrrWMA-----LTESDIFWNTTDTGWVKAAW-TLFSAWSNGACIFV 293
Cdd:cd05944 1 SDDVAAYFhTGGTTGTPKLAQHTHS----NEVYNA--WMLalnslFDPDDVLLCGLPLFHVNGSVvTLLTPLASGAHVVL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 294 -----HELPRVdAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRyKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEG 368
Cdd:cd05944 75 agpagYRNPGL-FDNFWKLVERYRITSLSTVPTVYAALLQVPVNA-DISSLRFAMSGAAPLPVELRARFEDATGLPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 369 YGQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQIV--DEEGNVL---PPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTA 442
Cdd:cd05944 153 YGLTEaTCLVAVNPPDGPKRPGSVGLRLPYARVRIKvlDGVGRLLrdcAPDEVGEICVA-GPG----VFGGYLYTEGNKN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 443 ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPA 522
Cdd:cd05944 228 AFVADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 26341010 523 yASHDPEALTRELQEHVKTVTApykYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05944 308 -AVVEEEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALR 353
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
222-568 |
3.01e-40 |
|
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: 149.33 E-value: 3.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPKMV-----------EHSQSSyGLGFVAGGRRWMALTESDIFwnttdtgwvKAAWTLFSAWSNGAC 290
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVllanktffavpDILQKE-GLNWVVGDVTYLPLPATHIG---------GLWWILTCLIHGGLC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 291 IFVHElpRVDAKTILNTLCRFPITTLCCVPTLFRLLVQE--DLTRYKFQcLRHCLTGGE-ALNPDVRD-KWKSQTGLELH 366
Cdd:cd17635 72 VTGGE--NTTYKSLFKILTTNAVTTTCLVPTLLSKLVSElkSANATVPS-LRLIGYGGSrAIAADVRFiEATGLTNTAQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 367 egYGQSET-VVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAvrIKPTRpfcFFNCYLDNPEKTAASE 445
Cdd:cd17635 149 --YGLSETgTALCLPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIW--IKSPA---NMLGYWNNPERTAEVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 446 QGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayaS 525
Cdd:cd17635 222 IDGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVAS----A 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 26341010 526 HDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:cd17635 298 ELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
90-571 |
3.59e-40 |
|
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: 152.08 E-value: 3.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVL--EGVcglQPGDRMMLVLPRLPDwwlisvacMRTGVVMIpgvsqltakdlkyrLQAARAksIVT 167
Cdd:cd17643 14 TYGELDARANRLARTLraEGV---GPGDRVALALPRSAE--------LIVALLAI--------------LKAGGA--YVP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SDALAP--QVDAISADCpslQTKLLVSDTSRPGWInfrellraaspehncvrtrsgdsvaIYfTSGTTGAPK--MVEHSQ 243
Cdd:cd17643 67 IDPAYPveRIAFILADS---GPSLLLTDPDDLAYV-------------------------IY-TSGSTGRPKgvVVSHAN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 244 SsygLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV--HELPRvDAKTILNTLCRFPITTLCCVPT 321
Cdd:cd17643 118 V---LALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVvpYEVAR-SPEDFARLLRDEGVTVLNQTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 322 LFRLLVQEDLTRYKFQ-CLRHCLTGGEALNPDVRDKWKSQTGL---ELHEGYGQSETVVicgnsrNSTIK---------- 387
Cdd:cd17643 194 AFYQLVEAADRDGRDPlALRYVIFGGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTV------HVTFRpldaadlpaa 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 388 -SGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAV-RIKPTRPfcffncYLDNPEKTA-------ASEQGD-FYITGDRAH 457
Cdd:cd17643 268 aASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVsGAGVARG------YLGRPELTAerfvanpFGGPGSrMYRTGDLAR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 458 MDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlspayASHDPEALTRELQE 537
Cdd:cd17643 342 RLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVV-----ADDGAAADIAELRA 416
|
490 500 510
....*....|....*....|....*....|....
gi 26341010 538 HVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17643 417 LLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-565 |
6.35e-40 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 149.07 E-value: 6.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 219 RSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGfVAGGRRWMALTESDIFW------NTTDTGWVKAA--------WTLFSA 284
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQEDIFRM-LMGGADFGTGEFTPSEDahkaaaAAAGTVMFPAPplmhgtgsWTAFGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 285 WSNGACIFVHElPRVDAKTILNTLCRFPITTLCCVPTLF-RLLVQE--DLTRYKFQCLRHCLTGGEALNPDVRDKW-KSQ 360
Cdd:cd05924 80 LLGGQTVVLPD-DRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDAlrDAGPYDLSSLFAISSGGALLSPEVKQGLlELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 361 TGLELHEGYGQSET-VVICGNSRNSTIKSGSMGKASPpyDVQIVDEEGNVLPPGKE--GNIAVR-IKPtrpfcffNCYLD 436
Cdd:cd05924 159 PNITLVDAFGSSETgFTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGgvGWIARRgHIP-------LGYYG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 437 NPEKTAAS--EQGD--FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 512
Cdd:cd05924 230 DEAKTAETfpEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 26341010 513 VKAFIVLSPAyasHDPEAltRELQEHVKTVTAPYKYPRKVAFISELPKTVSGK 565
Cdd:cd05924 310 VVAVVQLREG---AGVDL--EELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
222-568 |
1.26e-39 |
|
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: 147.65 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPK--MVEHSQS-----SYG-LGFVAGGRRWMALTEsdiFWNTTdtGWvKAAWtlFSAWSNGACIFV 293
Cdd:cd17638 1 DVSDIMFTSGTTGRSKgvMCAHRQTlraaaAWAdCADLTEDDRYLIINP---FFHTF--GY-KAGI--VACLLTGATVVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 294 HELprVDAKTILNTLCRFPITTLCCVPTLFR-LLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLE-LHEGYGQ 371
Cdd:cd17638 73 VAV--FDVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFEtVLTAYGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 372 SETVV--ICGNSRNSTIKSGSMGKASPPYDVQIVDEeGNVLPPGKegNIAVRikptrpfcffncYLDNPEKTAASEQGDF 449
Cdd:cd17638 151 TEAGVatMCRPGDDAETVATTCGRACPGFEVRIADD-GEVLVRGY--NVMQG------------YLDDPEATAEAIDADG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 450 YI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDP 528
Cdd:cd17638 216 WLhTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPG-VTLTE 294
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 26341010 529 EALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:cd17638 295 EDVIAWCRERL----ANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
228-573 |
2.12e-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: 146.71 E-value: 2.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 228 FTSGTTGAPKMVEHSQSSYgLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLF-SAWSNGAcifVHELPRVDAktILN 306
Cdd:cd17630 7 LTSGSTGTPKAVVHTAANL-LASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVrSLLAGAE---LVLLERNQA--LAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 307 TLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKwKSQTGLELHEGYGQSETVVICGNSRNSTI 386
Cdd:cd17630 81 DLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLER-AADRGIPLYTTYGMTETASQVATKRPDGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 387 KSGSMGKASPPYDVQIVDEegnvlppgkeGNIAVRikptrPFCFFNCYLDNPEKTAASEQGDFYiTGDRAHMDEDGYFWF 466
Cdd:cd17630 160 GRGGVGVLLPGRELRIVED----------GEIWVG-----GASLAMGYLRGQLVPEFNEDGWFT-TKDLGELHADGRLTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 467 LGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayashDPEALTRELQEHVKTVTAPY 546
Cdd:cd17630 224 LGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVG-------RGPADPAELRAWLKDKLARF 296
|
330 340
....*....|....*....|....*..
gi 26341010 547 KYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd17630 297 KLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
222-575 |
3.13e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 146.67 E-value: 3.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVA-IYFTSGTTGAPKMVEHSqssyglgfvaggRRWMAltesdifwntTDTGWVKAAWtlfsAWSnGACIFVHELP--R 298
Cdd:PRK07787 128 DAPAlIVYTSGTTGPPKGVVLS------------RRAIA----------ADLDALAEAW----QWT-ADDVLVHGLPlfH 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 299 VDAkTILNTL-----------------------CRFPITTLCCVPTLF-RLLVQEDLTRyKFQCLRHCLTGGEALNPDVR 354
Cdd:PRK07787 181 VHG-LVLGVLgplrignrfvhtgrptpeayaqaLSEGGTLYFGVPTVWsRIAADPEAAR-ALRGARLLVSGSAALPVPVF 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 355 DKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKE--GNIAVRiKPTrpfcFFN 432
Cdd:PRK07787 259 DRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVR-GPT----LFD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 433 CYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRND-DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRG 510
Cdd:PRK07787 334 GYLNRPDATAAAFTADgWFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLG 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26341010 511 EVVKAFIVlspayaSHDPEALTrELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQE 575
Cdd:PRK07787 414 QRIVAYVV------GADDVAAD-ELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
89-571 |
3.21e-38 |
|
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: 146.67 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 89 WTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTS 168
Cdd:cd12116 13 LSYAELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DALApqvDAISADCPSLQtkllvsdtsrpgwinfRELLRAASPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSYg 247
Cdd:cd12116 92 DALP---DRLPAGLPVLL----------------LALAAAAAAPAAPRTPVSPDDLAyVIYTSGSTGRPKGVVVSHRNL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 248 LGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVheLPR---VDAKTILNTLCRFPITTLCCVPTLFR 324
Cdd:cd12116 152 VNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVI--APRetqRDPEALARLIEAHSITVMQATPATWR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 325 LLVQEDltrykFQCLR--HCLTGGEALNPDVRDKWKSQTGlELHEGYGQSETVV------ICGNSRNSTIksgsmGKASP 396
Cdd:cd12116 230 MLLDAG-----WQGRAglTALCGGEALPPDLAARLLSRVG-SLWNLYGPTETTIwstaarVTAAAGPIPI-----GRPLA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 397 PYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAAS--------EQGDFYITGDRAHMDEDGYFWFLG 468
Cdd:cd12116 299 NTQVYVLDAALRPVPPGVPGELYIGGD-----GVAQGYLGRPALTAERfvpdpfagPGSRLYRTGDLVRRRADGRLEYLG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 469 RNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLspayasHDPEAL-TRELQEHVKTVTAPYK 547
Cdd:cd12116 374 RADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL------KAGAAPdAAALRAHLRATLPAYM 446
|
490 500
....*....|....*....|....
gi 26341010 548 YPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd12116 447 VPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
65-574 |
5.28e-38 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 147.43 E-value: 5.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 65 LEKTGHRPPNPAFwwVNGSGTEVkWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPG 144
Cdd:PLN02246 30 FERLSEFSDRPCL--IDGATGRV-YTYADVELLSRRVAAGLHKL-GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 145 VSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPslqTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSV 224
Cdd:PLN02246 106 NPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDDG---VTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 225 AIYFTSGTTGAPK--MVEH-SQSSYGLGFVAGGRRWMALTESDIfwnttdtgwVKAAWTLFSAWS----------NGACI 291
Cdd:PLN02246 183 ALPYSSGTTGLPKgvMLTHkGLVTSVAQQVDGENPNLYFHSDDV---------ILCVLPMFHIYSlnsvllcglrVGAAI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 292 FVheLPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQED-LTRYKFQCLRHCLTGGEALNPDVRDKWKSQ-TGLELHEGY 369
Cdd:PLN02246 254 LI--MPKFEIGALLELIQRHKVTIAPFVPPIVLAIAKSPvVEKYDLSSIRMVLSGAAPLGKELEDAFRAKlPNAVLGQGY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 370 GQSET---VVIC-GNSRNST-IKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVR----IKPtrpfcffncYLDNPE 439
Cdd:PLN02246 332 GMTEAgpvLAMClAFAKEPFpVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRgpqiMKG---------YLNDPE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 440 KTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIV 518
Cdd:PLN02246 403 ATANTIDKDGWLhTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 26341010 519 LSPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN02246 483 RSN-----GSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
112-566 |
1.76e-37 |
|
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: 145.17 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 112 QPGDRMMLVLPRLPDWWLISVACMRTGVVmiPGVSQLTA--KDLKYRLQAARAKSIVTSDAL-----APQVDAISADC-- 182
Cdd:cd05909 29 KEGENVGVMLPPSAGGALANFALALSGKV--PVMLNYTAglRELRACIKLAGIKTVLTSKQFieklkLHHLFDVEYDAri 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 183 ---PSLQTKLLVSD--------TSRPGWINFRELLRAASPEHNCVrtrsgdsvaIYFTSGTTGAPKMVEHSQSSYgLGFV 251
Cdd:cd05909 107 vylEDLRAKISKADkckaflagKFPPKWLLRIFGVAPVQPDDPAV---------ILFTSGSEGLPKGVVLSHKNL-LANV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 252 AGGRRWMALTESDIFWNTTDT----GWVKAAWTLFSAwsnGACIFVHELPrVDAKTILNTLCRFPITTLCCVPTLFRLLV 327
Cdd:cd05909 177 EQITAIFDPNPEDVVFGALPFfhsfGLTGCLWLPLLS---GIKVVFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 328 QEdLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNSRNSTIKSGSMGKASPPYDVQIVDEE 406
Cdd:cd05909 253 RA-AHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSpVISVNTPQSPNKEGTVGRPLPGMEVKIVSVE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 407 GNV-LPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRnddviNSSSYRIG--- 482
Cdd:cd05909 332 THEeVPIGEGGLLLVR-GPN----VMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGR-----LSRFAKIAgem 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 483 -PVE-VESALAEH-PAVLESAVVSSPDPIRGEVVKAFivlspayasHDPEALTR-ELQEHVKTVTAPYKY-PRKVAFISE 557
Cdd:cd05909 402 vSLEaIEDILSEIlPEDNEVAVVSVPDGRKGEKIVLL---------TTTTDTDPsSLNDILKNAGISNLAkPSYIHQVEE 472
|
....*....
gi 26341010 558 LPKTVSGKI 566
Cdd:cd05909 473 IPLLGTGKP 481
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
84-538 |
4.25e-37 |
|
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: 143.12 E-value: 4.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 84 GTEVKWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGLIA-LGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 164 SIVTSDAlapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgDSVA-IYFTSGTTGAPKMVEHS 242
Cdd:cd05907 80 ALFVEDP---------------------------------------------------DDLAtIIYTSGTTGRPKGVMLS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 243 QSSYgLGFVAGGRRWMALTESD----------IFWNTTDtgwvkaawtLFSAWSNGACIFVHElprvDAKTILNTLCRFP 312
Cdd:cd05907 109 HRNI-LSNALALAERLPATEGDrhlsflplahVFERRAG---------LYVPLLAGARIYFAS----SAETLLDDLSEVR 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 313 ITTLCCVPTLFR----LLVQEDLTRYK--------FQCLRHCLTGGEALNPDVrDKWKSQTGLELHEGYGQSETVVICGN 380
Cdd:cd05907 175 PTVFLAVPRVWEkvyaAIKVKAVPGLKrklfdlavGGRLRFAASGGAPLPAEL-LHFFRALGIPVYEGYGLTETSAVVTL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 381 SRNSTIKSGSMGKASPPYDVQIVDEegnvlppgkeGNIAVRIKPTrpfcfFNCYLDNPEKTAASEQGD-FYITGDRAHMD 459
Cdd:cd05907 254 NPPGDNRIGTVGKPLPGVEVRIADD----------GEILVRGPNV-----MLGYYKNPEATAEALDADgWLHTGDLGEID 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 460 EDGYFWFLGRNDDVI-NSSSYRIGPVEVESALAEHPAVLESAVVSSPDPirgeVVKAFIVLspayashDPEALTRELQEH 538
Cdd:cd05907 319 EDGFLHITGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVP-------DPEALEAWAEEH 387
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
86-574 |
8.20e-37 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 143.93 E-value: 8.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDwwlisvacM---RTGVVMIPGV-----SQLTAKDLKYRL 157
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPA--------MveaHFGVPMAGAVlntlnTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 158 QAARAKSIVTSDALAPQVDAISADCPSLqtKLLVSD--------TSRPGWINFRELLRAASPEHNCVRTRSG-DSVAIYF 228
Cdd:PRK08162 112 RHGEAKVLIVDTEFAEVAREALALLPGP--KPLVIDvddpeypgGRFIGALDYEAFLASGDPDFAWTLPADEwDAIALNY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 229 TSGTTGAPK-MVEHSQSSYglgfvaggrrWMALTesdifwNTTDTGWVKAA---WTL--FS------AWSNGACIFVHE- 295
Cdd:PRK08162 190 TSGTTGNPKgVVYHHRGAY----------LNALS------NILAWGMPKHPvylWTLpmFHcngwcfPWTVAARAGTNVc 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 296 LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEALNPDVRDKWKsQTGLELHEGYGQSET 374
Cdd:PRK08162 254 LRKVDPKLIFDLIREHGVTHYCGAPIVLSALINaPAEWRAGIDHPVHAMVAGAAPPAAVIAKME-EIGFDLTHVYGLTET 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 375 ---VVICG-----NSRNSTIKSGSMGKASPPYDVQivdEEGNVLPP---------GKE-GNIAVR----IKPtrpfcffn 432
Cdd:PRK08162 333 ygpATVCAwqpewDALPLDERAQLKARQGVRYPLQ---EGVTVLDPdtmqpvpadGETiGEIMFRgnivMKG-------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 433 cYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEV 512
Cdd:PRK08162 402 -YLKNPKATEEAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26341010 513 VKAFIVLSPAyASHDPEaltrELQEHVKTVTAPYKYPRKVAFiSELPKTVSGKILRSKLRNQ 574
Cdd:PRK08162 481 PCAFVELKDG-ASATEE----EIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
226-568 |
4.90e-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: 137.15 E-value: 4.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 226 IYFTSGTTGAPKMVEHSQSSYGLGFVAGgrrwmaltESDIFWNTTDTgwVKAAWTLFSAWSNGACIF-------VHELPR 298
Cdd:cd17633 5 IGFTSGTTGLPKAYYRSERSWIESFVCN--------EDLFNISGEDA--ILAPGPLSHSLFLYGAISalylggtFIGQRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 299 VDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLrhcLTGGEALNPDVRDKWKSQT-GLELHEGYGQSETVVI 377
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 378 CGNSRNSTIKSGSMGKASPPYDVQIVDEEGnvlppGKEGNIAVRIKptrpfCFFNCYLDNPEktaaSEQGDFYITGDRAH 457
Cdd:cd17633 152 TYNFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSE-----MVFSGYVRGGF----SNPDGWMSVGDIGY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 458 MDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSpayashdpEALTRELQE 537
Cdd:cd17633 218 VDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD--------KLTYKQLKR 289
|
330 340 350
....*....|....*....|....*....|.
gi 26341010 538 HVKTVTAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:cd17633 290 FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
228-573 |
1.90e-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: 139.21 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 228 FTSGTTGAPK--MVEHSQssyglgFVAGgrrwmALTESDIFWNTTDTGWVK-AAWT-------LFSAWSNGACIFV-HEL 296
Cdd:cd05918 113 FTSGSTGKPKgvVIEHRA------LSTS-----ALAHGRALGLTSESRVLQfASYTfdvsileIFTTLAAGGCLCIpSEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 297 PRVD--AKTIlntlCRFPITTLCCVPTLFRLLVQEDLTrykfqCLRHCLTGGEALNPDVRDKWKSqtGLELHEGYGQSET 374
Cdd:cd05918 182 DRLNdlAGFI----NRLRVTWAFLTPSVARLLDPEDVP-----SLRTLVLGGEALTQSDVDTWAD--RVRLINAYGPAEC 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 375 VVIC-GNSRNSTIKSGSMGkasPPYDVQ--IVDEEGN--VLPPGK------EGNIAVRikptrpfcffnCYLDNPEKTAA 443
Cdd:cd05918 251 TIAAtVSPVVPSTDPRNIG---RPLGATcwVVDPDNHdrLVPIGAvgelliEGPILAR-----------GYLNDPEKTAA 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 444 S--------------EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIR 509
Cdd:cd05918 317 AfiedpawlkqegsgRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVVKPKD 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26341010 510 GEVVK---AFIVLSPAYA------------SHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd05918 397 GSSSPqlvAFVVLDGSSSgsgdgdslflepSDEFRALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALRE 475
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
110-574 |
5.28e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 138.72 E-value: 5.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 110 GLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDA-----LAPQVDAISADC-P 183
Cdd:PRK06164 56 GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVVWPGfkgidFAAILAAVPPDAlP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 184 SLQTKLLVSDTSR--PGWINFRELLRAASP---EHNCVRTRSGDS---VAIYFTSGTTGAPKMVEHSQS----------- 244
Cdd:PRK06164 136 PLRAIAVVDDAADatPAPAPGARVQLFALPdpaPPAAAGERAADPdagALLFTTSGTTSGPKLVLHRQAtllrharaiar 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 245 SYGLGfvAGGRRWMALTESDIFWNTTdtgwvkaawtLFSAWSNGACifVHELPRVDAKTILNTLCRFPITTLCCVPTLFR 324
Cdd:PRK06164 216 AYGYD--PGAVLLAALPFCGVFGFST----------LLGALAGGAP--LVCEPVFDAARTARALRRHRVTHTFGNDEMLR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 325 LLVQEDLTRYKFQCLRHCltGGEALNPDVRD--KWKSQTGLELHEGYGQSETVVICGNSRNSTIKS----GSMGKASPPY 398
Cdd:PRK06164 282 RILDTAGERADFPSARLF--GFASFAPALGElaALARARGVPLTGLYGSSEVQALVALQPATDPVSvrieGGGRPASPEA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 399 DVQIVD-EEGNVLPPGKEGNIAVRiKPTRpfcfFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINS 476
Cdd:PRK06164 360 RVRARDpQDGALLPDGESGEIEIR-APSL----MRGYLDNPDATARALTDDgYFRTGDLGYTRGDGQFVYQTRMGDSLRL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 477 SSYRIGPVEVESALAEHPAVLESAVVSSpdPIRGE-VVKAFIVLSPAyASHDPEALTRELQEHVktvtAPYKYPRKVAFI 555
Cdd:PRK06164 435 GGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGKtVPVAFVIPTDG-ASPDEAGLMAACREAL----AGFKVPARVQVV 507
|
490 500
....*....|....*....|..
gi 26341010 556 SELPKTVSG---KILRSKLRNQ 574
Cdd:PRK06164 508 EAFPVTESAngaKIQKHRLREM 529
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-571 |
8.18e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 141.25 E-value: 8.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVL--EGVcglQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALiaRGV---GPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAA 4650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 164 SIVTSDALAPQVD-AISADCpslqtklLVSDTSRPgWINFrellraasPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEH 241
Cdd:PRK12316 4651 LLLTQSHLLQRLPiPDGLAS-------LALDRDED-WEGF--------PAHDPAVRLHPDNLAyVIYTSGSTGRPKGVAV 4714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 242 SQSSYgLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPT 321
Cdd:PRK12316 4715 SHGSL-VNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPV 4793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 322 LFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDK-WKSQTGLELHEGYGQSETVV--ICGNSRNSTIKSGS---MGKAS 395
Cdd:PRK12316 4794 YLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVtvLLWKARDGDACGAAympIGTPL 4873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 396 PPYDVQIVDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAA-------SEQGD-FYITGDRAHMDEDGYFWFL 467
Cdd:PRK12316 4874 GNRSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAErfvpdpfGAPGGrLYRTGDLARYRADGVIDYL 4948
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 468 GRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPE--ALTRELQEHVKTVTAP 545
Cdd:PRK12316 4949 GRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAqaELRDELKAALRERLPE 5028
|
490 500
....*....|....*....|....*.
gi 26341010 546 YKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK12316 5029 YMVPAHLVFLARMPLTPNGKLDRKAL 5054
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
102-572 |
1.25e-34 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 138.05 E-value: 1.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 102 ANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVV---MIPGVSQLTAKdlkyrlqaarAKSIVTSDALAPQVDAI 178
Cdd:PLN02574 80 AAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIvttMNPSSSLGEIK----------KRVVDCSVGLAFTSPEN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 179 SADCPSLQTK-LLVS-----DTSRPGWINFRELLRAASpeHNCVR--TRSGDSVAIYFTSGTTGAPKMVEHSQSSyglgF 250
Cdd:PLN02574 150 VEKLSPLGVPvIGVPenydfDSKRIEFPKFYELIKEDF--DFVPKpvIKQDDVAAIMYSSGTTGASKGVVLTHRN----L 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 251 VAGGRRWMALTESDIFWNTTDTGWVkAAWTLFSAW----------SNGACIFVheLPRVDAKTILNTLCRFPITTLCCVP 320
Cdd:PLN02574 224 IAMVELFVRFEASQYEYPGSDNVYL-AALPMFHIYglslfvvgllSLGSTIVV--MRRFDASDMVKVIDRFKVTHFPVVP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 321 TLFRLLVQ--EDLTRYKFQCLRHCLTGGEALNPD-VRDKWKSQTGLELHEGYGQSETVVICGNSRNS--TIKSGSMGKAS 395
Cdd:PLN02574 301 PILMALTKkaKGVCGEVLKSLKQVSCGAAPLSGKfIQDFVQTLPHVDFIQGYGMTESTAVGTRGFNTekLSKYSSVGLLA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 396 PPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDV 473
Cdd:PLN02574 381 PNMQAKVVDwSTGCLLPPGNCGELWIQ-GPG----VMKGYLNNPKATQSTIDKDGWLrTGDIAYFDEDGYLYIVDRLKEI 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 474 INSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyashdpEALTRE-LQEHVKTVTAPYKYPRKV 552
Cdd:PLN02574 456 IKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQG------STLSQEaVINYVAKQVAPYKKVRKV 529
|
490 500
....*....|....*....|
gi 26341010 553 AFISELPKTVSGKILRSKLR 572
Cdd:PLN02574 530 VFVQSIPKSPAGKILRRELK 549
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
85-572 |
1.29e-34 |
|
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: 137.66 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 85 TEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKS 164
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKY-GLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 165 IVTSDALAPQVDAISADCPSLQTKLLVSD-------------TSRPGWINFRELlRAASPEHNcvrtRSGDSVAIYFTSG 231
Cdd:cd17642 120 VFCSKKGLQKVLNVQKKLKIIKTIIILDSkedykgyqclytfITQNLPPGFNEY-DFKPPSFD----RDEQVALIMNSSG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 232 TTGAPKMVEHSQSSYGLGFvaggrrwmALTESDIFWNTT--DTGWVKA-----AWTLFSAWSNGACIF-VHELPRVDAKT 303
Cdd:cd17642 195 STGLPKGVQLTHKNIVARF--------SHARDPIFGNQIipDTAILTVipfhhGFGMFTTLGYLICGFrVVLMYKFEEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 304 ILNTLCRFPITTLCCVPTLFRLLVQEDLT-RYKFQCLRHCLTGGEALNPDVRDKWKSQTGLE-LHEGYGQSETVVICGNS 381
Cdd:cd17642 267 FLRSLQDYKVQSALLVPTLFAFFAKSTLVdKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTETTSAILIT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 382 RNSTIKSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYI-TGDRAHMD 459
Cdd:cd17642 347 PEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVK-GPM----IMKGYVNNPEATKALIDKDGWLhSGDIAYYD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 460 EDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLspayaSHDPEALTRELQEHV 539
Cdd:cd17642 422 EDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVL-----EAGKTMTEKEVMDYV 496
|
490 500 510
....*....|....*....|....*....|....
gi 26341010 540 KTVTAPYKYPR-KVAFISELPKTVSGKILRSKLR 572
Cdd:cd17642 497 ASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIR 530
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
218-572 |
2.82e-34 |
|
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: 135.19 E-value: 2.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 218 TRSGDSVA-IYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWmALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHEL 296
Cdd:cd17649 90 THHPRQLAyVIYTSGSTGTPKGVAVSHGPLAAHCQATAERY-GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPD 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 297 PR-VDAKTILNTLCRFPITTLCCVPTLFRLLVQE--DLTRYKFQCLRHCLTGGEALNPDVRDKWKsQTGLELHEGYGQSE 373
Cdd:cd17649 169 ELwASADELAEMVRELGVTVLDLPPAYLQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRWL-KAPVRLFNAYGPTE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 374 TVV---ICGNSRNSTIKSGSM--GKASPPYDVQIVDEEGNVLPPGKEGN--IAVRikptrpfCFFNCYLDNPEKTA---- 442
Cdd:cd17649 248 ATVtplVWKCEAGAARAGASMpiGRPLGGRSAYILDADLNPVPVGVTGElyIGGE-------GLARGYLGRPELTAerfv 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 443 ----ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIV 518
Cdd:cd17649 321 pdpfGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVV 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 26341010 519 LSPAYAShdpEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd17649 400 LRAAAAQ---PELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
288-564 |
1.48e-33 |
|
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: 130.50 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 288 GACIFVhelPRVDAKTILNTLCRFPIT-TLCCVPTLFRLLVQEDLTRYKFQCLRHCLT--GGEALNPDVRDKWKSQTGle 364
Cdd:cd17636 67 GTNVFV---RRVDAEEVLELIEAERCThAFLLPPTIDQIVELNADGLYDLSSLRSSPAapEWNDMATVDTSPWGRKPG-- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 365 lheGYGQSET---VVICGNSRNSTiksGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKT 441
Cdd:cd17636 142 ---GYGQTEVmglATFAALGGGAI---GGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPEVN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 442 AASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSP 521
Cdd:cd17636 211 ARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKP 290
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 26341010 522 AyASHDPEaltrELQEHVKTVTAPYKYPRKVAFISELPKTVSG 564
Cdd:cd17636 291 G-ASVTEA----ELIEHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
101-574 |
2.52e-33 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 134.16 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 101 AANVLEGvcGLQPGDRMMLVLPRlPDW---WLISVACMrtGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDA 177
Cdd:PLN02860 46 AAGLLRL--GLRNGDVVAIAALN-SDLyleWLLAVACA--GGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 178 I-SADCPSLQTKLLVSDTSRPGWINFRELLRaasPEHncVRTRSG------------DSVAIYFTSGTTGAPKMV--EHS 242
Cdd:PLN02860 121 LqNDRLPSLMWQVFLESPSSSVFIFLNSFLT---TEM--LKQRALgtteldyawapdDAVLICFTSGTTGRPKGVtiSHS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 243 ----QSSYGLGFVAGGrrwmaltESDIFWNTT---DTGWVKAAWTLFSAwsnGAC-IFvheLPRVDAKTILNTLCRFPIT 314
Cdd:PLN02860 196 alivQSLAKIAIVGYG-------EDDVYLHTAplcHIGGLSSALAMLMV---GAChVL---LPKFDAKAALQAIKQHNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 315 TLCCVPTLFRLLV---QEDLTRYKFQCLRHCLTGGEALNPDVRDKWK-------------------SQTGLELHEGYGQS 372
Cdd:PLN02860 263 SMITVPAMMADLIsltRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKklfpnaklfsaygmteacsSLTFMTLHDPTLES 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 373 ETVVICGNSRnstIKSGS--------MGKASPPYDVQIVDEEgnvlpPGKEGNIAvrikpTRPFCFFNCYLDNPEKTAAS 444
Cdd:PLN02860 343 PKQTLQTVNQ---TKSSSvhqpqgvcVGKPAPHVELKIGLDE-----SSRVGRIL-----TRGPHVMLGYWGQNSETASV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 445 EQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAY 523
Cdd:PLN02860 410 LSNDGWLdTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGW 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26341010 524 ASHDPEALTR---------ELQEHVKTVT-APYKYPRK-VAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN02860 490 IWSDNEKENAkknltlsseTLRHHCREKNlSRFKIPKLfVQWRKPFPLTTTGKIRRDEVRRE 551
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
80-571 |
3.65e-33 |
|
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: 132.39 E-value: 3.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 80 VNGSGTevkWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQA 159
Cdd:cd12114 7 ICGDGT---LTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 160 ARAKSIVTSDALAPQVDAISADCPSLQTKLlvsdtsrpgwinfrellrAASPEHNCVRTRSGDSVAIYFTSGTTGAPK-- 237
Cdd:cd12114 83 AGARLVLTDGPDAQLDVAVFDVLILDLDAL------------------AAPAPPPPVDVAPDDLAYVIFTSGSTGTPKgv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 238 MVEHSQSS---------YGLGfvaGGRRWMALTESDIfwnttDTgwvkAAWTLFSAWSNGACI-FVHELPRVDAKTILNT 307
Cdd:cd12114 145 MISHRAALntildinrrFAVG---PDDRVLALSSLSF-----DL----SVYDIFGALSAGATLvLPDEARRRDPAHWAEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 308 LCRFPITTLCCVPTLFRLLVQEDLTRYKFQC-LRHCLTGGEALNPDVRDKWKSQT-GLELHEGYGQSETVVIcgnSRNST 385
Cdd:cd12114 213 IERHGVTLWNSVPALLEMLLDVLEAAQALLPsLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIW---SIYHP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 386 IKSGSMGKASPPYDV-------QIVDEEGNVLPPGKEGNI-------AvrikptrpfcffNCYLDNPEKTAAS-----EQ 446
Cdd:cd12114 290 IDEVPPDWRSIPYGRplanqryRVLDPRGRDCPDWVPGELwiggrgvA------------LGYLGDPELTAARfvthpDG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 447 GDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVLSPAYASH 526
Cdd:cd12114 358 ERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPI 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 26341010 527 DPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd12114 437 APDALRAFLAQTL----PAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
110-574 |
5.09e-33 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 133.09 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 110 GLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKsIVTSDALAP-QVDAISADCPSLQTK 188
Cdd:PRK05852 64 GLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGAR-VVLIDADGPhDRAEPTTRWWPLTVN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 189 LLVSDTSRPGWINFRelLRAASPEHNCVRTRSG---DSVAIYFTSGTTGAPKMVEHSQ-----------SSYGLGFVAGG 254
Cdd:PRK05852 143 VGGDSGPSGGTLSVH--LDAATEPTPATSTPEGlrpDDAMIMFTGGTTGLPKMVPWTHaniassvraiiTGYRLSPRDAT 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 255 RRWMALTESDifwnttdtGWVKAawtLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ---EDL 331
Cdd:PRK05852 221 VAVMPLYHGH--------GLIAA---LLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLEraaTEP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 332 TRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSET--------VVICGNSRNSTIKSGSMGKASPPyDVQIV 403
Cdd:PRK05852 290 SGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEAthqvtttqIEGIGQTENPVVSTGLVGRSTGA-QIRIV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 404 DEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGP 483
Cdd:PRK05852 369 GSDGLPLPAGAVGEVWLR-GTT----VVRGYLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISP 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 484 VEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlsPAYASHdPEAltRELQEHVKTVTAPYKYPRKVAFISELPKTVS 563
Cdd:PRK05852 444 ERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIV--PRESAP-PTA--EELVQFCRERLAAFEIPASFQEASGLPHTAK 518
|
490
....*....|.
gi 26341010 564 GKILRSKLRNQ 574
Cdd:PRK05852 519 GSLDRRAVAEQ 529
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
115-573 |
5.30e-33 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 133.22 E-value: 5.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 115 DRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDAISADCPSLQTKL----- 189
Cdd:PLN03102 65 DVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAREVLHLLSSEDSNLnlpvi 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 190 LVSDTSRPGWINFRE-----LLRAASPEHN------CVRTRSgDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWM 258
Cdd:PLN03102 145 FIHEIDFPKRPSSEEldyecLIQRGEPTPSlvarmfRIQDEH-DPISLNYTSGTTADPKGVVISHRGAYLSTLSAIIGWE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 259 ALTESDIFWNTTD---TGWVkAAWTLFSAWSNGACIfvhelPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRYK 335
Cdd:PLN03102 224 MGTCPVYLWTLPMfhcNGWT-FTWGTAARGGTSVCM-----RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 336 FQCLR-HCLTGGEAlNPDVRDKWKSQTGLELHEGYGQSET---VVIC-----------GNSRNSTIKSGSMGKASPPYDV 400
Cdd:PLN03102 298 PRSGPvHVLTGGSP-PPAALVKKVQRLGFQVMHAYGLTEAtgpVLFCewqdewnrlpeNQQMELKARQGVSILGLADVDV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 401 QIVDEEGNVLPPGKE-GNIAVRIKptrpfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSY 479
Cdd:PLN03102 377 KNKETQESVPRDGKTmGEIVIKGS-----SIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 480 RIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEA---LTRE--LQEHVKTVTAPYKYPRKVAF 554
Cdd:PLN03102 452 NISSVEVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVdklVTRErdLIEYCRENLPHFMCPRKVVF 531
|
490
....*....|....*....
gi 26341010 555 ISELPKTVSGKILRSKLRN 573
Cdd:PLN03102 532 LQELPKNGNGKILKPKLRD 550
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
203-571 |
2.65e-32 |
|
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: 129.36 E-value: 2.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 203 RELLRAASPEHncVRTRSGDSVAIYFTSGTTGAPKMV--EHSQSSYGLgfvaggrRWMALTESDIFWN----TTDTGWVK 276
Cdd:cd12115 89 RFILEDAQARL--VLTDPDDLAYVIYTSGSTGRPKGVaiEHRNAAAFL-------QWAAAAFSAEELAgvlaSTSICFDL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 277 AAWTLFSAWSNGACIFVHE-------LPRVDAKTILNTlcrfpittlccVPTLFRLLVQEDLTRYKFQCLrhCLtGGEAL 349
Cdd:cd12115 160 SVFELFGPLATGGKVVLADnvlalpdLPAAAEVTLINT-----------VPSAAAELLRHDALPASVRVV--NL-AGEPL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 350 NPD-VRDKWKSQTGLELHEGYGQSET-------VVICGNSRNSTIksgsmGKASPPYDVQIVDEEGNVLPPGKEGNIAVR 421
Cdd:cd12115 226 PRDlVQRLYARLQVERVVNLYGPSEDttystvaPVPPGASGEVSI-----GRPLANTQAYVLDRALQPVPLGVPGELYIG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 422 -IKPTRpfcffnCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEH 493
Cdd:cd12115 301 gAGVAR------GYLGRPGLTAERflpdpfGPGArLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSI 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26341010 494 PAVLESAVVSSPDPIRGEVVKAFIVLSPAYAShdpeaLTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd12115 375 PGVREAVVVAIGDAAGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
165-576 |
2.78e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 127.84 E-value: 2.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 165 IVTSDALAPQVDAIsaDCPSLQtkLLVSDTsrPGWinfRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQS 244
Cdd:PRK13388 103 LVTDAEHRPLLDGL--DLPGVR--VLDVDT--PAY---AELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 245 SYG-LGFVAGGRRwmALTESDIFWNTT---DTGWVKAAWTlfSAWSNGACIFVHelPRVDAKTILNTLCRFPITTLCCV- 319
Cdd:PRK13388 174 RLAfAGRALTERF--GLTRDDVCYVSMplfHSNAVMAGWA--PAVASGAAVALP--AKFSASGFLDDVRRYGATYFNYVg 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 320 PTLFRLLVQEDLTRYKFQCLRHCLtGGEAlNPDVRDKWKSQTGLELHEGYGQSETVVICgnSRNSTIKSGSMGKASPpyD 399
Cdd:PRK13388 248 KPLAYILATPERPDDADNPLRVAF-GNEA-SPRDIAEFSRRFGCQVEDGYGSSEGAVIV--VREPGTPPGSIGRGAP--G 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 400 VQIV-------------DEEGNVLPPGKegniAV-RIKPTRPFCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFW 465
Cdd:PRK13388 322 VAIYnpetltecavarfDAHGALLNADE----AIgELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 466 FLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHDPEALTREL--QEHVKTVT 543
Cdd:PRK13388 398 FAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAAFLaaQPDLGTKA 476
|
410 420 430
....*....|....*....|....*....|...
gi 26341010 544 ApykyPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK13388 477 W----PRYVRIAADLPSTATNKVLKRELIAQGW 505
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
90-571 |
6.00e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.13 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK12467 539 SYAELNRQANRLAHVLIAA-GVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQS 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDaISADCPSLQtkllvsdtsrpgwINFRELLRAASPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSYgL 248
Cdd:PRK12467 618 HLLAQLP-VPAGLRSLC-------------LDEPADLLCGYSGHNPEVALDPDNLAyVIYTSGSTGQPKGVAISHGAL-A 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 249 GFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACifVHELPR---VDAKTILNTLCRFPITTLCCVPTLFRL 325
Cdd:PRK12467 683 NYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGAT--LHLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQA 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 326 LVQEDLTRykfQCLR-HCLT-GGEALNPDVRDKWKS-QTGLELHEGYGQSETVVICGNSR----NSTIKSGSMGKASPPY 398
Cdd:PRK12467 761 LLQASRVA---LPRPqRALVcGGEALQVDLLARVRAlGPGARLINHYGPTETTVGVSTYElsdeERDFGNVPIGQPLANL 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 399 DVQIVDEEGNVLPPGKEGNIAV------RIKPTRPFCFFNCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFLGRNDD 472
Cdd:PRK12467 838 GLYILDHYLNPVPVGVVGELYIggaglaRGYHRRPALTAERFVPDPFGADG---GRLYRTGDLARYRADGVIEYLGRMDH 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 473 VINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVkAFIVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKV 552
Cdd:PRK12467 915 QVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHL 993
|
490
....*....|....*....
gi 26341010 553 AFISELPKTVSGKILRSKL 571
Cdd:PRK12467 994 LLLDSLPLTPNGKLDRKAL 1012
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
90-573 |
2.80e-30 |
|
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: 123.19 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPgvsqltakdLKYRLQAARAKSIV-TS 168
Cdd:cd17653 24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVP---------LDAKLPSARIQAILrTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 169 DAlapqvdaisadcpslqtKLLVSDTSrpgwinfrellraaspehncvrtrsGDSVA-IYFTSGTTGAPK--MVEH---- 241
Cdd:cd17653 94 GA-----------------TLLLTTDS-------------------------PDDLAyIIFTSGSTGIPKgvMVPHrgvl 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 242 ---SQSSYGLgFVAGGRRwMALTESDIFWnttdtgwvKAAWTLFSAWSNGAcIFVHELPRVDAKTILNTLCRFPITtlcc 318
Cdd:cd17653 132 nyvSQPPARL-DVGPGSR-VAQVLSIAFD--------ACIGEIFSTLCNGG-TLVLADPSDPFAHVARTVDALMST---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 319 vPTLFRLLVQEDltrykFQCLRHCLTGGEALNPDVRDKWKSqtGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPY 398
Cdd:cd17653 197 -PSILSTLSPQD-----FPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 399 DVQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTAASEQGD-------FYITGDRAHMDEDGYFWFLGRN 470
Cdd:cd17653 269 TCYILDADLQPVPEGVVGEICISgVQVARG------YLGNPALTASKFVPDpfwpgsrMYRTGDYGRWTEDGGLEFLGRE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 471 DDVINSSSYRIGPVEVESALAEHPAVLESAVVSspdpirgeVVKAFIVLSPAYASHDPEALTRELQEHVktvtAPYKYPR 550
Cdd:cd17653 343 DNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI--------VVNGRLVAFVTPETVDVDGLRSELAKHL----PSYAVPD 410
|
490 500
....*....|....*....|...
gi 26341010 551 KVAFISELPKTVSGKILRSKLRN 573
Cdd:cd17653 411 RIIALDSFPLTANGKVDRKALRE 433
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
138-574 |
3.16e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 124.12 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 138 GVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDaiSADCPSLQtkllvsdtsrpgWINFRELLRAASPEHNCVR 217
Cdd:PRK07638 74 GWTCVPLDIKWKQDELKERLAISNADMIVTERYKLNDLP--DEEGRVIE------------IDEWKRMIEKYLPTYAPIE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 218 TRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFvaggrrwmALTESDIFWNTTDTgwVKAAWTLFSA-WSNGA--CIF-- 292
Cdd:PRK07638 140 NVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSF--------DCNVHDFHMKREDS--VLIAGTLVHSlFLYGAisTLYvg 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 293 --VHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDltRYKFQCLRhCLTGGEALNPDVRDKWKSQ-TGLELHEGY 369
Cdd:PRK07638 210 qtVHLMRKFIPNQVLDKLETENISVMYTVPTMLESLYKEN--RVIENKMK-IISSGAKWEAEAKEKIKNIfPYAKLYEFY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 370 GQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptRPFcFFNCYLDNPEKTAASEQGD 448
Cdd:PRK07638 287 GASElSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVK----SPQ-FFMGYIIGGVLARELNADG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 449 FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIvlspayashDP 528
Cdd:PRK07638 362 WMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KG 432
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 26341010 529 EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK07638 433 SATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
219-571 |
4.15e-30 |
|
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: 123.59 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 219 RSGDSVAIYFTSGTTGAPK--MVEHSQSSYglgFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV--H 294
Cdd:cd17655 135 KSDDLAYVIYTSGSTGKPKgvMIEHRGVVN---LVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIvrK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 295 ElPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTryKFQCLRHCLTGGEALNPDVRDKWKSQTGL--ELHEGYGQS 372
Cdd:cd17655 212 E-TVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDS--EGLSLKHLIVGGEALSTELAKKIIELFGTnpTITNAYGPT 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 373 ETVVIC--GNSRNSTIKSGS--MGKASPPYDVQIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTA 442
Cdd:cd17655 289 ETTVDAsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIggegvaR-----------GYLNRPELTA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 443 AS------EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKA 515
Cdd:cd17655 358 EKfvddpfVPGErMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCA 437
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 26341010 516 FIVlspayasHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17655 438 YIV-------SEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
125-576 |
6.60e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 123.64 E-value: 6.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 125 PDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDaisadcpSLQTKLLVSDTSRPGWINFRE 204
Cdd:PRK07867 65 PEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLD-------GLDPGVRVINVDSPAWADELA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 205 LLRAASPEHncVRTRSGDSVAIYFTSGTTGAPKMVEHSQssyglGFVAGGRRWMA----LTESDIFWNTT---DTGWVKA 277
Cdd:PRK07867 138 AHRDAEPPF--RVADPDDLFMLIFTSGTSGDPKAVRCTH-----RKVASAGVMLAqrfgLGPDDVCYVSMplfHSNAVMA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 278 AWTLfsAWSNGACIFVHelPRVDAKTILNTLCRFPITTLCCV-PTLFRLLVQEDLTRYKFQCLRhCLTGGEALNPDVrDK 356
Cdd:PRK07867 211 GWAV--ALAAGASIALR--RKFSASGFLPDVRRYGATYANYVgKPLSYVLATPERPDDADNPLR-IVYGNEGAPGDI-AR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 357 WKSQTGLELHEGYGQSETVVICgnSRNSTIKSGSMGKASPpyDVQIVD-EEGNVLPPGK-------EGNIAV--RIKPTR 426
Cdd:PRK07867 285 FARRFGCVVVDGFGSTEGGVAI--TRTPDTPPGALGPLPP--GVAIVDpDTGTECPPAEdadgrllNADEAIgeLVNTAG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 427 PfCFFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPD 506
Cdd:PRK07867 361 P-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPD 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 507 PIRGEVVKAFIVLSPAyASHDPEALTRELqeHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK07867 440 PVVGDQVMAALVLAPG-AKFDPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSAEGV 506
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
88-571 |
2.28e-29 |
|
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: 120.74 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd17645 23 SLTYKQLNEKANQLARHLRG-KGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SdalapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrSGDSVAIYFTSGTTGAPK--MVEHSQSs 245
Cdd:cd17645 102 N---------------------------------------------------PDDLAYVIYTSGSTGLPKgvMIEHHNL- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 246 ygLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACifVHELP---RVDAKTiLNTLCRFPITTLCCVPTL 322
Cdd:cd17645 130 --VNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAA--LHVVPserRLDLDA-LNDYFNQEGITISFLPTG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 323 frllVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKsqtgleLHEGYGQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQ 401
Cdd:cd17645 205 ----AAEQFMQLDNQSLRVLLTGGDKLKKIERKGYK------LVNNYGPTEnTVVATSFEIDKPYANIPIGKPIDNTRVY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 402 IVDEEGNVLPPGKEGNIAVRIKPtrpfcFFNCYLDNPEKTAASEQGD-------FYITGDRAHMDEDGYFWFLGRNDDVI 474
Cdd:cd17645 275 ILDEALQLQPIGVAGELCIAGEG-----LARGYLNRPELTAEKFIVHpfvpgerMYRTGDLAKFLPDGNIEFLGRLDQQV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 475 NSSSYRIGPVEVESALAEHPAVLESAVVSSPDpirGEVVKAFIvlspAYASHDPEALTRELQEHVKTVTAPYKYPRKVAF 554
Cdd:cd17645 350 KIRGYRIEPGEIEPFLMNHPLIELAAVLAKED---ADGRKYLV----AYVTAPEEIPHEELREWLKNDLPDYMIPTYFVH 422
|
490
....*....|....*..
gi 26341010 555 ISELPKTVSGKILRSKL 571
Cdd:cd17645 423 LKALPLTANGKVDRKAL 439
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
210-573 |
3.35e-29 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 122.54 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 210 SPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGA 289
Cdd:PTZ00237 243 SPFYEYVPVESSHPLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 290 CIFVHE----LPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQED------LTRYKFQCLRHCLTGGEALNPDVRDKWKS 359
Cdd:PTZ00237 323 TFVMFEggiiKNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTDpeatiiRSKYDLSNLKEIWCGGEVIEESIPEYIEN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 360 QTGLELHEGYGQSE---TVVICGNSRNSTIKSgsMGKASPPYDVQIVDEEGNVLPPGKEGNIAvrIKPTRPFCFFNCYLD 436
Cdd:PTZ00237 403 KLKIKSSRGYGQTEigiTYLYCYGHINIPYNA--TGVPSIFIKPSILSEDGKELNVNEIGEVA--FKLPMPPSFATTFYK 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 437 NPE--KTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVK 514
Cdd:PTZ00237 479 NDEkfKQLFSKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPI 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26341010 515 AFIVLSPAYASH--DPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PTZ00237 559 GLLVLKQDQSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
80-574 |
4.29e-29 |
|
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: 121.24 E-value: 4.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 80 VNGSGTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPR----LPDWWlisvACMRTGVVMIPgvsqlTAKDLKY 155
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAP-----LTVPPTY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 156 RLQAARAKS------------IVTSDALAPQVDAISADCPSLQTKLLVSdtsrpgwinfrELLRAASPEHNCVRTRSGDS 223
Cdd:cd05906 101 DEPNARLRKlrhiwqllgspvVLTDAELVAEFAGLETLSGLPGIRVLSI-----------EELLDTAADHDLPQSRPDDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 224 VAIYFTSGTTGAPKMVEHSQSSYgLGFVAGGRRWMALTESDIFWNttdtgWVkaawtlfsAWSN-GACIFVHELP----- 297
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTHRNI-LARSAGKIQHNGLTPQDVFLN-----WV--------PLDHvGGLVELHLRAvylgc 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 298 -RVDAKT---------ILNTLCRFPITTLCCVPTLFRLLVQ--EDLTRYKFQ--CLRHCLTGGEALNpdvrdkwkSQTG- 362
Cdd:cd05906 236 qQVHVPTeeiladplrWLDLIDRYRVTITWAPNFAFALLNDllEEIEDGTWDlsSLRYLVNAGEAVV--------AKTIr 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 363 --LELHE-----------GYGQSETV-VICGNSRNSTIKSG------SMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRi 422
Cdd:cd05906 308 rlLRLLEpyglppdairpAFGMTETCsGVIYSRSFPTYDHSqalefvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 423 KPTRpfcfFNCYLDNPEKTAASEQGD-FYITGDRAHMDeDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLES-- 499
Cdd:cd05906 387 GPVV----TKGYYNNPEANAEAFTEDgWFRTGDLGFLD-NGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSft 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 500 AVVSSPDPIRGEVVKAfIVLSPAYASHDP-EALTRELQEHVK---TVTAPYKYP-RKvafiSELPKTVSGKILRSKLRNQ 574
Cdd:cd05906 462 AAFAVRDPGAETEELA-IFFVPEYDLQDAlSETLRAIRSVVSrevGVSPAYLIPlPK----EEIPKTSLGKIQRSKLKAA 536
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
86-572 |
6.54e-29 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 120.87 E-value: 6.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQS-RKAANVLEGvcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGV-----SQLTAkdlkYRLQ- 158
Cdd:PRK10946 46 ERQFSYRELNQASdNLACSLRRQ--GIKPGDTALVQLGNVAEFYITFFALLKLGVAPVNALfshqrSELNA----YASQi 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 159 ------AARAKSIVTSDALapqVDAISADCPSLQTKLLVSDTSRpgwinfRELLRA-ASPEHNCVRTRS-GDSVAIYFTS 230
Cdd:PRK10946 120 epalliADRQHALFSDDDF---LNTLVAEHSSLRVVLLLNDDGE------HSLDDAiNHPAEDFTATPSpADEVAFFQLS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 231 G-TTGAPKMV--EHSQSSYGLgfvaggRRwmaltESDIFWNTTDTGWVKA--AWTLFSAWSNGAC-IFVHELPRVDAKTI 304
Cdd:PRK10946 191 GgSTGTPKLIprTHNDYYYSV------RR-----SVEICGFTPQTRYLCAlpAAHNYPMSSPGALgVFLAGGTVVLAPDP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 305 LNTLCrFP------ITTLCCVP---TLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV 375
Cdd:PRK10946 260 SATLC-FPliekhqVNVTALVPpavSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAEGL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 376 VicgnsrNST-------IKSGSMGKA-SPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTrpfcfFNCYLDNPEKTAAS--E 445
Cdd:PRK10946 339 V------NYTrlddsdeRIFTTQGRPmSPDDEVWVADADGNPLPQGEVGRLMTRGPYT-----FRGYYKSPQHNASAfdA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 446 QGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYas 525
Cdd:PRK10946 408 NG-FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPL-- 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 26341010 526 hDPEALTRELQEHvktVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK10946 485 -KAVQLRRFLREQ---GIAEFKLPDRVECVDSLPLTAVGKVDKKQLR 527
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
90-571 |
9.62e-29 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 122.07 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK10252 485 SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTA 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDAISADCPSLQTKLLVSDTSRPgwinfrelLRAASPEHncvrtrsgdSVAIYFTSGTTGAPK--MVEHS----- 242
Cdd:PRK10252 564 DQLPRFADVPDLTSLCYNAPLAPQGAAP--------LQLSQPHH---------TAYIIFTSGSTGRPKgvMVGQTaivnr 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 243 ----QSSYGLgfvaggrrwmalTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV-----HELPRVDAKTIlntlCRFPI 313
Cdd:PRK10252 627 llwmQNHYPL------------TADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMaepeaHRDPLAMQQFF----AEYGV 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 314 TTLCCVPTLFRLLVQE---DLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVV------ICGNSRNS 384
Cdd:PRK10252 691 TTTHFVPSMLAAFVASltpEGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVdvswypAFGEELAA 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 385 TiKSGSMGKASPPYDVQ--IVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTA-------ASEQGDFYITGD 454
Cdd:PRK10252 771 V-RGSSVPIGYPVWNTGlrILDARMRPVPPGVAGDLYLTgIQLAQG------YLGRPDLTAsrfiadpFAPGERMYRTGD 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 455 RAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHP----AVLESAVVSSPDPIRGEVVK--AFIVlspayaSHDP 528
Cdd:PRK10252 844 VARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPdveqAVTHACVINQAAATGGDARQlvGYLV------SQSG 917
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 26341010 529 EALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK10252 918 LPLDTSaLQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL 961
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
205-571 |
1.15e-28 |
|
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: 118.89 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 205 LLRAASPEhnCVRTRSGDSVAIYFTSGTTGAPK--MVEHSqssyGL-GFVAGGRRWMALTESDIFWNTTDTGWVKAAWTL 281
Cdd:cd17652 79 MLADARPA--LLLTTPDNLAYVIYTSGSTGRPKgvVVTHR----GLaNLAAAQIAAFDVGPGSRVLQFASPSFDASVWEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 282 FSAWSNGACIFVhelprVDAKTIL------NTLCRFPITTLCCVPTLFRLLVQEDLTRykfqcLRHCLTGGEALNPDVRD 355
Cdd:cd17652 153 LMALLAGATLVL-----APAEELLpgeplaDLLREHRITHVTLPPAALAALPPDDLPD-----LRTLVVAGEACPAELVD 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 356 KWKsqTGLELHEGYGQSETVVicgnsrNSTIKSGSMGKASPP-------YDVQIVDEEGNVLPPGKEGNIAVR-IKPTRP 427
Cdd:cd17652 223 RWA--PGRRMINAYGPTETTV------CATMAGPLPGGGVPPigrpvpgTRVYVLDARLRPVPPGVPGELYIAgAGLARG 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 428 fcffncYLDNPEKTAASEQGD--------FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLES 499
Cdd:cd17652 295 ------YLNRPGLTAERFVADpfgapgsrMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEA 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26341010 500 AVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17652 369 VVVVRDDRPGDKRLVAYVVPAP-----GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
84-555 |
2.61e-28 |
|
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: 118.73 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAK 163
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAALRAL-GLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 164 SIVTS-----DALAPQVDAisadcpSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKM 238
Cdd:cd05932 81 ALFVGklddwKAMAPGVPE------GLISISLPPPSAANCQYQWDDLIAQHPPLEERPTRFPEQLATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 239 VEHSQSSYGLGFVAGGRRwMALTESD----------IFWNT-TDTGWVKAAWTLFSAWSNGAciFVHEL----------- 296
Cdd:cd05932 155 VMLTFGSFAWAAQAGIEH-IGTEENDrmlsylplahVTERVfVEGGSLYGGVLVAFAESLDT--FVEDVqrarptlffsv 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 297 PRVDAKTILNTLCRFP---ITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDkWKSQTGLELHEGYGQSE 373
Cdd:cd05932 232 PRLWTKFQQGVQDKIPqqkLNLLLKIPVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNILEAYGMTE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 374 TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEegnvlppgkeGNIAVRIKPTrpfcfFNCYLDNPEKTAASEQGD-FYIT 452
Cdd:cd05932 311 NFAYSHLNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPAL-----MMGYYKDPEATAEAFTADgFLRT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 453 GDRAHMDEDGYFWFLGRNDDVINSSSYR-IGPVEVESALAEHPAVLESAVVSS--PDPIRGEVVKAFIVLSPAYAshDPE 529
Cdd:cd05932 376 GDKGELDADGNLTITGRVKDIFKTSKGKyVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVLSEEARLRADAF--ARA 453
|
490 500
....*....|....*....|....*.
gi 26341010 530 ALTRELQEHVKTVTAPYKYPRKVAFI 555
Cdd:cd05932 454 ELEASLRAHLARVNSTLDSHEQLAGI 479
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
121-574 |
4.33e-28 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 117.99 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 121 LPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALA------PQVDAISADCPSLQTKLLVSDT 194
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 195 S-----RPGWINFRELLRAASP-------EHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSyGLGFVAGGRRWMALTE 262
Cdd:PLN03051 81 PvavplREQDLSWCDFLGVAAAqgsvggnEYSPVYAPVESVTNILFSSGTTGEPKAIPWTHLS-PLRCASDGWAHMDIQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 263 SDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHElprvdAKTILNTLCRF----PITTLCCVPTLFR--------LLVQED 330
Cdd:PLN03051 160 GDVVCWPTNLGWMMGPWLLYSAFLNGATLALYG-----GAPLGRGFGKFvqdaGVTVLGLVPSIVKawrhtgafAMEGLD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 331 LTRYKFQClrhclTGGEALNPDvRDKWKSQT------------GLELHEGYGQSETVVICGnsrNSTIKSGSMGKAsppy 398
Cdd:PLN03051 235 WSKLRVFA-----STGEASAVD-DVLWLSSVrgyykpvieycgGTELASGYISSTLLQPQA---PGAFSTASLGTR---- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 399 dVQIVDEEGNVLPPGKE--GNIAVRIkptrPFCFFNCYLDNPEKTAASEQG--DFYITGD--RAHMDE-----DGYFWFL 467
Cdd:PLN03051 302 -FVLLNDNGVPYPDDQPcvGEVALAP----PMLGASDRLLNADHDKVYYKGmpMYGSKGMplRRHGDImkrtpGGYFCVQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 468 GRNDDVINSSSYRIGPVEVESALAE-HPAVLESAVVSSPDPIRGE----VVKAFIVLSPAYASHDPEALTRELQEHVKTV 542
Cdd:PLN03051 377 GRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQEAIQTN 456
|
490 500 510
....*....|....*....|....*....|..
gi 26341010 543 TAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN03051 457 LNPLFKVSRVKIVPELPRNASNKLLRRVLRDQ 488
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
179-572 |
5.15e-28 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 118.41 E-value: 5.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 179 SADCPSLQTKLlvsdtsRPGWINFRELLRAASPEHNCVRTRSG-DSVAIYFTSGTTGAPK-MVEHSQSSYglgfvaggrr 256
Cdd:PLN02479 158 TCDPKSLQYAL------GKGAIEYEKFLETGDPEFAWKPPADEwQSIALGYTSGTTASPKgVVLHHRGAY---------- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 257 WMALTESdIFWNTTDtGWVkAAWTLFSAWSNGAC----IFVHE-----LPRVDAKTILNTLCRFPITTLCCVPTLFRLLV 327
Cdd:PLN02479 222 LMALSNA-LIWGMNE-GAV-YLWTLPMFHCNGWCftwtLAALCgtnicLRQVTAKAIYSAIANYGVTHFCAAPVVLNTIV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 328 Q--EDLTRYKFQCLRHCLTGGEALNPDVRDKWkSQTGLELHEGYGQSETV---VICG----------------NSRNSTI 386
Cdd:PLN02479 299 NapKSETILPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHTYGLSETYgpsTVCAwkpewdslppeeqarlNARQGVR 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 387 KSGSMGkasppydVQIVDEEGNVLPP--GKE-GNIAVRIKPTrpfcfFNCYLDNPEKTAASEQGDFYITGDRAHMDEDGY 463
Cdd:PLN02479 378 YIGLEG-------LDVVDTKTMKPVPadGKTmGEIVMRGNMV-----MKGYLKNPKANEEAFANGWFHSGDLGVKHPDGY 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 464 FWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVKTVT 543
Cdd:PLN02479 446 IEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLKPGVDKSDEAALAEDIMKFCRERL 525
|
410 420
....*....|....*....|....*....
gi 26341010 544 APYKYPRKVAFiSELPKTVSGKILRSKLR 572
Cdd:PLN02479 526 PAYWVPKSVVF-GPLPKTATGKIQKHVLR 553
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
86-568 |
1.14e-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: 116.00 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEgVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLK-INGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 VTSDalapqvdaisadcpslqtkllvsdtsrpgwinfrellraasPEhncvrtrsgDSVAIYFTSGTTGAPK--MVEHSQ 243
Cdd:cd05914 84 FVSD-----------------------------------------ED---------DVALINYTSGTTGNSKgvMLTYRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 244 SsygLGFVAGGRRWMALTESDIFWNTTDTGWV-KAAWTLFSAWSNGACI-FVHELPrvDAKTILNTLCRFPITTLCCVPT 321
Cdd:cd05914 114 I---VSNVDGVKEVVLLGKGDKILSILPLHHIyPLTFTLLLPLLNGAHVvFLDKIP--SAKIIALAFAQVTPTLGVPVPL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 322 LFR------LLVQEDLTRYKFQC------------------------LRHCLTGGEALNPDVRDKWKSqTGLELHEGYGQ 371
Cdd:cd05914 189 VIEkifkmdIIPKLTLKKFKFKLakkinnrkirklafkkvheafggnIKEFVIGGAKINPDVEEFLRT-IGFPYTIGYGM 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 372 SETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEgnvlPPGKEGNIAVRIKptrpfcffNC---YLDNPEKTAA--SEQ 446
Cdd:cd05914 268 TETAPIISYSPPNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGP--------NVmkgYYKNPEATAEafDKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 447 GDFYiTGDRAHMDEDGYFWFLGRNDDVINSSSYR-IGPVEVESALAEHPAVLESAVVsspdpIRGEVVKAFIVLSPAYA- 524
Cdd:cd05914 336 GWFH-TGDLGKIDAEGYLYIRGRKKEMIVLSSGKnIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPDFLd 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 26341010 525 ------SHDPEALTRELQEHVKTVTAPYKYPRKVAFI-SELPKTVSGKILR 568
Cdd:cd05914 410 vkalkqRNIIDAIKWEVRDKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
485-565 |
6.34e-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: 6.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 485 EVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSG 564
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 26341010 565 K 565
Cdd:pfam13193 76 K 76
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
114-571 |
7.54e-27 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 114.72 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 114 GDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI-------VTSDALAP---QVDAISADCP 183
Cdd:PRK05857 66 GSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAAlvapgskMASSAVPEalhSIPVIAVDIA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 184 SLQTKLLVS-DTSRPgwinfrellrAASPEHNcvrtrSGDSVAIYFTSGTTGAPKMVEHSQSSYglgFV------AGGRR 256
Cdd:PRK05857 146 AVTRESEHSlDAASL----------AGNADQG-----SEDPLAMIFTSGTTGEPKAVLLANRTF---FAvpdilqKEGLN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 257 WMALTESDIFWNTTDTGWVKAAWTLFSAWSNGA-CIFVHElprvDAKTILNTLCRFPITTLCCVPTLFRLLVQE-DLTRY 334
Cdd:PRK05857 208 WVTWVVGETTYSPLPATHIGGLWWILTCLMHGGlCVTGGE----NTTSLLEILTTNAVATTCLVPTLLSKLVSElKSANA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 335 KFQCLRHCLTGG-EALNPDVRdkWKSQTGLELHEGYGQSET--VVIC---GNSRNSTIKSGSMGKASPPYDVQIVDEEG- 407
Cdd:PRK05857 284 TVPSLRLVGYGGsRAIAADVR--FIEATGVRTAQVYGLSETgcTALClptDDGSIVKIEAGAVGRPYPGVDVYLAATDGi 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 408 -----NVLPPGKEGNIAVRiKPTRPFCFFNcyldNPEKTAASEQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIG 482
Cdd:PRK05857 362 gptapGAGPSASFGTLWIK-SPANMLGYWN----NPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 483 PVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTV 562
Cdd:PRK05857 437 PDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQ 516
|
....*....
gi 26341010 563 SGKILRSKL 571
Cdd:PRK05857 517 SGKVMRASL 525
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
90-571 |
2.13e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 115.05 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK12316 2030 SYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALapqvdaiSADCPsLQTKLLVSDTSRPGWInfrellrAASPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSYGL 248
Cdd:PRK12316 2109 HL-------LERLP-LPAGVARLPLDRDAEW-------ADYPDTAPAVQLAGENLAyVIYTSGSTGLPKGVAVSHGALVA 2173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 249 GFVAGGRRWmALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQ 328
Cdd:PRK12316 2174 HCQAAGERY-ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAE 2252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 329 EDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLE-LHEGYGQSETVVI-----CGNSRNSTIKSGSMGKASPPYDVQI 402
Cdd:PRK12316 2253 HAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTpllwkCRPQDPCGAAYVPIGRALGNRRAYI 2332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 403 VDEEGNVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFWFLGRNDDVI 474
Cdd:PRK12316 2333 LDADLNLLAPGMAGELYLGGE-----GLARGYLNRPGLTAerfvpdpfSASGERLYRTGDLARYRADGVVEYLGRIDHQV 2407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 475 NSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIVlsPAYASHDpeaLTRELQEHVKTVTAPYKYPRKVAF 554
Cdd:PRK12316 2408 KIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVV--PDDAAED---LLAELRAWLAARLPAYMVPAHWVV 2481
|
490
....*....|....*..
gi 26341010 555 ISELPKTVSGKILRSKL 571
Cdd:PRK12316 2482 LERLPLNPNGKLDRKAL 2498
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
88-574 |
2.33e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 113.26 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLprlpdwW------LISVACMRTGVVMIPGVSQLTAKDLKYRLQAAR 161
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAAL-GVEPGDRVGTLA------WngyrhlEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 162 AKSIVTSDALAPQVDAISADCPSLQTKLLVSDTSR-PG----WINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAP 236
Cdd:PRK07008 112 DRYVLFDLTFLPLVDALAPQCPNVKGWVAMTDAAHlPAgstpLLCYETLVGAQDGDYDWPRFDENQASSLCYTSGTTGNP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 237 KMVEHSQSSYGL-GFVAGGRRWMALTESDIFWNTTDTGWVKAaWTL-FSAWSNGaCIFVHELPRVDAKTILNTLCRFPIT 314
Cdd:PRK07008 192 KGALYSHRSTVLhAYGAALPDAMGLSARDAVLPVVPMFHVNA-WGLpYSAPLTG-AKLVLPGPDLDGKSLYELIEAERVT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 315 TLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSE-----TVVICGNSRNSTIKS 388
Cdd:PRK07008 270 FSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEmsplgTLCKLKWKHSQLPLD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 389 GSM------GKASPPYDVQIVDEEGNVLP-PGKE-GNIAVRikptRPFCffncyLDNPEKTAASEQGD-FYITGDRAHMD 459
Cdd:PRK07008 350 EQRkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVR----GPWV-----IDRYFRGDASPLVDgWFPTGDVATID 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 460 EDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYashdpeALTR-ELQEH 538
Cdd:PRK07008 421 ADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGA------EVTReELLAF 494
|
490 500 510
....*....|....*....|....*....|....*.
gi 26341010 539 VKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK07008 495 YEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLREQ 530
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
90-573 |
3.88e-26 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 112.57 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWW--LISVACMrtGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:PRK05620 40 TFAAIGARAAALAHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SDALAPQVDAISADCPSLQTKLLVSD-------TSRPGWI---NFRELLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPK 237
Cdd:PRK05620 118 DPRLAEQLGEILKECPCVRAVVFIGPsdadsaaAHMPEGIkvySYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 238 MVEHSQSSYGLgfvaggrRWMALTESDIFWNTTDTGWVKA-------AWTL-FSAWSNGACIFvheLPRVD------AKT 303
Cdd:PRK05620 198 GVVYSHRSLYL-------QSLSLRTTDSLAVTHGESFLCCvpiyhvlSWGVpLAAFMSGTPLV---FPGPDlsaptlAKI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 304 ILNTLCRfpitTLCCVPTLF-RLLVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSR 382
Cdd:PRK05620 268 IATAMPR----VAHGVPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSPVGTVAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 383 NSTIKSG--------SMGKASPPYDVQIVDeEGNVLPPG--KEGNIAVRiKPTRPFCFFNCylDNPEKTAAS-------- 444
Cdd:PRK05620 344 PPSGVSGearwayrvSQGRFPASLEYRIVN-DGQVMESTdrNEGEIQVR-GNWVTASYYHS--PTEEGGGAAstfrgedv 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 445 EQGD-------FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFI 517
Cdd:PRK05620 420 EDANdrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVT 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 26341010 518 VLSPAYashDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRN 573
Cdd:PRK05620 500 VLAPGI---EPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
215-566 |
2.19e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 111.55 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 215 CVRTRSGDSVA-IYFTSGTTGAPKMVEHSqssyglgfvagGRRWMALTE--SDIFwNTTDTGWVKAAWTLFSA------- 284
Cdd:PRK08633 775 YGPTFKPDDTAtIIFSSGSEGEPKGVMLS-----------HHNILSNIEqiSDVF-NLRNDDVILSSLPFFHSfgltvtl 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 285 W----SNGACIFvHELPrVDAKTILNTLCRFPITTLCCVPTLFRLLvqedlTRYK------FQCLRHCLTGGEALNPDVR 354
Cdd:PRK08633 843 WlpllEGIKVVY-HPDP-TDALGIAKLVAKHRATILLGTPTFLRLY-----LRNKklhplmFASLRLVVAGAEKLKPEVA 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 355 DKWKSQTGLELHEGYGQSETV-VICGNSRNSTI---------KSGSMGKASPPYDVQIVD-EEGNVLPPGKEGNIAVRiK 423
Cdd:PRK08633 916 DAFEEKFGIRILEGYGATETSpVASVNLPDVLAadfkrqtgsKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-G 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 424 PTRpfcfFNCYLDNPEKTAA----SEQGDFYITGDRAHMDEDGYFWFLGRnddviNSSSYRIG----PV-EVESALAE-- 492
Cdd:PRK08633 995 PQV----MKGYLGDPEKTAEvikdIDGIGWYVTGDKGHLDEDGFLTITDR-----YSRFAKIGgemvPLgAVEEELAKal 1065
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26341010 493 HPAVLESAVVSSPDPIRGEVvkafIVLSPAYASHDPEALTRELQEhvKTVTAPYKyPRKVAFISELPKTVSGKI 566
Cdd:PRK08633 1066 GGEEVVFAVTAVPDEKKGEK----LVVLHTCGAEDVEELKRAIKE--SGLPNLWK-PSRYFKVEALPLLGSGKL 1132
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
86-571 |
3.74e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 111.20 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:PRK12316 3080 EQRLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL 3158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 VTSDALA-PQVDAISADCPSLQTkllvsdtsrpgwinfrELLRAASPEhncVRTRSGDSVAIYFTSGTTGAPKMVEHSQS 244
Cdd:PRK12316 3159 LSQSHLRlPLAQGVQVLDLDRGD----------------ENYAEANPA---IRTMPENLAYVIYTSGSTGKPKGVGIRHS 3219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 245 SYGLgFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFP-ITTLCCVPTLF 323
Cdd:PRK12316 3220 ALSN-HLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEgVDVLHAYPSML 3298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 324 RLLVQEDLTRyKFQCLRHCLTGGEALNPDVRDKWKSqtGLELHEGYGQSETVVICGNSRNSTIKSGS--MGKASPPYDVQ 401
Cdd:PRK12316 3299 QAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQVFA--GLPLYNLYGPTEATITVTHWQCVEEGKDAvpIGRPIANRACY 3375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 402 IVDEEGNVLPPGKEGNIAV------RIKPTRPFCFFNCYLDNPektaASEQGDFYITGDRAHMDEDGYFWFLGRNDDVIN 475
Cdd:PRK12316 3376 ILDGSLEPVPVGALGELYLggeglaRGYHNRPGLTAERFVPDP----FVPGERLYRTGDLARYRADGVIEYIGRVDHQVK 3451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 476 SSSYRIGPVEVESALAEHPAVLESAVVSspdpIRGEVVKAFIVLSPAYAshdpeALTRELQEHVKTVTAPYKYPRKVAFI 555
Cdd:PRK12316 3452 IRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVVPEDEAG-----DLREALKAHLKASLPEYMVPAHLLFL 3522
|
490
....*....|....*.
gi 26341010 556 SELPKTVSGKILRSKL 571
Cdd:PRK12316 3523 ERMPLTPNGKLDRKAL 3538
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
90-571 |
3.91e-25 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 111.02 E-value: 3.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIAL-GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQS 1679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 ALAPQVDAISAdcpslqTKLLVSDTSRpGWInfrellrAASPEHNCVRTRSGDSVA--IYfTSGTTGAPKMVEHSQSSYG 247
Cdd:PRK12467 1680 HLQARLPLPDG------LRSLVLDQED-DWL-------EGYSDSNPAVNLAPQNLAyvIY-TSGSTGRPKGAGNRHGALV 1744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 248 LGFVAGgRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFV--HELPRvDAKTILNTLCRFPITTLCCVPTLFRL 325
Cdd:PRK12467 1745 NRLCAT-QEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIapPGAHR-DPEQLIQLIERQQVTTLHFVPSMLQQ 1822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 326 LVQEDLTRYKFQCLRHCLTGGEALNPDVRDKWKSQTG-LELHEGYGQSETVV-----ICGNSRNSTIKSGSMGKASPPYD 399
Cdd:PRK12467 1823 LLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVdvthwTCRRKDLEGRDSVPIGQPIANLS 1902
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 400 VQIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTA--------ASEQGDFYITGDRAHMDEDGYFW 465
Cdd:PRK12467 1903 TYILDASLNPVPIGVAGELYLggvglaR-----------GYLNRPALTAerfvadpfGTVGSRLYRTGDLARYRADGVIE 1971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 466 FLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGEVVKAFIVLSPA---YASHDPEALTRELQEHVKTV 542
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPglvDDDEAQVALRAILKNHLKAS 2050
|
490 500
....*....|....*....|....*....
gi 26341010 543 TAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK12467 2051 LPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
84-574 |
5.16e-25 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 109.07 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 84 GTEVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVL----PRLPDWWLIsvacMRTGVVMIPGVSQLTAKDLKYRLQA 159
Cdd:PRK06018 35 GPIVRTTYAQIHDRALKVSQALDRD-GIKLGDRVATIAwntwRHLEAWYGI----MGIGAICHTVNPRLFPEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 160 ARAKSIVTSDALAPQVDAISADCPSLQTKLLVSD------TSRPGWINFRELLRAASPEHNCVRTRSGDSVAIYFTSGTT 233
Cdd:PRK06018 110 AEDRVVITDLTFVPILEKIADKLPSVERYVVLTDaahmpqTTLKNAVAYEEWIAEADGDFAWKTFDENTAAGMCYTSGTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 234 GAPKMVEHSQSSYGL-GFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIfVHELPRVDAKTILNTLCRFP 312
Cdd:PRK06018 190 GDPKGVLYSHRSNVLhALMANNGDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKL-VMPGAKLDGASVYELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 313 ITTLCCVPTLFRLLVQE-DLTRYKFQCLRHCLTGGEALnPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSGSM 391
Cdd:PRK06018 269 VTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAALKPPFSKLP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 392 GKAS---------PPYDVQ--IVDEEGNVLP-PGKE-GNIAVRiKPTRPFCFFNCyldnpEKTAASEQGdFYITGDRAHM 458
Cdd:PRK06018 348 GDARldvlqkqgyPPFGVEmkITDDAGKELPwDGKTfGRLKVR-GPAVAAAYYRV-----DGEILDDDG-FFDTGDVATI 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 459 DEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPayashDPEALTRELQEH 538
Cdd:PRK06018 421 DAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKP-----GETATREEILKY 495
|
490 500 510
....*....|....*....|....*....|....*.
gi 26341010 539 VKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PRK06018 496 MDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
226-571 |
6.03e-25 |
|
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: 107.91 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 226 IYFTSGTTGAPK--MVEHSQSsygLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGAC-IFVHELPRVDAK 302
Cdd:cd17644 111 VIYTSGSTGKPKgvMIEHQSL---VNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATlVLRPEEMRSSLE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 303 TILNTLCRFPITTLCCVPTLFRLLVQEDL--TRYKFQCLRHCLTGGEALNPDVRDKWKSQTG--LELHEGYGQSE---TV 375
Cdd:cd17644 188 DFVQYIQQWQLTVLSLPPAYWHLLVLELLlsTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGnfIQLINVYGPTEatiAA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 376 VICGNSRNST--IKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIavRIKPTRpfcFFNCYLDNPEKTA---------AS 444
Cdd:cd17644 268 TVCRLTQLTErnITSVPIGRPIANTQVYILDENLQPVPVGVPGEL--HIGGVG---LARGYLNRPELTAekfishpfnSS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 445 EQGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlsPAYa 524
Cdd:cd17644 343 ESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIV--PHY- 419
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 26341010 525 shDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17644 420 --EESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-571 |
2.20e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 108.89 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 33 EVVATWEAislgrqpVPEYFNFAHDVLDVW-SQLEKTghrPPNPAFwwVNGsgtEVKWTFEELGKQSRKAANVLEGvCGL 111
Cdd:PRK12316 495 QLVEGWNA-------TAAEYPLQRGVHRLFeEQVERT---PEAPAL--AFG---EETLDYAELNRRANRLAHALIE-RGV 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 112 QPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVDaisadcpsLQTKLLV 191
Cdd:PRK12316 559 GPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLP--------LAAGVQV 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 192 SDTSRPG-WInfrellrAASPEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSyglgfVAGGRRWM----ALTESDI 265
Cdd:PRK12316 631 LDLDRPAaWL-------EGYSEENPGTELNPENLAyVIYTSGSTGKPKGAGNRHRA-----LSNRLCWMqqayGLGVGDT 698
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 266 FWNTTDTGWVKAAWTLFSAWSNGACIFV--HELPRvDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRykfQC--LRH 341
Cdd:PRK12316 699 VLQKTPFSFDVSVWEFFWPLMSGARLVVaaPGDHR-DPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA---SCtsLRR 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 342 CLTGGEALNPDVRDKW---KSQTGLELHegYGQSETV--VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEG 416
Cdd:PRK12316 775 IVCSGEALPADAQEQVfakLPQAGLYNL--YGPTEAAidVTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLG 852
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 417 NIAVRIKP-TRPfcffncYLDNPEKTA----ASEQGD---FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVES 488
Cdd:PRK12316 853 ELYLAGRGlARG------YHGRPGLTAerfvPSPFVAgerMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEA 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 489 ALAEHPAVLESAVVSspdpIRGEVVKAFIVLSpayashDPEALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:PRK12316 927 RLLEHPWVREAAVLA----VDGKQLVGYVVLE------SEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLD 996
|
....
gi 26341010 568 RSKL 571
Cdd:PRK12316 997 RKAL 1000
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
72-576 |
3.15e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 108.33 E-value: 3.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 72 PPNPAFWWVNGSgtevkWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAK 151
Cdd:PRK05691 1145 PERIALVWDGGS-----LDYAELHAQANRLAHYLRD-KGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAE 1218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 152 DLKYRLQAARAKSIVTSDAL---APQVDAISAdcpslqtkllvsdtsrpgwINFRELLRAASPEHNCVRTRSGDSVA-IY 227
Cdd:PRK05691 1219 RLAYMLADSGVELLLTQSHLlerLPQAEGVSA-------------------IALDSLHLDSWPSQAPGLHLHGDNLAyVI 1279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 228 FTSGTTGAPKMVEHSQSSyglgfVAGGRRWM----ALTESDIFWNTTDTGWVKAAWTLFSAWSNGaCIFVHELP--RVDA 301
Cdd:PRK05691 1280 YTSGSTGQPKGVGNTHAA-----LAERLQWMqatyALDDSDVLMQKAPISFDVSVWECFWPLITG-CRLVLAGPgeHRDP 1353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 302 KTILNTLCRFPITTLCCVPTLFRLLVQEDLTRykfQC--LRHCLTGGEALNPDVRDKWKSQ-TGLELHEGYGQSETVVic 378
Cdd:PRK05691 1354 QRIAELVQQYGVTTLHFVPPLLQLFIDEPLAA---ACtsLRRLFSGGEALPAELRNRVLQRlPQVQLHNRYGPTETAI-- 1428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 379 gnsrNSTIK--SGSMGKASP---PYD---VQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTAA------ 443
Cdd:PRK05691 1429 ----NVTHWqcQAEDGERSPigrPLGnvlCRVLDAELNLLPPGVAGELCIGgAGLARG------YLGRPALTAErfvpdp 1498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 444 -SEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVsspdpIRGEVVKAFIV--- 518
Cdd:PRK05691 1499 lGEDGArLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVL-----VREGAAGAQLVgyy 1573
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 26341010 519 LSPAYASHDPEALTRELQEHVKTvtapYKYPRKVAFISELPKTVSGKILRSKLRNQEW 576
Cdd:PRK05691 1574 TGEAGQEAEAERLKAALAAELPE----YMVPAQLIRLDQMPLGPSGKLDRRALPEPVW 1627
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
226-571 |
4.03e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 106.23 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 226 IYFTSGTTGAPKMVEHS-QSSYGLGFvaggrrWMALTESdifwNTTDTG-WVKAAWTLFSAW---------SNGACIFVH 294
Cdd:PRK13383 179 VLLTSGTTGKPKGVPRApQLRSAVGV------WVTILDR----TRLRTGsRISVAMPMFHGLglgmlmltiALGGTVLTH 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 295 ElpRVDAKTILNTLCRFPITTLCCVP-TLFRLLVQEDLTRYK--FQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQ 371
Cdd:PRK13383 249 R--HFDAEAALAQASLHRADAFTAVPvVLARILELPPRVRARnpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGS 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 372 SEtVVICGNSRNSTIKSG--SMGKASPPYDVQIVDEEGNVLPPGKEGNIAV--RIKPTRpfcffncYLDNPEKTAASEQG 447
Cdd:PRK13383 327 TE-VGIGALATPADLRDApeTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVggELAGTR-------YTDGGGKAVVDGMT 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 448 DfyiTGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyASHD 527
Cdd:PRK13383 399 S---TGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPG-SGVD 474
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 26341010 528 PEAltreLQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK13383 475 AAQ----LRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
86-573 |
6.92e-24 |
|
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: 104.75 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEgVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSI 165
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLR-SLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 166 VtsdalapqvdaisadcpslqtkllvsdtsrpgwinfrellraaspehncVRTRSGDSVAIYFTSGTTGAPK--MVEH-- 241
Cdd:cd17640 82 V-------------------------------------------------VENDSDDLATIIYTSGTTGNPKgvMLTHan 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 242 --SQSSYGLGFVAG--GRRWMALTESdifWNTTDtgwvKAAWTLFSAWSnGACIFVhelprvDAKTILNTLCRFPITTLC 317
Cdd:cd17640 113 llHQIRSLSDIVPPqpGDRFLSILPI---WHSYE----RSAEYFIFACG-CSQAYT------SIRTLKDDLKRVKPHYIV 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 318 CVPTLFRLL---VQEDLTRYKF------------QCLRHCLTGGEALNPDVrDKWKSQTGLELHEGYGQSETVVICGNSR 382
Cdd:cd17640 179 SVPRLWESLysgIQKQVSKSSPikqflflfflsgGIFKFGISGGGALPPHV-DTFFEAIGIEVLNGYGLTETSPVVSARR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 383 NSTIKSGSMGKASPPYDVQIVDEEGN-VLPPGKEGNIAVRIKPTrpfcfFNCYLDNPEKTAASEQGD-FYITGDRAHMDE 460
Cdd:cd17640 258 LKCNVRGSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQV-----MKGYYKNPEATSKVLDSDgWFNTGDLGWLTC 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 461 DGYFWFLGRNDDVIN-SSSYRIGPVEVESALAEHPaVLESAVVSSPDPIRgevVKAFIVlsPayashDPEALTRELQEhv 539
Cdd:cd17640 333 GGELVLTGRAKDTIVlSNGENVEPQPIEEALMRSP-FIEQIMVVGQDQKR---LGALIV--P-----NFEELEKWAKE-- 399
|
490 500 510
....*....|....*....|....*....|....
gi 26341010 540 ktvtapykypRKVAFISELPKTVSGKILRSKLRN 573
Cdd:cd17640 400 ----------SGVKLANDRSQLLASKKVLKLYKN 423
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
90-538 |
8.68e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 105.37 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMI---PGVSQltaKDLKYRLQAARAksiv 166
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPGMGI---KNLKQCLAEAQP---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 167 tsDALAPQVDAISADC------PSLQTKLLVSDTSRPGWINFRELLRAASP-EHNCVRTRSGDSVAIYFTSGTTGAPKMV 239
Cdd:PRK09274 115 --DAFIGIPKAHLARRlfgwgkPSVRRLVTVGGRLLWGGTTLATLLRDGAAaPFPMADLAPDDMAAILFTSGSTGTPKGV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 240 EHSQSSyglgFVAGGRrwmALTES-DIFWNTTDTgwvkAAWTLFSAWS---NGACIfvheLPRVDA--------KTILNT 307
Cdd:PRK09274 193 VYTHGM----FEAQIE---ALREDyGIEPGEIDL----PTFPLFALFGpalGMTSV----IPDMDPtrpatvdpAKLFAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 308 LCRFPITTLCCVPTLFRLLVQEDLTR-YKFQCLRHCLTGG------------EALNPDVrdkwksqtglELHEGYGQSET 374
Cdd:PRK09274 258 IERYGVTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGapvpiavierfrAMLPPDA----------EILTPYGATEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 375 VVIC--------GNSRNSTIKSGS--MGKASPPYDVQIVD---------EEGNVLPPGKEGNIAVRiKP--TRpfcffnC 433
Cdd:PRK09274 328 LPISsiesreilFATRAATDNGAGicVGRPVDGVEVRIIAisdapipewDDALRLATGEIGEIVVA-GPmvTR------S 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 434 YLDNPEKTAAS----EQGDFY-ITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPi 508
Cdd:PRK09274 401 YYNRPEATRLAkipdGQGDVWhRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVGVGVP- 479
|
490 500 510
....*....|....*....|....*....|
gi 26341010 509 rGEVVKAFIVLSPAYASHDPEALTRELQEH 538
Cdd:PRK09274 480 -GAQRPVLCVELEPGVACSKSALYQELRAL 508
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
211-571 |
1.42e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 102.93 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 211 PEHNCVRTRSGDSVA-IYFTSGTTGAPKMVEHSQSSyglgfVAGGRRWMA----LTESDIFWNTTDTGWVKAAWTLFSAW 285
Cdd:PRK12467 3226 SENNPSTRVMGENLAyVIYTSGSTGKPKGVGVRHGA-----LANHLCWIAeayeLDANDRVLLFMSFSFDGAQERFLWTL 3300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 286 SNGACIFVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQeDLTRYKFQCLRHCLTGGEALNPDVRDKWKS---QTG 362
Cdd:PRK12467 3301 ICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAE-DAGGADCASLDIYVFGGEAVPPAAFEQVKRklkPRG 3379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 363 LelHEGYGQSETVVI-----CGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAV------RIKPTRPFCFF 431
Cdd:PRK12467 3380 L--TNGYGPTEAVVTvtlwkCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIggvglaRGYHQRPSLTA 3457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 432 NCYLDNPEKTAAseqGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSpDPIRGE 511
Cdd:PRK12467 3458 ERFVADPFSGSG---GRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGK 3533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26341010 512 VVKAFIVLspayasHDP-EALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK12467 3534 QLVAYVVP------ADPqGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKAL 3588
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
88-571 |
1.52e-22 |
|
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: 101.01 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd17656 13 KLTYRELNERSNQLARFLREK-GVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 sdalapQVDAISADCPSLQTKLLVSDtsrpgwINFRELLRAASPEHNcvrtrSGDSVAIYFTSGTTGAPK--MVEHSQSs 245
Cdd:cd17656 92 ------QRHLKSKLSFNKSTILLEDP------SISQEDTSNIDYINN-----SDDLLYIIYTSGTTGKPKgvQLEHKNM- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 246 ygLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIF-VHELPRVDAKTILNTLCRFPITTLCCVPTLFR 324
Cdd:cd17656 154 --VNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYiIREETKRDVEQLFDLVKRHNIEVVFLPVAFLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 325 LLVQE-DLTRYKFQCLRHCLTGGEAL--NPDVRDKWKSQtGLELHEGYGQSETVVICGNSRNSTIKSGSM---GKASPPY 398
Cdd:cd17656 232 FIFSErEFINRFPTCVKHIITAGEQLviTNEFKEMLHEH-NVHLHNHYGPSETHVVTTYTINPEAEIPELppiGKPISNT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 399 DVQIVDEEGNVLPPGKEGNIAVR-IKPTRPfcffncYLDNPEKTAASEQGD-------FYITGDRAHMDEDGYFWFLGRN 470
Cdd:cd17656 311 WIYILDQEQQLQPQGIVGELYISgASVARG------YLNRQELTAEKFFPDpfdpnerMYRTGDLARYLPDGNIEFLGRA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 471 DDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYAshdpealTRELQEHVKTVTAPYKYPR 550
Cdd:cd17656 385 DHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN-------ISQLREYLAKQLPEYMIPS 457
|
490 500
....*....|....*....|.
gi 26341010 551 KVAFISELPKTVSGKILRSKL 571
Cdd:cd17656 458 FFVPLDQLPLTPNGKVDRKAL 478
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
80-572 |
3.41e-22 |
|
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: 100.20 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 80 VNGSGT--EVKWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRL 157
Cdd:cd05915 14 VSRLHTgeVHRTTYAEVYQRARRLMGGLRAL-GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 158 QAARAKSI-VTSDALApqvdaISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVR-TRSGDSVAIYFTSGTTGA 235
Cdd:cd05915 93 NHAEDKVLlFDPNLLP-----LVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVrVPERAACGMAYTTGTTGL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 236 PKMVEHSQSSYGLGFVAGG-RRWMALTESDIFWNTTD----TGWVkAAWTLFSAwsNGACIFVHELPrvDAKTILNTLCR 310
Cdd:cd05915 168 PKGVVYSHRALVLHSLAASlVDGTALSEKDVVLPVVPmfhvNAWC-LPYAATLV--GAKQVLPGPRL--DPASLVELFDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 311 FPITTLCCVPTLFRLLVQ-EDLTRYKFQCLRHCLTGGEAlNPDVRDKWKSQTGLELHEGYGQSE-----TVVICGNSRNS 384
Cdd:cd05915 243 EGVTFTAGVPTVWLALADyLESTGHRLKTLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTEtspvvVQNFVKSHLES 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 385 TIKSGSM------GKASPPYDVQIVDEEGNVLP-PGKegniAVRIKPTRPFCFFNCYLDNPEKTAASE-QGDFYITGDRA 456
Cdd:cd05915 322 LSEEEKLtlkaktGLPIPLVRLRVADEEGRPVPkDGK----ALGEVQLKGPWITGGYYGNEEATRSALtPDGFFRTGDIA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 457 HMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyashdpEALTRELQ 536
Cdd:cd05915 398 VWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGE------KPTPEELN 471
|
490 500 510
....*....|....*....|....*....|....*..
gi 26341010 537 EHVKTVTAPYKY-PRKVAFISELPKTVSGKILRSKLR 572
Cdd:cd05915 472 EHLLKAGFAKWQlPDAYVFAEEIPRTSAGKFLKRALR 508
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
205-571 |
4.22e-22 |
|
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: 99.47 E-value: 4.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 205 LLRAASPEHNCVRTRSGDSVAIyFTSGTTGAPKMVEHSQSSYgLGFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFSA 284
Cdd:cd17654 103 LSFTPEHRHFNIRTDECLAYVI-HTSGTTGTPKIVAVPHKCI-LPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 285 WSNGACIFV--HELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQEDLTRY---KFQCLRHCLTGGEALNPDVRDKWKS 359
Cdd:cd17654 181 LSSGATLLIvpTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTvlsATSSLRVLALGGEPFPSLVILSSWR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 360 QTGLELH--EGYGQSETvviCGNSRNSTIKSGSMGK--ASPPYD--VQIVDEEGNvlppgkEGNIAVRIKPTRPFCFFNC 433
Cdd:cd17654 261 GKGNRTRifNIYGITEV---SCWALAYKVPEEDSPVqlGSPLLGtvIEVRDQNGS------EGTGQVFLGGLNRVCILDD 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 434 YLDNPEktaaseqGDFYITGDRAHMdEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDpirgEVV 513
Cdd:cd17654 332 EVTVPK-------GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQ----QRL 399
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 26341010 514 KAFIVlspayashDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17654 400 IAFIV--------GESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
90-574 |
5.21e-22 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 100.54 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSD 169
Cdd:PLN03052 210 TLSELRSQVSRVANALDAL-GFEKGDAIAIDMPMNVHAVIIYLAIILAGCVVVSIADSFAPSEIATRLKISKAKAIFTQD 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 -----------------ALAPQVDAISADCPSLQTKLLVSDTSrpgWINFRELL--RAASPEHNCVRtRSGDSVA-IYFT 229
Cdd:PLN03052 289 vivrggksiplysrvveAKAPKAIVLPADGKSVRVKLREGDMS---WDDFLARAngLRRPDEYKAVE-QPVEAFTnILFS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 230 SGTTGAPKMVEHSQSSyglGFVAGGRRW--MALTESDIFWNTTDTGWVKAAWTLFSAWSNGACI--------------FV 293
Cdd:PLN03052 365 SGTTGEPKAIPWTQLT---PLRAAADAWahLDIRKGDIVCWPTNLGWMMGPWLVYASLLNGATLalyngsplgrgfakFV 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 294 HelprvDAKtilntlcrfpITTLCCVPTLFRLL----VQEDLTRYKFQCLRhclTGGEALNPDvRDKWKSQT-------- 361
Cdd:PLN03052 442 Q-----DAK----------VTMLGTVPSIVKTWkntnCMAGLDWSSIRCFG---STGEASSVD-DYLWLMSRagykpiie 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 362 ---GLELHEGYgqsetvvICGnsrnSTIKSGSMGKASPP---YDVQIVDEEGNVLPPGKEGNIAVRIKPTrpfcFFNC-- 433
Cdd:PLN03052 503 ycgGTELGGGF-------VTG----SLLQPQAFAAFSTPamgCKLFILDDSGNPYPDDAPCTGELALFPL----MFGAss 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 434 YLDNPEKTAASEQGDFYITGD--RAHMDE-----DGYFWFLGRNDDVINSSSYRIGPVEVESAL-AEHPAVLESAVVSSP 505
Cdd:PLN03052 568 TLLNADHYKVYFKGMPVFNGKilRRHGDIfertsGGYYRAHGRADDTMNLGGIKVSSVEIERVCnAADESVLETAAIGVP 647
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26341010 506 DPIRG--EVVKAFIVLSPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:PLN03052 648 PPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFKVSAVVIVPSFPRTASNKVMRRVLRQQ 718
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
41-567 |
3.82e-20 |
|
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: 94.26 E-value: 3.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 41 ISLGRQPVPEYF-----NFAHDVLdvwsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEGvCGLQPGD 115
Cdd:cd05943 54 VSGRIMPGARWFpgarlNYAENLL--------RHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRA-LGVKPGD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 116 RMMLVLPRLPDwwlISVACMRT--------------GVvmiPGVSQltakdlkyRLQAARAKSIVTSDA---------LA 172
Cdd:cd05943 125 RVAGYLPNIPE---AVVAMLATasigaiwsscspdfGV---PGVLD--------RFGQIEPKVLFAVDAytyngkrhdVR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 173 PQVDAISADCPSLQTKLLVSDTSRPGWINFRE----------LLRAASPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHS 242
Cdd:cd05943 191 EKVAELVKGLPSLLAVVVVPYTVAAGQPDLSKiakaltledfLATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIVHG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 243 qssyglgfvAGGRRWMALTE---------SD-IFWNTTdTGWVKAAWtLFSAWSNGACI----------FVHELPRVDAK 302
Cdd:cd05943 271 ---------AGGTLLQHLKEhilhcdlrpGDrLFYYTT-CGWMMWNW-LVSGLAVGATIvlydgspfypDTNALWDLADE 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 303 TilntlcrfPITTLCCVPTLFRLLVQEDL---TRYKFQCLRHCLTGGEALNPD----VRDKWKSqtGLELHEGYGQSETV 375
Cdd:cd05943 340 E--------GITVFGTSAKYLDALEKAGLkpaETHDLSSLRTILSTGSPLKPEsfdyVYDHIKP--DVLLASISGGTDII 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 376 -VICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFCFFNcyldnpeKTAASEQGDFYIT-- 452
Cdd:cd05943 410 sCFVGGNPLLPVYRGEIQCRGLGMAVEAFDEEGKPVWGEKGELVCTKPFPSMPVGFWN-------DPDGSRYRAAYFAky 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 453 ------GDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAyash 526
Cdd:cd05943 483 pgvwahGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG---- 558
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 26341010 527 dpEALTRELQEHVKTVTA----PYKYPRKVAFISELPKTVSGKIL 567
Cdd:cd05943 559 --VELDDELRKRIRSTIRsalsPRHVPAKIIAVPDIPRTLSGKKV 601
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
88-574 |
1.13e-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: 92.03 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVt 167
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 sdalapqVDAisadcpslqtkllvsdtsrpgwinfrellraaspehncvrtrsgdsvAIY-FTSGTTGAPK--MVEHSQS 244
Cdd:cd05940 81 -------VDA-----------------------------------------------ALYiYTSGTTGLPKaaIISHRRA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 245 SYGLGFVAGgrrWMALTESDIFWNTTD--------TGWVK---AAWTL-----FSA---WS----NGACIFVHelprvda 301
Cdd:cd05940 107 WRGGAFFAG---SGGALPSDVLYTCLPlyhstaliVGWSAclaSGATLvirkkFSAsnfWDdirkYQATIFQY------- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 302 ktiLNTLCRFpittLCCVPtlfrllvQEDLTRykfqclRHCLTG--GEALNPDVRDKWKSQTGL-ELHEGYGQSETVVIC 378
Cdd:cd05940 177 ---IGELCRY----LLNQP-------PKPTER------KHKVRMifGNGLRPDIWEEFKERFGVpRIAEFYAATEGNSGF 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 379 GN--------SRNSTIKSGSMGKASPPYDVQ----IVDEEGNV--LPPGKEGNIAVRIKPTRPFcffNCYLDNPEKTA-- 442
Cdd:cd05940 237 INffgkpgaiGRNPSLLRKVAPLALVKYDLEsgepIRDAEGRCikVPRGEPGLLISRINPLEPF---DGYTDPAATEKki 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 443 ---ASEQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV--VSSPDpIRGEVVKAF 516
Cdd:cd05940 314 lrdVFKKGDAWFnTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAA 392
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 26341010 517 IVLSPAYaSHDPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:cd05940 393 IVLQPNE-EFDLSALAAHLEKNL----PGYARPLFLRLQPEMEITGTFKQQKVDLRNE 445
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
157-571 |
2.42e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.92 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 157 LQAARAKSIVTSDAlAPqVDAISADCPSLQTKLL--VSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVA-IYFTSGTT 233
Cdd:PRK05691 3804 LPAQRLQRIIELSR-TP-VLVCSAACREQARALLdeLGCANRPRLLVWEEVQAGEVASHNPGIYSGPDNLAyVIYTSGST 3881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 234 GAPK--MVE-HSQSSYGLGFVAggrrWMALTESDIFWNTTDTGWVKAAWTLFSAWSNGAcifvhelpRVDakTILNTLCR 310
Cdd:PRK05691 3882 GLPKgvMVEqRGMLNNQLSKVP----YLALSEADVIAQTASQSFDISVWQFLAAPLFGA--------RVE--IVPNAIAH 3947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 311 FP-----------ITTLCCVPTLFRLLVQEDltRYKFQCLRHCLTGGEALNPDVRDKW-KSQTGLELHEGYGQSETV--- 375
Cdd:PRK05691 3948 DPqgllahvqaqgITVLESVPSLIQGMLAED--RQALDGLRWMLPTGEAMPPELARQWlQRYPQIGLVNAYGPAECSddv 4025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 376 ----VICGNSRNSTIKSGSmgkaspPYD---VQIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTA 442
Cdd:PRK05691 4026 affrVDLASTRGSYLPIGS------PTDnnrLYLLDEALELVPLGAVGELCVagtgvgR-----------GYVGDPLRTA 4088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 443 AS-------EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVK 514
Cdd:PRK05691 4089 LAfvphpfgAPGErLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGV-NGKHLV 4167
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 26341010 515 AFIVlsPAYASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK05691 4168 GYLV--PHQTVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
90-571 |
5.17e-19 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 89.83 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSd 169
Cdd:cd17650 14 TYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLLTQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 170 alapqvdaisadcpslqtkllvsdtsrpgwinfrellraasPEhncvrtrsgDSVAIYFTSGTTGAPK--MVEHS----- 242
Cdd:cd17650 92 -----------------------------------------PE---------DLAYVIYTSGTTGKPKgvMVEHRnvaha 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 243 ----QSSYGLGFVAGGRRWMALTESDIFwnttdtgwvkAAWTLFSAWSNGACIFVHELPRVDAKTILNTLCRFPITTLCC 318
Cdd:cd17650 122 ahawRREYELDSFPVRLLQMASFSFDVF----------AGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMES 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 319 VPTLFRLLVQE-DLTRYKFQCLRHCLTGGEAlnpdVRDKWKSQTGLELHEG------YGQSETVVICG---NSRNSTIKS 388
Cdd:cd17650 192 TPALIRPVMAYvYRNGLDLSAMRLLIVGSDG----CKAQDFKTLAARFGQGmriinsYGVTEATIDSTyyeEGRDPLGDS 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 389 GS--MGKASPPYDVQIVDEEGNVLPPGKEGNIAV------RikptrpfcffnCYLDNPEKTAA-------SEQGDFYITG 453
Cdd:cd17650 268 ANvpIGRPLPNTAMYVLDERLQPQPVGVAGELYIggagvaR-----------GYLNRPELTAErfvenpfAPGERMYRTG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 454 DRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEV-VKAFIVlspayASHDPEalT 532
Cdd:cd17650 337 DLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEArLCAYVV-----AAATLN--T 408
|
490 500 510
....*....|....*....|....*....|....*....
gi 26341010 533 RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17650 409 AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
89-538 |
5.38e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 90.70 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 89 WTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVV--MIPgvSQLTAKDLKYRLQAARAKSIV 166
Cdd:PRK08279 63 ISYAELNARANRYAHWAAAR-GVGKGDVVALLMENRPEYLAAWLGLAKLGAVvaLLN--TQQRGAVLAHSLNLVDAKHLI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 167 TSDALAPQVDAISADcPSLQTKLLVSD----TSRPGWINFRELLRAAsPEHNCVRTRS--GDSVAIY-FTSGTTGAPKMV 239
Cdd:PRK08279 140 VGEELVEAFEEARAD-LARPPRLWVAGgdtlDDPEGYEDLAAAAAGA-PTTNPASRSGvtAKDTAFYiYTSGTTGLPKAA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 240 EHSQssyglgfvaggRRWM----------ALTESDIFWNTT----DTGWVkAAWTlfSAWSNGACI----------FVHE 295
Cdd:PRK08279 218 VMSH-----------MRWLkamggfggllRLTPDDVLYCCLplyhNTGGT-VAWS--SVLAAGATLalrrkfsasrFWDD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 296 LPRVDAKTI--LNTLCRFpittLCCVPtlfrllVQEDLTRYKfqcLRHCLtgGEALNPDVRDKWKSQTGLE-LHEGYGQS 372
Cdd:PRK08279 284 VRRYRATAFqyIGELCRY----LLNQP------PKPTDRDHR---LRLMI--GNGLRPDIWDEFQQRFGIPrILEFYAAS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 373 ETVVICGNSRNstiKSGSMGKaSPP----------YDVQ----IVDEEGNVLP--PGKEGNIAVRIKPTRPfcfFNCYLD 436
Cdd:PRK08279 349 EGNVGFINVFN---FDGTVGR-VPLwlahpyaivkYDVDtgepVRDADGRCIKvkPGEVGLLIGRITDRGP---FDGYTD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 437 nPEKTAAS------EQGDFYI-TGDRAHMDEDGYFWFLGRNDDvinssSYR-----IGPVEVESALAEHPAVLESAV--V 502
Cdd:PRK08279 422 -PEASEKKilrdvfKKGDAWFnTGDLMRDDGFGHAQFVDRLGD-----TFRwkgenVATTEVENALSGFPGVEEAVVygV 495
|
490 500 510
....*....|....*....|....*....|....*.
gi 26341010 503 SSPDpIRGEVVKAFIVLSPAyASHDPEALTRELQEH 538
Cdd:PRK08279 496 EVPG-TDGRAGMAAIVLADG-AEFDLAALAAHLYER 529
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
86-566 |
8.52e-19 |
|
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: 89.38 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 86 EVKWTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRlPDWWLISV-ACMRTGVVMIPgvsqltakdlkyrlqaaraks 164
Cdd:cd17648 10 DKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIAIlAVWKAGAAYVP--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 165 ivtsdalapqvdaISADCPSLQTKLLVSDTSRPGWInfrellraaspehncvrTRSGDSVAIYFTSGTTGAPK--MVEHs 242
Cdd:cd17648 68 -------------IDPSYPDERIQFILEDTGARVVI-----------------TNSTDLAYAIYTSGTTGKPKgvLVEH- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 243 QSSYGLgFVAGGRRWMALTESDifwnttdtgwvkAAWTLFSAWsngacIFVHELPR-VDAKTILNTLCRFPITTLCCVPT 321
Cdd:cd17648 117 GSVVNL-RTSLSERYFGRDNGD------------EAVLFFSNY-----VFDFFVEQmTLALLNGQKLVVPPDEMRFDPDR 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 322 LFRLLVQEDLT----------RYKFQCLRH--CLTG-GEALNPDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTI-- 386
Cdd:cd17648 179 FYAYINREKVTylsgtpsvlqQYDLARLPHlkRVDAaGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDqr 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 387 KSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRikptrPFCFFNCYLDNPEKTA--------ASEQ-------GDFYI 451
Cdd:cd17648 259 FDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLG-----GDGVARGYLNRPELTAerflpnpfQTEQerargrnARLYK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 452 TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDP-IRGEVVKAFIVlspAYASHDPEA 530
Cdd:cd17648 334 TGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDAsQAQSRIQKYLV---GYYLPEPGH 410
|
490 500 510
....*....|....*....|....*....|....*..
gi 26341010 531 LTR-ELQEHVKTVTAPYKYPRKVAFISELPKTVSGKI 566
Cdd:cd17648 411 VPEsDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
88-522 |
3.32e-18 |
|
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: 87.86 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd17641 11 EFTWADYADRVRAFALGLLAL-GVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 SDAlaPQVD---AISADCPSLQtKLLVSDT------SRPGWINF---RELLRAASPEH-----NCVRTRSGDSVAIY-FT 229
Cdd:cd17641 90 EDE--EQVDkllEIADRIPSVR-YVIYCDPrgmrkyDDPRLISFedvVALGRALDRRDpglyeREVAAGKGEDVAVLcTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 230 SGTTGAPKMVEHSQSSYgLGFVAGGRRWMALTESDIFWNTTDTGWV-KAAWTLFSAWSNGACI-FVHEL----------- 296
Cdd:cd17641 167 SGTTGKPKLAMLSHGNF-LGHCAAYLAADPLGPGDEYVSVLPLPWIgEQMYSVGQALVCGFIVnFPEEPetmmedlreig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 297 -------PRV-------------DAKTILNTL-----------------CRFPITTLCCVPTLFRLLVQEDL-TRYKFQC 338
Cdd:cd17641 246 ptfvllpPRVwegiaadvrarmmDATPFKRFMfelgmklglraldrgkrGRPVSLWLRLASWLADALLFRPLrDRLGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 339 LRHCLTGGEALNPDVRDKWKSqTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIvDEEGNVLppgkegni 418
Cdd:cd17641 326 LRSAATGGAALGPDTFRFFHA-IGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRI-DEVGEIL-------- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 419 avrikpTRPFCFFNCYLDNPEKTAASEQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSS-SYRIGPVEVESALAEHPAV 496
Cdd:cd17641 396 ------VRSPGVFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTTSdGTRFSPQFIENKLKFSPYI 469
|
490 500
....*....|....*....|....*.
gi 26341010 497 LESAVVSSPDPIrgevVKAFIVLSPA 522
Cdd:cd17641 470 AEAVVLGAGRPY----LTAFICIDYA 491
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
226-568 |
1.20e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 85.47 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 226 IYFTSGTTGAPKMVEHSQS-------SYGLGFVAggrrwmaltesdifwNTTDTGWVKAAWT--------LFSAWSNGAC 290
Cdd:PRK08308 106 LQYSSGTTGEPKLIRRSWTeidreieAYNEALNC---------------EQDETPIVACPVThsyglicgVLAALTRGSK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 291 ifVHELPRVDAKTILNTLCRFPITTLCCVPTLFRLLVQedLTRYKFQcLRHCLTGGEALNPDVRDKWKSQTgLELHEGYG 370
Cdd:PRK08308 171 --PVIITNKNPKFALNILRNTPQHILYAVPLMLHILGR--LLPGTFQ-FHAVMTSGTPLPEAWFYKLRERT-TYMMQQYG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 371 QSET--VVICGNSRNStiksGSMGKASPPYDVQIVDEEGNvlpPGKegnIAVRIKptrpfcffncyldnpEKTAAseqgd 448
Cdd:PRK08308 245 CSEAgcVSICPDMKSH----LDLGNPLPHVSVSAGSDENA---PEE---IVVKMG---------------DKEIF----- 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 449 fyiTGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAfivlspAYASH-- 526
Cdd:PRK08308 295 ---TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKA------KVISHee 365
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 26341010 527 -DPEALTRELQEHVktvtAPYKYPRKVAFISELPKTVSGKILR 568
Cdd:PRK08308 366 iDPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSR 404
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
222-571 |
1.33e-17 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 85.72 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPKMVEHSQSSYgLGFVaggrRWM----ALTESDIFWNttdtgwvKA---------AW--TLFSaws 286
Cdd:PRK04813 144 DNYYIIFTSGTTGKPKGVQISHDNL-VSFT----NWMledfALPEGPQFLN-------QApysfdlsvmDLypTLAS--- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 287 nGACIFVheLPRV---DAKTILNTLCRFPITTLCCVPTLFRL-LVQEDLTRYKFQCLRHCLTGGEALnpdvrdkwKSQTG 362
Cdd:PRK04813 209 -GGTLVA--LPKDmtaNFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHFLFCGEEL--------PHKTA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 363 LELHE---------GYGQSETVV----------ICgnsrnSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVrIK 423
Cdd:PRK04813 278 KKLLErfpsatiynTYGPTEATVavtsieitdeML-----DQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVI-SG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 424 PtrpfCFFNCYLDNPEKTAA---SEQGD-FYITGDRAHMDeDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVlES 499
Cdd:PRK04813 352 P----SVSKGYLNNPEKTAEaffTFDGQpAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYV-ES 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26341010 500 AVVSspdPI-RGEVVK---AFIVLSPayasHDPE---ALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK04813 426 AVVV---PYnKDHKVQyliAYVVPKE----EDFErefELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
319-572 |
2.22e-17 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 84.66 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 319 VPTLFRLLVQEDLTRykFQCLRHCLTGGEALNPDVRDKWKsQTGLELHEGYGQSETVvicgnSRNSTIK-------SGSM 391
Cdd:PRK07445 214 VPTQLQRLLQLRPQW--LAQFRTILLGGAPAWPSLLEQAR-QLQLRLAPTYGMTETA-----SQIATLKpddflagNNSS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 392 GKASPPYDVQIVdeegnvlpPGKEGNIAVRIKPTrpfcFFNCYldnPEKTAASEqgdFYITGDRAHMDEDGYFWFLGRND 471
Cdd:PRK07445 286 GQVLPHAQITIP--------ANQTGNITIQAQSL----ALGYY---PQILDSQG---IFETDDLGYLDAQGYLHILGRNS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 472 DVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVlsPAYASHDPEaltrELQEHVKTVTAPYKYPRK 551
Cdd:PRK07445 348 QKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYV--PKDPSISLE----ELKTAIKDQLSPFKQPKH 421
|
250 260
....*....|....*....|.
gi 26341010 552 VAFISELPKTVSGKILRSKLR 572
Cdd:PRK07445 422 WIPVPQLPRNPQGKINRQQLQ 442
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
90-574 |
2.91e-17 |
|
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: 85.04 E-value: 2.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDW---WL------ISVACMRTgvvmipgvsQLTAKDLKYRLQAA 160
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFlwiWLglaklgCPVAFLNT---------NIRSKSLLHCFRCC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 161 RAKSIVTSDALapqVDAISADCPSLQTK-----LLVSDTSRPGWINFRELLRAASPEHNCVRTRSG---DSVAIY-FTSG 231
Cdd:cd05938 78 GAKVLVVAPEL---QEAVEEVLPALRADgvsvwYLSHTSNTEGVISLLDKVDAASDEPVPASLRAHvtiKSPALYiYTSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 232 TTGAPK--MVEHSQSSYGLGFVaggrRWMALTESDIFWNTTD-----------TGWVKAAWTL-----FSA---WSNgaC 290
Cdd:cd05938 155 TTGLPKaaRISHLRVLQCSGFL----SLCGVTADDVIYITLPlyhssgfllgiGGCIELGATCvlkpkFSAsqfWDD--C 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 291 ifvhELPRVDAKTILNTLCRFpittLCCVPTlfrllvQEDLTRYKFQclrhcLTGGEALNPDVRDKWKSQTG-LELHEGY 369
Cdd:cd05938 229 ----RKHNVTVIQYIGELLRY----LCNQPQ------SPNDRDHKVR-----LAIGNGLRADVWREFLRRFGpIRIREFY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 370 GQSEtvvicGN--SRNSTIKSGSMGKAS-------P----PYDVQ----IVDEEGNVLP--PGKEGNIAVRIKPTRPfcf 430
Cdd:cd05938 290 GSTE-----GNigFFNYTGKIGAVGRVSylykllfPfeliKFDVEkeepVRDAQGFCIPvaKGEPGLLVAKITQQSP--- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 431 FNCYLDNPEKTAAS------EQGDFYI-TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV-- 501
Cdd:cd05938 362 FLGYAGDKEQTEKKllrdvfKKGDVYFnTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVyg 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26341010 502 VSSPDpIRGEVVKAFIVLSPayashdPEALT-RELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:cd05938 442 VTVPG-HEGRIGMAAVKLKP------GHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEE 508
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
69-572 |
5.33e-17 |
|
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: 84.21 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 69 GHRPPNPAFWWVN-GSGTEVKWTFEELGKQSRKAANVLEGVCGlqPGDRMMLVLPRLPDWWLISVACMRTGVVMIPgVSQ 147
Cdd:cd05931 4 AARPDRPAYTFLDdEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVP-LPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 148 LTAKDLKYRLQA----ARAKSIVTSDALAPQVDAISADCPSLQTkllvsdtsrpGWINFRELLRAASPEHNCVRTRSGDS 223
Cdd:cd05931 81 PTPGRHAERLAAiladAGPRVVLTTAAALAAVRAFAASRPAAGT----------PRLLVVDLLPDTSAADWPPPSPDPDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 224 VA-IYFTSGTTGAPK--MVEH----SQssyglgFVAGGRRWMAltesdifwnttDTGWVKAAW-----------TLFSAW 285
Cdd:cd05931 151 IAyLQYTSGSTGTPKgvVVTHrnllAN------VRQIRRAYGL-----------DPGDVVVSWlplyhdmgligGLLTPL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 286 SNGACI-------FVHElPRvdakTILNTLCRFPITT---------LCCvptlfRLLVQEDLTRYKFQCLRHCLTGGEAL 349
Cdd:cd05931 214 YSGGPSvlmspaaFLRR-PL----RWLRLISRYRATIsaapnfaydLCV-----RRVRDEDLEGLDLSSWRVALNGAEPV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 350 NPDVRDKWK---SQTGLE---LHEGYGQSETVVI-----CGNSRNSTIKSG---------------------SMGKASPP 397
Cdd:cd05931 284 RPATLRRFAeafAPFGFRpeaFRPSYGLAEATLFvsggpPGTGPVVLRVDRdalagravavaaddpaarelvSCGRPLPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 398 YDVQIVDEEGN-VLPPGKEGNIAVRIKPTRPfcffnCYLDNPEKTAASEQ-------GDFYITGDRAHMDeDGYFWFLGR 469
Cdd:cd05931 364 QEVRIVDPETGrELPDGEVGEIWVRGPSVAS-----GYWGRPEATAETFGalaatdeGGWLRTGDLGFLH-DGELYITGR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 470 NDDVINSSSYRIGPVEVESALAEHPAVLES---AVVSSPDPIRGEVVkAFIVLSPAYASHDPEALTRELQEHVKT---VT 543
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATAEEAHPALRPgcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA 516
|
570 580 590
....*....|....*....|....*....|.
gi 26341010 544 apykyPRKVAFIS--ELPKTVSGKILRSKLR 572
Cdd:cd05931 517 -----PADVVLVRpgSIPRTSSGKIQRRACR 542
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
226-571 |
1.33e-15 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 80.98 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 226 IYfTSGTTGAPKMVEHSQSSYGLGFVAGGRRWmALTESDIFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRVDAKTIL 305
Cdd:PRK05691 2339 IY-TSGSTGKPKGVVVSHGEIAMHCQAVIERF-GMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEIC 2416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 306 NTLCRFPITTLCCVPTLFRLLVQEDLTRYKFQCLRHCLTGGEALNPD----VRDKWKSQtglELHEGYGQSETVVI---- 377
Cdd:PRK05691 2417 QLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEhlqrIRQAFAPQ---LFFNAYGPTETVVMplac 2493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 378 -CGNSRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPtrpfcFFNCYLDNPEKTA--------ASEQGD 448
Cdd:PRK05691 2494 lAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAG-----LAQGYHDRPGLTAerfvadpfAADGGR 2568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 449 FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLEsAVVSSPDPIRGEVVKAFIVLSPAYASHDP 528
Cdd:PRK05691 2569 LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVRE-AVVLALDTPSGKQLAGYLVSAVAGQDDEA 2647
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 26341010 529 EALTRE-LQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:PRK05691 2648 QAALREaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
88-574 |
3.51e-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: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 88 KWTFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVT 167
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 168 sDALAPQVDAISADCPSLQTKllvsdtsrpgwiNFRELLraaspehncvrtrsgdsVAIYfTSGTTGAPKMVEHSQSSYg 247
Cdd:cd05939 82 -NLLDPLLTQSSTEPPSQDDV------------NFRDKL-----------------FYIY-TSGTTGLPKAAVIVHSRY- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 248 LGFVAGGRRWMALTESDIFWNT-----TDTGWVKAAWTL-----------FSAwSNgaciFVHELPRVDAKTI--LNTLC 309
Cdd:cd05939 130 YRIAAGAYYAFGMRPEDVVYDClplyhSAGGIMGVGQALlhgstvvirkkFSA-SN----FWDDCVKYNCTIVqyIGEIC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 310 RFpittlccvptlfrLLVQEDLTRYKFQCLRhcLTGGEALNPDVRDKWKSQTGL-ELHEGYGQSEtvvicGNSR--NSTI 386
Cdd:cd05939 205 RY-------------LLAQPPSEEEQKHNVR--LAVGNGLRPQIWEQFVRRFGIpQIGEFYGATE-----GNSSlvNIDN 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 387 KSGSMGKAS--PP--YDVQIV-----------DEEGNVLP--PGKEGNIAVRIKPTRPFCFFNCYLD---NPEKTAAS-- 444
Cdd:cd05939 265 HVGACGFNSriLPsvYPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNegaTNKKIARDvf 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 445 EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAV--VSSPDpIRGEVVKAFIVlSP 521
Cdd:cd05939 345 KKGDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIV-DP 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 26341010 522 AyASHDPEALTRELQEhvktVTAPYKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:cd05939 423 E-RKVDLDRFSAVLAK----SLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
343-572 |
2.04e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.08 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 343 LTGGEALNPDVRDKwKSQTGLELHEGYGQSETvviCGnsrnstiksGSM--GKASPPYDVQIVDEE----GNVLPPGkeg 416
Cdd:PRK07824 157 LVGGGPAPAPVLDA-AAAAGINVVRTYGMSET---SG---------GCVydGVPLDGVRVRVEDGRialgGPTLAKG--- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 417 niavrikptrpfcffncYLDNPEKTAASEQGDFyITGDRAHMDeDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAV 496
Cdd:PRK07824 221 -----------------YRNPVDPDPFAEPGWF-RTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAV 281
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26341010 497 LESAVVSSPDPIRGEVVKAFIVlspayASHDPEALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKLR 572
Cdd:PRK07824 282 ADCAVFGLPDDRLGQRVVAAVV-----GDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
112-565 |
2.20e-13 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 73.21 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 112 QPGDRMMLVLPRLPdwwlISVACMrTGVVM---IPGVSQLTA--KDLKYRLQAARAKSIVTSDA---------LAPQVDA 177
Cdd:PRK08043 253 VEGERIGLMLPNAT----ISAAVI-FGASLrrrIPAMMNYTAgvKGLTSAITAAEIKTIFTSRQfldkgklwhLPEQLTQ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 178 IS-------ADCPSLQTKLlvsdtsrpgWInFRELLraaSPEHNCVRTRSGDSVAIYFTSGTTGAPKMVEHSQSSYgLGF 250
Cdd:PRK08043 328 VRwvyledlKDDVTTADKL---------WI-FAHLL---MPRLAQVKQQPEDAALILFTSGSEGHPKGVVHSHKSL-LAN 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 251 VAGGRRWMALTESDIFwnttdtgwvKAAWTLFSAWS----------NGACIFVHELP---RVDAKTILNTLCrfpiTTLC 317
Cdd:PRK08043 394 VEQIKTIADFTPNDRF---------MSALPLFHSFGltvglftpllTGAEVFLYPSPlhyRIVPELVYDRNC----TVLF 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 318 CVPTLFrllvqEDLTR----YKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNSRNSTiKSGSMG 392
Cdd:PRK08043 461 GTSTFL-----GNYARfanpYDFARLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECApVVSINVPMAA-KPGTVG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 393 KASPPYDVQIVD----EEGNVLPPgKEGNIavrikptrpfcfFNCYL--DNPEK----TAASEQGD----FYITGDRAHM 458
Cdd:PRK08043 535 RILPGMDARLLSvpgiEQGGRLQL-KGPNI------------MNGYLrvEKPGVlevpTAENARGEmergWYDTGDIVRF 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 459 DEDGYFWFLGRNDDVINSSSYRIGPVEVES-ALAEHPAVLESAVVSSpDPIRGEVVKAFivlspayaSHDPEaLTRE-LQ 536
Cdd:PRK08043 602 DEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKS-DASKGEALVLF--------TTDSE-LTREkLQ 671
|
490 500 510
....*....|....*....|....*....|
gi 26341010 537 EHVKTVTAP-YKYPRKVAFISELPKTVSGK 565
Cdd:PRK08043 672 QYAREHGVPeLAVPRDIRYLKQLPLLGSGK 701
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
324-574 |
3.08e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 72.34 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 324 RLLVQEDLTRYKFQCLRHCLTGGEALNP-DVRDKWKSQTGLELHEG-----YGQSETVVI-----CGN------------ 380
Cdd:PRK07768 263 RLRRQAKPGAFDLSSLRFALNGAEPIDPaDVEDLLDAGARFGLRPEailpaYGMAEATLAvsfspCGAglvvdevdadll 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 381 ---------SRNSTIKSGSMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPFcffncYLDNPEKTAASEQGDFYI 451
Cdd:PRK07768 343 aalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPG-----YLTMDGFIPAQDADGWLD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 452 TGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPiRGEVVKAFIVLSPAYASHDPEAL 531
Cdd:PRK07768 418 TGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAEV 496
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 26341010 532 TRELQEHVKTVTAPYKY-PRKVAFIS--ELPKTVSGKILRSKLRNQ 574
Cdd:PRK07768 497 RRIRHQVAHEVVAEVGVrPRNVVVLGpgSIPKTPSGKLRRANAAEL 542
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
90-502 |
6.29e-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: 67.87 E-value: 6.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMI---PGvsqLTAKDLKYRLQAAraksiv 166
Cdd:cd05910 4 SFRELDERSDRIAQGLTAY-GIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVlidPG---MGRKNLKQCLQEA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 167 tsdalAPQvdaisadcpslqtkllvsdtsrpGWINFrellraaspehncvrTRSGDSVAIYFTSGTTGAPKMVEHSQSSY 246
Cdd:cd05910 74 -----EPD-----------------------AFIGI---------------PKADEPAAILFTSGSTGTPKGVVYRHGTF 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 247 G---------LGFVAGGRrwmaltesDIfwnttdtgwvkAAWTLFSAWsNGACIFVHELP--------RVDAKTILNTLC 309
Cdd:cd05910 111 AaqidalrqlYGIRPGEV--------DL-----------ATFPLFALF-GPALGLTSVIPdmdptrpaRADPQKLVGAIR 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 310 RFPITTLCCVPTLFRLLvqedlTRY------KFQCLRHCLTGGEALNPDVRDKWKS--QTGLELHEGYGQSETVVICGNS 381
Cdd:cd05910 171 QYGVSIVFGSPALLERV-----ARYcaqhgiTLPSLRRVLSAGAPVPIALAARLRKmlSDEAEILTPYGATEALPVSSIG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 382 RNSTIKSGS----------MGKASPPYDVQIV--DEEG-------NVLPPGKEGNIAVRIKPTRPfcffnCYLDNPEKTA 442
Cdd:cd05910 246 SRELLATTTaatsggagtcVGRPIPGVRVRIIeiDDEPiaewddtLELPRGEIGEITVTGPTVTP-----TYVNRPVATA 320
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26341010 443 ASE-----QGDFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVV 502
Cdd:cd05910 321 LAKiddnsEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALV 385
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
53-567 |
6.47e-12 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 68.28 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 53 NFAHDVLdvwsqlekTGHRPPNPAFWWVNGSGTEVKWTFEELGKQSRKAANVLEgVCGLQPGDRMMLVLPRLPDWWLISV 132
Cdd:PRK03584 87 NYAENLL--------RHRRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALR-ALGVGPGDRVAAYLPNIPETVVAML 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 133 ACMRTGVVM--------IPGV----SQLTAKDL----KYRLQAaraKSIVTSDALApqvdAISADCPSLQTKLLVSDTSR 196
Cdd:PRK03584 158 ATASLGAIWsscspdfgVQGVldrfGQIEPKVLiavdGYRYGG---KAFDRRAKVA----ELRAALPSLEHVVVVPYLGP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 197 PG----------WINFRELLRAASPEhnCVRTRSGDSVAIYFTSGTTGAPKMVEHSqssyglgfvAGG---------RRW 257
Cdd:PRK03584 231 AAaaaalpgallWEDFLAPAEAAELE--FEPVPFDHPLWILYSSGTTGLPKCIVHG---------HGGillehlkelGLH 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 258 MALTESD-IFWNTTdTGWVKAAWtLFSAWSNGACIFVHE----LPRVDAktilntlcrfpittlccvptLFRLLVQEDLT 332
Cdd:PRK03584 300 CDLGPGDrFFWYTT-CGWMMWNW-LVSGLLVGATLVLYDgspfYPDPNV--------------------LWDLAAEEGVT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 333 ---------------------RYKFQCLRHCLTGGEALNPD----VRDKWKSqtGLELHEGYGQSEtVVIC--GNSRNST 385
Cdd:PRK03584 358 vfgtsakyldacekaglvpgeTHDLSALRTIGSTGSPLPPEgfdwVYEHVKA--DVWLASISGGTD-ICSCfvGGNPLLP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 386 IKSGSMGKASPPYDVQIVDEEGN-VLppGKEGNIAVrikpTRPF-----CFFNcyldnpektaaSEQGDFYIT------- 452
Cdd:PRK03584 435 VYRGEIQCRGLGMAVEAWDEDGRpVV--GEVGELVC----TKPFpsmplGFWN-----------DPDGSRYRDayfdtfp 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 453 -----GDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYASHD 527
Cdd:PRK03584 498 gvwrhGDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDD 577
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 26341010 528 peALTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKIL 567
Cdd:PRK03584 578 --ALRARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKKV 615
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
90-534 |
2.05e-11 |
|
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: 66.69 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 90 TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPgVS---QLTAKDLKyRLQAARAK--- 163
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDL-GLSAERPLLILSGNSIEHALMALAAMYAGVPAAP-VSpaySLMSQDLA-KLKHLFELlkp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 164 SIVTSDALAPQVDAISADCPsLQTKLLVSDTSRPG--WINFRELL----RAASPEhncVRTRSG-DSVAIY-FTSGTTGA 235
Cdd:cd05921 104 GLVFAQDAAPFARALAAIFP-LGTPLVVSRNAVAGrgAISFAELAatppTAAVDA---AFAAVGpDTVAKFlFTSGSTGL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 236 PKMVEHSQSSYGLGFVAGGRRWMALTESD------IFWNTTDTGWVKAAWTLFsawsNGACIFVHE---LPRVDAKTILN 306
Cdd:cd05921 180 PKAVINTQRMLCANQAMLEQTYPFFGEEPpvlvdwLPWNHTFGGNHNFNLVLY----NGGTLYIDDgkpMPGGFEETLRN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 307 tLCRFPITTLCCVPTLFRLLVQ-----EDLTRYKFQCLRHCLTGGEALNPDVRDKWKS----QTG--LELHEGYGQSETV 375
Cdd:cd05921 256 -LREISPTVYFNVPAGWEMLVAalekdEALRRRFFKRLKLMFYAGAGLSQDVWDRLQAlavaTVGerIPMMAGLGATETA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 376 VICGNSRNSTIKSGSMGKASPPYDVQIVdeegnvlPPGkeGNIAVRIK-PTrpfcFFNCYLDNPEKTAAS--EQGdFYIT 452
Cdd:cd05921 335 PTATFTHWPTERSGLIGLPAPGTELKLV-------PSG--GKYEVRVKgPN----VTPGYWRQPELTAQAfdEEG-FYCL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 453 GDRAHM----DEDGYFWFLGR--NDDVINSSSY-RIGPVEVESALAEHPAVLEsAVVSSPDpirGEVVKAFIV------- 518
Cdd:cd05921 401 GDAAKLadpdDPAKGLVFDGRvaEDFKLASGTWvSVGPLRARAVAACAPLVHD-AVVAGED---RAEVGALVFpdllacr 476
|
490
....*....|....*..
gi 26341010 519 -LSPAYASHDPEALTRE 534
Cdd:cd05921 477 rLVGLQEASDAEVLRHA 493
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
334-566 |
4.92e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 65.76 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 334 YKFQCLRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETV-VICGNS--RNstiKSGSMGKASPPYD-----VQIVDE 405
Cdd:PRK06814 904 YDFRSLRYVFAGAEKVKEETRQTWMEKFGIRILEGYGVTETApVIALNTpmHN---KAGTVGRLLPGIEyrlepVPGIDE 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 406 EGNVLPPGKegNIAVRikptrpfcffncYL--DNPEKTAASEQGdFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGP 483
Cdd:PRK06814 981 GGRLFVRGP--NVMLG------------YLraENPGVLEPPADG-WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISL 1045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 484 VEVESALAEHPAVLESAVVSSPDPIRGEVvkafIVLSPayashDPEALTRE-LQEHVKTVTAPYKY-PRKVAFISELPKT 561
Cdd:PRK06814 1046 AAVEELAAELWPDALHAAVSIPDARKGER----IILLT-----TASDATRAaFLAHAKAAGASELMvPAEIITIDEIPLL 1116
|
....*
gi 26341010 562 VSGKI 566
Cdd:PRK06814 1117 GTGKI 1121
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
346-576 |
4.80e-10 |
|
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: 62.06 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 346 GEALNPDVRDKWKSQTGL-ELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYD---------VQIVDEEGNVL----- 410
Cdd:cd05937 209 GNGLRPDIWERFRERFNVpEIGEFYAATEGVFALTNHNVGDFGAGAIGHHGLIRRwkfenqvvlVKMDPETDDPIrdpkt 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 411 ------PPGKEGNIAVRIkPTRPFCFFNCYLDNPEKTAAS------EQGD-FYITGDRAHMDEDGYFWFLGRNDDVINSS 477
Cdd:cd05937 289 gfcvraPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESKlvrdvfRKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 478 SYRIGPVEVESALAEHPAVLESAVVSSPDP-IRGEVVKAFIVLSPAYASHDPEALTReLQEHVKTVTAPYKYPRKVAFIS 556
Cdd:cd05937 368 SENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITLEESSAVPTEFTKSL-LASLARKNLPSYAVPLFLRLTE 446
|
250 260
....*....|....*....|
gi 26341010 557 ELPKTVSGKILRSKLRNQEW 576
Cdd:cd05937 447 EVATTDNHKQQKGVLRDEGV 466
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
351-574 |
1.04e-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: 60.97 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 351 PDVRDKWKSQTGLELHEGYGQSETVVICGNSRNSTIKSgsMGKASPPYDVQIVDEEGNVLPPGKEGNIAVRIKPTRPfcf 430
Cdd:cd05908 278 PKAQSPFKTITLGRRHVTHGEPEPEVDKKDSECLTFVE--VGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP--- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 431 fnCYLDNPEKTAA--SEQGdFYITGDRAHMdEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLESAVVS---SP 505
Cdd:cd05908 353 --GYYNNPEATAKvfTDDG-WLKTGDLGFI-RNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNN 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26341010 506 DPIRGEVVKAFIVlsPAYASHDPEALTRELQEHVKTVTApyKYPRKVAFISELPKTVSGKILRSKLRNQ 574
Cdd:cd05908 429 SNTRNEEIFCFIE--HRKSEDDFYPLGKKIKKHLNKRGG--WQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
392-573 |
8.27e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.09 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 392 GKASPPYDVQIVDEEGNVLPPGKEGNIAVRiKPTrpfcFFNCYLDNPEKTAASEQGDFYITGDRAHMdEDGYFWFLGRND 471
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GPS----LMSGYFRDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 472 DVINSSSYRIGPVEVESALAEHPAVL--ESAVVSSPDPIRGEVVkafiVLSPAYAShDPE---ALTRELQEHVKTVTApy 546
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIV----LLVQCRIS-DEErrgQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*....
gi 26341010 547 kYPRKVAFIS--ELPKTVSGKILRSKLRN 573
Cdd:PRK09192 535 -VEAAVELVPphSLPRTSSGKLSRAKAKK 562
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
222-493 |
6.81e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 55.21 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 222 DSVAIYFTSGTTGAPKMVEHSQSSyglgFVAGGRRWMAltesdiFWNTTDTGWVKAAWTLFSAWSNGACIFVHELPRV-- 299
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHAN----LLANQRACLK------FFSPKEDDVMMSFLPPFHAYGFNSCTLFPLLSGVpv 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 300 -------DAKTILNTLCRFPITTLCCVPTLFRLLvqedLTRYKFQ-----CLRHCLTGGEALNPDVRDK-WKSQTGLELH 366
Cdd:PRK06334 254 vfaynplYPKKIVEMIDEAKVTFLGSTPVFFDYI----LKTAKKQesclpSLRFVVIGGDAFKDSLYQEaLKTFPHIQLR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 367 EGYGQSE-TVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNV-LPPGKEGNIAvrikpTRPFCFFNCYLDNPEKTAAS 444
Cdd:PRK06334 330 QGYGTTEcSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVL-----TRGTSLFSGYLGEDFGQGFV 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 26341010 445 EQG--DFYITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEH 493
Cdd:PRK06334 405 ELGgeTWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
209-543 |
2.36e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 53.23 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 209 ASPEHNCVRtrsgdsvaIYFTSGTTGAPKMVEHSQSSYGL--GFVAGGRRWMALTESDIFWNTTDTGWVKAAWTLFS-AW 285
Cdd:COG1541 79 AVPLEEIVR--------IHASSGTTGKPTVVGYTRKDLDRwaELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYgAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 286 SNGACIFVHELprVDAKTILNTLCRFPITTLCCVPTLFRLLVQE------DLTRYKfqcLRHCLTGGEALNPDVRDKWKS 359
Cdd:COG1541 151 RLGATVIPAGG--GNTERQLRLMQDFGPTVLVGTPSYLLYLAEVaeeegiDPRDLS---LKKGIFGGEPWSEEMRKEIEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 360 QTGLELHEGYGQSETVVICGNSrnstiksgsmgkaSPPYD----------VQIVDEE-GNVLPPGKEGNIAVrikptrpf 428
Cdd:COG1541 226 RWGIKAYDIYGLTEVGPGVAYE-------------CEAQDglhiwedhflVEIIDPEtGEPVPEGEEGELVV-------- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 429 cffncyldnpekTAASEQGdF----YITGDRAHMDED-----------GYfwFLGRNDDVInssSYR---IGPVEVESAL 490
Cdd:COG1541 285 ------------TTLTKEA-MplirYRTGDLTRLLPEpcpcgrthpriGR--ILGRADDML---IIRgvnVFPSQIEEVL 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 26341010 491 AEHPAVLESAVVSSPDPIRGEVVKAFIVLSPAYashDPEALTRELQEHVKTVT 543
Cdd:COG1541 347 LRIPEVGPEYQIVVDREGGLDELTVRVELAPGA---SLEALAEAIAAALKAVL 396
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
125-462 |
3.60e-07 |
|
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: 52.99 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 125 PDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALApqvdaisadcpslqtklLVSdtsrpgWINFRE 204
Cdd:cd05927 43 PEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAGVK-----------------VYS------LEEFEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 205 LLRAA-------SPEHNCVrtrsgdsvaIYFTSGTTGAPKMVEHSQSSyglgFVAGGRRWMALTESDIFWNTTDTgwvka 277
Cdd:cd05927 100 LGKKNkvpppppKPEDLAT---------ICYTSGTTGNPKGVMLTHGN----IVSNVAGVFKILEILNKINPTDV----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 278 awtLFS---------------AWSNGACIFVHelpRVDAKTILNTLCRFPITTLCCVPTLF-RLL------VQED--LTR 333
Cdd:cd05927 162 ---YISylplahifervvealFLYHGAKIGFY---SGDIRLLLDDIKALKPTVFPGVPRVLnRIYdkifnkVQAKgpLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 334 --------YKFQCLRH---------------------------CLTGGEALNPDVRDKWKSQTGLELHEGYGQSETVVIC 378
Cdd:cd05927 236 klfnfalnYKLAELRSgvvraspfwdklvfnkikqalggnvrlMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 379 GNSRNSTIKSGSMGKASPPYDVQIVD-EEGN--VLPPGKEGNIAVRikptrPFCFFNCYLDNPEKTA-ASEQGDFYITGD 454
Cdd:cd05927 316 TLTLPGDTSVGHVGGPLPCAEVKLVDvPEMNydAKDPNPRGEVCIR-----GPNVFSGYYKDPEKTAeALDEDGWLHTGD 390
|
....*...
gi 26341010 455 RAHMDEDG 462
Cdd:cd05927 391 IGEWLPNG 398
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
81-454 |
5.89e-07 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 52.57 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 81 NGSGTEVKWTFEELGKQSRKAANVLEGvCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPgVS---QLTAKD---LK 154
Cdd:PRK08180 62 GADGGWRRLTYAEALERVRAIAQALLD-RGLSAERPLMILSGNSIEHALLALAAMYAGVPYAP-VSpaySLVSQDfgkLR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 155 YRLQAARAKSIVTSDAlAPQVDAISADCPsLQTKLLVSDTSRPG--WINFRELL-----RAASPEHNCVRtrsGDSVAIY 227
Cdd:PRK08180 140 HVLELLTPGLVFADDG-AAFARALAAVVP-ADVEVVAVRGAVPGraATPFAALLatpptAAVDAAHAAVG---PDTIAKF 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 228 -FTSGTTGAPKMVEHSQSSYGLGFVAGGRRWMALTESD------IFWNTTDTGWVKAAWTLFsawsNGACIFVHE---LP 297
Cdd:PRK08180 215 lFTSGSTGLPKAVINTHRMLCANQQMLAQTFPFLAEEPpvlvdwLPWNHTFGGNHNLGIVLY----NGGTLYIDDgkpTP 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 298 RVDAKTILNtLCRFPITTLCCVPTLFRLLVQ-----EDLTRYKFQCLRHCLTGGEALNPDVRDKwksqtgleLHE----- 367
Cdd:PRK08180 291 GGFDETLRN-LREISPTVYFNVPKGWEMLVPalerdAALRRRFFSRLKLLFYAGAALSQDVWDR--------LDRvaeat 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 368 ---------GYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEegnvlppgkEGNIAVRIK-PTrpfcFFNCYLDN 437
Cdd:PRK08180 362 cgerirmmtGLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKLVPV---------GGKLEVRVKgPN----VTPGYWRA 428
|
410
....*....|....*....
gi 26341010 438 PEKTAAS--EQGdFYITGD 454
Cdd:PRK08180 429 PELTAEAfdEEG-YYRSGD 446
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
338-492 |
2.14e-06 |
|
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: 50.43 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 338 CLRhCLTGGEALNPDVRDKWKSqTGLELHEGYGQSETVVICGNSRNSTIKSGSMGKASPPYDVQIVDEEGNvlppgKEGN 417
Cdd:cd05933 322 CQK-FFTGAAPISRETLEFFLS-LNIPIMELYGMSETSGPHTISNPQAYRLLSCGKALPGCKTKIHNPDAD-----GIGE 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 418 IavrikptrpfCF-----FNCYLDNPEKTAASEQGDFYI-TGDRAHMDEDGYFWFLGRNDD-VINSSSYRIGPVEVESAL 490
Cdd:cd05933 395 I----------CFwgrhvFMGYLNMEDKTEEAIDEDGWLhSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAV 464
|
..
gi 26341010 491 AE 492
Cdd:cd05933 465 KK 466
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
67-247 |
8.79e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 49.01 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 67 KTGHRPPNPAFWWVNGSGTE-VKWTFEELGKQSRKAANVLEGVCGlqPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGV 145
Cdd:PRK05691 18 RAAQTPDRLALRFLADDPGEgVVLSYRDLDLRARTIAAALQARAS--FGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 146 SQLTAKdlkyRLQAARAKSIVtSDALAPQVDAISADCPSLQTKLLVSDTSRPGWINFRELLRAASPEHNCVRTRSGDSVA 225
Cdd:PRK05691 96 PPESAR----RHHQERLLSII-ADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQPDDIAF 170
|
170 180
....*....|....*....|..
gi 26341010 226 IYFTSGTTGAPKMVehsQSSYG 247
Cdd:PRK05691 171 LQYTSGSTALPKGV---QVSHG 189
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
391-574 |
7.09e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.53 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 391 MGKASPPYDVQIVDEEGNVLPPGKE-GNIAVRIKptrpfCFFNCYLDNpektAASEQGDFYITGDRAHMDEDGYFwFLGR 469
Cdd:PRK05851 347 LGNPIPGMEVRISPGDGAAGVAGREiGEIEIRGA-----SMMSGYLGQ----APIDPDDWFPTGDLGYLVDGGLV-VCGR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 470 NDDVINSSSYRIGPVEVESALAEHPAVLESAVVSSPDPIRGevVKAFIVLSPAYASHDPEALTRELQEHVKTVTApyKYP 549
Cdd:PRK05851 417 AKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAAEFRGPDEAGARSEVVQRVASECG--VVP 492
|
170 180
....*....|....*....|....*..
gi 26341010 550 RKVAFIS--ELPKTVSGKILRSKLRNQ 574
Cdd:PRK05851 493 SDVVFVApgSLPRTSSGKLRRLAVKRS 519
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
450-571 |
1.27e-04 |
|
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: 44.82 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 450 YITGDRAHMDEDGYFWFLGRNDDVINSSSYRIGPVEVESALAEHPAVLES------------AVVS--SPDPIRGEVVKA 515
Cdd:cd17647 374 YRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPDDESF 453
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26341010 516 FIVLSPAYASHDPEA--------LTRELQEHVKTVTAPYKYPRKVAFISELPKTVSGKILRSKL 571
Cdd:cd17647 454 AQEDVPKEVSTDPIVkgligyrkLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
57-576 |
1.41e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 41.72 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 57 DVLDVWSQLEKTGHR-PPNPAFWW---VNGSGTEVKW-TFEELGKQSRKAANVLEGVcGLQPGDRMMLVLPRLPDWWLIS 131
Cdd:PLN02430 40 DITTAWDIFSKSVEKyPDNKMLGWrriVDGKVGPYMWkTYKEVYEEVLQIGSALRAS-GAEPGSRVGIYGSNCPQWIVAM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 132 VACMRTGVVMIPGVSQLTAKDLKYRLQAARAKSIVTSDALAPQVdaISADCPSLQ-TKLLVSDTS--------------R 196
Cdd:PLN02430 119 EACAAHSLICVPLYDTLGPGAVDYIVDHAEIDFVFVQDKKIKEL--LEPDCKSAKrLKAIVSFTSvteeesdkasqigvK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 197 P-GWINFRELLRAaSPEHNCVrTRSGDSVAIYFTSGTTGAPKMVEHSQSSYGLgFVAGGRRWM-----ALTESDIFWNTT 270
Cdd:PLN02430 197 TySWIDFLHMGKE-NPSETNP-PKPLDICTIMYTSGTSGDPKGVVLTHEAVAT-FVRGVDLFMeqfedKMTHDDVYLSFL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 271 DTGWV--KAAWTLFsaWSNGACI-FVHElprvDAKTILNTLCRFPITTLCCVPTLF-----------------RLLVQED 330
Cdd:PLN02430 274 PLAHIldRMIEEYF--FRKGASVgYYHG----DLNALRDDLMELKPTLLAGVPRVFerihegiqkalqelnprRRLIFNA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 331 LTRYKFQC-----------------------------LRHCLTGGEALNPDVRDKWKSQTGLELHEGYGQSETvviCGNS 381
Cdd:PLN02430 348 LYKYKLAWmnrgyshkkaspmadflafrkvkaklggrLRLLISGGAPLSTEIEEFLRVTSCAFVVQGYGLTET---LGPT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 382 R----NSTIKSGSMGKASPPYDVQI--VDEEG-NVLPPGKEGNIAVRIKptrpfCFFNCYLDNPEKTAASEQGDFYITGD 454
Cdd:PLN02430 425 TlgfpDEMCMLGTVGAPAVYNELRLeeVPEMGyDPLGEPPRGEICVRGK-----CLFSGYYKNPELTEEVMKDGWFHTGD 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 455 RAHMDEDGYFWFLGRNDDVINSSSYRIGPVE-VESALAEHPAVLESAVVsspdpirGEVVKAFIVlspAYASHDPEALTR 533
Cdd:PLN02430 500 IGEILPNGVLKIIDRKKNLIKLSQGEYVALEyLENVYGQNPIVEDIWVY-------GDSFKSMLV---AVVVPNEENTNK 569
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 26341010 534 --ELQEHVKTVTAPYKYPR-KVAFISELPKTVSgkilRSKLRNQEW 576
Cdd:PLN02430 570 waKDNGFTGSFEELCSLPElKEHILSELKSTAE----KNKLRGFEY 611
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
80-174 |
1.71e-03 |
|
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: 41.18 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 80 VNGSGTEVK-WTFEELGKQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQ 158
Cdd:cd05905 5 LDSKGKEATtLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLG 84
|
90
....*....|....*.
gi 26341010 159 AARAKSIVTSDALAPQ 174
Cdd:cd05905 85 TCKVRVALTVEACLKG 100
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
80-241 |
2.92e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 40.47 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 80 VNGSGTEVKW-TFEELGkQSRKAANVLEGVCGLQPGDRMMLVLPRLPDWWLISVACMRTGVVMIPGVSQLTAKDLKYRLQ 158
Cdd:PLN02736 69 VDGTVGEYKWmTYGEAG-TARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26341010 159 AARAKSIVTSDALAPQVDAISADCPSLQ--------TKLLVSDTSRPG--WINFRELLRAASPEHNCVRTRSGDSVA-IY 227
Cdd:PLN02736 148 HAEVAAIFCVPQTLNTLLSCLSEIPSVRlivvvggaDEPLPSLPSGTGveIVTYSKLLAQGRSSPQPFRPPKPEDVAtIC 227
|
170
....*....|....*.
gi 26341010 228 FTSGTTGAPK--MVEH 241
Cdd:PLN02736 228 YTSGTTGTPKgvVLTH 243
|
|
| |
