|
Name |
Accession |
Description |
Interval |
E-value |
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
46-573 |
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: 979.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 46 PEEFNFASDVLDHWTQMEKEGKRSPNPALWWVNDQGDEVKWSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWW 125
Cdd:cd05928 2 PEYFNFASDVLDQWADKEKAGKRPPNPALWWVNGKGDEVKWSFRELGSLSRKAANVLSGACGLQRGDRVAVILPRVPEWW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 126 LVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSREGWLDFRSLVKS 205
Cdd:cd05928 82 LVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDSVASECPSLKTKLLVSEKSRDGWLNFKELLNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 206 ASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTA 285
Cdd:cd05928 162 ASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWSSLFEPWIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 286 GSTVFAHHLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQ 365
Cdd:cd05928 242 GACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 366 AYGQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTRPIGLFMYYENNPEKTAEVECG 445
Cdd:cd05928 322 GYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIRG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 446 DFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRD 525
Cdd:cd05928 402 DFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVLAPQFLSHD 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 529006476 526 PGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKE 573
Cdd:cd05928 482 PEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
86-571 |
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: 558.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 86 WSFREMTDLTCRTANVLTQtCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTT 165
Cdd:cd05972 1 WSFRELKRESAKAANVLAK-LGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 166 DTlapevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPKMAKHSHGFALr 245
Cdd:cd05972 80 AE---------------------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPL- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 246 SYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAAPSVYRMIL 325
Cdd:cd05972 108 GHIPTAAYWLGLRPDDIHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLI 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 326 QQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKG 405
Cdd:cd05972 188 KQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 406 NIQPPNTEGNIGIRIKptrPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVE 485
Cdd:cd05972 268 RELPPGEEGDIAIKLP---PPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 486 NALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIK 565
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSE--ELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIR 422
|
....*.
gi 529006476 566 RSELRK 571
Cdd:cd05972 423 RVELRD 428
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
39-573 |
0e+00 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 544.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 39 RWndyDRPEEFNFASDVLDHWTQMEKEgkrspNPALWWVNDQGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALIL 118
Cdd:COG0365 1 RW---FVGGRLNIAYNCLDRHAEGRGD-----KVALIWEGEDGEERTLTYAELRREVNRFANAL-RALGVKKGDRVAIYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 119 PRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD---------TLAPEVESVAPECPSLKTKLLV- 188
Cdd:COG0365 72 PNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITADgglrggkviDLKEKVDEALEELPSLEHVIVVg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 189 ---SDHSREGWLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSH-GFALRSYFPAcRKLLQLKMSDVFW 264
Cdd:COG0365 152 rtgADVPMEGDLDWDELLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHgGYLVHAATTA-KYVLDLKPGDVFW 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 265 CLSDTGWILAALGSLLEPWTAGSTVFAHH-LPQF-DPKV---IIEtffKYPITQCLAAPSVYRMILQQNYTSLR---FPT 336
Cdd:COG0365 231 CTADIGWATGHSYIVYGPLLNGATVVLYEgRPDFpDPGRlweLIE---KYGVTVFFTAPTAIRALMKAGDEPLKkydLSS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 337 LEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAG-ISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGN 415
Cdd:COG0365 308 LRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 416 IGIRiKPtRPiGLFMYYENNPEKTAEV---ECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHP 492
Cdd:COG0365 388 LVIK-GP-WP-GMFRGYWNDPERYRETyfgRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 493 AVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:COG0365 465 AVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSD--ELAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542
|
.
gi 529006476 573 E 573
Cdd:COG0365 543 A 543
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
44-573 |
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: 522.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 44 DRPEEFNFASDVLDHWTQMEKEgkrspNPALWWVNDQGDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPE 123
Cdd:cd05970 11 NVPENFNFAYDVVDAMAKEYPD-----KLALVWCDDAGEERIFTFAELADYSDKTANFFKAM-GIGKGDTVMLTLKRRYE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 124 WWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTT--DTLAPEVESVAPECPSLKTKLLVSDHSREGWLDFRS 201
Cdd:cd05970 85 FWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIaeDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 202 LVKSASPD----HICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGFALRSYFPAcrKLLQ-LKMSDVFWCLSDTGWILAAL 276
Cdd:cd05970 165 LIKNASPDferpTANSYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTA--KYWQnVREGGLHLTVADTGWGKAVW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 277 GSLLEPWTAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWK 356
Cdd:cd05970 243 GKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 357 RQTGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTRPIGLFMYYENNP 436
Cdd:cd05970 323 EKTGIKLMEGFGQTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKGKPVGLFGGYYKDA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 437 EKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIV 516
Cdd:cd05970 403 EKTAEVWHDGYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 529006476 517 LNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKE 573
Cdd:cd05970 483 LAKGYEPSE--ELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
65-575 |
7.38e-121 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 368.45 E-value: 7.38e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 65 EGKRSPNPALWWVNDQGDEvKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQ 144
Cdd:PRK04319 54 DGGRKDKVALRYLDASRKE-KYTYKELKELSNKFANVL-KELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 145 MKAKDILYRLQVSGAKAIVTTDTLAPEVesVAPECPSLKTKLLVSDHSR--EGWLDFRSLVKSASPDHICIKSKTLDPMA 222
Cdd:PRK04319 132 FMEEAVRDRLEDSEAKVLITTPALLERK--PADDLPSLKHVLLVGEDVEegPGTLDFNALMEQASDEFDIEWTDREDGAI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPKMAKHSHGFALRSYFPAcRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGST-VFAHhlPQFDPKV 301
Cdd:PRK04319 210 LHYTSGSTGKPKGVLHVHNAMLQHYQTG-KYVLDLHEDDVYWCTADPGWVTGTSYGIFAPWLNGATnVIDG--GRFSPER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 302 IIETFFKYPITQCLAAPSVYRMI------LQQNYtslRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAG-I 374
Cdd:PRK04319 287 WYRILEDYKVTVWYTAPTAIRMLmgagddLVKKY---DLSSLRHILSVGEPLNPEVVRWGMKVFGLPIHDNWWMTETGgI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 375 SCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIriKPTRPiGLFMYYENNPEKTAEVECGDFYNTGDRA 454
Cdd:PRK04319 364 MIANYPAMDIKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAI--KKGWP-SMMRGIWNNPEKYESYFAGDWYVSGDSA 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 455 TIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgELTKELQ 534
Cdd:PRK04319 441 YMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYEPSE--ELKEEIR 518
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 529006476 535 QHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEFG 575
Cdd:PRK04319 519 GFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKAWELG 559
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
80-570 |
2.97e-120 |
|
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: 362.52 E-value: 2.97e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 80 QGDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGA 159
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEI-GLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 160 KAIVTTDtlapevesvapecpslktkllvSDhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPKMAKHS 239
Cdd:cd05971 80 SALVTDG----------------------SD----------------------------DPALIIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 240 HGFALrSYFPACRKLLQL--KMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAA 317
Cdd:cd05971 110 HRVLL-GHLPGVQFPFNLfpRDGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 318 PSVYRMILQQNYTSLRFP-TLEHCCTGGEALlPEEQEQW-KRQTGVLLYQAYGQSEAGI---SCGTLrgMKIKPGSMGKA 392
Cdd:cd05971 189 PTALKMMRQQGEQLKHAQvKLRAIATGGESL-GEELLGWaREQFGVEVNEFYGQTECNLvigNCSAL--FPIKPGSMGKP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 393 IPPFDIQIIDDKGNIQPPNTEGNIGIRikptRPIGL-FMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDV 471
Cdd:cd05971 266 IPGHRVAIVDDNGTPLPPGEVGEIAVE----LPDPVaFLGYWNNPSATEKKMAGDWLLTGDLGRKDSDGYFWYVGRDDDV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 472 INASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVE 551
Cdd:cd05971 342 ITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSD--ALAREIQELVKTRLAAHEYPREIE 419
|
490
....*....|....*....
gi 529006476 552 FVSELPKTITGKIKRSELR 570
Cdd:cd05971 420 FVNELPRTATGKIRRRELR 438
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
82-571 |
6.46e-116 |
|
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: 351.81 E-value: 6.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:COG0318 21 GGRRLTYAELDARARRLAAAL-RALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTtdtlapevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktldpMAIFFTSGTTGFPKMAKHSHG 241
Cdd:COG0318 100 LVT--------------------------------------------------------ALILYTSGTTGRPKGVMLTHR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 242 FALRSYFpACRKLLQLKMSDVF-WCLS---DTGWILAALGSLLepwtAGSTVfaHHLPQFDPKVIIETFFKYPITQCLAA 317
Cdd:COG0318 124 NLLANAA-AIAAALGLTPGDVVlVALPlfhVFGLTVGLLAPLL----AGATL--VLLPRFDPERVLELIERERVTVLFGV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 318 PSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAG--ISCGTLRGMKIKPGSMGKAIP 394
Cdd:COG0318 197 PTMLARLLRHpEFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSpvVTVNPEDPGERRPGSVGRPLP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 395 PFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINA 474
Cdd:COG0318 277 GVEVRIVDEDGRELPPGEVGEIVVR-----GPNVMKGYWNDPEATAEAFRDGWLRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 475 SGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfSSRDPGELTKELQQHVksvtAPYKYPRKVEFVS 554
Cdd:COG0318 352 GGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPG-AELDAEELRAFLRERL----ARYKVPRRVEFVD 426
|
490
....*....|....*..
gi 529006476 555 ELPKTITGKIKRSELRK 571
Cdd:COG0318 427 ELPRTASGKIDRRALRE 443
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-573 |
4.80e-113 |
|
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: 343.78 E-value: 4.80e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAkaivttd 166
Cdd:cd05974 2 SFAEMSARSSRVANFL-RSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVAPEcpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPKMAKHSHgfalRS 246
Cdd:cd05974 74 VYAAVDENTHAD----------------------------------------DPMLLYFTSGTTSKPKLVEHTH----RS 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 247 YfP----ACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAAPSVYR 322
Cdd:cd05974 110 Y-PvghlSTMYWIGLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWR 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 323 MILQQNYTSLRFPtLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQIID 402
Cdd:cd05974 189 MLIQQDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLD 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 403 DKGNiqpPNTEGNIGIRIKPTRPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPA 482
Cdd:cd05974 268 PDGA---PATEGEVALDLGDTRPVGLMKGYAGDPDKTAHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPF 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 483 EVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNpefSSRDPG-ELTKELQQHVKSVTAPYKYPRKVEFVsELPKTIT 561
Cdd:cd05974 345 ELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVLR---AGYEPSpETALEIFRFSRERLAPYKRIRRLEFA-ELPKTIS 420
|
490
....*....|..
gi 529006476 562 GKIKRSELRKKE 573
Cdd:cd05974 421 GKIRRVELRRRE 432
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
86-573 |
2.25e-112 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 342.17 E-value: 2.25e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 86 WSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTT 165
Cdd:cd05969 1 YTFAQLKVLSARFANVL-KSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 166 DTLApevESVAPEcpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPKMAKHSHGfALR 245
Cdd:cd05969 80 EELY---ERTDPE----------------------------------------DPTLLHYTSGTTGTPKGVLHVHD-AMI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 246 SYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHHlPQFDPKVIIETFFKYPITQCLAAPSVYRMIL 325
Cdd:cd05969 116 FYYFTGKYVLDLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYE-GRFDAESWYGIIERVKVTVWYTAPTAIRMLM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 326 QQNYTSLR---FPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAG-ISCGTLRGMKIKPGSMGKAIPPFDIQII 401
Cdd:cd05969 195 KEGDELARkydLSSLRFIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTETGsIMIANYPCMPIKPGSMGKPLPGVKAAVV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 402 DDKGNIQPPNTEGNIGIriKPTRPiGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGP 481
Cdd:cd05969 275 DENGNELPPGTKGILAL--KPGWP-SMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 482 AEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSELPKTIT 561
Cdd:cd05969 352 FEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSD--ELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRS 429
|
490
....*....|..
gi 529006476 562 GKIKRSELRKKE 573
Cdd:cd05969 430 GKIMRRVLKAKE 441
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
219-565 |
3.14e-105 |
|
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: 320.00 E-value: 3.14e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFWCLSDTGWIlAALGSLLEPWTAGSTVFahHLPQFD 298
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHR-NLLAAAAALAASGGLTEGDVFLSTLPLFHI-GGLFGLLGALLAGGTVV--LLPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 299 PKVIIETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAG--IS 375
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKApESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 376 CGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAEVECGDFYNTGDRAT 455
Cdd:cd04433 157 TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGP-----SVMKGYWNNPEATAAVDEDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 456 IDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFssrdpGELTKELQQ 535
Cdd:cd04433 232 LDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGA-----DLDAEELRA 306
|
330 340 350
....*....|....*....|....*....|
gi 529006476 536 HVKSVTAPYKYPRKVEFVSELPKTITGKIK 565
Cdd:cd04433 307 HVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
67-570 |
3.63e-99 |
|
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: 309.11 E-value: 3.63e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 67 KRSPNPALWWvndqgDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMK 146
Cdd:cd05936 11 RFPDKTALIF-----MGRKLTYRELDALAEAFAAGL-QNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 147 AKDILYRLQVSGAKAIVTTDTLapevesvapecpslkTKLLVSDHSREGWldfrslvKSASPDhiciksktlDPMAIFFT 226
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSF---------------TDLLAAGAPLGER-------VALTPE---------DVAVLQYT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 227 SGTTGFPKMAKHSHGfALRSYFPACRKLLQ--LKMSDVFwclsdtgwiLAAL---------GSLLEPWTAGSTVFAhhLP 295
Cdd:cd05936 134 SGTTGVPKGAMLTHR-NLVANALQIKAWLEdlLEGDDVV---------LAALplfhvfgltVALLLPLALGATIVL--IP 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 296 QFDPKVIIETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAG- 373
Cdd:cd05936 202 RFRPIGVLKEIRKHRVTIFPGVPTMYIALLNApEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSp 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 374 -ISCGTLRGmKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrpiG--LFMYYENNPEKTAEVECGDFYNT 450
Cdd:cd05936 282 vVAVNPLDG-PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVR-------GpqVMKGYWNRPEETAEAFVDGWLRT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 451 GDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefssRDPGELT 530
Cdd:cd05936 354 GDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVL------KEGASLT 427
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 529006476 531 K-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:cd05936 428 EeEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
87-571 |
5.86e-96 |
|
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: 299.82 E-value: 5.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTd 166
Cdd:cd05973 2 TFGELRALSARFANAL-QELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 tlapevesvapecpslktkllvsdhsregwLDFRSLVKSaspdhiciksktlDPMAIFFTSGTTGFPKMAKHSHGfALRS 246
Cdd:cd05973 80 ------------------------------AANRHKLDS-------------DPFVMMFTSGTTGLPKGVPVPLR-ALAA 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 247 YFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHHLPqFDPKVIIETFFKYPITQCLAAPSVYRMILQ 326
Cdd:cd05973 116 FGAYLRDAVDLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGG-FSVESTWRVIERLGVTNLAGSPTAYRLLMA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 327 QNYTSLRFPT--LEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGISCGTLRGMK--IKPGSMGKAIPPFDIQIID 402
Cdd:cd05973 195 AGAEVPARPKgrLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEhpVHAGSAGRAMPGWRVAVLD 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 403 DKGNIQPPNTEGNIGIRIKPTrPIGLFMYYENNPEKTAEvecGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPA 482
Cdd:cd05973 275 DDGDELGPGEPGRLAIDIANS-PLMWFRGYQLPDTPAID---GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 483 EVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFssRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITG 562
Cdd:cd05973 351 DVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGH--EGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSG 428
|
....*....
gi 529006476 563 KIKRSELRK 571
Cdd:cd05973 429 KIQRFLLRR 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
47-570 |
3.56e-92 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 292.35 E-value: 3.56e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 47 EEFNFASDVLDHwtqmeKEGKRSPNPALwwVNDQGdevKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWL 126
Cdd:cd05959 1 EKYNAATLVDLN-----LNEGRGDKTAF--IDDAG---SLTYAELEAEARRVAGAL-RALGVKREERVLLIMLDTVDFPT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 127 VCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSRE--GWLDFRSLVK 204
Cdd:cd05959 70 AFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPeaGALLLAELVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 205 SASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHgfalRSYFPAC----RKLLQLKMSDVfwCLSDTGWILA-ALG-S 278
Cdd:cd05959 150 AEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLH----ADIYWTAelyaRNVLGIREDDV--CFSAAKLFFAyGLGnS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 279 LLEPWTAGSTVFAhhLPQF-DPKVIIETFFKYPITQCLAAPSVYR-MILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWK 356
Cdd:cd05959 224 LTFPLSVGATTVL--MPERpTPAAVFKRIRRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 357 RQTGVLLYQAYGQSEAG-ISCGTLRGmKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTRpiglfMYYENN 435
Cdd:cd05959 302 ARFGLDILDGIGSTEMLhIFLSNRPG-RVRYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSA-----TMYWNN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 436 PEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFI 515
Cdd:cd05959 376 RDKTRDTFQGEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFV 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 529006476 516 VLNPEFSsrDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:cd05959 456 VLRPGYE--DSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
82-572 |
4.61e-89 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 284.39 E-value: 4.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLTQtCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:PRK06187 28 DGRRTTYAELDERVNRLANALRA-LGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTLAPEVESVAPECPSLKTKLLVSDHSREG----WLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAK 237
Cdd:PRK06187 107 VLVDSEFVPLLAAILPQLPTVRTVIVEGDGPAAPlapeVGEYEELLAAASDTFDFPDIDENDAAAMLYTSGTTGHPKGVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 238 HSHgfalRSYF---PACRKLLQLKMSDVF-----------WclsdtGWILAALgsllepwTAGST-VFAHHlpqFDPKVI 302
Cdd:PRK06187 187 LSH----RNLFlhsLAVCAWLKLSRDDVYlvivpmfhvhaW-----GLPYLAL-------MAGAKqVIPRR---FDPENL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 303 IETFFKYPITQCLAAPSVYRMILQ------QNYTSLRfptlEHCCtGGEALLPEEQEQWKRQTGVLLYQAYGQSEAG--I 374
Cdd:PRK06187 248 LDLIETERVTFFFAVPTIWQMLLKaprayfVDFSSLR----LVIY-GGAALPPALLREFKEKFGIDLVQGYGMTETSpvV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 375 SCGTLR----GMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTE--GNIGIRiKPTRPIGlfmYYeNNPEKTAEVECGDFY 448
Cdd:PRK06187 323 SVLPPEdqlpGQWTKRRSAGRPLPGVEARIVDDDGDELPPDGGevGEIIVR-GPWLMQG---YW-NRPEATAETIDGGWL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 449 NTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfssRDPGE 528
Cdd:PRK06187 398 HTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLKPG---ATLDA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 529006476 529 ltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PRK06187 475 --KELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
83-570 |
1.71e-87 |
|
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: 277.82 E-value: 1.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQvsgaKAI 162
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD----KAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 163 VTTDTLAPEVESVapecpslktkllvsdhsregwldfrslvksaspDHICIksktldpmaIFFTSGTTGFPKMAKHSHgf 242
Cdd:cd05958 84 ITVALCAHALTAS---------------------------------DDICI---------LAFTSGTTGAPKATMHFH-- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 243 alRSYFPAC----RKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAhhLPQFDPKVIIETFFKYPITQCLAAP 318
Cdd:cd05958 120 --RDPLASAdryaVNVLRLREDDRFVGSPPLAFTFGLGGVLLFPFGVGASGVL--LEEATPDLLLSAIARYKPTVLFTAP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 319 SVYRMIL------QQNYTSLRFptlehCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEA---GISCgtlRGMKIKPGSM 389
Cdd:cd05958 196 TAYRAMLahpdaaGPDLSSLRK-----CVSAGEALPAALHRAWKEATGIPIIDGIGSTEMfhiFISA---RPGDARPGAT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 390 GKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRpiglfmyYENNPEKTAEVECGDFYN-TGDRATIDEEGYFWFLGRS 468
Cdd:cd05958 268 GKPVPGYEAKVVDDEGNPVPDGTIGRLAVR-GPTG-------CRYLADKRQRTYVQGGWNiTGDTYSRDPDGYFRHQGRS 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 469 DDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSsrdPGE-LTKELQQHVKSVTAPYKYP 547
Cdd:cd05958 340 DDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVI---PGPvLARELQDHAKAHIAPYKYP 416
|
490 500
....*....|....*....|...
gi 529006476 548 RKVEFVSELPKTITGKIKRSELR 570
Cdd:cd05958 417 RAIEFVTELPRTATGKLQRFALR 439
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
33-564 |
2.48e-81 |
|
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: 266.36 E-value: 2.48e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 33 SGAGTLRWNdydRPEEFNFASDVLDHwtQMEKEGKRSpnpALWWVNDQGDEVK-WSFREMTDLTCRTANVLtQTCGLQTG 111
Cdd:cd17634 39 PGAPSIKWF---EDATLNLAANALDR--HLRENGDRT---AIIYEGDDTSQSRtISYRELHREVCRFAGTL-LDLGVKKG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 112 DRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD---------TLAPEV-ESVAPECPS 181
Cdd:cd17634 110 DRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvPLKKNVdDALNPNVTS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 182 LKTKLLVSdhsREG---------WLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGFALRSYFPACR 252
Cdd:cd17634 190 VEHVIVLK---RTGsdidwqegrDLWWRDLIAKASPEHQPEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 253 KLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHH-LPQF-DPKVIIETFFKYPITQCLAAPSVYRM------- 323
Cdd:cd17634 267 YVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLYEgVPNWpTPARMWQVVDKHGVNILYTAPTAIRAlmaagdd 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 324 -ILQQNYTSLRfpTLEhccTGGEALLPEEQEQWKRQTGVL---LYQAYGQSEAGISCGTLRGMKI--KPGSMGKAIPPFD 397
Cdd:cd17634 347 aIEGTDRSSLR--ILG---SVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTETGGFMITPLPGAIelKAGSATRPVFGVQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 398 IQIIDDKGNIQPPNTEGNIGIRIK-PTRPIGLFMYYENNpEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASG 476
Cdd:cd17634 422 PAVVDNEGHPQPGGTEGNLVITDPwPGQTRTLFGDHERF-EQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAG 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 477 YRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPefSSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSEL 556
Cdd:cd17634 501 HRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNH--GVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSL 578
|
....*...
gi 529006476 557 PKTITGKI 564
Cdd:cd17634 579 PKTRSGKI 586
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
82-572 |
5.95e-81 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 262.92 E-value: 5.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:PRK07656 27 GDQRLTYAELNARVRRAAAALAAL-GIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTLAPEVESVAPECPSLKTKLLV----SDHSREGWLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAK 237
Cdd:PRK07656 106 LFVLGLFLGVDYSATTRLPALEHVVICeteeDDPHTEKMKTFTDFLAAGDPAERAPEVDPDDVADILFTSGTTGRPKGAM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 238 HSHGFALRSY--FPAC-------RKLLQLKMSDVFwCLsdTGWILAALgsllepwTAGSTVFAHhlPQFDPKVIIETFFK 308
Cdd:PRK07656 186 LTHRQLLSNAadWAEYlgltegdRYLAANPFFHVF-GY--KAGVNAPL-------MRGATILPL--PVFDPDEVFRLIET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 309 YPITQCLAAPSVYRMILQQ------NYTSLRFptlehCCTGGEALLPEEQEQWKRQTGV-LLYQAYGQSEA-GISCGTL- 379
Cdd:PRK07656 254 ERITVLPGPPTMYNSLLQHpdrsaeDLSSLRL-----AVTGAASMPVALLERFESELGVdIVLTGYGLSEAsGVTTFNRl 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 380 -RGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmYYENnPEKTAEVECGD-FYNTGDRATID 457
Cdd:PRK07656 329 dDDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR-GPNVMKG---YYDD-PEATAAAIDADgWLHTGDLGRLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 458 EEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfssrdpGELTKE-LQQH 536
Cdd:PRK07656 404 EEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLKPG------AELTEEeLIAY 477
|
490 500 510
....*....|....*....|....*....|....*.
gi 529006476 537 VKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PRK07656 478 CREHLAKYKVPRSIEFLDELPKNATGKVLKRALREK 513
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
67-571 |
8.16e-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: 260.19 E-value: 8.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 67 KRSPN-PALWWV-NDQGDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQ 144
Cdd:cd05966 64 KERGDkVAIIWEgDEPDQSRTITYRELLREVCRFANVLKSL-GVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 145 MKAKDILYRLQVSGAKAIVTTD---------TLAPEVESVAPECPSLKTKLLVSDHSREGW------LDFRSLVKSASPD 209
Cdd:cd05966 143 FSAESLADRINDAQCKLVITADggyrggkviPLKEIVDEALEKCPSVEKVLVVKRTGGEVPmtegrdLWWHDLMAKQSPE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 210 HICIKSKTLDPMAIFFTSGTTGFPKMAKHSH-GFALRSYFpACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGST 288
Cdd:cd05966 223 CEPEWMDSEDPLFILYTSGSTGKPKGVVHTTgGYLLYAAT-TFKYVFDYHPDDIYWCTADIGWITGHSYIVYGPLANGAT 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 289 VF----AHHLPQFDPKV-IIEtffKYPITQCLAAPSVYRMILQQ--------NYTSLRfptleHCCTGGEALLPEEQEQW 355
Cdd:cd05966 302 TVmfegTPTYPDPGRYWdIVE---KHKVTIFYTAPTAIRALMKFgdewvkkhDLSSLR-----VLGSVGEPINPEAWMWY 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 356 KRQTG---VLLYQAYGQSEAG---ISCgtLRG-MKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptRPI-G 427
Cdd:cd05966 374 YEVIGkerCPIVDTWWQTETGgimITP--LPGaTPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIK----RPWpG 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 428 LFMYYENNPE---KTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPD 504
Cdd:cd05966 448 MARTIYGDHEryeDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPH 527
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529006476 505 PVRGEVVKAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd05966 528 DIKGEAIYAFVTLKDGEEPSD--ELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRK 592
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
73-571 |
8.51e-79 |
|
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: 260.64 E-value: 8.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 73 ALWWVNDQGDEV-KWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDIL 151
Cdd:TIGR02188 75 AIIWEGDEPGEVrKITYRELHREVCRFANVLKSL-GVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFGGFSAEALA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 152 YRLQVSGAKAIVTTDT---------LAPEVESVAPECPSLKTKLLVSDHSREG---W-----LDFRSLVKSASPDHICIK 214
Cdd:TIGR02188 154 DRINDAGAKLVITADEglrggkvipLKAIVDEALEKCPVSVEHVLVVRRTGNPvvpWvegrdVWWHDLMAKASAYCEPEP 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 215 SKTLDPMAIFFTSGTTGFPKMAKHSH-GFALRSYFpACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHH 293
Cdd:TIGR02188 234 MDSEDPLFILYTSGSTGKPKGVLHTTgGYLLYAAM-TMKYVFDIKDGDIFWCTADVGWITGHSYIVYGPLANGATTVMFE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 294 -LPQF-DPKVIIETFFKYPITQCLAAPSVYRMILQQ--------NYTSLRfptLEHccTGGEALLPEEQEQWKRQTG--- 360
Cdd:TIGR02188 313 gVPTYpDPGRFWEIIEKHKVTIFYTAPTAIRALMRLgdewvkkhDLSSLR---LLG--SVGEPINPEAWMWYYKVVGker 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 361 VLLYQAYGQSEAGiscgtlrGMKI---------KPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIgIRIKPTRPiGLFMY 431
Cdd:TIGR02188 388 CPIVDTWWQTETG-------GIMItplpgatptKPGSATLPFFGIEPAVVDEEGNPVEGPGEGGY-LVIKQPWP-GMLRT 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 432 YENNPEKTAEVECGDF---YNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRG 508
Cdd:TIGR02188 459 IYGDHERFVDTYFSPFpgyYFTGDGARRDKDGYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKG 538
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529006476 509 EVVKAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:TIGR02188 539 QAIYAFVTLKDGYEPDD--ELRKELRKHVRKEIGPIAKPDKIRFVPGLPKTRSGKIMRRLLRK 599
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
68-564 |
1.12e-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: 254.84 E-value: 1.12e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 68 RSPN-PALWWvndqgDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMK 146
Cdd:cd17631 7 RHPDrTALVF-----GGRSLTYAELDERVNRLAHALRAL-GVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 147 AKDILYRLQVSGAKAIVTtdtlapevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFT 226
Cdd:cd17631 81 PPEVAYILADSGAKVLFD------------------------------------------------------DLALLMYT 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 227 SGTTGFPKMAKHSHgfalRSYFPACRKLL---QLKMSDVFWC---LSDTGWI-LAALGSLLepwtAGSTVfaHHLPQFDP 299
Cdd:cd17631 107 SGTTGRPKGAMLTH----RNLLWNAVNALaalDLGPDDVLLVvapLFHIGGLgVFTLPTLL----RGGTV--VILRKFDP 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 300 KVIIETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRqTGVLLYQAYGQSEAGISCGT 378
Cdd:cd17631 177 ETVLDLIERHRVTSFFLVPTMIQALLQHpRFATTDLSSLRAVIYGGAPMPERLLRALQA-RGVKFVQGYGMTETSPGVTF 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 379 LRG--MKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmyYENNPEKTAEVECGDFYNTGDRATI 456
Cdd:cd17631 256 LSPedHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVR-GPHVMAG----YWNRPEATAAAFRDGWFHTGDLGRL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 457 DEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefssRDPGELT-KELQQ 535
Cdd:cd17631 331 DEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVP------RPGAELDeDELIA 404
|
490 500
....*....|....*....|....*....
gi 529006476 536 HVKSVTAPYKYPRKVEFVSELPKTITGKI 564
Cdd:cd17631 405 HCRERLARYKIPKSVEFVDALPRNATGKI 433
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
63-473 |
4.66e-77 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 249.92 E-value: 4.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 63 EKEGKRSPN-PALwwvnDQGDEVKWSFREMTDLTCRTANVLTQtCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPG 141
Cdd:pfam00501 2 ERQAARTPDkTAL----EVGEGRRLTYRELDERANRLAAGLRA-LGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 142 TTQMKAKDILYRLQVSGAKAIVTTDTL-APEVESVAPECPSLKTKLLVsdhSREGWLDFRSLVKSASPDHICIKSKTL-- 218
Cdd:pfam00501 77 NPRLPAEELAYILEDSGAKVLITDDALkLEELLEALGKLEVVKLVLVL---DRDPVLKEEPLPEEAKPADVPPPPPPPpd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 --DPMAIFFTSGTTGFPKMAKHSHG---FALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGST-VFAH 292
Cdd:pfam00501 154 pdDLAYIIYTSGTTGKPKGVMLTHRnlvANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATvVLPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 293 HLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTS-LRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSE 371
Cdd:pfam00501 234 GFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKrALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 A-GISCGTLRGM--KIKPGSMGKAIPPFDIQIIDDK-GNIQPPNTEGNIGIRikptRPiGLFMYYENNPEKTAEV-ECGD 446
Cdd:pfam00501 314 TtGVVTTPLPLDedLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVR----GP-GVMKGYLNDPELTAEAfDEDG 388
|
410 420
....*....|....*....|....*..
gi 529006476 447 FYNTGDRATIDEEGYFWFLGRSDDVIN 473
Cdd:pfam00501 389 WYRTGDLGRRDEDGYLEIVGRKKDQIK 415
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
87-570 |
4.40e-76 |
|
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: 248.15 E-value: 4.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:cd05919 12 TYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 tlapevesvapecpslktkllvsdhsregwldfrslvksaspDHICIksktldpmaIFFTSGTTGFPKMAKHSHGFALRS 246
Cdd:cd05919 91 ------------------------------------------DDIAY---------LLYSSGTTGPPKGVMHAHRDPLLF 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 247 YFPACRKLLQLKMSDVFWCLSDT--GWILAalGSLLEPWTAGSTVFAHHLPQfDPKVIIETFFKYPITQCLAAPSVY-RM 323
Cdd:cd05919 120 ADAMAREALGLTPGDRVFSSAKMffGYGLG--NSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYaNL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 324 ILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQIIDD 403
Cdd:cd05919 197 LDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 404 KGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAE 483
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGP-----SAAVGYWNNPEKSRATFNGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 484 VENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRdpGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 563
Cdd:cd05919 352 VESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQ--ESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGK 429
|
....*..
gi 529006476 564 IKRSELR 570
Cdd:cd05919 430 LQRFKLR 436
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
65-571 |
7.55e-73 |
|
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: 244.53 E-value: 7.55e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 65 EGKRSPNPALWWVN-DQGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTT 143
Cdd:cd05967 61 EAGRGDQIALIYDSpVTGTERTYTYAELLDEVSRLAGVL-RKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 144 QMKAKDILYRLQVSGAKAIVTTDtLAPEVESVAPECPSLKTKLLVSDH------------------SREGWLDFRSLVKS 205
Cdd:cd05967 140 GFAAKELASRIDDAKPKLIVTAS-CGIEPGKVVPYKPLLDKALELSGHkphhvlvlnrpqvpadltKPGRDLDWSELLAK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 206 ASPdHICIKSKTLDPMAIFFTSGTTGFPK-MAKHSHGFALRSYFpACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWT 284
Cdd:cd05967 219 AEP-VDCVPVAATDPLYILYTSGTTGKPKgVVRDNGGHAVALNW-SMRNIYGIKPGDVWWAASDVGWVVGHSYIVYGPLL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 285 AG-STVFAHHLPQF--DPKVIIETFFKYPITQCLAAPSVYRMILQQ--NYTSLR---FPTLEHCCTGGEALLPEEQEQWK 356
Cdd:cd05967 297 HGaTTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpDGKYIKkydLSSLRTLFLAGERLDPPTLEWAE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 357 RQTGVLLYQAYGQSEAG-ISCGTLRG---MKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIkPTRPiGLFMYY 432
Cdd:cd05967 377 NTLGVPVIDHWWQTETGwPITANPVGlepLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPP-GCLLTL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 433 ENNPEKTAEVECGDF---YNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGE 509
Cdd:cd05967 455 WKNDERFKKLYLSKFpgyYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDELKGQ 534
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529006476 510 VVKAFIVLNPEFsSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd05967 535 VPLGLVVLKEGV-KITAEELEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRK 595
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
47-571 |
1.22e-72 |
|
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: 240.90 E-value: 1.22e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 47 EEFNFASDVLDHWTQMEKEGKrspnpaLWWVNDQGdevKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWL 126
Cdd:TIGR02262 1 EKYNAAEDLLDRNVVEGRGGK------TAFIDDIS---SLSYGELEAQVRRLAAAL-RRLGVKREERVLLLMLDGVDFPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 127 VCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDhSREGWLDFRSLVKSA 206
Cdd:TIGR02262 71 AFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSGALLPVIKAALGKSPHLEHRVVVGR-PEAGEVQLAELLATE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 207 SPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLLQLKMSDVfwCLSDTGWILA-ALG-SLLEPWT 284
Cdd:TIGR02262 150 SEQFKPAATQADDPAFWLYSSGSTGMPKGVVHTHSNPYWTAELYARNTLGIREDDV--CFSAAKLFFAyGLGnALTFPMS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 285 AGST-VFAHHLPQfdPKVIIETFFKYPITQCLAAPSVYR-MILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVL 362
Cdd:TIGR02262 228 VGATtVLMGERPT--PDAVFDRLRRHQPTIFYGVPTLYAaMLADPNLPSEDQVRLRLCTSAGEALPAEVGQRWQARFGVD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 363 LYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNiqpPNTEGNIGiRIKPTRPIGLFMYYeNNPEKTAEV 442
Cdd:TIGR02262 306 IVDGIGSTEMLHIFLSNLPGDVRYGTSGKPVPGYRLRLVGDGGQ---DVADGEPG-ELLISGPSSATMYW-NNRAKSRDT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 443 ECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFs 522
Cdd:TIGR02262 381 FQGEWTRSGDKYVRNDDGSYTYAGRTDDMLKVSGIYVSPFEIESALIQHPAVLEAAVVGVADEDGLIKPKAFVVLRPGQ- 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 529006476 523 srdpGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:TIGR02262 460 ----TALETELKEHVKDRLAPYKYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
85-570 |
4.57e-71 |
|
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: 234.49 E-value: 4.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 85 KWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVT 164
Cdd:cd05934 3 RWTYAELLRESARIAAAL-AALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 165 tdtlapevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPKMAKHSHGFAL 244
Cdd:cd05934 82 ------------------------------------------------------DPASILYTSGTTGPPKGVVITHANLT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 245 RS-YFPACRklLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAhhLPQFDPKVIIETFFKYPITQCLAAPSVYRM 323
Cdd:cd05934 108 FAgYYSARR--FGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 324 ILQQnytslrfPTLE----HC--CTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGisCGTL--RGMKIKPGSMGKAIPP 395
Cdd:cd05934 184 LLAQ-------PPSPddraHRlrAAYGAPNPPELHEEFEERFGVRLLEGYGMTETI--VGVIgpRDEPRRPGSIGRPAPG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 396 FDIQIIDDKGNIQPPNTEGNIGIRikPTRPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINAS 475
Cdd:cd05934 255 YEVRIVDDDGQELPAGEPGELVIR--GLRGWGFFKGYYNMPEATAEAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 476 GYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfSSRDPGELTKELQQHVksvtAPYKYPRKVEFVSE 555
Cdd:cd05934 333 GENISSAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPG-ETLDPEELFAFCEGQL----AYFKVPRYIRFVDD 407
|
490
....*....|....*
gi 529006476 556 LPKTITGKIKRSELR 570
Cdd:cd05934 408 LPKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
83-571 |
1.49e-70 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 235.98 E-value: 1.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTcGLQTGDRLAlILPRVPEWWLVC-VGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:PRK08316 34 DRSWTYAELDAAVNRVAAALLDL-GLKKGDRVA-ALGHNSDAYALLwLACARAGAVHVPVNFMLTGEELAYILDHSGARA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTLAPEVESVAPECPSLKTKLLVS---DHSREGWLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKH 238
Cdd:PRK08316 112 FLVDPALAPTAEAALALLPVDTLILSLVlggREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTSGTESLPKGAML 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 SHGfALRSYFPACRKLLQLKMSDV-------FWClsdtgwilAALGSLLEPWTA-GSTVfaHHLPQFDPKVIIETFFKYP 310
Cdd:PRK08316 192 THR-ALIAEYVSCIVAGDMSADDIplhalplYHC--------AQLDVFLGPYLYvGATN--VILDAPDPELILRTIEAER 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 311 ITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGeALLPEE--QEQWKRQTGVLLYQAYGQSEAGISCGTLR--GMKIK 385
Cdd:PRK08316 261 ITSFFAPPTVWISLLRHpDFDTRDLSSLRKGYYGA-SIMPVEvlKELRERLPGLRFYNCYGQTEIAPLATVLGpeEHLRR 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 386 PGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptRPIGLFMYYeNNPEKTAEVECGDFYNTGDRATIDEEGYFWFL 465
Cdd:PRK08316 340 PGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHR----SPQLMLGYW-DDPEKTAEAFRGGWFHSGDLGVMDEEGYITVV 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 466 GRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefssRDPGELT-KELQQHVKSVTAPY 544
Cdd:PRK08316 415 DRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVP------KAGATVTeDELIAHCRARLAGF 488
|
490 500
....*....|....*....|....*..
gi 529006476 545 KYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK08316 489 KVPKRVIFVDELPRNPSGKILKRELRE 515
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
73-571 |
2.79e-68 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 232.72 E-value: 2.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 73 ALWWVNDQGDEV-KWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGII-------Fmpgttq 144
Cdd:PRK00174 85 AIIWEGDDPGDSrKITYRELHREVCRFANALKSL-GVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvfggF------ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 145 mKAKDILYRLQVSGAKAIVTTD---------TLAPEVESVAPECPSLKTKLLVSdhsREG----WLDFR-----SLVKSA 206
Cdd:PRK00174 158 -SAEALADRIIDAGAKLVITADegvrggkpiPLKANVDEALANCPSVEKVIVVR---RTGgdvdWVEGRdlwwhELVAGA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 207 SPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGfalrSYfpacrkLLQLKMS----------DVFWCLSDTGWILA-- 274
Cdd:PRK00174 234 SDECEPEPMDAEDPLFILYTSGSTGKPKGVLHTTG----GY------LVYAAMTmkyvfdykdgDVYWCTADVGWVTGhs 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 275 --ALGSLLEpwtaGSTVFAHH-LPQFdPKV-----IIEtffKYPITQCLAAPSVYRMILQQ--------NYTSLRfptLE 338
Cdd:PRK00174 304 yiVYGPLAN----GATTLMFEgVPNY-PDPgrfweVID---KHKVTIFYTAPTAIRALMKEgdehpkkyDLSSLR---LL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 339 HccTGGEALLPEEQEqWkrqtgvlLYQAYG-----------QSEAG---IScgTLRG-MKIKPGSMGKAIPPFDIQIIDD 403
Cdd:PRK00174 373 G--SVGEPINPEAWE-W-------YYKVVGgercpivdtwwQTETGgimIT--PLPGaTPLKPGSATRPLPGIQPAVVDE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 404 KGNIQPPNTEGNIGIRiKP----TRPIglfmyYeNNPE---KTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASG 476
Cdd:PRK00174 441 EGNPLEGGEGGNLVIK-DPwpgmMRTI-----Y-GDHErfvKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSG 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 477 YRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSEL 556
Cdd:PRK00174 514 HRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSD--ELRKELRNWVRKEIGPIAKPDVIQFAPGL 591
|
570
....*....|....*
gi 529006476 557 PKTITGKIKRSELRK 571
Cdd:PRK00174 592 PKTRSGKIMRRILRK 606
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
84-564 |
8.94e-68 |
|
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: 227.48 E-value: 8.94e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 84 VKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIV 163
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGL-RKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 164 TTDTLAPEVESVAPECPSLKTKLLVSDH-----SREGWLDFRSLVKSASPDHICIKSKTlDPMAIFFTSGTTGFPKMAKH 238
Cdd:cd05911 88 TDPDGLEKVKEAAKELGPKDKIIVLDDKpdgvlSIEDLLSPTLGEEDEDLPPPLKDGKD-DTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 SH-GFALRSYFPACRKLLQLKMSDVFWCLSDTGWI---LAALGSLLepwtAGSTVFAHhlPQFDPKVIIETFFKYPITQC 314
Cdd:cd05911 167 SHrNLIANLSQVQTFLYGNDGSNDVILGFLPLYHIyglFTTLASLL----NGATVIIM--PKFDSELFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 315 LAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQW-KRQTGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKA 392
Cdd:cd05911 241 YLVPPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLaKRFPNATIKQGYGMTETGGILTVNPDGDDKPGSVGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 393 IPPFDIQIIDDKGN-IQPPNTEGNIGIRIkPTRPIGlfmYYeNNPEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDD 470
Cdd:cd05911 321 LPNVEAKIVDDDGKdSLGPNEPGEICVRG-PQVMKG---YY-NNPEATKETFDEDgWLHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 471 VINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFssrdpgELT-KELQQHVKSVTAPYKYPRK 549
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGE------KLTeKEVKDYVAKKVASYKQLRG 469
|
490
....*....|....*.
gi 529006476 550 -VEFVSELPKTITGKI 564
Cdd:cd05911 470 gVVFVDEIPKSASGKI 485
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
50-576 |
1.03e-67 |
|
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: 230.84 E-value: 1.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 50 NFASDVLDHWtqmekEGKRSPNPALWWVNDQGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCV 129
Cdd:cd05968 61 NIVEQLLDKW-----LADTRTRPALRWEGEDGTSRTLTYGELLYEVKRLANGL-RALGVGKGDRVGIYLPMIPEIVPAFL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 130 GCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD---------TLAPEVESVAPECPSLKtKLLVSDHSREGWL--- 197
Cdd:cd05968 135 AVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADgftrrgrevNLKEEADKACAQCPTVE-KVVVVRHLGNDFTpak 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 198 -DFRS--LVKSASPDHICiKSKTLDPMAIFFTSGTTGFPKMAKHSH-GFALRS----YFPacrklLQLKMSD-VFWcLSD 268
Cdd:cd05968 214 gRDLSydEEKETAGDGAE-RTESEDPLMIIYTSGTTGKPKGTVHVHaGFPLKAaqdmYFQ-----FDLKPGDlLTW-FTD 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 269 TGWIL---AALGSLLepwtAGSTVFAHH-LPQFD-PKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTG 343
Cdd:cd05968 287 LGWMMgpwLIFGGLI----LGATMVLYDgAPDHPkADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 344 GEALLPEEQEQW--------KRQTGVLLYQAYGQSEAGISCGTLRgMKIKPGSMGKAIPPFDIQIIDDKGNIQPPnTEGN 415
Cdd:cd05968 363 GSTGEPWNPEPWnwlfetvgKGRNPIINYSGGTEISGGILGNVLI-KPIKPSSFNGPVPGMKADVLDESGKPARP-EVGE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 416 IGIRiKPTrpIGLFMYYENNPEKTAEV---ECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHP 492
Cdd:cd05968 441 LVLL-APW--PGMTRGFWRDEDRYLETywsRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHP 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 493 AVAESAVVSSPDPVRGEVVKAFIVLNPEFSsrDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:cd05968 518 AVLESAAIGVPHPVKGEAIVCFVVLKPGVT--PTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAA 595
|
....
gi 529006476 573 EFGQ 576
Cdd:cd05968 596 YLGK 599
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
59-576 |
6.76e-67 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 226.77 E-value: 6.76e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 59 WTQMEKEGKRSPN-PALWWVndqGDEVkwSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGII 137
Cdd:PRK08314 13 FHNLEVSARRYPDkTAIVFY---GRAI--SYRELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 138 FMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVA-----------------PECPS------LKTKLLVSDHSRE 194
Cdd:PRK08314 88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVgnlrlrhvivaqysdylPAEPEiavpawLRAEPPLQALAPG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 195 GWLDFRSLVKS--------ASPDHICIksktldpmaIFFTSGTTGFPKMAKHSHGFALRSYFPACRkLLQLKMSDVFwcl 266
Cdd:PRK08314 168 GVVAWKEALAAglappphtAGPDDLAV---------LPYTSGTTGVPKGCMHTHRTVMANAVGSVL-WSNSTPESVV--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 267 sdtgwiLAAL---------GSLLEPWTAGSTVFAhhLPQFDPKVIIETFFKYPITQCLAAPSvyrMIL---------QQN 328
Cdd:PRK08314 235 ------LAVLplfhvtgmvHSMNAPIYAGATVVL--MPRWDREAAARLIERYRVTHWTNIPT---MVVdflaspglaERD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 329 YTSLRfptlehCCTGGEALLPEE-QEQWKRQTGVLLYQAYGQSEagiscgTLRGMKIKPGSMGK----AIPPFDI--QII 401
Cdd:PRK08314 304 LSSLR------YIGGGGAAMPEAvAERLKELTGLDYVEGYGLTE------TMAQTHSNPPDRPKlqclGIPTFGVdaRVI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 402 D-DKGNIQPPNTEGNIGIRikptrpiG--LFMYYENNPEKTA----EVECGDFYNTGDRATIDEEGYFWFLGRSDDVINA 474
Cdd:PRK08314 372 DpETLEELPPGEVGEIVVH-------GpqVFKGYWNRPEATAeafiEIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 475 SGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFssrdPGELTKE-LQQHVKSVTAPYKYPRKVEFV 553
Cdd:PRK08314 445 SGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEA----RGKTTEEeIIAWAREHMAAYKYPRIVEFV 520
|
570 580
....*....|....*....|...
gi 529006476 554 SELPKTITGKIKRSELRKKEFGQ 576
Cdd:PRK08314 521 DSLPKSGSGKILWRQLQEQEKAR 543
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
82-571 |
1.30e-66 |
|
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: 223.32 E-value: 1.30e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:cd05941 8 DGDSITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IvttdtlapevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktLDPMAIFFTSGTTGFPKMAKHSHG 241
Cdd:cd05941 88 V-------------------------------------------------------LDPALILYTSGTTGRPKGVVLTHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 242 fALRSYFPACRKLLQLKMSDVFW-CLS---DTGWILAALGSLLepwtAGSTVfaHHLPQFDPKVIIETFFKYPITQCLAA 317
Cdd:cd05941 113 -NLAANVRALVDAWRWTEDDVLLhVLPlhhVHGLVNALLCPLF----AGASV--EFLPKFDPKEVAISRLMPSITVFMGV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 318 PSVYRMILQQNYTSLRFPTLEH--CC-------TGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGI--SCGtLRGmKIKP 386
Cdd:cd05941 186 PTIYTRLLQYYEAHFTDPQFARaaAAerlrlmvSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMalSNP-LDG-ERRP 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 387 GSMGKAIPPFDIQIIDDKGN-IQPPNTEGNIGIRiKPTrpigLFMYYENNPEKTAEVECGD-FYNTGDRATIDEEGYFWF 464
Cdd:cd05941 264 GTVGMPLPGVQARIVDEETGePLPRGEVGEIQVR-GPS----VFKEYWNKPEATKEEFTDDgWFKTGDLGVVDEDGYYWI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 465 LGR-SDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDPGELTkelqQHVKSVTAP 543
Cdd:cd05941 339 LGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLEELK----EWAKQRLAP 414
|
490 500
....*....|....*....|....*...
gi 529006476 544 YKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd05941 415 YKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
87-569 |
7.66e-65 |
|
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: 218.12 E-value: 7.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:cd05935 3 TYLELLEVVKKLASFL-SNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLApevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPKMAKHSHGFALRS 246
Cdd:cd05935 82 ELD-------------------------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAAN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 247 yfpacrkllqlKMSDVFWC-LSDTGWILAAL---------GSLLEPWTAGSTVFAhhLPQFDPKVIIETFFKYPITQCLA 316
Cdd:cd05935 113 -----------ALQSAVWTgLTPSDVILACLplfhvtgfvGSLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTN 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 317 APSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAgISCGTLRGMKiKPGSMGKAIPP 395
Cdd:cd05935 180 IPTMLVDLLATpEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET-MSQTHTNPPL-RPKLQCLGIP* 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 396 FDIQ--IID-DKGNIQPPNTEGNIGIRiKPTrpigLFMYYENNPEKTAE--VECG--DFYNTGDRATIDEEGYFWFLGRS 468
Cdd:cd05935 258 FGVDarVIDiETGRELPPNEVGEIVVR-GPQ----IFKGYWNRPEETEEsfIEIKgrRFFRTGDLGYMDEEGYFFFVDRV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 469 DDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSsrdpGELTKE-LQQHVKSVTAPYKYP 547
Cdd:cd05935 333 KRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYR----GKVTEEdIIEWAREQMAAYKYP 408
|
490 500
....*....|....*....|..
gi 529006476 548 RKVEFVSELPKTITGKIKRSEL 569
Cdd:cd05935 409 REVEFVDELPRSASGKILWRLL 430
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
53-569 |
3.22e-64 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 220.30 E-value: 3.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 53 SDVLDHWTQmekegKRSPNPALWWVndqGDEVkwSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCI 132
Cdd:PRK06178 36 TEYLRAWAR-----ERPQRPAIIFY---GHVI--TYAELDELSDRFAALLRQR-GVGAGDRVAVFLPNCPQFHIVFFGIL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 133 RTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPEC-----------------PSLKTKLLVSDHSR-- 193
Cdd:PRK06178 105 KLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhvivtsladvlpaePTLPLPDSLRAPRLaa 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 194 EGWLDFRSLVkSASPDHICIKSKTLD-PMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLLQLKMSDVFWCLSDTGWI 272
Cdd:PRK06178 185 AGAIDLLPAL-RACTAPVPLPPPALDaLAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEFWI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 273 LAALGSLLEPWTAGSTVFAhhLPQFDPKVIIETFFKYPITQC----------LAAPSVYrmilQQNYTSLRFPtleHCCT 342
Cdd:PRK06178 264 AGENFGLLFPLFSGATLVL--LARWDAVAFMAAVERYRVTRTvmlvdnavelMDHPRFA----EYDLSSLRQV---RVVS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 343 GGEALLPEEQEQWKRQTGVLLYQA-YGQSEAGiSCGTL-RGM-------KIKPGSMGKAIPPFDIQIID-DKGNIQPPNT 412
Cdd:PRK06178 335 FVKKLNPDYRQRWRALTGSVLAEAaWGMTETH-TCDTFtAGFqdddfdlLSQPVFVGLPVPGTEFKICDfETGELLPLGA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 413 EGNIGIRiKPTrpigLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHP 492
Cdd:PRK06178 414 EGEIVVR-TPS----LLKGYWNKPEATAEALRDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006476 493 AVAESAVVSSPDPVRGEVVKAFIVLNPEFssrdpgELTKE-LQQHVKSVTAPYKYPrKVEFVSELPKTITGKIKRSEL 569
Cdd:PRK06178 489 AVLGSAVVGRPDPDKGQVPVAFVQLKPGA------DLTAAaLQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
71-571 |
1.11e-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: 211.40 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 71 NPALwwVNDQGDEVkWSFREMTDLTCRTANVLTqTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDI 150
Cdd:cd05926 3 APAL--VVPGSTPA-LTYADLAELVDDLARQLA-ALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 151 LYRLQVSGAKAIVT-TDTLAPEVESvAPECPSLKTKLLVSDHSREGWLDFRSLVkSASPDHICIKSKTL----DPMAIFF 225
Cdd:cd05926 79 EFYLADLGSKLVLTpKGELGPASRA-ASKLGLAILELALDVGVLIRAPSAESLS-NLLADKKNAKSEGVplpdDLALILH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 226 TSGTTGFPKMAKHSHGFALRSYFPACRKLlQLKMSDVFWCLSDTGWILAALGSLLEPWTAG-STVFAhhlPQFDPKVIIE 304
Cdd:cd05926 157 TSGTTGRPKGVPLTHRNLAASATNITNTY-KLTPDDRTLVVMPLFHVHGLVASLLSTLAAGgSVVLP---PRFSASTFWP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 305 TFFKYPITQCLAAPSVYRMILQ-------QNYTSLRFptlehCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAG--IS 375
Cdd:cd05926 233 DVRDYNATWYTAVPTIHQILLNrpepnpeSPPPKLRF-----IRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAhqMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 376 CGTLRGMKIKPGSMGKAIPPfDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmyYENNPEKTAEV-ECGDFYNTGDRA 454
Cdd:cd05926 308 SNPLPPGPRKPGSVGKPVGV-EVRILDEDGEILPPGVVGEICLR-GPNVTRG----YLNNPEANAEAaFKDGWFRTGDLG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 455 TIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefssRDPGELTK-EL 533
Cdd:cd05926 382 YLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVL------REGASVTEeEL 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 529006476 534 QQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd05926 456 RAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
58-572 |
5.63e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 208.09 E-value: 5.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 58 HWT-QMEKEGKRSPN-PALWWVndqGDEVKWsfREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTG 135
Cdd:PRK07786 18 NWVnQLARHALMQPDaPALRFL---GNTTTW--RELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 136 IIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSREGWLDFRSLVKSASPDHICIKS 215
Cdd:PRK07786 92 AIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAHAPVDI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 216 KTLDPMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLLQLKMSDVFWCLSDTGWIlAALGSLLEPWTAGSTVFAHHLP 295
Cdd:PRK07786 172 PNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHI-AGIGSMLPGLLLGAPTVIYPLG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 296 QFDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTGG----EALLPEEQEQWKrqtGVLLYQAYGQSE 371
Cdd:PRK07786 251 AFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAapasDTLLRQMAATFP---EAQILAAFGQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 -AGISCGTLRGMKI-KPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTrpigLFMYYENNPEKTAEVECGDFYN 449
Cdd:PRK07786 328 mSPVTCMLLGEDAIrKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYR-APT----LMSGYWNNPEATAEAFAGGWFH 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 450 TGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDPGEL 529
Cdd:PRK07786 403 SGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAALTLEDL 482
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 529006476 530 TKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PRK07786 483 AEFLTDRL----ARYKHPKALEIVDALPRNPAGKVLKTELRER 521
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
84-573 |
5.25e-59 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 207.50 E-value: 5.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 84 VKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFmPGTTQMKAKDILYRLQVSGAKAIV 163
Cdd:PRK07529 57 ETWTYAELLADVTRTANLLHSL-GVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAELLRAAGAKVLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 164 T------TDtLAPEVESVAPECPSLKTKLLV-----------------SDHSREGWLDFRSLVKSASPDH-ICIKSKTLD 219
Cdd:PRK07529 135 TlgpfpgTD-IWQKVAEVLAALPELRTVVEVdlarylpgpkrlavpliRRKAHARILDFDAELARQPGDRlFSGRPIGPD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 220 PMAIFF-TSGTTGFPKMAKHSHGFALRSYFPACRkLLQLKMSDVFWClsdtGWIL----AALGSLLEPWTAG-STVFAHH 293
Cdd:PRK07529 214 DVAAYFhTGGTTGMPKLAQHTHGNEVANAWLGAL-LLGLGPGDTVFC----GLPLfhvnALLVTGLAPLARGaHVVLATP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 294 LPQFDPKV------IIEtffKYPITQCLAAPSVYRMILQQ-----NYTSLRFptlehcCTGGEALLPEE-QEQWKRQTGV 361
Cdd:PRK07529 289 QGYRGPGVianfwkIVE---RYRINFLSGVPTVYAALLQVpvdghDISSLRY------ALCGAAPLPVEvFRRFEAATGV 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 362 LLYQAYGQSEA--GISCGTLRGMKiKPGSMGKAIPPFDIQII--DDKGNIQ---PPNTEGNIGIRiKPTRPIGlfmYYEN 434
Cdd:PRK07529 360 RIVEGYGLTEAtcVSSVNPPDGER-RIGSVGLRLPYQRVRVVilDDAGRYLrdcAVDEVGVLCIA-GPNVFSG---YLEA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 435 NPEKTAEVEcGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAF 514
Cdd:PRK07529 435 AHNKGLWLE-DGWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAY 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 529006476 515 IVLNPEfSSRDPGELTKELQQHVKSVTApykYPRKVEFVSELPKTITGKIKRSELRKKE 573
Cdd:PRK07529 514 VQLKPG-ASATEAELLAFARDHIAERAA---VPKHVRILDALPKTAVGKIFKPALRRDA 568
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
67-570 |
6.90e-58 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 202.14 E-value: 6.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 67 KRSPN-PALWWvndqgDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCV-----GCIRTGIIFMp 140
Cdd:PRK06188 23 KRYPDrPALVL-----GDTRLTYGQLADRISRYIQAF-EALGLGTGDAVALLSLNRPEVLMAIGaaqlaGLRRTALHPL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 141 GTTQmkakDILYRLQVSGAKAIVTTDTLAPE-VESVAPECPSLKTKLLVSDhsREGWLDFRSLVKSASPDHICIKSKTLD 219
Cdd:PRK06188 96 GSLD----DHAYVLEDAGISTLIVDPAPFVErALALLARVPSLKHVLTLGP--VPDGVDLLAAAAKFGPAPLVAAALPPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 220 PMAIFFTSGTTGFPKMAKHSHgfalRSYfpacrkllqLKMSDvfWCLSDTGW-----------ILAALGSLLEP--WTAG 286
Cdd:PRK06188 170 IAGLAYTGGTTGKPKGVMGTH----RSI---------ATMAQ--IQLAEWEWpadprflmctpLSHAGGAFFLPtlLRGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 287 STVFahhLPQFDPKVIIETFFKYPITQCLAAPS-VYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQ 365
Cdd:PRK06188 235 TVIV---LAKFDPAEVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPIFAQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 366 AYGQSEAGISCGTLRGMKIKP------GSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPtrpigLFMY-YENNPEK 438
Cdd:PRK06188 312 YYGQTEAPMVITYLRKRDHDPddpkrlTSCGRPTPGLRVALLDEDGREVAQGEVGEICVR-GP-----LVMDgYWNRPEE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 439 TAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLN 518
Cdd:PRK06188 386 TAEAFRDGWLHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLR 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 529006476 519 PEfSSRDPGeltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK06188 466 PG-AAVDAA----ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALR 512
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
82-569 |
2.36e-55 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 193.13 E-value: 2.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWwLVCV-GCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:cd05930 9 GDQSLTYAELDARANRLARYL-RERGVGPGDLVAVLLERSLEM-VVAIlAVLKAGAAYVPLDPSYPAERLAYILEDSGAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTTDTlapevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPKMAKHSH 240
Cdd:cd05930 87 LVLTDPD---------------------------------------------------DLAYVIYTSGSTGKPKGVMVEH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 GfALRSYFPACRKLLQLKMSDVFWCLSDTGWIlAALGSLLEPWTAGSTVfaHHLPQ---FDPKVIIETFFKYPITQCLAA 317
Cdd:cd05930 116 R-GLVNLLLWMQEAYPLTPGDRVLQFTSFSFD-VSVWEIFGALLAGATL--VVLPEevrKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 318 PSVYRMILQQNYTSlRFPTLEHCCTGGEALLPEEQEQW-KRQTGVLLYQAYGQSEAGI--SCGTLRGMKIKPGSM--GKA 392
Cdd:cd05930 192 PSLLRLLLQELELA-ALPSLRLVLVGGEALPPDLVRRWrELLPGARLVNLYGPTEATVdaTYYRVPPDDEEDGRVpiGRP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 393 IPPFDIQIIDDKGNIQPPNTEGNI---GIrikptrpiGLFMYYENNPEKTAEVECGD-------FYNTGDRATIDEEGYF 462
Cdd:cd05930 271 IPNTRVYVLDENLRPVPPGVPGELyigGA--------GLARGYLNRPELTAERFVPNpfgpgerMYRTGDLVRWLPDGNL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 463 WFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPefssrDPGELTKELQQHVKSVTA 542
Cdd:cd05930 343 EFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDE-----GGELDEEELRAHLAERLP 417
|
490 500
....*....|....*....|....*..
gi 529006476 543 PYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd05930 418 DYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
80-572 |
7.38e-55 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 193.58 E-value: 7.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 80 QGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGA 159
Cdd:PRK08276 6 APSGEVVTYGELEARSNRLAHGL-RALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 160 KAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSREGWLDFRSLVKSASPDHICIKSKTLDpMAifFTSGTTGFPK----- 234
Cdd:PRK08276 85 KVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAAQPDTPIADETAGAD-ML--YSSGTTGRPKgikrp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 235 -------------MAKHSHGFalrSYFPACRKLlqlkMSDVFWCLSDTGWILAALgsllepwTAGSTVFAhhLPQFDPKV 301
Cdd:PRK08276 162 lpgldpdeapgmmLALLGFGM---YGGPDSVYL----SPAPLYHTAPLRFGMSAL-------ALGGTVVV--MEKFDAEE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 302 IIETFFKYPITQCLAAPSVY-RMI-----LQQNY--TSLRFPTleHcctgGEALLPEEQeqwKRQT----GVLLYQAYGQ 369
Cdd:PRK08276 226 ALALIERYRVTHSQLVPTMFvRMLklpeeVRARYdvSSLRVAI--H----AAAPCPVEV---KRAMidwwGPIIHEYYAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 370 SEAG----ISCGT-LRgmkiKPGSMGKAIPPfDIQIIDDKGNIQPPNTEGNIGIRikptRPIGLFMYYeNNPEKTAEVEC 444
Cdd:PRK08276 297 SEGGgvtvITSEDwLA----HPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFE----MDGYPFEYH-NDPEKTAAARN 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 445 G-DFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAfiVLNPEFSS 523
Cdd:PRK08276 367 PhGWVTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--VVQPADGA 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 529006476 524 RDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PRK08276 445 DAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
58-570 |
1.06e-54 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 193.36 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 58 HWTQM--EKEGKRSPNPALWWVNDQGDEVKWSFREMTDLTCRTANvLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTG 135
Cdd:PRK08008 8 HLRQMwdDLADVYGHKTALIFESSGGVVRRYSYLELNEEINRTAN-LFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 136 IIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSR---EGWLDFRSLvKSASPDHIC 212
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQFYPMYRQIQQEDATPLRHICLTRVALpadDGVSSFTQL-KAQQPATLC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 213 --IKSKTLDPMAIFFTSGTTGFPKMAKHSHG---FAlrSYFPACRklLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGS 287
Cdd:PRK08008 166 yaPPLSTDDTAEILFTSGTTSRPKGVVITHYnlrFA--GYYSAWQ--CALRDDDVYLTVMPAFHIDCQCTAAMAAFSAGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 288 TVfahhlpqfdpkVIIETF-----------FKYPITQCLaaPSVYRMILQQnytslrfPTLE----HCCTGGEALLP--- 349
Cdd:PRK08008 242 TF-----------VLLEKYsarafwgqvckYRATITECI--PMMIRTLMVQ-------PPSAndrqHCLREVMFYLNlsd 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 350 EEQEQWKRQTGVLLYQAYGQSEA--GIsCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTRPIg 427
Cdd:PRK08008 302 QEKDAFEERFGVRLLTSYGMTETivGI-IGDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVPGKTI- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 428 lFMYYENNPEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPV 506
Cdd:PRK08008 380 -FKEYYLDPKATAKVLEADgWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSI 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006476 507 RGEVVKAFIVLNpefssrdPGE-LTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK08008 459 RDEAIKAFVVLN-------EGEtLSEEeFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
81-572 |
2.39e-54 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 192.01 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTDLTCRTANVLTQtCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:PRK07514 24 PDGLRYTYGDLDAASARLANLLVA-LGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTTDTLAPEVESVAPECPSlkTKLLVSDHSREGWLDFRSlvKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSH 240
Cdd:PRK07514 103 LVVCDPANFAWLSKIAAAAGA--PHVETLDADGTGSLLEAA--AAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 G------FALRSY--FPACRKLLQlkMSDVFwclsDT-GWILAALGSLLepwTAGSTVFahhLPQFDPKVIIEtffKYPI 311
Cdd:PRK07514 179 GnllsnaLTLVDYwrFTPDDVLIH--ALPIF----HThGLFVATNVALL---AGASMIF---LPKFDPDAVLA---LMPR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 312 TQCL-AAPSVYRMILQQNytslRFpTLEHC-----CTGGEA-LLPEEQEQWKRQTGVLLYQAYGQSEAG-ISCGTLRGMK 383
Cdd:PRK07514 244 ATVMmGVPTFYTRLLQEP----RL-TREAAahmrlFISGSApLLAETHREFQERTGHAILERYGMTETNmNTSNPYDGER 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 384 IkPGSMGKAIPPFDIQIID-DKGNIQPPNTEGNIGIRikptrpiG--LFMYYENNPEKTAEVECGD-FYNTGDRATIDEE 459
Cdd:PRK07514 319 R-AGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK-------GpnVFKGYWRMPEKTAEEFRADgFFITGDLGKIDER 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 460 GYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfSSRDPGELTKELQQHVks 539
Cdd:PRK07514 391 GYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPKPG-AALDEAAILAALKGRL-- 467
|
490 500 510
....*....|....*....|....*....|...
gi 529006476 540 vtAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PRK07514 468 --ARFKQPKRVFFVDELPRNTMGKVQKNLLREQ 498
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-570 |
8.35e-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: 341246 [Multi-domain] Cd Length: 457 Bit Score: 186.88 E-value: 8.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 107 GLQTGDRLALILPRVPEW-WL---VCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSL 182
Cdd:cd05922 14 GGVRGERVVLILPNRFTYiELsfaVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDALPASPDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 183 KTKLLVsdhsrEGWLDFRSLVKSASPDHIciksktlDPMAIFFTSGTTGFPKMAKHSHgFALRSYFPACRKLLQLKMSDV 262
Cdd:cd05922 94 GTVLDA-----DGIRAARASAPAHEVSHE-------DLALLLYTSGSTGSPKLVRLSH-QNLLANARSIAEYLGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 263 FWCLSDTGWIlAALGSLLEPWTAGSTVFAHHLPQFDpKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCT 342
Cdd:cd05922 161 ALTVLPLSYD-YGLSVLNTHLLRGATLVLTNDGVLD-DAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 343 GGEALlPEEQEQWKRQTGVL--LYQAYGQSEAGISCGTLRGMKI--KPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGi 418
Cdd:cd05922 239 AGGRL-PQETIARLRELLPGaqVYVMYGQTEATRRMTYLPPERIleKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEIV- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 419 rikPTRPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESA 498
Cdd:cd05922 317 ---HRGPNVMKGYWNDPPYRRKEGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529006476 499 VVSSPDPVrGEVVKAFIVlnpefssRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:cd05922 394 AVGLPDPL-GEKLALFVT-------APDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
87-573 |
9.32e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 189.09 E-value: 9.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:PRK06710 51 TFSVFHDKVKRFANYL-QKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVA-------------------------PECPSLKTKLLV---SDHSREGWLDFRSLVKSASpDHICIKSKTL 218
Cdd:PRK06710 130 LVFPRVTNVQsatkiehvivtriadflpfpknllyPFVQKKQSNLVVkvsESETIHLWNSVEKEVNTGV-EVPCDPENDL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAifFTSGTTGFPKMAKHSHgfalrsyfpacRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHH----- 293
Cdd:PRK06710 209 ALLQ--YTGGTTGFPKGVMLTH-----------KNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVYGMTAVMNLsimqg 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 294 -----LPQFDPKVIIETFFKYPITQCLAAPSVYRMIL------QQNYTSLRfptlehCCTGGEALLPEE-QEQWKRQTGV 361
Cdd:PRK06710 276 ykmvlIPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLnspllkEYDISSIR------ACISGSAPLPVEvQEKFETVTGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 362 LLYQAYGQSEAG-ISCGTLRGMKIKPGSMGKAIPPFDIQIID-DKGNIQPPNTEGNIGIRiKPTrpigLFMYYENNPEKT 439
Cdd:PRK06710 350 KLVEGYGLTESSpVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVK-GPQ----IMKGYWNKPEET 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 440 AEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNP 519
Cdd:PRK06710 425 AAVLQDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKE 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 529006476 520 EFSSRDpgeltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKR-----SELRKKE 573
Cdd:PRK06710 505 GTECSE-----EELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRrvlieEEKRKNE 558
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
81-571 |
4.71e-52 |
|
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: 186.50 E-value: 4.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGII---FMPGttqMKAKDILYRLQVS 157
Cdd:COG1021 46 DGERRLSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFALFRAGAIpvfALPA---HRRAEISHFAEQS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 158 GAKAIVTTDT-----LAPEVESVAPECPSLKTKLLVSDHsrEGWLDFRSLVKSASPDHICikskTLDP--MAIFFTS-GT 229
Cdd:COG1021 122 EAVAYIIPDRhrgfdYRALARELQAEVPSLRHVLVVGDA--GEFTSLDALLAAPADLSEP----RPDPddVAFFQLSgGT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 230 TGFPKMAKHSH---GFALRSYFPACRkllqLKMSDVFWC---------LSDTGwILAALgsllepWTAGSTVFAhhlPQF 297
Cdd:COG1021 196 TGLPKLIPRTHddyLYSVRASAEICG----LDADTVYLAalpaahnfpLSSPG-VLGVL------YAGGTVVLA---PDP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 298 DPKVIIETFFKYPITQCLAAPSVYRMILQ-QNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEaGISC 376
Cdd:COG1021 262 SPDTAFPLIERERVTVTALVPPLALLWLDaAERSRYDLSSLRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAE-GLVN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 377 GTLRGmkiKP-----GSMGKAIPPFD-IQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmYYeNNPEKTAEVECGD-FYN 449
Cdd:COG1021 341 YTRLD---DPeevilTTQGRPISPDDeVRIVDEDGNPVPPGEVGELLTR-GPYTIRG---YY-RAPEHNARAFTPDgFYR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 450 TGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfssrdpgEL 529
Cdd:COG1021 413 TGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGE-------PL 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 529006476 530 T-KELQQHVKSV-TAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:COG1021 486 TlAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKALRA 529
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
81-569 |
2.21e-51 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 183.91 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:PRK06839 23 TEEEEMTYKQLHEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTTDTLAPEVESvapecpsLKTKLLVSdhsREGWLDFRSLVKSASPDHICIKSKTlDPMAIFFTSGTTGFPKmakhsh 240
Cdd:PRK06839 103 VLFVEKTFQNMALS-------MQKVSYVQ---RVISITSLKEIEDRKIDNFVEKNES-ASFIICYTSGTTGKPK------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 GFALRS---YFPACRKL--LQLKMSDVfwclSDTGWILAALGSL----LEPWTAGSTVFAHHlpQFDPKVIIETFFKYPI 311
Cdd:PRK06839 166 GAVLTQenmFWNALNNTfaIDLTMHDR----SIVLLPLFHIGGIglfaFPTLFAGGVIIVPR--KFEPTKALSMIEKHKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 312 TQCLAAPSVYRMILQqnyTSLRF-PTLEHC--CTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGISCGTL--RGMKIKP 386
Cdd:PRK06839 240 TVVMGVPTIHQALIN---CSKFEtTNLQSVrwFYNGGAPCPEELMREFIDRGFLFGQGFGMTETSPTVFMLseEDARRKV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 387 GSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTrpigLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLG 466
Cdd:PRK06839 317 GSIGKPVLFCDYELIDENKNKVEVGEVGELLIR-GPN----VMKEYWNRPDATEETIQDGWLCTGDLARVDEDGFVYIVG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 467 RSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgeltKELQQHVKSVTAPYKY 546
Cdd:PRK06839 392 RKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIE-----KDVIEHCRLFLAKYKI 466
|
490 500
....*....|....*....|...
gi 529006476 547 PRKVEFVSELPKTITGKIKRSEL 569
Cdd:PRK06839 467 PKEIVFLKELPKNATGKIQKAQL 489
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
87-569 |
1.12e-50 |
|
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: 182.05 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTqTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:cd05904 34 TYAELERRVRRLAAGLA-KRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVApecpsLKTKLLVSDHSReGWLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPK--MAKHSHGFAL 244
Cdd:cd05904 113 ELAEKLASLA-----LPVVLLDSAEFD-SLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKgvMLTHRNLIAM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 245 RSYFPAcRKLLQLKMSDVFWCL-------SDTGWILAALGsllepwtAGSTVFAhhLPQFDPKVIIETFFKYPITQCLAA 317
Cdd:cd05904 187 VAQFVA-GEGSNSDSEDVFLCVlpmfhiyGLSSFALGLLR-------LGATVVV--MPRFDLEELLAAIERYKVTHLPVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 318 PS-VYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQ-TGVLLYQAYGQSEAG---ISCGTLRGMKIKPGSMGKA 392
Cdd:cd05904 257 PPiVLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfPNVDLGQGYGMTESTgvvAMCFAPEKDRAKYGSVGRL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 393 IPPFDIQIID-DKGNIQPPNTEGNIGIRiKPTRPIGlfmyYENNPEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDD 470
Cdd:cd05904 337 VPNVEAKIVDpETGESLPPNQTGELWIR-GPSIMKG----YLNNPEATAATIDKEgWLHTGDLCYIDEDGYLFIVDRLKE 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 471 VINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfssrdpGELT-KELQQHVKSVTAPYKYPRK 549
Cdd:cd05904 412 LIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPG------SSLTeDEIMDFVAKQVAPYKKVRK 485
|
490 500
....*....|....*....|
gi 529006476 550 VEFVSELPKTITGKIKRSEL 569
Cdd:cd05904 486 VAFVDAIPKSPSGKILRKEL 505
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
83-570 |
7.76e-50 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 181.12 E-value: 7.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAI 162
Cdd:PRK12583 43 ALRYTWRQLADAVDRLARGLLAL-GVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 163 VTTDT------------LAPEVESVAPEC------PSLKTKLLVSDHSREGWLDFRSLVKSA---SPDHICIKSKTL--- 218
Cdd:PRK12583 122 ICADAfktsdyhamlqeLLPGLAEGQPGAlacerlPELRGVVSLAPAPPPGFLAWHELQARGetvSREALAERQASLdrd 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHGFALRS-YFPACRklLQLKMSDV-------FWCLsdtGWILAALGSLlepwTAGSTVF 290
Cdd:PRK12583 202 DPINIQYTSGTTGFPKGATLSHHNILNNgYFVAES--LGLTEHDRlcvpvplYHCF---GMVLANLGCM----TVGACLV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 291 ahhLPQ--FDPKVIIETFFKypiTQCLAAPSVYRMILQQ---------NYTSLRfptlehccTGGEALLPEEQEQWKRQT 359
Cdd:PRK12583 273 ---YPNeaFDPLATLQAVEE---ERCTALYGVPTMFIAEldhpqrgnfDLSSLR--------TGIMAGAPCPIEVMRRVM 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 360 GVL----LYQAYGQSEAG-ISCGTLRG--MKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGirikpTRPIGLFMYY 432
Cdd:PRK12583 339 DEMhmaeVQIAYGMTETSpVSLQTTAAddLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELC-----TRGYSVMKGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 433 ENNPEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVV 511
Cdd:PRK12583 414 WNNPEATAESIDEDgWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEI 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 529006476 512 KAFIVLNPEFSSRDpgeltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK12583 494 VAWVRLHPGHAASE-----EELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMR 547
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
87-570 |
1.48e-49 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 180.07 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:PRK08751 52 TYREADQLVEQFAAYLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVID 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVAPECPSLKT------------------------KLLVSDHSREGWLDFRSLVKSASPDHICIKSKTLDPMA 222
Cdd:PRK08751 132 NFGTTVQQVIADTPVKQVittglgdmlgfpkaalvnfvvkyvKKLVPEYRINGAIRFREALALGRKHSMPTLQIEPDDIA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IF-FTSGTTGFPKMAKHSHgfalrsyfpacRKLLQlKMSDVFWCLSDTGWILAA---LGSLLEPW-----TAGSTVF--- 290
Cdd:PRK08751 212 FLqYTGGTTGVAKGAMLTH-----------RNLVA-NMQQAHQWLAGTGKLEEGcevVITALPLYhifalTANGLVFmki 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 291 --AHHL---PQfDPKVIIETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLY 364
Cdd:PRK08751 280 ggCNHLisnPR-DMPGFVKELKKTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTLV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 365 QAYGQSEAG-ISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmyYENNPEKTAEVE 443
Cdd:PRK08751 359 EAYGLTETSpAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIK-GPQVMKG----YWKRPEETAKVM 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 444 CGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVlnpefs 522
Cdd:PRK08751 434 DADgWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIV------ 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 529006476 523 SRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK08751 508 KKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELR 555
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
85-576 |
3.58e-49 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 177.46 E-value: 3.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 85 KWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVT 164
Cdd:PRK03640 27 KVTFMELHEAVVSVAGKLAAL-GVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 165 TDTLAPEVESVAPecpslktkllvsdhsregwLDFRSLVKSASPDHICIKSKTLDPMA-IFFTSGTTGFPKMAKHSHGfa 243
Cdd:PRK03640 106 DDDFEAKLIPGIS-------------------VKFAELMNGPKEEAEIQEEFDLDEVAtIMYTSGTTGKPKGVIQTYG-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 244 lRSYFPACRKLLQLKMSDvfwclsDTGWiLAA--------LGSLLEPWTAGSTVFAHhlPQFDPKVIIETFFKYPITqcl 315
Cdd:PRK03640 165 -NHWWSAVGSALNLGLTE------DDCW-LAAvpifhisgLSILMRSVIYGMRVVLV--EKFDAEKINKLLQTGGVT--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 316 aAPSVYRMILQQ--------NY-TSLR----------FPTLEHCctggeallpeeqeqwkRQTGVLLYQAYGQSEAGISC 376
Cdd:PRK03640 232 -IISVVSTMLQRllerlgegTYpSSFRcmllgggpapKPLLEQC----------------KEKGIPVYQSYGMTETASQI 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 377 GTL--RGMKIKPGSMGKAIPPFDIQIIDDkGNIQPPNTEGNIGIRiKPTRPIGlfmyYENNPEKTAEVECGDFYNTGDRA 454
Cdd:PRK03640 295 VTLspEDALTKLGSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVK-GPNVTKG----YLNREDATRETFQDGWFKTGDIG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 455 TIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSrdpgeltKELQ 534
Cdd:PRK03640 369 YLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTE-------EELR 441
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 529006476 535 QHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEFGQ 576
Cdd:PRK03640 442 HFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
84-570 |
1.42e-48 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 177.71 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 84 VKWSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIV 163
Cdd:PRK12492 48 VTLSYAELERHSAAFAAYLQQHTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 164 TTDTLAPEVESVAPEC--------------PSLK----------TKLLVSDHSREGWLDFRSLVKSASPDHICIKSKTLD 219
Cdd:PRK12492 128 YLNMFGKLVQEVLPDTgieylieakmgdllPAAKgwlvntvvdkVKKMVPAYHLPQAVPFKQALRQGRGLSLKPVPVGLD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 220 PMAIF-FTSGTTGFPKMAKHSHGFalrsyfpacrklLQLKMSDVFWCLSDTGwilAALGSLLEpwtAGSTVFAHHLPQF- 297
Cdd:PRK12492 208 DIAVLqYTGGTTGLAKGAMLTHGN------------LVANMLQVRACLSQLG---PDGQPLMK---EGQEVMIAPLPLYh 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 298 ----------------------DPKVI---IETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEE 351
Cdd:PRK12492 270 iyaftancmcmmvsgnhnvlitNPRDIpgfIKELGKWRFSALLGLNTLFVALMDHpGFKDLDFSALKLTNSGGTALVKAT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 352 QEQWKRQTGVLLYQAYGQSEAG-ISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfm 430
Cdd:PRK12492 350 AERWEQLTGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIK-GPQVMKG--- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 431 yYENNPEKTAEV-ECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGE 509
Cdd:PRK12492 426 -YWQQPEATAEAlDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGE 504
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529006476 510 VVKAFIVlnpefsSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK12492 505 AVKLFVV------ARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELR 559
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
81-571 |
1.54e-48 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 176.67 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILprvpewW-----LVC---VGCIrtGIIFMPGTTQMKAKDILY 152
Cdd:cd12119 21 GEVHRYTYAEVAERARRLANALRRL-GVKPGDRVATLA------WnthrhLELyyaVPGM--GAVLHTINPRLFPEQIAY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 153 RLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSR------EGWLDFRSLVKSASPDHICIKSKTLDPMAIFFT 226
Cdd:cd12119 92 IINHAEDRVVFVDRDFLPLLEAIAPRLPTVEHVVVMTDDAAmpepagVGVLAYEELLAAESPEYDWPDFDENTAAAICYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 227 SGTTGFPKMAKHSHgfalRSYFPACrklLQLKMSDVF-WCLSDT-----------GWILaalgsllePWTAGSTVFAHHL 294
Cdd:cd12119 172 SGTTGNPKGVVYSH----RSLVLHA---MAALLTDGLgLSESDVvlpvvpmfhvnAWGL--------PYAAAMVGAKLVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 295 PQ--FDPKVIIETFFKYPITQCLAAPSVYRMILQ-QNYTSLRFPTLEHCCTGGEALlPEEQEQWKRQTGVLLYQAYGQSE 371
Cdd:cd12119 237 PGpyLDPASLAELIEREGVTFAAGVPTVWQGLLDhLEANGRDLSSLRRVVIGGSAV-PRSLIEAFEERGVRVIHAWGMTE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 A---GISCGTLRGMKIKPG--------SMGKAIPPFDIQIIDDKGNIQP--PNTEGNIGIRiKPTRPIGlfmYYeNNPEK 438
Cdd:cd12119 316 TsplGTVARPPSEHSNLSEdeqlalraKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVR-GPWVTKS---YY-KNDEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 439 TAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLn 518
Cdd:cd12119 391 SEALTEDGWLRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVL- 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 529006476 519 pefssRDPGELT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd12119 470 -----KEGATVTaEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
77-571 |
5.27e-48 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 175.71 E-value: 5.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 77 VNDQGdeVKWSFREMTDLTCRTANVLTQtCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQV 156
Cdd:PRK06087 43 VDNHG--ASYTYSALDHAASRLANWLLA-KGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLNK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 157 SGAKAIVT------TDTLaPEVESVAPECPSLKTKLLVSDHSREgwldfrslVKSASPDHICIKSKTL---------DPM 221
Cdd:PRK06087 120 CQAKMFFAptlfkqTRPV-DLILPLQNQLPQLQQIVGVDKLAPA--------TSSLSLSQIIADYEPLttaitthgdELA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 222 AIFFTSGTTGFPKMAKHSHG---FALRSYFpacrKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAhhLPQFD 298
Cdd:PRK06087 191 AVLFTSGTEGLPKGVMLTHNnilASERAYC----ARLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVL--LDIFT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 299 PKVIIETFFKYPITQCLAA-PSVYRMI--LQQNYTslRFPTLEHCCTGGeALLPEEQEQWKRQTGVLLYQAYGQSEagiS 375
Cdd:PRK06087 265 PDACLALLEQQRCTCMLGAtPFIYDLLnlLEKQPA--DLSALRFFLCGG-TTIPKKVARECQQRGIKLLSVYGSTE---S 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 376 C---------GTLRGMkikpGSMGKAIPPFDIQIIDDKGNIQPPNTEGNigiriKPTRPIGLFMYYENNPEKTAEV--EC 444
Cdd:PRK06087 339 SphavvnlddPLSRFM----HTDGYAAAGVEIKVVDEARKTLPPGCEGE-----EASRGPNVFMGYLDEPELTARAldEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 445 GDFYnTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSR 524
Cdd:PRK06087 410 GWYY-SGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSL 488
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 529006476 525 DPGELTKEL-QQHVksvtAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK06087 489 TLEEVVAFFsRKRV----AKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
69-570 |
5.70e-48 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 174.81 E-value: 5.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 69 SPNPALWWVNDQGDEVkwSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAK 148
Cdd:PRK13390 10 APDRPAVIVAETGEQV--SYRQLDDDSAALARVL-YDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 149 DILYRLQVSGAKAIVTTDTLAPEVESVAPECPslktkLLVSDHSR-EGWLDFRSLVKSASPdhicikSKTLDP--MAIFF 225
Cdd:PRK13390 87 EADYIVGDSGARVLVASAALDGLAAKVGADLP-----LRLSFGGEiDGFGSFEAALAGAGP------RLTEQPcgAVMLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 226 TSGTTGFPKmakhshgfALRSYFPA-------------CRKLLQLKMSDVF-------------WClsdtgWILAALGsl 279
Cdd:PRK13390 156 SSGTTGFPK--------GIQPDLPGrdvdapgdpivaiARAFYDISESDIYyssapiyhaaplrWC-----SMVHALG-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 280 lepwtaGSTVFAHhlpQFDPKVIIETFFKYPITQCLAAPSVYRMILQQN---YTSLRFPTLE---HCCTGGEALLPEEQE 353
Cdd:PRK13390 221 ------GTVVLAK---RFDAQATLGHVERYRITVTQMVPTMFVRLLKLDadvRTRYDVSSLRaviHAAAPCPVDVKHAMI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 354 QWkrqTGVLLYQAYGQSEAgiscgtlRGMKI--------KPGSMGKAIPPfDIQIIDDKGNIQPPnteGNIG-IRIKPTR 424
Cdd:PRK13390 292 DW---LGPIVYEYYSSTEA-------HGMTFidspdwlaHPGSVGRSVLG-DLHICDDDGNELPA---GRIGtVYFERDR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 425 pigLFMYYENNPEKTAEVE--CGDFYNT-GDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVS 501
Cdd:PRK13390 358 ---LPFRYLNDPEKTAAAQhpAHPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIG 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529006476 502 SPDPVRGEVVKAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK13390 435 VPDPEMGEQVKAVIQLVEGIRGSD--ELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
82-570 |
6.12e-48 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 175.33 E-value: 6.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:PRK06155 43 GGTRWTYAEAARAAAAAAHAL-AAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTLAPEVESVAPECPSLKTKLLVSDHSREGW---LDFRSLVKSASPDHiCIKSKTLDPMAIFFTSGTTGFPKMAKH 238
Cdd:PRK06155 122 LVVEAALLAALEAADPGDLPLPAVWLLDAPASVSVpagWSTAPLPPLDAPAP-AAAVQPGDTAAILYTSGTTGPSKGVCC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 SHG-FALRSYFPAcrKLLQLKMSDVFWC---LSDTGwilaALGSLLEPWTAGSTVFahhlpqFDPKVIIETFFkyPITQC 314
Cdd:PRK06155 201 PHAqFYWWGRNSA--EDLEIGADDVLYTtlpLFHTN----ALNAFFQALLAGATYV------LEPRFSASGFW--PAVRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 315 LAAPSVYRM-----ILQQNYTSL--RFPTLEHCCTGGEAllPEEQEQWKRQTGVLLYQAYGQSEAGISCGTLRGMKiKPG 387
Cdd:PRK06155 267 HGATVTYLLgamvsILLSQPAREsdRAHRVRVALGPGVP--AALHAAFRERFGVDLLDGYGSTETNFVIAVTHGSQ-RPG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 388 SMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPtrPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGR 467
Cdd:PRK06155 344 SMGRLAPGFEARVVDEHDQELPDGEPGELLLRADE--PFAFATGYFGMPEKTVEAWRNLWFHTGDRVVRDADGWFRFVDR 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 468 SDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfSSRDPGELTKelqqHVKSVTAPYKYP 547
Cdd:PRK06155 422 IKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDG-TALEPVALVR----HCEPRLAYFAVP 496
|
490 500
....*....|....*....|...
gi 529006476 548 RKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK06155 497 RYVEFVAALPKTENGKVQKFVLR 519
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
72-569 |
1.07e-47 |
|
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: 172.82 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 72 PALWWVNDqgdevKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPgttqmkakdil 151
Cdd:cd05945 8 PAVVEGGR-----TLTYRELKERADALAAAL-ASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVP----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 152 yrlqvsgakaiVTTDTLAPEVESVAPECpslKTKLLVSDhsregwldfrslvksasPDhiciksktlDPMAIFFTSGTTG 231
Cdd:cd05945 71 -----------LDASSPAERIREILDAA---KPALLIAD-----------------GD---------DNAYIIFTSGSTG 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 232 FPKMAKHSHGfALRSYFPACRKLLQLKMSDVFWCLSDTGWILAaLGSLLEPWTAGSTVFAhhLP---QFDPKVIIETFFK 308
Cdd:cd05945 111 RPKGVQISHD-NLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLS-VMDLYPALASGATLVP--VPrdaTADPKQLFRFLAE 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 309 YPITQCLAAPSVYRMILQ-QNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQT-GVLLYQAYGQSEAGISCGT-------L 379
Cdd:cd05945 187 HGITVWVSTPSFAAMCLLsPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYievtpevL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 380 RGMKIKPgsMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmyYENNPEKTAEV----ECGDFYNTGDRAT 455
Cdd:cd05945 267 DGYDRLP--IGYAKPGAKLVILDEDGRPVPPGEKGELVIS-GPSVSKG----YLNNPEKTAAAffpdEGQRAYRTGDLVR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 456 IDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVssPDPVRGEVVK--AFIVLNPEfssrDPGELTKEL 533
Cdd:cd05945 340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVV--PKYKGEKVTEliAFVVPKPG----AEAGLTKAI 413
|
490 500 510
....*....|....*....|....*....|....*.
gi 529006476 534 QQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd05945 414 KAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
294-566 |
1.81e-47 |
|
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: 168.99 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 294 LPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCcTGGEAllPEEQEQWKRQTGVLLYQAYGQSE- 371
Cdd:cd17637 72 MEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAaEKSGVDLSSLRHV-LGLDA--PETIQRFEETTGATFWSLYGQTEt 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 AGIScgTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTrpigLFMYYENNPEKTAEVECGDFYNTG 451
Cdd:cd17637 149 SGLV--TLSPYRERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVR-GPL----VFQGYWNLPELTAYTFRNGWHHTG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 452 DRATIDEEGYFWFLGRS--DDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSsrdpgeL 529
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGAT------L 295
|
250 260 270
....*....|....*....|....*....|....*...
gi 529006476 530 T-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKR 566
Cdd:cd17637 296 TaDELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
87-499 |
5.41e-47 |
|
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: 169.75 E-value: 5.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVAPECpslktkLLVSDhsregwLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGfALRS 246
Cdd:TIGR01733 81 ALASRLAGLVLPV------ILLDP------LELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHR-SLVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 247 YFPACRKLLQLKMSDVFWCLS----DtgwilAALGSLLEPWTAGSTVF--AHHLPQFDPKVIIETFFKYPITQCLAAPSV 320
Cdd:TIGR01733 148 LLAWLARRYGLDPDDRVLQFAslsfD-----ASVEEIFGALLAGATLVvpPEDEERDDAALLAALIAEHPVTVLNLTPSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 321 YRMILQQNYTSLrfPTLEHCCTGGEALLPEEQEQWKRQTG-VLLYQAYGQSEAGISCGTLRGMKIKPGSM-----GKAIP 394
Cdd:TIGR01733 223 LALLAAALPPAL--ASLRLVILGGEALTPALVDRWRARGPgARLINLYGPTETTVWSTATLVDPDDAPREspvpiGRPLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 395 PFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAEV---------ECGDFYNTGDRATIDEEGYFWFL 465
Cdd:TIGR01733 301 NTRLYVLDDDLRPVPVGVVGELYIG-----GPGVARGYLNRPELTAERfvpdpfaggDGARLYRTGDLVRYLPDGNLEFL 375
|
410 420 430
....*....|....*....|....*....|....
gi 529006476 466 GRSDDVINASGYRVGPAEVENALAEHPAVAESAV 499
Cdd:TIGR01733 376 GRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
87-570 |
1.16e-46 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 172.13 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:PRK07059 50 TYGELDELSRALAAWL-QSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVAPECP-------SL----------------KTKLLVSDHSREGWLDFRSLVKSASpdHICIKSKTLDPMAI 223
Cdd:PRK07059 129 NFATTVQQVLAKTAvkhvvvaSMgdllgfkghivnfvvrRVKKMVPAWSLPGHVRFNDALAEGA--RQTFKPVKLGPDDV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 224 FF---TSGTTGFPKMAKHSHgfalrsyfpacRKLLQLKMSDVFWCLS--------DTGWILAAL----------GSLLEP 282
Cdd:PRK07059 207 AFlqyTGGTTGVSKGATLLH-----------RNIVANVLQMEAWLQPafekkprpDQLNFVCALplyhifaltvCGLLGM 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 283 WTAGSTVFahhLPqfDPKVI---IETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRQ 358
Cdd:PRK07059 276 RTGGRNIL---IP--NPRDIpgfIKELKKYQVHIFPAVNTLYNALLNNpDFDKLDFSKLIVANGGGMAVQRPVAERWLEM 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 359 TGVLLYQAYGQSEAG--ISCGTLRGMKIKpGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmyYENNP 436
Cdd:PRK07059 351 TGCPITEGYGLSETSpvATCNPVDATEFS-GTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIR-GPQVMAG----YWNRP 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 437 EKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFI 515
Cdd:PRK07059 425 DETAKVMTADgFFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFV 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 529006476 516 VlnpefsSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK07059 505 V------KKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRRELR 553
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
85-570 |
1.24e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 170.76 E-value: 1.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 85 KWSFREMTDLTCRTANVLtQTCGLQTGDRLAlILPRVPEWWLVC-VGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIV 163
Cdd:PRK09088 22 RWTYAELDALVGRLAAVL-RRRGCVDGERLA-VLARNSVWLVALhFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 164 TTDTLA---PEVESVApecpslktkllvsdhsregwlDFRSLVKSASPDhiciKSKTLDPMA---IFFTSGTTGFPKMAK 237
Cdd:PRK09088 100 GDDAVAagrTDVEDLA---------------------AFIASADALEPA----DTPSIPPERvslILFTSGTSGQPKGVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 238 HS--------HGFALrsyfpacrkLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHhlPQFDPKVIIETF--F 307
Cdd:PRK09088 155 LSernlqqtaHNFGV---------LGRVDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVS--NGFEPKRTLGRLgdP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 308 KYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRQtGVLLYQAYGQSEAG------ISCGTLR 380
Cdd:PRK09088 224 ALGITHYFCVPQMAQAFRAQpGFDAAALRHLTALFTGGAPHAAEDILGWLDD-GIPMVDGFGMSEAGtvfgmsVDCDVIR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 381 GmkiKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTrpigLFMYYENNPEKTAEVECGD-FYNTGDRATIDEE 459
Cdd:PRK09088 303 A---KAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLR-GPN----LSPGYWRRPQATARAFTGDgWFRTGDIARRDAD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 460 GYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfssrDPGELtKELQQHVKS 539
Cdd:PRK09088 375 GFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADG----APLDL-ERIRSHLST 449
|
490 500 510
....*....|....*....|....*....|.
gi 529006476 540 VTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK09088 450 RLAKYKVPKHLRLVDALPRTASGKLQKARLR 480
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
87-573 |
2.28e-46 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 171.39 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:PRK08974 50 TFRKLEERSRAFAAYLQNGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVIVS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVAPECPsLKTKLLvsdhSREG-WLDF--RSLV------------KSASPDHICIKsKTL------------- 218
Cdd:PRK08974 130 NFAHTLEKVVFKTP-VKHVIL----TRMGdQLSTakGTLVnfvvkyikrlvpKYHLPDAISFR-SALhkgrrmqyvkpel 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 --DPMAIF-FTSGTTGFPKMAKHSHGF-------ALRSYFPACRK-----LLQLKMSDVFwclsdtgwilaALgsllepw 283
Cdd:PRK08974 204 vpEDLAFLqYTGGTTGVAKGAMLTHRNmlanleqAKAAYGPLLHPgkelvVTALPLYHIF-----------AL------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 284 TAGSTVFAH----HLPQFDPKVI---IETFFKYPITQCLAAPSVYRMILQ-QNYTSLRFPTLEHCCTGGEALLPEEQEQW 355
Cdd:PRK08974 266 TVNCLLFIElggqNLLITNPRDIpgfVKELKKYPFTAITGVNTLFNALLNnEEFQELDFSSLKLSVGGGMAVQQAVAERW 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 356 KRQTGVLLYQAYGQSEAG--ISCGTLrGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmyYE 433
Cdd:PRK08974 346 VKLTGQYLLEGYGLTECSplVSVNPY-DLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVK-GPQVMLG----YW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 434 NNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKA 513
Cdd:PRK08974 420 QRPEATDEVIKDGWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAVGVPSEVSGEAVKI 499
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529006476 514 FIVlnpefsSRDPGeLTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKE 573
Cdd:PRK08974 500 FVV------KKDPS-LTEeELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEA 553
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
87-571 |
5.26e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 170.57 E-value: 5.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:PRK05605 59 TYAELGKQVRRAAAGL-RALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVES----VAPE----------------------CPSLKTKLLVSDHSREGWLDFRSLVKSASPDHICIKSK---T 217
Cdd:PRK05605 138 KVAPTVERlrrtTPLEtivsvnmiaampllqrlalrlpIPALRKARAALTGPAPGTVPWETLVDAAIGGDGSDVSHprpT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 218 LDPMA-IFFTSGTTGFPKMAKHSHGfALRSyfpacrKLLQLKMsdvfWC--LSDTG-WILAAL----------GSLLEPW 283
Cdd:PRK05605 218 PDDVAlILYTSGTTGKPKGAQLTHR-NLFA------NAAQGKA----WVpgLGDGPeRVLAALpmfhaygltlCLTLAVS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 284 TAGSTVFahhLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQ------NYTSLRFPTlehccTGGEALLPEEQEQWKR 357
Cdd:PRK05605 287 IGGELVL---LPAPDIDLILDAMKKHPPTWLPGVPPLYEKIAEAaeergvDLSGVRNAF-----SGAMALPVSTVELWEK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 358 QTGVLLYQAYGQSE-AGISCGTLRGMKIKPGSMGKAIPPFDIQIID--DKGNIQPPNTEGNIGIRiKPTRpiglFMYYEN 434
Cdd:PRK05605 359 LTGGLLVEGYGLTEtSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVR-GPQV----FKGYWN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 435 NPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAF 514
Cdd:PRK05605 434 RPEETAKSFLDGWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAA 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 529006476 515 IVLnpefssrDPGELTKE--LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK05605 514 VVL-------EPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
87-577 |
6.21e-46 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 169.10 E-value: 6.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTcGLQTGDRLALIL---PRVPEwwlVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIV 163
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSL-GLKRGDHVAIFMennLRYLE---VCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 164 TTDTLAPEVESVAPECPSLKTKLLV-SDHSREGWLDFRSLVKSASPDHICIKSkTLDPMaiFFTSGTTGFPKMAK----H 238
Cdd:PRK13391 102 TSAAKLDVARALLKQCPGVRHRLVLdGDGELEGFVGYAEAVAGLPATPIADES-LGTDM--LYSSGTTGRPKGIKrplpE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 SHGFALRSYFPACRKLLQLKMSDVFWC---LSDTGwILAALGSLLEpwTAGSTVFAHHlpqFDPKVIIETFFKYPITQCL 315
Cdd:PRK13391 179 QPPDTPLPLTAFLQRLWGFRSDMVYLSpapLYHSA-PQRAVMLVIR--LGGTVIVMEH---FDAEQYLALIEEYGVTHTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 316 AAPSVY-RMILQQNYTSLRF--PTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEA-GISCGTLRGMKIKPGSMGK 391
Cdd:PRK13391 253 LVPTMFsRMLKLPEEVRDKYdlSSLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGlGFTACDSEEWLAHPGTVGR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 392 AIppF-DIQIIDDKGNIQPPNTEGNIgiRIKPTRPiglFMYYeNNPEKTAEV--ECGDFYNTGDRATIDEEGYFWFLGRS 468
Cdd:PRK13391 333 AM--FgDLHILDDDGAELPPGEPGTI--WFEGGRP---FEYL-NDPAKTAEArhPDGTWSTVGDIGYVDEDGYLYLTDRA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 469 DDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPefsSRDPG-ELTKELQQHVKSVTAPYKYP 547
Cdd:PRK13391 405 AFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVD---GVDPGpALAAELIAFCRQRLSRQKCP 481
|
490 500 510
....*....|....*....|....*....|
gi 529006476 548 RKVEFVSELPKTITGKIKRSELRKKEFGQK 577
Cdd:PRK13391 482 RSIDFEDELPRLPTGKLYKRLLRDRYWGNK 511
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
213-571 |
7.04e-46 |
|
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: 166.75 E-value: 7.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 213 IKSKTLDPMAIFFTSGTTGFPKMAKHSHGfalRSYFPACRKLLQLKMSDvfwclsDTGWILA-------ALGSLLEPWTA 285
Cdd:cd05912 72 SDVKLDDIATIMYTSGTTGKPKGVQQTFG---NHWWSAIGSALNLGLTE------DDNWLCAlplfhisGLSILMRSVIY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 286 GSTVFAHhlPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQnYTSLRFPTLEHCCTGGEALLPEEQEQWKrQTGVLLYQ 365
Cdd:cd05912 143 GMTVYLV--DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEI-LGEGYPNNLRCILLGGGPAPKPLLEQCK-EKGIPVYQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 366 AYGQSEAGISCGTL--RGMKIKPGSMGKAIPPFDIQIIDDKgniQPPNTEGNIGIRiKPTRPIGlfmyYENNPEKTAEVE 443
Cdd:cd05912 219 SYGMTETCSQIVTLspEDALNKIGSAGKPLFPVELKIEDDG---QPPYEVGEILLK-GPNVTKG----YLNRPDATEESF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 444 CGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSS 523
Cdd:cd05912 291 ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISE 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 529006476 524 rdpgeltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd05912 371 -------EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
87-571 |
8.91e-46 |
|
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: 167.17 E-value: 8.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:cd05903 3 TYSELDTRADRLAAGLAAL-GVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 tlapevesvapecpslktkllvsdhsregwlDFRSLVKSASPDHICiksktldpmAIFFTSGTTGFPKMAKHSHGFALRS 246
Cdd:cd05903 82 -------------------------------RFRQFDPAAMPDAVA---------LLLFTSGTTGEPKGVMHSHNTLSAS 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 247 YFPACRKLlQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVfaHHLPQFDPKVIIETFFKYPITQCLAAPS-VYRMIL 325
Cdd:cd05903 122 IRQYAERL-GLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPV--VLQDIWDPDKALALMREHGVTFMMGATPfLTDLLN 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 326 QQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEagiSCGTLRGMKIKP-----GSMGKAIPPFDIQI 400
Cdd:cd05903 199 AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTE---CPGAVTSITPAPedrrlYTDGRPLPGVEIKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 401 IDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVG 480
Cdd:cd05903 276 VDDTGATLAPGVEGELLSRGP-----SVFLGYLDRPDLTADAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIP 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 481 PAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefssRDPGELT-KELQQHVKSV-TAPYKYPRKVEFVSELPK 558
Cdd:cd05903 351 VLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVT------KSGALLTfDELVAYLDRQgVAKQYWPERLVHVDDLPR 424
|
490
....*....|...
gi 529006476 559 TITGKIKRSELRK 571
Cdd:cd05903 425 TPSGKVQKFRLRE 437
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
66-572 |
9.81e-46 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 169.07 E-value: 9.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 66 GKRSPN-PALWWvndqGDEVkWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQ 144
Cdd:PRK07470 17 ARRFPDrIALVW----GDRS-WTWREIDARVDALAAAL-AARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 145 MKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKllVSDHSREGWLDFRSLV--------KSASPDHIciksk 216
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADFPEHAAAVRAASPDLTHV--VAIGGARAGLDYEALVarhlgarvANAAVDHD----- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 217 tlDPMAIFFTSGTTGFPKMAKHSHG---FALRSY----FPAcrkLLQLKMSDVFWCLSDTgwilAALGSLLEPWTAGSTV 289
Cdd:PRK07470 164 --DPCWFFFTSGTTGRPKAAVLTHGqmaFVITNHladlMPG---TTEQDASLVVAPLSHG----AGIHQLCQVARGAATV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 290 FahhLP--QFDPKVIIETFFKYPITQCLAAPSVYRMIL------QQNYTSLRfptleHCCTGGEALLPEEQEQWKRQTGV 361
Cdd:PRK07470 235 L---LPseRFDPAEVWALVERHRVTNLFTVPTILKMLVehpavdRYDHSSLR-----YVIYAGAPMYRADQKRALAKLGK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 362 LLYQAYGQSE--------------------AGI-SCGTLR-GMKIkpgsmgkaippfdiQIIDDKGNIQPPNTEGNIGIR 419
Cdd:PRK07470 307 VLVQYFGLGEvtgnitvlppalhdaedgpdARIgTCGFERtGMEV--------------QIQDDEGRELPPGETGEICVI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 420 IKPtrpigLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV 499
Cdd:PRK07470 373 GPA-----VFAGYYNNPEANAKAFRDGWFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAV 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529006476 500 VSSPDPVRGEVVKAFIVLnpefssRDPGELTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PRK07470 448 LGVPDPVWGEVGVAVCVA------RDGAPVDEaELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREE 515
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
87-576 |
1.53e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 169.17 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:PRK05677 51 TYGELYKLSGAFAAWLQQHTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVAPEC--------------PSLK----------TKLLVSDHSREGWLDFRSLVKSASPDHICIKSKTLDPMA 222
Cdd:PRK05677 131 NMAHLAEKVLPKTgvkhvivtevadmlPPLKrllinavvkhVKKMVPAYHLPQAVKFNDALAKGAGQPVTEANPQADDVA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IF-FTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKmsdvfwcLSDTGWILAALGSLLEPWT------AGSTVFAHHLP 295
Cdd:PRK05677 211 VLqYTGGTTGVAKGAMLTHR-NLVANMLQCRALMGSN-------LNEGCEILIAPLPLYHIYAftfhcmAMMLIGNHNIL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 296 QFDPKVI---IETFFKYPITQCLAAPSVYRMILQ-QNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSE 371
Cdd:PRK05677 283 ISNPRDLpamVKELGKWKFSGFVGLNTLFVALCNnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGCAICEGYGMTE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 AG-ISCGTLRGmKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmyYENNPEKTAEVECGD-FYN 449
Cdd:PRK05677 363 TSpVVSVNPSQ-AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVK-GPQVMKG----YWQRPEATDEILDSDgWLK 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 450 TGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSsrdpgeL 529
Cdd:PRK05677 437 TGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVVKPGET------L 510
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 529006476 530 TKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEFGQ 576
Cdd:PRK05677 511 TKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKK 558
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
83-571 |
2.71e-45 |
|
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: 166.71 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAI 162
Cdd:cd12118 27 DRRYTWRQTYDRCRRLASALAAL-GISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 163 VTtdtlapevesvapecpslktkllvsDHSregwLDFRSLVKSASPDH--ICIKSKTlDPMAIFFTSGTTGFPKMAKHSH 240
Cdd:cd12118 106 FV-------------------------DRE----FEYEDLLAEGDPDFewIPPADEW-DPIALNYTSGTTGRPKGVVYHH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 -GFALRSYF--------PACRKLLQLKMsdvF----WCLSdtgWILAALGsllepwtaGSTVFahhLPQFDPKVIIETFF 307
Cdd:cd12118 156 rGAYLNALAnilewemkQHPVYLWTLPM---FhcngWCFP---WTVAAVG--------GTNVC---LRKVDAKAIYDLIE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 308 KYPITQCLAAPSVYRMILQ-QNYTSLRFPTLEHCCTGGeALLPEEQEQWKRQTGVLLYQAYGQSEA---GISCGTLRGMK 383
Cdd:cd12118 219 KHKVTHFCGAPTVLNMLANaPPSDARPLPHRVHVMTAG-APPPAAVLAKMEELGFDVTHVYGLTETygpATVCAWKPEWD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 384 IKPG---SMGKA------IPPFDIQIIDDKGNIQPP---NTEGNIGIRikptrpiG-LFM--YYeNNPEKTAEVECGDFY 448
Cdd:cd12118 298 ELPTeerARLKArqgvryVGLEEVDVLDPETMKPVPrdgKTIGEIVFR-------GnIVMkgYL-KNPEATAEAFRGGWF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 449 NTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefssRDPGE 528
Cdd:cd12118 370 HSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVEL------KEGAK 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 529006476 529 LT-KELQQHVKSVTAPYKYPRKVEFvSELPKTITGKIKRSELRK 571
Cdd:cd12118 444 VTeEEIIAFCREHLAGFMVPKTVVF-GELPKTSTGKIQKFVLRD 486
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
42-566 |
7.20e-45 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 168.20 E-value: 7.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 42 DYDRPE--------EFNFASDVLDHWTQmekegKRSPNPALWWVNDQGDEVK-WSFREMTDLTCRTANVLtQTCGLQTGD 112
Cdd:PRK10524 37 DYSNPPfarwfvggRTNLCHNAVDRHLA-----KRPEQLALIAVSTETDEERtYTFRQLHDEVNRMAAML-RSLGVQRGD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 113 RLALILPRVPEWWLVCVGCIRTGIIfmpgttqmkakdilyRLQVSGAKAivtTDTLAPEVESVAPecpslktKLLVSDH- 191
Cdd:PRK10524 111 RVLIYMPMIAEAAFAMLACARIGAI---------------HSVVFGGFA---SHSLAARIDDAKP-------VLIVSADa 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 192 -SREG-WLDFRSLVKSA------SPDHICIKSKTLDPMA---------------------------------IFFTSGTT 230
Cdd:PRK10524 166 gSRGGkVVPYKPLLDEAialaqhKPRHVLLVDRGLAPMArvagrdvdyatlraqhlgarvpvewlesnepsyILYTSGTT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 231 GFPKMAKHS---HGFALRSyfpACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAG-STVFAHHLP-QFDPKV---I 302
Cdd:PRK10524 246 GKPKGVQRDtggYAVALAT---SMDTIFGGKAGETFFCASDIGWVVGHSYIVYAPLLAGmATIMYEGLPtRPDAGIwwrI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 303 IEtffKYPITQCLAAPSVYRMILQQNYTSLR---FPTLEHCCTGGEALlPEEQEQWKRQT-GVLLYQAYGQSEAG---IS 375
Cdd:PRK10524 323 VE---KYKVNRMFSAPTAIRVLKKQDPALLRkhdLSSLRALFLAGEPL-DEPTASWISEAlGVPVIDNYWQTETGwpiLA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 376 -CGTLRGMKIKPGSMGKAIPPFDIQIIDDK-GNIQPPNTEGNIGIRikPTRPIGlFM-------------YYENNPEKTa 440
Cdd:PRK10524 399 iARGVEDRPTRLGSPGVPMYGYNVKLLNEVtGEPCGPNEKGVLVIE--GPLPPG-CMqtvwgdddrfvktYWSLFGRQV- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 441 evecgdfYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPE 520
Cdd:PRK10524 475 -------YSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDS 547
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 529006476 521 FSSRDPG---ELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKR 566
Cdd:PRK10524 548 DSLADREarlALEKEIMALVDSQLGAVARPARVWFVSALPKTRSGKLLR 596
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
81-569 |
1.25e-44 |
|
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: 164.31 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:cd05907 1 GVWQPITWAEFAEEVRALAKGL-IALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTTDtlapevesvapecpslktkllvsdhsregwldfrslvksasPDhiciksktlDPMAIFFTSGTTGFPKMAKHSH 240
Cdd:cd05907 80 ALFVED-----------------------------------------PD---------DLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 GfALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTV-FAHhlpqfDPKVIIETFFKYPITQCLAAPS 319
Cdd:cd05907 110 R-NILSNALALAERLPATEGDRHLSFLPLAHVFERRAGLYVPLLAGARIyFAS-----SAETLLDDLSEVRPTVFLAVPR 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 320 VYRM----ILQQNYTSLR--------FPTLEHCCTGGeALLPEEQEQWKRQTGVLLYQAYGQSE--AGISCGTLRgmKIK 385
Cdd:cd05907 184 VWEKvyaaIKVKAVPGLKrklfdlavGGRLRFAASGG-APLPAELLHFFRALGIPVYEGYGLTEtsAVVTLNPPG--DNR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 386 PGSMGKAIPPFDIQIIDDkGNIQppntegnigirikpTRPIGLFMYYENNPEKTAEVECGD-FYNTGDRATIDEEGYFWF 464
Cdd:cd05907 261 IGTVGKPLPGVEVRIADD-GEIL--------------VRGPNVMLGYYKNPEATAEALDADgWLHTGDLGEIDEDGFLHI 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 465 LGRSDDVI-NASGYRVGPAEVENALAEHPAVAESAVVSSPDPvrgeVVKAFIVLNPEF----------SSRDPGELTK-- 531
Cdd:cd05907 326 TGRKKDLIiTSGGKNISPEPIENALKASPLISQAVVIGDGRP----FLVALIVPDPEAleawaeehgiAYTDVAELAAnp 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 529006476 532 ----ELQQHVKSVTA---PYKYPRKVEFVSElPKTI-------TGKIKRSEL 569
Cdd:cd05907 402 avraEIEAAVEAANArlsRYEQIKKFLLLPE-PFTIengeltpTLKLKRPVI 452
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-570 |
1.65e-44 |
|
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: 161.29 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSH-GFALRSYFPACRklLQLKMSDV-------FWCLsdtGWILAALGSLlepwTAGST-V 289
Cdd:cd05917 3 DVINIQFTSGTTGSPKGATLTHhNIVNNGYFIGER--LGLTEQDRlcipvplFHCF---GSVLGVLACL----THGATmV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 290 FAHhlPQFDPKVIIETFFKYPITQCLAAPSVY-RMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQ-AY 367
Cdd:cd05917 74 FPS--PSFDPLAVLEAIEKEKCTALHGVPTMFiAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTiAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 368 GQSEAG-ISCGTLRGMKI--KPGSMGKAIPPFDIQIIDDKGNIQPP-NTEGNIGIRikptrPIGLFMYYENNPEKTAEVE 443
Cdd:cd05917 152 GMTETSpVSTQTRTDDSIekRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIR-----GYSVMKGYWNDPEKTAEAI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 444 CGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfs 522
Cdd:cd05917 227 DGDgWLHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEG-- 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 529006476 523 srdpGELTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:cd05917 305 ----AELTEEdIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKLR 349
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
48-563 |
1.34e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 163.13 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 48 EFNFAsDVLDHWTqmEKEGKRspnPALWWvndqGDEVkWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLV 127
Cdd:PRK07798 2 AWNIA-DLFEAVA--DAVPDR---VALVC----GDRR-LTYAELEERANRLAHYLIAQ-GLGPGDHVGIYARNRIEYVEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 128 CVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHS----REGWLDFRSLV 203
Cdd:PRK07798 70 MLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVVEDGSgndlLPGAVDYEDAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 204 KSASPDHICIKsKTLDPMAIFFTSGTTGFPK--MAKHSHGFalRSYFPACRKLLQLKMSDVfWCLSDTG-------WI-- 272
Cdd:PRK07798 150 AAGSPERDFGE-RSPDDLYLLYTGGTTGMPKgvMWRQEDIF--RVLLGGRDFATGEPIEDE-EELAKRAaagpgmrRFpa 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 273 ---------LAALGSLLepwtAGSTVFAHHLPQFDP----------KVIIETF----FKYPITQCLAAPSVYrmilqqNY 329
Cdd:PRK07798 226 pplmhgagqWAAFAALF----SGQTVVLLPDVRFDAdevwrtiereKVNVITIvgdaMARPLLDALEARGPY------DL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 330 TSLRFPTlehccTGGEALLPEEQEQWKRQ-TGVLLYQAYGQSEAGiSCGTlrGMKiKPGSMGKAIPPFDIQ----IIDDK 404
Cdd:PRK07798 296 SSLFAIA-----SGGALFSPSVKEALLELlPNVVLTDSIGSSETG-FGGS--GTV-AKGAVHTGGPRFTIGprtvVLDED 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 405 GNIQPPNtEGNIG-IRIKPTRPIGlfmYYeNNPEKTA----EVEcGDFYN-TGDRATIDEEGYFWFLGRSDDVINASGYR 478
Cdd:PRK07798 367 GNPVEPG-SGEIGwIARRGHIPLG---YY-KDPEKTAetfpTID-GVRYAiPGDRARVEADGTITLLGRGSVCINTGGEK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 479 VGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfSSRDPGeltkELQQHVKSVTAPYKYPRKVEFVSELPK 558
Cdd:PRK07798 441 VFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREG-ARPDLA----ELRAHCRSSLAGYKVPRAIWFVDEVQR 515
|
....*
gi 529006476 559 TITGK 563
Cdd:PRK07798 516 SPAGK 520
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
67-572 |
2.71e-43 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 163.35 E-value: 2.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 67 KRSPNPALWWVNDQGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLV-----CVGCIRTGIifmpG 141
Cdd:COG1022 22 ARFPDRVALREKEDGIWQSLTWAEFAERVRALAAGL-LALGVKPGDRVAILSDNRPEWVIAdlailAAGAVTVPI----Y 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 142 TTQMkAKDILYRLQVSGAKAIVT-TDTLAPEVESVAPECPSLKT-----KLLVSDHSREGWLD--------------FRS 201
Cdd:COG1022 97 PTSS-AEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHivvldPRGLRDDPRLLSLDellalgrevadpaeLEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 202 LVKSASPDhiciksktlDPMAIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFWC---LSdtgWILA---A 275
Cdd:COG1022 176 RRAAVKPD---------DLATIIYTSGTTGRPKGVMLTHR-NLLSNARALLERLPLGPGDRTLSflpLA---HVFErtvS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 276 LGSLlepwTAGSTV--------FAHHLPQFDPkviieTFFkypitqcLAAP----SVYRMILQQ---------------- 327
Cdd:COG1022 243 YYAL----AAGATVafaespdtLAEDLREVKP-----TFM-------LAVPrvweKVYAGIQAKaeeagglkrklfrwal 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 328 ---------NYTSLRFPT------------------------LEHCCTGGEALLPEEQEqWKRQTGVLLYQAYGQSE--A 372
Cdd:COG1022 307 avgrryaraRLAGKSPSLllrlkhaladklvfsklrealggrLRFAVSGGAALGPELAR-FFRALGIPVLEGYGLTEtsP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 373 GISCGTLRgmKIKPGSMGKAIPPFDIQIIDDkGNIQppntegnigirikpTRPIGLFM-YYeNNPEKTAEVECGD-FYNT 450
Cdd:COG1022 386 VITVNRPG--DNRIGTVGPPLPGVEVKIAED-GEIL--------------VRGPNVMKgYY-KNPEATAEAFDADgWLHT 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 451 GDRATIDEEGYFWFLGRSDDVI-NASGYRVGPAEVENALAEHPAVAESAVVsspdpvrGE----VVkAFIVLNPEF---- 521
Cdd:COG1022 448 GDIGELDEDGFLRITGRKKDLIvTSGGKNVAPQPIENALKASPLIEQAVVV-------GDgrpfLA-ALIVPDFEAlgew 519
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006476 522 -------------SSRDPgELTKELQQHVKSVT---APYKYPRKVEFvseLPK---------TITGKIKRSELRKK 572
Cdd:COG1022 520 aeenglpytsyaeLAQDP-EVRALIQEEVDRANaglSRAEQIKRFRL---LPKeftiengelTPTLKLKRKVILEK 591
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
68-569 |
8.85e-43 |
|
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: 160.13 E-value: 8.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 68 RSPN-PALWWvndqgDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMK 146
Cdd:cd17646 10 RTPDaPAVVD-----EGRTLTYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 147 AKDILYRLQVSGAKAIVTTDTLA--PEVESVAPECPslktkllvsdhsREGWLDFRSLVKSAS--PDHiciksktldPMA 222
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTADLAarLPAGGDVALLG------------DEALAAPPATPPLVPprPDN---------LAY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPK--MAKHsHGFA-----LRSYFP--ACRKLLQlKMSDVFwclsDTgwilaALGSLLEPWTAGST-VFAH 292
Cdd:cd17646 143 VIYTSGSTGRPKgvMVTH-AGIVnrllwMQDEYPlgPGDRVLQ-KTPLSF----DV-----SVWELFWPLVAGARlVVAR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 293 HLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQNyTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEA 372
Cdd:cd17646 212 PGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAEP-AAGSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 373 GI--SCGTLRGMKIKPG-SMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAEVECGD--- 446
Cdd:cd17646 291 AIdvTHWPVRGPAETPSvPIGRPVPNTRLYVLDDALRPVPVGVPGELYLG-----GVQLARGYLGRPALTAERFVPDpfg 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 447 ----FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFS 522
Cdd:cd17646 366 pgsrMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAA 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 529006476 523 SRDPGELTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd17646 446 GPDTAALRAHLAERL----PEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
60-573 |
1.50e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 160.48 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 60 TQMEKEGKRSPN-PALwwVNDQGdevKWSFREMTDLTCRTANVLtQTCGLQTGDRLAlILPRVPEWWLVC-VGCIRTG-- 135
Cdd:PRK07788 53 GLVAHAARRAPDrAAL--IDERG---TLTYAELDEQSNALARGL-LALGVRAGDGVA-VLARNHRGFVLAlYAAGKVGar 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 136 IIFM-PGTTQMKAKDILYRLqvsGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSD---HSREGWLDFRSLVKSAS---- 207
Cdd:PRK07788 126 IILLnTGFSGPQLAEVAARE---GVKALVYDDEFTDLLSALPPDLGRLRAWGGNPDddePSGSTDETLDDLIAGSStapl 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 208 -----PDHIciksktldpmaIFFTSGTTGFPKMAKHSH--GFA----LRSYFPACRKLLQLKMSDVFwclSDTGWILAAL 276
Cdd:PRK07788 203 pkppkPGGI-----------VILTSGTTGTPKGAPRPEpsPLAplagLLSRVPFRAGETTLLPAPMF---HATGWAHLTL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 277 GSLLepwtaGSTVFAHHlpQFDPKVIIETFFKYPITQCLAAPSVYRMILQ------QNY--TSLRFptlehCCTGGEALL 348
Cdd:PRK07788 269 AMAL-----GSTVVLRR--RFDPEATLEDIAKHKATALVVVPVMLSRILDlgpevlAKYdtSSLKI-----IFVSGSALS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 349 PEEQEQWKRQTGVLLYQAYGQSEAGI-SCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTrpig 427
Cdd:PRK07788 337 PELATRALEAFGPVLYNLYGSTEVAFaTIATPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFP---- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 428 lFMYYENNPEKtaeVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVR 507
Cdd:PRK07788 413 -FEGYTDGRDK---QIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEF 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006476 508 GEVVKAFIVLNPEfSSRDPgeltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKE 573
Cdd:PRK07788 489 GQRLRAFVVKAPG-AALDE----DAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-571 |
1.63e-42 |
|
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: 156.10 E-value: 1.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHGFALrsYFPACRKLLQL-KMSDVFWCLSDTGWILAALGSLLEPWTAG-STVFAHHLPQ 296
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEV--YNAWMLALNSLfDPDDVLLCGLPLFHVNGSVVTLLTPLASGaHVVLAGPAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 297 FDPKVIiETFFK----YPITQCLAAPSVYRMILQ----QNYTSLRFptlehcCTGGEALLPEE-QEQWKRQTGVLLYQAY 367
Cdd:cd05944 81 RNPGLF-DNFWKlverYRITSLSTVPTVYAALLQvpvnADISSLRF------AMSGAAPLPVElRARFEDATGLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 368 GQSEAgiSCGT---LRGMKIKPGSMGKAIPPFDIQI--IDDKGNIQPPNTEGNIGIRIKPTRPI-GLFMYYENNpeKTAE 441
Cdd:cd05944 154 GLTEA--TCLVavnPPDGPKRPGSVGLRLPYARVRIkvLDGVGRLLRDCAPDEVGEICVAGPGVfGGYLYTEGN--KNAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 442 VECGdFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEf 521
Cdd:cd05944 230 VADG-WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPG- 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 529006476 522 SSRDPGELTKELQQHVKSVTApykYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd05944 308 AVVEEEELLAWARDHVPERAA---VPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
81-569 |
3.90e-42 |
|
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: 157.87 E-value: 3.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:cd05920 36 DGDRRLTYRELDRRADRLAAGLRGL-GIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTTDTLAPevesvapecpslktkllvsdhsregwLDFRSL---VKSASPDhiciksktldpMAIFFTS-GTTGFPKMA 236
Cdd:cd05920 115 AYIVPDRHAG--------------------------FDHRALareLAESIPE-----------VALFLLSgGTTGTPKLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 237 KHSH---GFALRsyfpACRKLLQLKMSDVFWC---------LSDTGwilaALGSLlepWTAGSTVFAhhlPQFDPKVIIE 304
Cdd:cd05920 158 PRTHndyAYNVR----ASAEVCGLDQDTVYLAvlpaahnfpLACPG----VLGTL---LAGGRVVLA---PDPSPDAAFP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 305 TFFKYPITQCLAAPSVYRMILQ-QNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEaGISCGTLRG-- 381
Cdd:cd05920 224 LIEREGVTVTALVPALVSLWLDaAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAE-GLLNYTRLDdp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 382 MKIKPGSMGKAIPPFD-IQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmYYeNNPEKTAEVECGD-FYNTGDRATIDEE 459
Cdd:cd05920 303 DEVIIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTR-GPYTIRG---YY-RAPEHNARAFTPDgFYRTGDLVRRTPD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 460 GYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefssRDPGELTKELQQHVKS 539
Cdd:cd05920 378 GYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVL------RDPPPSAAQLRRFLRE 451
|
490 500 510
....*....|....*....|....*....|.
gi 529006476 540 V-TAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd05920 452 RgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
223-572 |
4.56e-42 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 158.77 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPKMAKHShgfALRSYFPacrklLQLKMSDVFWCLSDTGWILAALgslLEPWTAGSTVFAHHLP------- 295
Cdd:PRK13382 201 ILLTSGTTGTPKGARRS---GPGGIGT-----LKAILDRTPWRAEEPTVIVAPM---FHAWGFSQLVLAASLActivtrr 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 296 QFDPKVIIETFFKYPITQCLAAPSVYRMILQ---QNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEA 372
Cdd:PRK13382 270 RFDPEATLDLIDRHRATGLAVVPVMFDRIMDlpaEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 373 G-ISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPtrpigLFMYYenNPEKTAEVECGdFYNTG 451
Cdd:PRK13382 350 GmIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDT-----QFDGY--TSGSTKDFHDG-FMASG 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 452 DRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSsrdpgELTK 531
Cdd:PRK13382 422 DVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGAS-----ATPE 496
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 529006476 532 ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
79-575 |
6.72e-42 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 158.82 E-value: 6.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 79 DQGdeVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSG 158
Cdd:PRK08315 39 DQG--LRWTYREFNEEVDALAKGLLAL-GIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEYALNQSG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 159 AKAIVTTD------------TLAPEVESVAPEC------PSLKTKLLVSDHSREGWLDFRSLV---KSASPDHICIKSKT 217
Cdd:PRK08315 116 CKALIAADgfkdsdyvamlyELAPELATCEPGQlqsarlPELRRVIFLGDEKHPGMLNFDELLalgRAVDDAELAARQAT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 218 L---DPMAIFFTSGTTGFPKMAKHSHGFALRS-YFPAcrKLLQLKMSD-------VFWCLsdtGWILAALGSLlepwTAG 286
Cdd:PRK08315 196 LdpdDPINIQYTSGTTGFPKGATLTHRNILNNgYFIG--EAMKLTEEDrlcipvpLYHCF---GMVLGNLACV----THG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 287 ST-VFAhhLPQFDPKVIIETFFKypiTQCLAAPSVYRMILQQ---------NYTSLRfptlehccTG---GeALLPEEQe 353
Cdd:PRK08315 267 ATmVYP--GEGFDPLATLAAVEE---ERCTALYGVPTMFIAEldhpdfarfDLSSLR--------TGimaG-SPCPIEV- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 354 qWKR------QTGVLLyqAYGQSEAG-ISCGTLRGMKI--KPGSMGKAIPPFDIQIID-DKGNIQPPNTEGNIGIRikpt 423
Cdd:PRK08315 332 -MKRvidkmhMSEVTI--AYGMTETSpVSTQTRTDDPLekRVTTVGRALPHLEVKIVDpETGETVPRGEQGELCTR---- 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 424 rpiG-LFM--YYeNNPEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV 499
Cdd:PRK08315 405 ---GySVMkgYW-NDPEKTAEAIDADgWMHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDVQV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 500 VSSPDPVRGEVVKAFIVLnpefssRDPGELTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR---KKEFG 575
Cdd:PRK08315 481 VGVPDEKYGEEVCAWIIL------RPGATLTEEdVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKIQKFKMRemmIEELG 554
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
90-570 |
8.14e-42 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 160.58 E-value: 8.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 90 EMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLA 169
Cdd:PRK06060 35 QIHDGAARLGEVLRNR-GLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 170 PEVESVAPECPSLktklLVSDHSREGWLDFRSLVKSAspdhiciksktldpmAIF--FTSGTTGFPKMAKHSHGFALRSY 247
Cdd:PRK06060 114 DRFQPSRVAEAAE----LMSEAARVAPGGYEPMGGDA---------------LAYatYTSGTTGPPKAAIHRHADPLTFV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 248 FPACRKLLQLKMSDVFWC---------LSDTGWILAALGS--LLEPWTAGSTVFAHHLPQFDPKVI--IETFFKYPITQC 314
Cdd:PRK06060 175 DAMCRKALRLTPEDTGLCsarmyfaygLGNSVWFPLATGGsaVINSAPVTPEAAAILSARFGPSVLygVPNFFARVIDSC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 315 laAPSVYRmilqqnytSLRfptlehCC-TGGEALLPEEQEQWKRQ-TGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKA 392
Cdd:PRK06060 255 --SPDSFR--------SLR------CVvSAGEALELGLAERLMEFfGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 393 IPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTrpigLFMYYENNPEKTaeVECGDFYNTGDRATIDEEGYFWFLGRSDDVI 472
Cdd:PRK06060 319 LPPYEIRVVAPDGTTAGPGVEGDLWVR-GPA----IAKGYWNRPDSP--VANEGWLDTRDRVCIDSDGWVTYRCRADDTE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 473 NASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVlnPEFSSRDPGELTKELQQHVKSVTAPYKYPRKVEF 552
Cdd:PRK06060 392 VIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLV--ATSGATIDGSVMRDLHRGLLNRLSAFKVPHRFAV 469
|
490
....*....|....*...
gi 529006476 553 VSELPKTITGKIKRSELR 570
Cdd:PRK06060 470 VDRLPRTPNGKLVRGALR 487
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
81-570 |
1.99e-41 |
|
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: 156.35 E-value: 1.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTdltcRTANVLTQTC---GLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVS 157
Cdd:cd17651 16 AEGRRLTYAELD----RRANRLAHRLrarGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 158 GAKAIVT----TDTLAPEVESVAPECPSLKTKLLVSDHSREgwldfrslvksASPDHiciksktldPMAIFFTSGTTGFP 233
Cdd:cd17651 92 GPVLVLThpalAGELAVELVAVTLLDQPGAAAGADAEPDPA-----------LDADD---------LAYVIYTSGSTGRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 234 KMAKHSHG------FALRSYFPACRKLLQLKMS----DV-FWclsdtgWILAALgsllepwTAGSTVfahHLP----QFD 298
Cdd:cd17651 152 KGVVMPHRslanlvAWQARASSLGPGARTLQFAglgfDVsVQ------EIFSTL-------CAGATL---VLPpeevRTD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 299 PKVIIETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEE--QEQWKRQTGVLLYQAYGQSEAGI- 374
Cdd:cd17651 216 PPALAAWLDEQRISRVFLPTVALRALAEHgRPLGVRLAALRYLLTGGEQLVLTEdlREFCAGLPGLRLHNHYGPTETHVv 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 375 SCGTLRGMKIKPG---SMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAE-------VEC 444
Cdd:cd17651 296 TALSLPGDPAAWPappPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGA-----GLARGYLNRPELTAErfvpdpfVPG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 445 GDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfSSR 524
Cdd:cd17651 371 ARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPE-APV 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 529006476 525 DPGELTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:cd17651 450 DAAELRAALATHL----PEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
220-570 |
2.84e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 155.53 E-value: 2.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 220 PMAIFFTSGTTGFPKMAKHShgfalRSYFPACRKLLqlkmSDVF-WCLSDT-----------GWILAALGSLlepwTAGS 287
Cdd:PRK07787 130 PALIVYTSGTTGPPKGVVLS-----RRAIAADLDAL----AEAWqWTADDVlvhglplfhvhGLVLGVLGPL----RIGN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 288 TVfaHHLPQFDPKVIIETFfKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAY 367
Cdd:PRK07787 197 RF--VHTGRPTPEAYAQAL-SEGGTLYFGVPTVWSRIAADPEAARALRGARLLVSGSAALPVPVFDRLAALTGHRPVERY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 368 GQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTE--GNIGIRiKPTrpigLFMYYENNPEKTAEVECG 445
Cdd:PRK07787 274 GMTETLITLSTRADGERRPGWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVR-GPT----LFDGYLNRPDATAAAFTA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 446 D-FYNTGDRATIDEEGYFWFLGR-SDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVlnpefSS 523
Cdd:PRK07787 349 DgWFRTGDVAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVV-----GA 423
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 529006476 524 RDPGEltKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK07787 424 DDVAA--DELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLL 468
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
80-570 |
3.76e-41 |
|
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: 154.45 E-value: 3.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 80 QGDEvKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPgttqmkakdilyrlqvsga 159
Cdd:cd17649 8 FGDQ-SLSYAELDARANRLAHRL-RALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVP------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 160 kaivttdtlapevesVAPECPSLKTKLLVSDhSREGWLDfrslvkSASPDHiciksktldPMAIFFTSGTTGFPKMAKHS 239
Cdd:cd17649 67 ---------------LDPEYPAERLRYMLED-SGAGLLL------THHPRQ---------LAYVIYTSGSTGTPKGVAVS 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 240 HGfALRSYFPACRKLLQLKMSDV---FWCLS-DtgwilAALGSLLEPWTAGSTVFAHHLPQF-DPKVIIETFFKYPITQC 314
Cdd:cd17649 116 HG-PLAAHCQATAERYGLTPGDRelqFASFNfD-----GAHEQLLPPLICGACVVLRPDELWaSADELAEMVRELGVTVL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 315 LAAPSVYRMILQQ--NYTSLRFPTLEHCCTGGEALLPEEQEQWkRQTGVLLYQAYGQSEAGIS---CGTLRGMKIKPGSM 389
Cdd:cd17649 190 DLPPAYLQQLAEEadRTGDGRPPSLRLYIFGGEALSPELLRRW-LKAPVRLFNAYGPTEATVTplvWKCEAGAARAGASM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 390 --GKAIPPFDIQIIDDKGNIQPPNTEGN--IGIRikptrpiGLFMYYENNPEKTAE--------VECGDFYNTGDRATID 457
Cdd:cd17649 269 piGRPLGGRSAYILDADLNPVPVGVTGElyIGGE-------GLARGYLGRPELTAErfvpdpfgAPGSRLYRTGDLARWR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 458 EEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVkAFIVLNpefSSRDPGELTKELQQHV 537
Cdd:cd17649 342 DDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLV-AYVVLR---AAAAQPELRAQLRTAL 417
|
490 500 510
....*....|....*....|....*....|...
gi 529006476 538 KSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:cd17649 418 RASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
80-570 |
8.68e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 155.29 E-value: 8.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 80 QGDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGA 159
Cdd:PRK06164 30 IDEDRPLSRAELRALVDRLAAWLAAQ-GVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 160 KAIVTTDT-----LAPEVESVAPEC-PSLKTKLLVS-------DHSREGWLDFRSLVKSASPDHICIKSKTLDPMAIFFT 226
Cdd:PRK06164 109 RWLVVWPGfkgidFAAILAAVPPDAlPPLRAIAVVDdaadatpAPAPGARVQLFALPDPAPPAAAGERAADPDAGALLFT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 227 -SGTTGFPKMAKHSHGFALR---------SYFPACRKLLQLKMSDVFwclsdtgwilaALGSLLEPWTAGSTVfaHHLPQ 296
Cdd:PRK06164 189 tSGTTSGPKLVLHRQATLLRharaiarayGYDPGAVLLAALPFCGVF-----------GFSTLLGALAGGAPL--VCEPV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 297 FDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCctGGEALLPEEQE--QWKRQTGVLLYQAYGQSE--A 372
Cdd:PRK06164 256 FDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLF--GFASFAPALGElaALARARGVPLTGLYGSSEvqA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 373 GISCGTLR---GMKIKPGSMgKAIPPFDIQIID-DKGNIQPPNTEGNIGIRiKPtrpiGLFMYYENNPEKTAEVECGD-F 447
Cdd:PRK06164 334 LVALQPATdpvSVRIEGGGR-PASPEARVRARDpQDGALLPDGESGEIEIR-AP----SLMRGYLDNPDATARALTDDgY 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 448 YNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVkAFIVLNPEfSSRDPG 527
Cdd:PRK06164 408 FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV-AFVIPTDG-ASPDEA 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 529006476 528 ELTKELQQHVksvtAPYKYPRKVEFVSELPKTITG---KIKRSELR 570
Cdd:PRK06164 486 GLMAACREAL----AGFKVPARVQVVEAFPVTESAngaKIQKHRLR 527
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
83-571 |
1.51e-40 |
|
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: 154.61 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAI 162
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEAL-KKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 163 VTTDTLAPEVESVAPECPSLKTKLLVSdhSREGWLDFRSLVK-SASPDHICIKSKTLDPMA---------IFFTSGTTGF 232
Cdd:cd17642 121 FCSKKGLQKVLNVQKKLKIIKTIIILD--SKEDYKGYQCLYTfITQNLPPGFNEYDFKPPSfdrdeqvalIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 233 PKMAKHSHGFALrSYFPACRKllqlkmsdvfwclsdtgwilAALGSLLEPWTAGSTVFA-HH------------------ 293
Cdd:cd17642 199 PKGVQLTHKNIV-ARFSHARD--------------------PIFGNQIIPDTAILTVIPfHHgfgmfttlgylicgfrvv 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 294 -LPQFDPKVIIETFFKYPITQCLAAPSVYRMI----LQQNYTslrFPTLEHCCTGGEALLPEEQEQWKRQTGV-LLYQAY 367
Cdd:cd17642 258 lMYKFEEELFLRSLQDYKVQSALLVPTLFAFFakstLVDKYD---LSNLHEIASGGAPLSKEVGEAVAKRFKLpGIRQGY 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 368 GQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQIID-DKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAEVECGD 446
Cdd:cd17642 335 GLTETTSAILITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGP-----MIMKGYVNNPEATKALIDKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 447 -FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNpefSSRD 525
Cdd:cd17642 410 gWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLE---AGKT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 529006476 526 PGEltKELQQHVKSVTAPYKYPR-KVEFVSELPKTITGKIKRSELRK 571
Cdd:cd17642 487 MTE--KEVMDYVASQVSTAKRLRgGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
97-570 |
5.80e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 152.35 E-value: 5.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 97 RTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLApevesvA 176
Cdd:PRK06145 39 QAAGMLHAR-GIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDEEFD------A 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 177 PecPSLKTKLLVSDHSREGwlDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHG-FALRSYFPACRklL 255
Cdd:PRK06145 112 I--VALETPKIVIDAAAQA--DSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGnLHWKSIDHVIA--L 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 256 QLKMSDVFWCLSDtgwiLAALGSLLEPWTA----GSTVFAHHlpQFDPKVIIETFFKYPITQCLAAPSVYRMILQQNyTS 331
Cdd:PRK06145 186 GLTASERLLVVGP----LYHVGAFDLPGIAvlwvGGTLRIHR--EFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVP-DR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 332 LRF--PTLEHCCTGGEALlPEEQ--EQWKRQTGVLLYQAYGQSEagiSCG--TL--RGMKI-KPGSMGKAIPPFDIQIID 402
Cdd:PRK06145 259 DRFdlDSLAWCIGGGEKT-PESRirDFTRVFTRARYIDAYGLTE---TCSgdTLmeAGREIeKIGSTGRALAHVEIRIAD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 403 DKGNIQPPNTEGNIGIR-IKPTRPiglfmyYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGP 481
Cdd:PRK06145 335 GAGRWLPPNMKGEICMRgPKVTKG------YWKDPEKTAEAFYGDWFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIAS 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 482 AEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDPgeltkELQQHVKSVTAPYKYPRKVEFVSELPKTIT 561
Cdd:PRK06145 409 SEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLE-----ALDRHCRQRLASFKVPRQLKVRDELPRNPS 483
|
....*....
gi 529006476 562 GKIKRSELR 570
Cdd:PRK06145 484 GKVLKRVLR 492
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
72-570 |
7.49e-40 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 152.90 E-value: 7.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 72 PALWWVNDQGDEV-KWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDI 150
Cdd:PRK13295 41 TAVTAVRLGTGAPrRFTYRELAALVDRVAVGLARL-GVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFREREL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 151 LYRLQVSGAKAIVTTDTL-----APEVESVAPECPSLKTKLLVSDhsrEGWLDFRSLV-----KSASPDHICIKSKTLDP 220
Cdd:PRK13295 120 SFMLKHAESKVLVVPKTFrgfdhAAMARRLRPELPALRHVVVVGG---DGADSFEALLitpawEQEPDAPAILARLRPGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 221 ---MAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLlQLKMSDVFWCLS----DTGWILAalgsLLEPWTAGSTVFahH 293
Cdd:PRK13295 197 ddvTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERL-GLGADDVILMASpmahQTGFMYG----LMMPVMLGATAV--L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 294 LPQFDPKVIIETFFKYPITQCLAA-PSVYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEA 372
Cdd:PRK13295 270 QDIWDPARAAELIRTEGVTFTMAStPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 373 GISCGTLRG--MKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAEVECGdFYNT 450
Cdd:PRK13295 350 GAVTLTKLDdpDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVR-----GCSNFGGYLKRPQLNGTDADG-WFDT 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 451 GDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfSSRDPGELT 530
Cdd:PRK13295 424 GDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPG-QSLDFEEMV 502
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 529006476 531 KELQQHvkSVTAPYkYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK13295 503 EFLKAQ--KVAKQY-IPERLVVRDALPRTPSGKIQKFRLR 539
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
74-571 |
2.73e-39 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 152.74 E-value: 2.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 74 LWWVNDQGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTG----IIFMPGTTQMKAKD 149
Cdd:PLN02654 109 YWEGNEPGFDASLTYSELLDRVCQLANYL-KDVGVKKGDAVVIYLPMLMELPIAMLACARIGavhsVVFAGFSAESLAQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 150 IL---YRLQVS------GAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHS---REG--WLDFRSL----VKSASPDHI 211
Cdd:PLN02654 188 IVdckPKVVITcnavkrGPKTINLKDIVDAALDESAKNGVSVGICLTYENQLamkREDtkWQEGRDVwwqdVVPNYPTKC 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 212 CIK-SKTLDPMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVF 290
Cdd:PLN02654 268 EVEwVDAEDPLFLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYAFDYKPTDVYWCTADCGWITGHSYVTYGPMLNGATVL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 291 AHH-LPQF-DPKVIIETFFKYPITQCLAAPSVYRMILQQN---YTSLRFPTLEHCCTGGEALLPEeqeQWKRQTGVL--- 362
Cdd:PLN02654 348 VFEgAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGdeyVTRHSRKSLRVLGSVGEPINPS---AWRWFFNVVgds 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 363 ---LYQAYGQSE-AGISCGTLRGM-KIKPGSmgKAIPPFDIQ--IIDDKGNiqppNTEGNIG--IRIKPTRPIGLFMYYE 433
Cdd:PLN02654 425 rcpISDTWWQTEtGGFMITPLPGAwPQKPGS--ATFPFFGVQpvIVDEKGK----EIEGECSgyLCVKKSWPGAFRTLYG 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 434 NNP--EKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVV 511
Cdd:PLN02654 499 DHEryETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGI 578
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 512 KAFIVLNPEFSSRDpgELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PLN02654 579 YAFVTLVEGVPYSE--ELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRK 636
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
86-572 |
2.40e-38 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 148.59 E-value: 2.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 86 WSFREMTDLTCRTANVLTqTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTT 165
Cdd:PLN02330 56 VTYGEVVRDTRRFAKALR-SLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 166 DTLAPEVESVapECPSLktklLVSDHSREGWLDFRSLVKSA-----SPDHICIKSKtlDPMAIFFTSGTTGFPK--MAKH 238
Cdd:PLN02330 135 DTNYGKVKGL--GLPVI----VLGEEKIEGAVNWKELLEAAdragdTSDNEEILQT--DLCALPFSSGTTGISKgvMLTH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 --------SHGFALRSYFPAcrKLLQLKMSDVFWCLSDTGWILAALGSllepwtAGSTVFahhLPQFDpkviIETFFKYP 310
Cdd:PLN02330 207 rnlvanlcSSLFSVGPEMIG--QVVTLGLIPFFHIYGITGICCATLRN------KGKVVV---MSRFE----LRTFLNAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 311 ITQCLA-APSVYRMIL---------QQNYTSLRfptLEHCCTGGEALLPEEQEQWKRQ-TGVLLYQAYGQSEAgiSCGTL 379
Cdd:PLN02330 272 ITQEVSfAPIVPPIILnlvknpiveEFDLSKLK---LQAIMTAAAPLAPELLTAFEAKfPGVQVQEAYGLTEH--SCITL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 380 ------RGMKI-KPGSMGKAIPPFDIQIID-DKGNIQPPNTEGNIGIRIKPTrpigLFMYYENNPEKTAEVECGDFYNTG 451
Cdd:PLN02330 347 thgdpeKGHGIaKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCV----MQGYYNNKEETDRTIDEDGWLHTG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 452 DRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSsrdpgELTK 531
Cdd:PLN02330 423 DIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAK-----ESEE 497
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 529006476 532 ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PLN02330 498 DILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEK 538
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
81-570 |
4.46e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 147.15 E-value: 4.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKwSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:PRK12406 8 GDRRR-SFDELAQRAARAAGGL-AALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTTDTLAPEVESVAPEC---------PSLKTKLLVSDHSR---EGWLDFRS-LVKSASPDhiciKSKTLDPMAIFFTS 227
Cdd:PRK12406 86 VLIAHADLLHGLASALPAGvtvlsvptpPEIAAAYRISPALLtppAGAIDWEGwLAQQEPYD----GPPVPQPQSMIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 228 GTTGFPK-----------------MAKHSHGFAlrsyfPACRKLLQLKMsdvfWCLSDTGWILAALgsllepwTAGSTVF 290
Cdd:PRK12406 162 GTTGHPKgvrraaptpeqaaaaeqMRALIYGLK-----PGIRALLTGPL----YHSAPNAYGLRAG-------RLGGVLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 291 AhhLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQ------QNY--TSLRFPTleHcctgGEALLPEEQEQ-----Wkr 357
Cdd:PRK12406 226 L--QPRFDPEELLQLIERHRITHMHMVPTMFIRLLKlpeevrAKYdvSSLRHVI--H----AAAPCPADVKRamiewW-- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 358 qtGVLLYQAYGQSEAGIS--CGTLRGMKiKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIkptRPIGLFMYYeNN 435
Cdd:PRK12406 296 --GPVIYEYYGSTESGAVtfATSEDALS-HPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRI---AGNPDFTYH-NK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 436 PEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFI 515
Cdd:PRK12406 369 PEKRAEIDRGGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 529006476 516 VLNPEfSSRDPGELTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK12406 449 EPQPG-ATLDEADIRAQLKARL----AGYKVPKHIEIMAELPREDSGKIFKRRLR 498
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
92-572 |
8.14e-38 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 146.66 E-value: 8.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 92 TDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTtdtLAPE 171
Cdd:PLN02246 56 VELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT---QSCY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 172 VESVAPECPSLKTKLLVSDHSREGWLDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPK--MAKHshgfalRSYFP 249
Cdd:PLN02246 133 VDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKgvMLTH------KGLVT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 250 ACRKL-------LQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAhhLPQFDPKVIIETFFKYPITqclAAPSVYR 322
Cdd:PLN02246 207 SVAQQvdgenpnLYFHSDDVILCVLPMFHIYSLNSVLLCGLRVGAAILI--MPKFEIGALLELIQRHKVT---IAPFVPP 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 323 MILQ-------QNY--TSLRFptlehcCTGGEALLPEEQEQWKRQT--GVLLYQAYGQSEAGiscgTLRGM--------- 382
Cdd:PLN02246 282 IVLAiakspvvEKYdlSSIRM------VLSGAAPLGKELEDAFRAKlpNAVLGQGYGMTEAG----PVLAMclafakepf 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 383 KIKPGSMGKAIPPFDIQIID-DKGNIQPPNTEGNIGIRikptrpiG--LFMYYENNPEKTAE-VECGDFYNTGDRATIDE 458
Cdd:PLN02246 352 PVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIR-------GpqIMKGYLNDPEATANtIDKDGWLHTGDIGYIDD 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 459 EGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVlnpefssRDPG-ELTK-ELQQH 536
Cdd:PLN02246 425 DDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV-------RSNGsEITEdEIKQF 497
|
490 500 510
....*....|....*....|....*....|....*.
gi 529006476 537 VKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PLN02246 498 VAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRAK 533
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
223-566 |
3.89e-37 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 140.71 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPKMAKHSHGFALRSYFPACrKLLQLKMSDVFWCLS--------DTGWILAALgsllepwtAGSTVFAHHL 294
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWA-DCADLTEDDRYLIINpffhtfgyKAGIVACLL--------TGATVVPVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 295 pqFDPKVIIETFFKYPITQCLAAPSVYRMILQQ------NYTSLRFPTlehccTGGEALLPEEQEQWKRQTGV-LLYQAY 367
Cdd:cd17638 76 --FDVDAILEAIERERITVLPGPPTLFQSLLDHpgrkkfDLSSLRAAV-----TGAATVPVELVRRMRSELGFeTVLTAY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 368 GQSEAGisCGTLrgmkIKPG--------SMGKAIPPFDIQIIDDkgniqppnteGNIGIRiKPTRPIGlfmyYENNPEKT 439
Cdd:cd17638 149 GLTEAG--VATM----CRPGddaetvatTCGRACPGFEVRIADD----------GEVLVR-GYNVMQG----YLDDPEAT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 440 AE-VECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLn 518
Cdd:cd17638 208 AEaIDADGWLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 529006476 519 pefssRDPGELTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKR 566
Cdd:cd17638 287 -----RPGVTLTEEdVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
220-570 |
6.88e-37 |
|
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: 142.90 E-value: 6.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 220 PMAIFFTSGTTGFPKMAKHSHGFALRSYFP--ACRKLLQLKMSDVFWC---LSDTGWILAALGSLLepwtAGSTVFAhhL 294
Cdd:cd05929 127 GWKMLYSGGTTGRPKGIKRGLPGGPPDNDTlmAAALGFGPGADSVYLSpapLYHAAPFRWSMTALF----MGGTLVL--M 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 295 PQFDPKVIIETFFKYPITQCLAAPSVYRMILQQnYTSLR----FPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQS 370
Cdd:cd05929 201 EKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKL-PEAVRnaydLSSLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGT 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 371 EA-GISCGTLRGMKIKPGSMGKAIPPfDIQIIDDKGNIQPPNTEGNIGIRIKPTrpiglfMYYENNPEKTAE-VECGDFY 448
Cdd:cd05929 280 EGqGLTIINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPG------FEYTNDPEKTAAaRNEGGWS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 449 NTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAfiVLNPEFSSRDPGE 528
Cdd:cd05929 353 TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHA--VVQPAPGADAGTA 430
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 529006476 529 LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:cd05929 431 LAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLLR 472
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
82-569 |
9.45e-37 |
|
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: 142.82 E-value: 9.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:cd12116 9 DDRSLSYAELDERANRLAARL-RARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTLAPEVESVAPECPSLKTKLLVSDHSREGwldfrslvkSASPDhiciksktlDPMAIFFTSGTTGFPKMAKHSHG 241
Cdd:cd12116 88 VLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRT---------PVSPD---------DLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 242 fALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAAPSVY 321
Cdd:cd12116 150 -NLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 322 RMILQQNYTSLRfpTLEHCCtGGEALLPEEQEQWKRQTGVLlYQAYGQSEAGI-SCGTLRGMKIKPGSMGKAIPPFDIQI 400
Cdd:cd12116 229 RMLLDAGWQGRA--GLTALC-GGEALPPDLAARLLSRVGSL-WNLYGPTETTIwSTAARVTAAAGPIPIGRPLANTQVYV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 401 IDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAEV--------ECGDFYNTGDRATIDEEGYFWFLGRSDDVI 472
Cdd:cd12116 305 LDAALRPVPPGVPGELYIG-----GDGVAQGYLGRPALTAERfvpdpfagPGSRLYRTGDLVRRRADGRLEYLGRADGQV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 473 NASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVkAFIVLnPEFSSRDPGELTKELQQHVKSvtapYKYPRKVEF 552
Cdd:cd12116 380 KIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLV-AYVVL-KAGAAPDAAALRAHLRATLPA----YMVPSAFVR 453
|
490
....*....|....*..
gi 529006476 553 VSELPKTITGKIKRSEL 569
Cdd:cd12116 454 LDALPLTANGKLDRKAL 470
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
219-566 |
3.32e-35 |
|
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: 135.47 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHgfalRSYFPAcrkLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAHHL-PQF 297
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLAN----KTFFAV---PDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLcVTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 298 DPKVIIETFFK----YPITQCLAAPSVYRMILQQNYTSLRF-PTLEHCCTGGEALLPEEQE--QWKRQTGVLlyQAYGQS 370
Cdd:cd17635 75 GENTTYKSLFKilttNAVTTTCLVPTLLSKLVSELKSANATvPSLRLIGYGGSRAIAADVRfiEATGLTNTA--QVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 371 EAGISC--GTLRGMKiKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptRPIGLFMYYeNNPEKTAEVECGDFY 448
Cdd:cd17635 153 ETGTALclPTDDDSI-EINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIK----SPANMLGYW-NNPERTAEVLIDGWV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 449 NTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefSSRDPGE 528
Cdd:cd17635 227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVA----SAELDEN 302
|
330 340 350
....*....|....*....|....*....|....*...
gi 529006476 529 LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKR 566
Cdd:cd17635 303 AIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
196-571 |
8.24e-35 |
|
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: 137.46 E-value: 8.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 196 WLDFRSLVKSASPDhiciksktlDPMAIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFwclsdtgwiLAA 275
Cdd:cd05909 134 WLLRIFGVAPVQPD---------DPAVILFTSGSEGLPKGVVLSHK-NLLANVEQITAIFDPNPEDVV---------FGA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 276 L---------GSLLEPWTAGSTVFAHHLPqFDPKVIIETFFKYPITQCLAAPSVYRMILQ--QNYTslrFPTLEHCCTGG 344
Cdd:cd05909 195 LpffhsfgltGCLWLPLLSGIKVVFHPNP-LDYKKIPELIYDKKATILLGTPTFLRGYARaaHPED---FSSLRLVVAGA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 345 EALLPEEQEQWKRQTGVLLYQAYGQSEAG--ISCGTLRgMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNigiRIKP 422
Cdd:cd05909 271 EKLKDTLRQEFQEKFGIRILEGYGTTECSpvISVNTPQ-SPNKEGTVGRPLPGMEVKIVSVETHEEVPIGEGG---LLLV 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 423 TRPiGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEH-PAVAESAVVS 501
Cdd:cd05909 347 RGP-NVMLGYLNEPELTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVS 425
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529006476 502 SPDPVRGEVVKAFIVlnPEFSSRDpgeltkELQQHVKSVTAPYKY-PRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd05909 426 VPDGRKGEKIVLLTT--TTDTDPS------SLNDILKNAGISNLAkPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
223-572 |
8.41e-35 |
|
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: 134.00 E-value: 8.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVfWCLSDTGWILAALGSLLEPWTAGSTVfahHLPQFDPKVI 302
Cdd:cd17630 5 VILTSGSTGTPKAVVHTAA-NLLASAAGLHSRLGFGGGDS-WLLSLPLYHVGGLAILVRSLLAGAEL---VLLERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 303 IETFfKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQtGVLLYQAYGQSEAGISCGTLRGM 382
Cdd:cd17630 80 EDLA-PPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 383 KIKPGSMGKAIPPFDIQIIDDkgniqppnteGNIGIRikptrPIGLFMYYENNPEKTAEVECGDFYnTGDRATIDEEGYF 462
Cdd:cd17630 158 GFGRGGVGVLLPGRELRIVED----------GEIWVG-----GASLAMGYLRGQLVPEFNEDGWFT-TKDLGELHADGRL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 463 WFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfssRDPgeltKELQQHVKSVTA 542
Cdd:cd17630 222 TVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP---ADP----AELRAWLKDKLA 294
|
330 340 350
....*....|....*....|....*....|
gi 529006476 543 PYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:cd17630 295 RFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
107-571 |
2.56e-34 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 137.24 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 107 GLQTGDRLAlILPRVPEW---WLVCVGCIrtGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTL---APEVESvaPECP 180
Cdd:PLN02860 53 GLRNGDVVA-IAALNSDLyleWLLAVACA--GGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCsswYEELQN--DRLP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 181 SLKTKLLVSDHSREGWLDFRSLVksaSPDHI---CIKSKTLDP-------MAIFFTSGTTGFPKMAKHSH-GFALRSYfp 249
Cdd:PLN02860 128 SLMWQVFLESPSSSVFIFLNSFL---TTEMLkqrALGTTELDYawapddaVLICFTSGTTGRPKGVTISHsALIVQSL-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 250 acrkllqLKMSDVFWCLSDT----------GWILAALGSLLepwTAGSTVFahhLPQFDPKVIIETFFKYPITQCLAAPS 319
Cdd:PLN02860 203 -------AKIAIVGYGEDDVylhtaplchiGGLSSALAMLM---VGACHVL---LPKFDAKAALQAIKQHNVTSMITVPA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 320 VYRMILQQNYTSLR---FPTLEHCCTGGEA----LLPEEQEQWKRQTgvlLYQAYGQSEAgisCGTLRGM---------- 382
Cdd:PLN02860 270 MMADLISLTRKSMTwkvFPSVRKILNGGGSlssrLLPDAKKLFPNAK---LFSAYGMTEA---CSSLTFMtlhdptlesp 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 383 --------KIKPGS--------MGKAIPPFDIQIIDDKgniqpPNTEGNIGIRikptRPIGLFMYYENNPEkTAEVECGD 446
Cdd:PLN02860 344 kqtlqtvnQTKSSSvhqpqgvcVGKPAPHVELKIGLDE-----SSRVGRILTR----GPHVMLGYWGQNSE-TASVLSND 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 447 FY-NTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVL-------- 517
Cdd:PLN02860 414 GWlDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLrdgwiwsd 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 529006476 518 NPEFSSRDPGELTKE-LQQHV--KSVTApYKYPRK-VEFVSELPKTITGKIKRSELRK 571
Cdd:PLN02860 494 NEKENAKKNLTLSSEtLRHHCreKNLSR-FKIPKLfVQWRKPFPLTTTGKIRRDEVRR 550
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
167-570 |
2.81e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 136.76 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 TLAPEVESVAPECPSLKTKLLVSDHSR-----EGWLDFRSLVKSASPDHiciKSKTLDPMA---IFFTSGTTGFPKMAKH 238
Cdd:PRK07008 120 TFLPLVDALAPQCPNVKGWVAMTDAAHlpagsTPLLCYETLVGAQDGDY---DWPRFDENQassLCYTSGTTGNPKGALY 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 SH-GFALRSYFPACRKLLQLKMSDVF-----------WCLSDTGwilaalgsllePWTAGSTVFAHhlPQFDPKVIIETF 306
Cdd:PRK07008 197 SHrSTVLHAYGAALPDAMGLSARDAVlpvvpmfhvnaWGLPYSA-----------PLTGAKLVLPG--PDLDGKSLYELI 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 307 FKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGiSCGTLRGMKIK 385
Cdd:PRK07008 264 EAERVTFSAGVPTVWLGLLNHmREAGLRFSTLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMS-PLGTLCKLKWK 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 386 PGSM------------GKAIPPFDIQIIDDKGNIQPPN--TEGNIGIRikptRPIGLFMYYENnpEKTAEVEcgDFYNTG 451
Cdd:PRK07008 343 HSQLpldeqrkllekqGRVIYGVDMKIVGDDGRELPWDgkAFGDLQVR----GPWVIDRYFRG--DASPLVD--GWFPTG 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 452 DRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEvvKAFIVLnpefsSRDPG-ELT 530
Cdd:PRK07008 415 DVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDE--RPLLVV-----VKRPGaEVT 487
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 529006476 531 K-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK07008 488 ReELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLR 528
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
83-572 |
6.36e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 135.46 E-value: 6.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAI 162
Cdd:PRK08162 41 DRRRTWAETYARCRRLASALARR-GIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 163 VTTDTLAPEVESVAPECPslKTKLLVSD--------HSREGWLDFRSLVKSASPDHICIKSK-TLDPMAIFFTSGTTGFP 233
Cdd:PRK08162 120 IVDTEFAEVAREALALLP--GPKPLVIDvddpeypgGRFIGALDYEAFLASGDPDFAWTLPAdEWDAIALNYTSGTTGNP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 234 K-MAKHSHGfalrSYFPACRKLLQLKMSD---------VFWClsdTGWILaalgsllePWT----AGSTVFahhLPQFDP 299
Cdd:PRK08162 198 KgVVYHHRG----AYLNALSNILAWGMPKhpvylwtlpMFHC---NGWCF--------PWTvaarAGTNVC---LRKVDP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 300 KVIIETFFKYPITQCLAAPSVYRMILqqNYTSLRFPTLEHCCTG--GEALLPEEQEQWKRQTGVLLYQAYGQSE------ 371
Cdd:PRK08162 260 KLIFDLIREHGVTHYCGAPIVLSALI--NAPAEWRAGIDHPVHAmvAGAAPPAAVIAKMEEIGFDLTHVYGLTEtygpat 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 -----AGISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQP-PN---TEGNIGIRikptrpiG-LFMY-YENNPEKTA 440
Cdd:PRK08162 338 vcawqPEWDALPLDERAQLKARQGVRYPLQEGVTVLDPDTMQPvPAdgeTIGEIMFR-------GnIVMKgYLKNPKATE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 441 EVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpe 520
Cdd:PRK08162 411 EAFAGGWFHTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVEL--- 487
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 529006476 521 fssRDPGELTK-ELQQHVKSVTAPYKYPRKVEFvSELPKTITGKIKRSELRKK 572
Cdd:PRK08162 488 ---KDGASATEeEIIAHCREHLAGFKVPKAVVF-GELPKTSTGKIQKFVLREQ 536
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
82-569 |
7.66e-34 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 134.64 E-value: 7.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:cd12117 19 GDRSLTYAELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTLAPEVesvapecPSLKTKLLVSDHSREGwlDFRSLVKSASPDHICIksktldpmaIFFTSGTTGFPKMAKHSHG 241
Cdd:cd12117 98 LLTDRSLAGRA-------GGLEVAVVIDEALDAG--PAGNPAVPVSPDDLAY---------VMYTSGSTGRPKGVAVTHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 242 FALRSYFPacRKLLQLKMSDVFWCLSDTGWILAAL---GSLLepwTAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAAP 318
Cdd:cd12117 160 GVVRLVKN--TNYVTLGPDDRVLQTSPLAFDASTFeiwGALL---NGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 319 SVYRMILQQNYTSLRfpTLEHCCTGGEALLPEEQEQWKRQT-GVLLYQAYGQSEAGI--SCGTLRGMKIKPGS--MGKAI 393
Cdd:cd12117 235 ALFNQLADEDPECFA--GLRELLTGGEVVSPPHVRRVLAACpGLRLVNGYGPTENTTftTSHVVTELDEVAGSipIGRPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 394 PPFDIQIIDDKGNIQPPNTEGNI---GIrikptrpiGLFMYYENNPEKTAE--VEC-----GDFYNTGDRATIDEEGYFW 463
Cdd:cd12117 313 ANTRVYVLDEDGRPVPPGVPGELyvgGD--------GLALGYLNRPALTAErfVADpfgpgERLYRTGDLARWLPDGRLE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 464 FLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV-VSSPDPVRGEVVkAFIVLNPEFSsrdpgelTKELQQHVKSVTA 542
Cdd:cd12117 385 FLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVvVREDAGGDKRLV-AYVVAEGALD-------AAELRAFLRERLP 456
|
490 500
....*....|....*....|....*..
gi 529006476 543 PYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd12117 457 AYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
73-571 |
9.65e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 134.81 E-value: 9.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 73 ALWWVNDQG---DEVKWSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMK--- 146
Cdd:PRK07867 13 PLAEDDDRGlyfEDSFTSWREHIRGSAARAAALRARLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRgaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 147 -AKDILY---RLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSREgwlDFRSlvksASPDhiciksktlDPMA 222
Cdd:PRK07867 93 lARDIAHadcQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAEP---PFRV----ADPD---------DLFM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPKMAKHSH------GFALRSYFPACRkllqlkmSDVFWC---LSDTGWILAAlgsllepWT----AGSTV 289
Cdd:PRK07867 157 LIFTSGTSGDPKAVRCTHrkvasaGVMLAQRFGLGP-------DDVCYVsmpLFHSNAVMAG-------WAvalaAGASI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 290 -----FAhhLPQFDPKV--IIETFFKY---PITQCLAAP-------SVYRMILqqnytslrfptlehcctGGEALlPEEQ 352
Cdd:PRK07867 223 alrrkFS--ASGFLPDVrrYGATYANYvgkPLSYVLATPerpddadNPLRIVY-----------------GNEGA-PGDI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 353 EQWKRQTGVLLYQAYGQSEAGISCGtlRGMKIKPGSMGKAIPpfDIQIID-DKGNIQPP---------NTEGNIGIRIKP 422
Cdd:PRK07867 283 ARFARRFGCVVVDGFGSTEGGVAIT--RTPDTPPGALGPLPP--GVAIVDpDTGTECPPaedadgrllNADEAIGELVNT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 423 TRPiGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSS 502
Cdd:PRK07867 359 AGP-GGFEGYYNDPEADAERMRGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529006476 503 PDPVRGEVVKAFIVLNP--EFssrDPGELTKELqqHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK07867 438 PDPVVGDQVMAALVLAPgaKF---DPDAFAEFL--AAQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
219-566 |
9.94e-34 |
|
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: 130.60 E-value: 9.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHgfalRSY---FPACRKLLQLKMSD---VFWCLSDTGWILAALGSLlepWTAGStvfAH 292
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSE----RSWiesFVCNEDLFNISGEDailAPGPLSHSLFLYGAISAL---YLGGT---FI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 293 HLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLehcCTGGEALLPEEQEQWKRQTGVL-LYQAYGQSE 371
Cdd:cd17633 71 GQRKFNPKSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKSI---FSSGQKLFESTKKKLKNIFPKAnLIEFYGTSE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 AGISCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQppnteGNIGIRiKPTRPIGLFMYYENNPEKtaevecgdFYNTG 451
Cdd:cd17633 148 LSFITYNFNQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVK-SEMVFSGYVRGGFSNPDG--------WMSVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 452 DRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNpefssrdpgELT- 530
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---------KLTy 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 529006476 531 KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKR 566
Cdd:cd17633 285 KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
81-571 |
3.31e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 132.60 E-value: 3.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKwSFREMTDLTCRTANVLTQTCGLQtgDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:PRK07638 23 NDRVL-TYKDWFESVCKVANWLNEKESKN--KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERLAISNAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTTDTLAPEVESVapecpslKTKLLVSDHSREgwldfrsLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSH 240
Cdd:PRK07638 100 MIVTERYKLNDLPDE-------EGRVIEIDEWKR-------MIEKYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 GFALRSYFPACRKLlQLKMSDVfwclsdtgwILAAlGSLLEP---WTAGSTVF----AHHLPQFDPKVIIETFFKYPITQ 313
Cdd:PRK07638 166 QSWLHSFDCNVHDF-HMKREDS---------VLIA-GTLVHSlflYGAISTLYvgqtVHLMRKFIPNQVLDKLETENISV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 314 CLAAPSVYRMILQQNytslRFPTLEHCCTGGEALLPEEQEQwKRQTG---VLLYQAYGQSEAG-ISCGTLRGMKIKPGSM 389
Cdd:PRK07638 235 MYTVPTMLESLYKEN----RVIENKMKIISSGAKWEAEAKE-KIKNIfpyAKLYEFYGASELSfVTALVDEESERRPNSV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 390 GKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRpiglFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSD 469
Cdd:PRK07638 310 GRPFHNVQVRICNEAGEEVQKGEIGTVYVK-SPQF----FMGYIIGGVLARELNADGWMTVRDVGYEDEEGFIYIVGREK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 470 DVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIvlnpefssrDPGELTKELQQHVKSVTAPYKYPRK 549
Cdd:PRK07638 385 NMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---------KGSATKQQLKSFCLQRLSSFKIPKE 455
|
490 500
....*....|....*....|..
gi 529006476 550 VEFVSELPKTITGKIKRSELRK 571
Cdd:PRK07638 456 WHFVDEIPYTNSGKIARMEAKS 477
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
68-566 |
5.96e-33 |
|
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: 134.98 E-value: 5.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 68 RSPN-PALWWvndqgDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWwLVCV-GCIRTGIIFMPGTTQM 145
Cdd:COG1020 488 RTPDaVAVVF-----GDQSLTYAELNARANRLAHHL-RALGVGPGDLVGVCLERSLEM-VVALlAVLKAGAAYVPLDPAY 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 146 KAKDILYRLQVSGAKAIVTTDTLAPEVesvapecPSLKTKLLVSDHSREGWLDFRSLVKSASPDHIciksktldpmA-IF 224
Cdd:COG1020 561 PAERLAYMLEDAGARLVLTQSALAARL-------PELGVPVLALDALALAAEPATNPPVPVTPDDL----------AyVI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 225 FTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVfWCLsdtgwiLAALG---SLLE---PWTAGST-VFAHHLPQF 297
Cdd:COG1020 624 YTSGSTGRPKGVMVEHR-ALVNLLAWMQRRYGLGPGDR-VLQ------FASLSfdaSVWEifgALLSGATlVLAPPEARR 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 298 DPKVIIETFFKYPITQCLAAPSVYRMILQqnYTSLRFPTLEHCCTGGEALLPEEQEQW-KRQTGVLLYQAYGQSEAGI-- 374
Cdd:COG1020 696 DPAALAELLARHRVTVLNLTPSLLRALLD--AAPEALPSLRLVLVGGEALPPELVRRWrARLPGARLVNLYGPTETTVds 773
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 375 SCGTLRGMKIKPGSM--GKAIPPFDIQIIDDKGNIQPPNTEGNI---GIrikptrpiGLFMYYENNPEKTAE--VEC--- 444
Cdd:COG1020 774 TYYEVTPPDADGGSVpiGRPIANTRVYVLDAHLQPVPVGVPGELyigGA--------GLARGYLNRPELTAErfVADpfg 845
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 445 --GD-FYNTGDRATIDEEGYFWFLGRSDD-V-INasGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNP 519
Cdd:COG1020 846 fpGArLYRTGDLARWLPDGNLEFLGRADDqVkIR--GFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEA 923
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 529006476 520 EfssrdPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKR 566
Cdd:COG1020 924 G-----AAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDR 965
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
54-577 |
2.04e-32 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 131.16 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 54 DVLDHWTQmekegkRSPN-PALWWVNDQgdeVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCI 132
Cdd:PRK05852 20 DLVEVAAT------RLPEaPALVVTADR---IAISYRDLARLVDDLAGQLTRS-GLLPGDRVALRMGSNAEFVVALLAAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 133 RTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSREGWLDFrSLVKSASPDHIC 212
Cdd:PRK05852 90 RADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSV-HLDAATEPTPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 213 IKSKTL--DPMAIFFTSGTTGFPKMAKHSHG---FALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLlepwTAGS 287
Cdd:PRK05852 169 STPEGLrpDDAMIMFTGGTTGLPKMVPWTHAniaSSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATL----ASGG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 288 TV-------FAHHLPQFDPKVIIETFFKypitqclAAPSVYRMILQQNYT--------SLRFptLEHCCTggeALLPEEQ 352
Cdd:PRK05852 245 AVllpargrFSAHTFWDDIKAVGATWYT-------AVPTIHQILLERAATepsgrkpaALRF--IRSCSA---PLTAETA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 353 EQWKRQTGVLLYQAYGQSEA----------GISCGTLRGMKikPGSMGKAIPPfDIQIIDDKGNIQPPNTEGNIGIRiKP 422
Cdd:PRK05852 313 QALQTEFAAPVVCAFGMTEAthqvtttqieGIGQTENPVVS--TGLVGRSTGA-QIRIVGSDGLPLPAGAVGEVWLR-GT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 423 TRPIGlfmyYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSS 502
Cdd:PRK05852 389 TVVRG----YLGDPTITAANFTDGWLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGV 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006476 503 PDPVRGEVVKAFIVlnpefsSRDPGELT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELrKKEFGQK 577
Cdd:PRK05852 465 PDQLYGEAVAAVIV------PRESAPPTaEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV-AEQFGHS 533
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
198-570 |
1.01e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 128.99 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 198 DFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLlQLKMSDVFWCLSD--------T 269
Cdd:PRK13388 130 AYAELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERF-GLTRDDVCYVSMPlfhsnavmA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 270 GW--ILAALGSLLEPWTAGSTVFahhLPqfDPKVIIETFFKY---PITQCLAAPSvyRMILQQNYTSLRFptlehcctGG 344
Cdd:PRK13388 209 GWapAVASGAAVALPAKFSASGF---LD--DVRRYGATYFNYvgkPLAYILATPE--RPDDADNPLRVAF--------GN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 345 EALlPEEQEQWKRQTGVLLYQAYGQSEAGIScgTLRGMKIKPGSMGKAIPpfDIQIID-DKGNIQPP----------NTE 413
Cdd:PRK13388 274 EAS-PRDIAEFSRRFGCQVEDGYGSSEGAVI--VVREPGTPPGSIGRGAP--GVAIYNpETLTECAVarfdahgallNAD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 414 GNIGiRIKPTRPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPA 493
Cdd:PRK13388 349 EAIG-ELVNTAGAGFFEGYYNNPEATAERMRHGMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPA 427
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529006476 494 VAESAVVSSPDPVRGEVVKAFIVLNPEfSSRDPGELTKELqqHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PRK13388 428 INRVAVYAVPDERVGDQVMAALVLRDG-ATFDPDAFAAFL--AAQPDLGTKAWPRYVRIAADLPSTATNKVLKRELI 501
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
87-571 |
1.18e-31 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 127.43 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTD 166
Cdd:cd17653 24 TYGELDAASNALANRLLQL-GVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 tlapevesvapecpslktkllvsdhsregwldfrslvksaSPDhiciksktlDPMAIFFTSGTTGFPK--MAKHSHGFAL 244
Cdd:cd17653 103 ----------------------------------------SPD---------DLAYIIFTSGSTGIPKgvMVPHRGVLNY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 245 RSYFPA------CRKLLQLkMSDVFWCLsdTGWILAALGSllepwtAGSTVFAHHLPQFDPKVIIETFFkyPITqclaaP 318
Cdd:cd17653 134 VSQPPArldvgpGSRVAQV-LSIAFDAC--IGEIFSTLCN------GGTLVLADPSDPFAHVARTVDAL--MST-----P 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 319 SVYRMILQQnytslRFPTLEHCCTGGEALLPEEQEQWKRqtGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPPFDI 398
Cdd:cd17653 198 SILSTLSPQ-----DFPNLKTIFLGGEAVPPSLLDRWSP--GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTC 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 399 QIIDdkGNIQPPnTEGNIG-IRIKPtrpIGLFMYYENNPEKTAE--VECGD-----FYNTGDRATIDEEGYFWFLGRSDD 470
Cdd:cd17653 271 YILD--ADLQPV-PEGVVGeICISG---VQVARGYLGNPALTASkfVPDPFwpgsrMYRTGDYGRWTEDGGLEFLGREDN 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 471 VINASGYRVG-PAEVENALAEHPAVAESAVVsspdpVRGEVVKAFIVlnPEfsSRDPGELTKELQQHVKSvtapYKYPRK 549
Cdd:cd17653 345 QVKVRGFRINlEEIEEVVLQSQPEVTQAAAI-----VVNGRLVAFVT--PE--TVDVDGLRSELAKHLPS----YAVPDR 411
|
490 500
....*....|....*....|..
gi 529006476 550 VEFVSELPKTITGKIKRSELRK 571
Cdd:cd17653 412 IIALDSFPLTANGKVDRKALRE 433
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
82-571 |
3.32e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 130.08 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:PRK12316 4573 DEEKLTYAELNRRANRLAHALIAR-GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAAL 4651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTLAPEVESVApecpslKTKLLVSDHSREgWLDFrslvksasPDHICIKSKTLDPMA-IFFTSGTTGFPKMAKHSH 240
Cdd:PRK12316 4652 LLTQSHLLQRLPIPD------GLASLALDRDED-WEGF--------PAHDPAVRLHPDNLAyVIYTSGSTGRPKGVAVSH 4716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 GfALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGsLLEPWTAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAAPSV 320
Cdd:PRK12316 4717 G-SLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEG-LYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVY 4794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 321 YRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQ-WKRQTGVLLYQAYGQSEAGISCGTLRGMK-IKPGS----MGKAIP 394
Cdd:PRK12316 4795 LQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLWKARDgDACGAaympIGTPLG 4874
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 395 PFDIQIIDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAE--------VECGDFYNTGDRATIDEEGYFWFLG 466
Cdd:PRK12316 4875 NRSGYVLDGQLNPLPVGVAGELYLGGE-----GVARGYLERPALTAErfvpdpfgAPGGRLYRTGDLARYRADGVIDYLG 4949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 467 RSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDP--GELTKELQQHVKSVTAPY 544
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEaqAELRDELKAALRERLPEY 5029
|
490 500
....*....|....*....|....*..
gi 529006476 545 KYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRKALPQ 5056
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
39-573 |
3.86e-31 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 129.90 E-value: 3.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 39 RWNdydrPEEFNFASDVLDHWtqMEKEGKRSPN-PALWWvndqgDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALI 117
Cdd:PRK12467 501 RWN----APATEYAPDCVHQL--IEAQARQHPErPALVF-----GEQVLSYAELNRQANRLAHVL-IAAGVGPDVLVGIA 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 118 LPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTdtlaPEVESVAPECPSLKTKLLVSDhsrEGWL 197
Cdd:PRK12467 569 VERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ----SHLLAQLPVPAGLRSLCLDEP---ADLL 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 198 DFRSLVKSA---SPDHICIksktldpmaIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVfWCLSDTgwiLA 274
Cdd:PRK12467 642 CGYSGHNPEvalDPDNLAY---------VIYTSGSTGQPKGVAISHG-ALANYVCVIAERLQLAADDS-MLMVST---FA 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 275 ALGSLLE---PWTAGSTVfaHHLPQ---FDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLrfPTLEHCCT-GGEAL 347
Cdd:PRK12467 708 FDLGVTElfgALASGATL--HLLPPdcaRDAEAFAALMADQGVTVLKIVPSHLQALLQASRVAL--PRPQRALVcGGEAL 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 348 LPEEQEQWKR-QTGVLLYQAYGQSEA--GISCGTLRGMKIKPGS--MGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKp 422
Cdd:PRK12467 784 QVDLLARVRAlGPGARLINHYGPTETtvGVSTYELSDEERDFGNvpIGQPLANLGLYILDHYLNPVPVGVVGELYIGGA- 862
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 423 trpiGLFMYYENNPEKTAE--------VECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAV 494
Cdd:PRK12467 863 ----GLARGYHRRPALTAErfvpdpfgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 529006476 495 AESAVVSSPDPVRGEVVkAFIVLNPEFSSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKE 573
Cdd:PRK12467 939 REAVVLAQPGDAGLQLV-AYLVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPD 1016
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
84-572 |
7.18e-31 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 126.88 E-value: 7.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 84 VKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIV 163
Cdd:PLN02479 44 VRYTWAQTYQRCRRLASALAKR-SIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKSEVVM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 164 TTD---TLAPEVESVAPECP--SLKTKLLV--SDHS----------REGWLDFRSLVKSASPDHICIKSK-TLDPMAIFF 225
Cdd:PLN02479 123 VDQeffTLAEEALKILAEKKksSFKPPLLIviGDPTcdpkslqyalGKGAIEYEKFLETGDPEFAWKPPAdEWQSIALGY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 226 TSGTTGFPKMAKHSHGFAlrsYFPACRKLLQLKMSD--VF-----------WCLSdtgWILAALgsllepwtAGSTVFah 292
Cdd:PLN02479 203 TSGTTASPKGVVLHHRGA---YLMALSNALIWGMNEgaVYlwtlpmfhcngWCFT---WTLAAL--------CGTNIC-- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 293 hLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQ--QNYTSLRFPTLEHCCTGGEA----LLPEEQEQWKRQTgvllyQA 366
Cdd:PLN02479 267 -LRQVTAKAIYSAIANYGVTHFCAAPVVLNTIVNapKSETILPLPRVVHVMTAGAApppsVLFAMSEKGFRVT-----HT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 367 YGQSEA-GIScgTLRGMKIKPGSMgkaiPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTRPI---------------GLFM 430
Cdd:PLN02479 341 YGLSETyGPS--TVCAWKPEWDSL----PPEEQARLNARQGVRYIGLEGLDVVDTKTMKPVpadgktmgeivmrgnMVMK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 431 YYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEV 510
Cdd:PLN02479 415 GYLKNPKANEEAFANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGES 494
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529006476 511 VKAFIVLNPEFSSRDPGELTKELQQHVKSVTAPYKYPRKVEFvSELPKTITGKIKRSELRKK 572
Cdd:PLN02479 495 PCAFVTLKPGVDKSDEAALAEDIMKFCRERLPAYWVPKSVVF-GPLPKTATGKIQKHVLRAK 555
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
82-569 |
9.25e-31 |
|
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: 125.46 E-value: 9.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLTQtCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMP-GTTQMKAKdILYRLQVSGAK 160
Cdd:cd12114 9 GDGTLTYGELAERARRVAGALKA-AGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPvDIDQPAAR-REAILADAGAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTTDTLAPEVESVAPecpslktkLLVSDHSREGWLDFRSLVKSAsPDhiciksktlDPMAIFFTSGTTGFPK--MAKH 238
Cdd:cd12114 87 LVLTDGPDAQLDVAVFD--------VLILDLDALAAPAPPPPVDVA-PD---------DLAYVIFTSGSTGTPKgvMISH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 S----------HGFALRsyfPACRKL----LQLKMS--DVFwclsdtgwilAALGSllepwtAGSTVFAHHLPQFDPKVI 302
Cdd:cd12114 149 RaalntildinRRFAVG---PDDRVLalssLSFDLSvyDIF----------GALSA------GATLVLPDEARRRDPAHW 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 303 IETFFKYPITQCLAAPSVYRMIL------QQNYTSLRFPTLehcctGGE----ALLPEEQEQWKRQTGVLLYqayGQSEA 372
Cdd:cd12114 210 AELIERHGVTLWNSVPALLEMLLdvleaaQALLPSLRLVLL-----SGDwiplDLPARLRALAPDARLISLG---GATEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 373 GISCGTLRGMKIKPGSmgKAIP---PFDIQ---IIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAE--VEC 444
Cdd:cd12114 282 SIWSIYHPIDEVPPDW--RSIPygrPLANQryrVLDPRGRDCPDWVPGELWIG-----GRGVALGYLGDPELTAArfVTH 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 445 GD---FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPvRGEVVKAFIVLNPEF 521
Cdd:cd12114 355 PDgerLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDG 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 529006476 522 SSRDPGELTKELQQHVKSvtapYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd12114 434 TPIAPDALRAFLAQTLPA----YMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
219-563 |
9.11e-30 |
|
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: 120.56 E-value: 9.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPK--MAKH-----------SHGF----------------ALRSYFPACRkllqlkmsdvfwCLSDT 269
Cdd:cd05924 4 DDLYILYTGGTTGMPKgvMWRQedifrmlmggaDFGTgeftpsedahkaaaaaAGTVMFPAPP------------LMHGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 270 GWiLAALGSLlepwTAGSTVFAHHlPQFDPKVIIETFFKYPIT------QCLAAPSVYRMILQQNYTslrFPTLEHCCTG 343
Cdd:cd05924 72 GS-WTAFGGL----LGGQTVVLPD-DRFDPEEVWRTIEKHKVTsmtivgDAMARPLIDALRDAGPYD---LSSLFAISSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 344 GEALLPEEQEQWKRQT-GVLLYQAYGQSEAG-ISCGTLRGMKIKPGSMGKAIPpfDIQIIDDKGNIQPPNTEGNIGIRIK 421
Cdd:cd05924 143 GALLSPEVKQGLLELVpNITLVDAFGSSETGfTGSGHSAGSGPETGPFTRANP--DTVVLDDDGRVVPPGSGGVGWIARR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 422 PTRPIGlfmyYENNPEKTAE--VECGD--FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAES 497
Cdd:cd05924 221 GHIPLG----YYGDEAKTAEtfPEVDGvrYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDV 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529006476 498 AVVSSPDPVRGEVVKAFIVLnpefssRDPGELT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 563
Cdd:cd05924 297 LVVGRPDERWGQEVVAVVQL------REGAGVDlEELREHCRTRIARYKLPKQVVFVDEIERSPAGK 357
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
79-566 |
2.08e-29 |
|
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: 121.40 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 79 DQGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSG 158
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLL-KINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 159 AKAIVTTDtlapevesvapecpslktkllvsdhsregwldfrslvksasPDhiciksktlDPMAIFFTSGTTGFPK--MA 236
Cdd:cd05914 80 AKAIFVSD-----------------------------------------ED---------DVALINYTSGTTGNSKgvML 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 237 KHSHgfaLRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVfahHLPQFDPKVIIETFFKYPITQCLA 316
Cdd:cd05914 110 TYRN---IVSNVDGVKEVVLLGKGDKILSILPLHHIYPLTFTLLLPLLNGAHV---VFLDKIPSAKIIALAFAQVTPTLG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 317 APSVYRM------------------------ILQQNYTSLRFPTL--------EHCCTGGeALLPEEQEQWKRQTGVLLY 364
Cdd:cd05914 184 VPVPLVIekifkmdiipkltlkkfkfklakkINNRKIRKLAFKKVheafggniKEFVIGG-AKINPDVEEFLRTIGFPYT 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 365 QAYGQSEAG-ISCGTLRGmKIKPGSMGKAIPPFDIQIIDDkgniQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAEV- 442
Cdd:cd05914 263 IGYGMTETApIISYSPPN-RIRLGSAGKVIDGVEVRIDSP----DPATGEGEIIVRGP-----NVMKGYYKNPEATAEAf 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 443 -ECGDFYnTGDRATIDEEGYFWFLGRSDDVI-NASGYRVGPAEVENALAEHPAVAESAVVsspdpVRGEVVKAFIVLNPE 520
Cdd:cd05914 333 dKDGWFH-TGDLGKIDAEGYLYIRGRKKEMIvLSSGKNIYPEEIEAKINNMPFVLESLVV-----VQEKKLVALAYIDPD 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 521 FssrdpgELTKELQQ-------------HVKSVTAPYKYPRKVEFV-SELPKTITGKIKR 566
Cdd:cd05914 407 F------LDVKALKQrniidaikwevrdKVNQKVPNYKKISKVKIVkEEFEKTPKGKIKR 460
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
83-570 |
2.89e-29 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 122.05 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTqTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAI 162
Cdd:PLN03102 37 KTRFTWPQTYDRCCRLAASLI-SLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAILRHAKPKIL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 163 VTTDTLAPEVESVAPECPSLKTKL-----LVSD-------HSREgwLDFRSLVKSASPDHICIKSKTL-----DPMAIFF 225
Cdd:PLN03102 116 FVDRSFEPLAREVLHLLSSEDSNLnlpviFIHEidfpkrpSSEE--LDYECLIQRGEPTPSLVARMFRiqdehDPISLNY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 226 TSGTTGFPKMAKHSHGFAlrsYFPACRKLLQLKMS---------DVFWClsdTGWILaalgsllePWT----AGSTVFAH 292
Cdd:PLN03102 194 TSGTTADPKGVVISHRGA---YLSTLSAIIGWEMGtcpvylwtlPMFHC---NGWTF--------TWGtaarGGTSVCMR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 293 HLPQfdPKvIIETFFKYPITQCLAAPSVYRMILQQNYTSL--RFPTLeHCCTGGE---ALLPEEQEQwkrqTGVLLYQAY 367
Cdd:PLN03102 260 HVTA--PE-IYKNIEMHNVTHMCCVPTVFNILLKGNSLDLspRSGPV-HVLTGGSpppAALVKKVQR----LGFQVMHAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 368 GQSEA----------------------------GISCGTLRGMKIKPGSMGKAIPPfdiqiiDDKgniqppnTEGNIGIR 419
Cdd:PLN03102 332 GLTEAtgpvlfcewqdewnrlpenqqmelkarqGVSILGLADVDVKNKETQESVPR------DGK-------TMGEIVIK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 420 IKptrpiGLFMYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV 499
Cdd:PLN03102 399 GS-----SIMKGYLKNPKATSEAFKHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAV 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006476 500 VSSPDPVRGEVVKAFIVLN---PEFSSRDPGELTKE--LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PLN03102 474 VAMPHPTWGETPCAFVVLEkgeTTKEDRVDKLVTRErdLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLR 549
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
285-562 |
3.17e-29 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 118.17 E-value: 3.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 285 AGSTVFahhLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQQN------YTSLRFPTLEHcctGGEALLPEEQEQWKRQ 358
Cdd:cd17636 66 GGTNVF---VRRVDAEEVLELIEAERCTHAFLLPPTIDQIVELNadglydLSSLRSSPAAP---EWNDMATVDTSPWGRK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 359 TGvllyqAYGQSE-AGISCGTLRGMKIKpGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTrpigLFMYYENNPE 437
Cdd:cd17636 140 PG-----GYGQTEvMGLATFAALGGGAI-GGAGRPSPLVQVRILDEDGREVPDGEVGEIVAR-GPT----VMAGYWNRPE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 438 KTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVL 517
Cdd:cd17636 209 VNARRTRGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVL 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 529006476 518 NPEfSSRDPGELTkelqQHVKSVTAPYKYPRKVEFVSELPKTITG 562
Cdd:cd17636 289 KPG-ASVTEAELI----EHCRARIASYKKPKSVEFADALPRTAGG 328
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
68-569 |
6.91e-29 |
|
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: 120.31 E-value: 6.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 68 RSPNPalWWVNDQGDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKA 147
Cdd:cd05923 13 RAPDA--CAIADPARGLRLTYSELRARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 148 KDILYRLQVSGAKAIVTTDTLAPevesvAPECPSLKTKLLvsdhsREGWLDFRSLVKSASPdhiCIKSKTLDPMA---IF 224
Cdd:cd05923 90 AELAELIERGEMTAAVIAVDAQV-----MDAIFQSGVRVL-----ALSDLVGLGEPESAGP---LIEDPPREPEQpafVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 225 FTSGTTGFPKMAKHSH-GFALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVFAhhLPQFDPKVII 303
Cdd:cd05923 157 YTSGTTGLPKGAVIPQrAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVV--VEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 304 ETFFKYPITQCLAAPSVYR-MILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGIScgtLRGM 382
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDaLAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNS---LYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 383 KIKPGSMGKAIPPFDIQIIDDKGNIQ---PPNTEGNIgirIKPTRPIGLFMYYENNPEKTAEVECGDFYNTGDRATIDEE 459
Cdd:cd05923 312 DARTGTEMRPGFFSEVRIVRIGGSPDealANGEEGEL---IVAAAADAAFTGYLNQPEATAKKLQDGWYRTGDVGYVDPS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 460 GYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgeltkELQQHVK- 538
Cdd:cd05923 389 GDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSAD------ELDQFCRa 462
|
490 500 510
....*....|....*....|....*....|.
gi 529006476 539 SVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd05923 463 SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
483-563 |
1.38e-28 |
|
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: 108.40 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 483 EVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPefssrDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITG 562
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKP-----GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSG 75
|
.
gi 529006476 563 K 563
Cdd:pfam13193 76 K 76
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
207-573 |
2.94e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 117.06 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 207 SPDHICIKSKTLD---PMAIFFTSGTTGFPKM---AKHSHGFALRSY---FPACRKLLQLKMSDV-----FWClsdtGwI 272
Cdd:PRK08308 87 ESDFTKLEAVNYLaeePSLLQYSSGTTGEPKLirrSWTEIDREIEAYneaLNCEQDETPIVACPVthsygLIC----G-V 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 273 LAALgsllepwTAGSTVfaHHLPQFDPKVIIETFFKYPITQCLAAPSVYrmilqqnYTSLRFP----TLEHCCTGGeALL 348
Cdd:PRK08308 162 LAAL-------TRGSKP--VIITNKNPKFALNILRNTPQHILYAVPLML-------HILGRLLpgtfQFHAVMTSG-TPL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 349 PEEQEQWKRQTGVLLYQAYGQSEAG-IS-CGTLRgmkiKPGSMGKAIPPFDIQIIDDKGniQPpnteGNIGIRIKpTRPI 426
Cdd:PRK08308 225 PEAWFYKLRERTTYMMQQYGCSEAGcVSiCPDMK----SHLDLGNPLPHVSVSAGSDEN--AP----EEIVVKMG-DKEI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 427 glfmyyennpektaevecgdfyNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPV 506
Cdd:PRK08308 294 ----------------------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPV 351
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 507 RGEVVKAfivlnpEFSSR---DPGELTKELQQHVksvtAPYKYPRKVEFVSELPKTITGKIKRSELRKKE 573
Cdd:PRK08308 352 AGERVKA------KVISHeeiDPVQLREWCIQHL----APYQVPHEIESVTEIPKNANGKVSRKLLELGE 411
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
83-571 |
3.42e-28 |
|
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: 118.30 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAI 162
Cdd:cd05915 22 VHRTTYAEVYQRARRLMGGLRAL-GVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 163 VTTDtlapEVESVAPECPSLKTKLLVSDHSREGWLDFRSLVKSASPDHICIKS-KTLDPMAIFFTSGTTGFPKMAKHSH- 240
Cdd:cd05915 101 LFDP----NLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALGEEADPVRvPERAACGMAYTTGTTGLPKGVVYSHr 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 GFALRSYFPACRKLLQLKMSDVFWCLSD----TGWILAalgsllepWT--AGSTVFAHHLPQFDPKVIIETFFKYPITQC 314
Cdd:cd05915 177 ALVLHSLAASLVDGTALSEKDVVLPVVPmfhvNAWCLP--------YAatLVGAKQVLPGPRLDPASLVELFDGEGVTFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 315 LAAPSVYRMILQ-QNYTSLRFPTLEHCCTGGEALlPEEQEQWKRQTGVLLYQAYGQSEA---GISCGTLRGMKIKPGSMG 390
Cdd:cd05915 249 AGVPTVWLALADyLESTGHRLKTLRRLVVGGSAA-PRSLIARFERMGVEVRQGYGLTETspvVVQNFVKSHLESLSEEEK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 391 KAIPPFD-IQIIDDKGNIQPPNT-----EGNIgIRIKPTRPIGLFMYYENNPEKT-AEVECGDFYNTGDRATIDEEGYFW 463
Cdd:cd05915 328 LTLKAKTgLPIPLVRLRVADEEGrpvpkDGKA-LGEVQLKGPWITGGYYGNEEATrSALTPDGFFRTGDIAVWDEEGYVE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 464 FLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNpEFSSRDpgeltKELQQHVKSVTAP 543
Cdd:cd05915 407 IKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR-GEKPTP-----EELNEHLLKAGFA 480
|
490 500
....*....|....*....|....*....
gi 529006476 544 YKY-PRKVEFVSELPKTITGKIKRSELRK 571
Cdd:cd05915 481 KWQlPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
63-569 |
3.97e-28 |
|
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: 117.81 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 63 EKEGKRSPN-PALWWVNDQgdevkWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPG 141
Cdd:cd17655 4 EEQAEKTPDhTAVVFEDQT-----LTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 142 TTQMKAKDILYRLQVSGAKAIVTTDTLAPevesvapecPSLKTKLLVSDHSREgwldfrslVKSASPDHICIKSKTLDPM 221
Cdd:cd17655 78 DPDYPEERIQYILEDSGADILLTQSHLQP---------PIAFIGLIDLLDEDT--------IYHEESENLEPVSKSDDLA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 222 AIFFTSGTTGFPK--MAKHShgfALRSYFPACRKLLQLKMSDVFWCLS----DtgwilAALGSLLEPWTAGSTVF-AHHL 294
Cdd:cd17655 141 YVIYTSGSTGKPKgvMIEHR---GVVNLVEWANKVIYQGEHLRVALFAsisfD-----ASVTEIFASLLSGNTLYiVRKE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 295 PQFDPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSlrFPTLEHCCTGGEALLPEEQEQWKRQ--TGVLLYQAYGQSEA 372
Cdd:cd17655 213 TVLDGQALTQYIRQNRITIIDLTPAHLKLLDAADDSE--GLSLKHLIVGGEALSTELAKKIIELfgTNPTITNAYGPTET 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 373 GISC--GTLRGMKIKPGS--MGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAE------- 441
Cdd:cd17655 291 TVDAsiYQYEPETDQQVSvpIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGE-----GVARGYLNRPELTAEkfvddpf 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 442 VECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEF 521
Cdd:cd17655 366 VPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKEL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 529006476 522 ssrDPGELTKELQQHVKSVTAPyKYPRKVEfvsELPKTITGKIKRSEL 569
Cdd:cd17655 446 ---PVAQLREFLARELPDYMIP-SYFIKLD---EIPLTPNGKVDRKAL 486
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
80-572 |
5.94e-28 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 117.93 E-value: 5.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 80 QGDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALI---LPRVPEWWLvcvGCIRTGIIFMPGTTQMKAKDILYRLQV 156
Cdd:PRK06018 34 EGPIVRTTYAQIHDRALKVSQALDRD-GIKLGDRVATIawnTWRHLEAWY---GIMGIGAICHTVNPRLFPEQIAWIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 157 SGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSDHSR------EGWLDFRSLVKSASPDhicIKSKTLD---PMAIFFTS 227
Cdd:PRK06018 110 AEDRVVITDLTFVPILEKIADKLPSVERYVVLTDAAHmpqttlKNAVAYEEWIAEADGD---FAWKTFDentAAGMCYTS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 228 GTTGFPKMAKHSH-GFALRSYFPACRKLLQLKMSD----VFWCLSDTGWILAALGsllePWTAGSTVFAHhlPQFDPKVI 302
Cdd:PRK06018 187 GTTGDPKGVLYSHrSNVLHALMANNGDALGTSAADtmlpVVPLFHANSWGIAFSA----PSMGTKLVMPG--AKLDGASV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 303 IETFFKYPITQCLAAPSVYRMILQQ-NYTSLRFPTLEHCCTGGEALlPEEQEQWKRQTGVLLYQAYGQSEAGiSCGTLRG 381
Cdd:PRK06018 261 YELLDTEKVTFTAGVPTVWLMLLQYmEKEGLKLPHLKMVVCGGSAM-PRSMIKAFEDMGVEVRHAWGMTEMS-PLGTLAA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 382 MKIK----PGS------MGKAIPPF--DIQIIDDKGNIQPpnTEGNIGIRIKPTRPIGLFMYYEnnpEKTAEVECGDFYN 449
Cdd:PRK06018 339 LKPPfsklPGDarldvlQKQGYPPFgvEMKITDDAGKELP--WDGKTFGRLKVRGPAVAAAYYR---VDGEILDDDGFFD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 450 TGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNP-EFSSRDpge 528
Cdd:PRK06018 414 TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPgETATRE--- 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 529006476 529 ltkELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:PRK06018 491 ---EILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQ 531
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
83-571 |
6.30e-28 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 117.78 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTcGLQTGDRlALI-LPRVPEWWLVCVGCIRTGI-----IFMPGTTQMK--AKDILYRL 154
Cdd:PRK10946 46 ERQFSYRELNQASDNLACSLRRQ-GIKPGDT-ALVqLGNVAEFYITFFALLKLGVapvnaLFSHQRSELNayASQIEPAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 155 QV-SGAKAIVTTDTLapeVESVAPECPSLKTKLLvsdHSREGWLDFRSLVKSASPDHICIKSKTlDPMAIFFTSG-TTGF 232
Cdd:PRK10946 124 LIaDRQHALFSDDDF---LNTLVAEHSSLRVVLL---LNDDGEHSLDDAINHPAEDFTATPSPA-DEVAFFQLSGgSTGT 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 233 PKMAKHSHG---FALRSYFPACrkllQLKMSDVFWC---------LSDTGwilaALGSLLepwTAGSTVFAHhlpqfDPK 300
Cdd:PRK10946 197 PKLIPRTHNdyyYSVRRSVEIC----GFTPQTRYLCalpaahnypMSSPG----ALGVFL---AGGTVVLAP-----DPS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 301 V-----IIEtffKYPITQCLAAPSVYRMILQ-----QNYTSLRfpTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQS 370
Cdd:PRK10946 261 AtlcfpLIE---KHQVNVTALVPPAVSLWLQaiaegGSRAQLA--SLKLLQVGGARLSETLARRIPAELGCQLQQVFGMA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 371 EaGISCGTlR---GMKIKPGSMGKAIPPFD-IQIIDDKGNIQPPNTEGNIGIRIKPTrpiglFMYYENNPEKTAEVECGD 446
Cdd:PRK10946 336 E-GLVNYT-RlddSDERIFTTQGRPMSPDDeVWVADADGNPLPQGEVGRLMTRGPYT-----FRGYYKSPQHNASAFDAN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 447 -FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVlnpefsSRD 525
Cdd:PRK10946 409 gFYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLV------VKE 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 529006476 526 PGElTKELQQHVKSV-TAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK10946 483 PLK-AVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQ 528
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
87-570 |
1.11e-27 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 117.25 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIfmpgTTQMKAKDIL--YRLQVSG---AKA 161
Cdd:PLN02574 68 SYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGI----VTTMNPSSSLgeIKKRVVDcsvGLA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTlapeVESVAPECPSLktkLLVS-----DHSREGWLDFRSLVKSaSPDhICIKS--KTLDPMAIFFTSGTTGFPK 234
Cdd:PLN02574 144 FTSPEN----VEKLSPLGVPV---IGVPenydfDSKRIEFPKFYELIKE-DFD-FVPKPviKQDDVAAIMYSSGTTGASK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 235 MAKHSHG-----------FALRSY-FPACRK--LLQLKMSDVFwclsdtGWILAALGSLlepwTAGSTVFAhhLPQFDPK 300
Cdd:PLN02574 215 GVVLTHRnliamvelfvrFEASQYeYPGSDNvyLAALPMFHIY------GLSLFVVGLL----SLGSTIVV--MRRFDAS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 301 VIIETFFKYPITQCLAAPSVYRMILQ--QNYTSLRFPTLEHCCTGGEALLPEE-QEQWKRQTGVLLYQAYGQSEAgISCG 377
Cdd:PLN02574 283 DMVKVIDRFKVTHFPVVPPILMALTKkaKGVCGEVLKSLKQVSCGAAPLSGKFiQDFVQTLPHVDFIQGYGMTES-TAVG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 378 TlRGMKIKP----GSMGKAIPPFDIQIID-DKGNIQPPNTEGNIGIRiKPtrpiGLFMYYENNPEKTAEVECGD-FYNTG 451
Cdd:PLN02574 362 T-RGFNTEKlskySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQ-GP----GVMKGYLNNPKATQSTIDKDgWLRTG 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 452 DRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVlnpefssRDPGELTK 531
Cdd:PLN02574 436 DIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV-------RRQGSTLS 508
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 529006476 532 ELQ--QHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PLN02574 509 QEAviNYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELK 549
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
81-572 |
1.26e-27 |
|
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: 116.41 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:cd05932 2 GQVVEFTWGEVADKARRLAAAL-RALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVT--TDTLAPEVESVAPECPSLKTKLLVSDHSREGWLDfrsLVKSASPDhicIKSKTLDP---MAIFFTSGTTGFPKM 235
Cdd:cd05932 81 ALFVgkLDDWKAMAPGVPEGLISISLPPPSAANCQYQWDD---LIAQHPPL---EERPTRFPeqlATLIYTSGTTGQPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 236 AKHSHG-FA-----------------LRSYFPACRKllqlkmsdvfwclsdTGWILAALGSLLepwtAGSTV-FAHHLPQ 296
Cdd:cd05932 155 VMLTFGsFAwaaqagiehigteendrMLSYLPLAHV---------------TERVFVEGGSLY----GGVLVaFAESLDT 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 297 F--DPKVIIET-FFKYPITQCLAAPSVYRMILQQNYTSL-RFPT--------------LEHC--CTGGEALLPEEQEQWK 356
Cdd:cd05932 216 FveDVQRARPTlFFSVPRLWTKFQQGVQDKIPQQKLNLLlKIPVvnslvkrkvlkglgLDQCrlAGCGSAPVPPALLEWY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 357 RQTGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPpfDIQI-IDDKGNIQppntegnigirikpTRPIGLFMYYENN 435
Cdd:cd05932 296 RSLGLNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGP--GVEVrISEDGEIL--------------VRSPALMMGYYKD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 436 PEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDDVINAS-GYRVGPAEVENALAEHPAVAESAVVSS--PDPVRGEVV 511
Cdd:cd05932 360 PEATAEAFTADgFLRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSglPAPLALVVL 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529006476 512 KAFIVLNPEFSSRdpGELTKELQQHVKSVTA---PYKYPRKVEFVSElPKTI-------TGKIKRSELRKK 572
Cdd:cd05932 440 SEEARLRADAFAR--AELEASLRAHLARVNStldSHEQLAGIVVVKD-PWSIdngiltpTLKIKRNVLEKA 507
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
82-569 |
1.38e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 116.63 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:PRK13383 57 DDGALSYRELQRATESLARRLTRD-GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHIST 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTLAPEVESVApecpslkTKLLVSDHSREGWLDFRSLVKSASPDHIciksktldpmaIFFTSGTTGFPKMAKHSHg 241
Cdd:PRK13383 136 VVADNEFAERIAGAD-------DAVAVIDPATAGAEESGGRPAVAAPGRI-----------VLLTSGTTGKPKGVPRAP- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 242 fALRSYFPACRKLLQL-------KMSDVFWCLSDTGwilaaLGSLLEPWTAGSTVFAHHlpQFDPKVIIETFFKYPITQC 314
Cdd:PRK13383 197 -QLRSAVGVWVTILDRtrlrtgsRISVAMPMFHGLG-----LGMLMLTIALGGTVLTHR--HFDAEAALAQASLHRADAF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 315 LAAPSVYRMILQ---QNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGI-SCGTLRGMKIKPGSMG 390
Cdd:PRK13383 269 TAVPVVLARILElppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIgALATPADLRDAPETVG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 391 KAIPPFDIQIIDDKGNIQPPNTEGNI--GIRIKPTRpiglfmyYENNPEKTAeveCGDFYNTGDRATIDEEGYFWFLGRS 468
Cdd:PRK13383 349 KPVAGCPVRILDRNNRPVGPRVTGRIfvGGELAGTR-------YTDGGGKAV---VDGMTSTGDMGYLDNAGRLFIVGRE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 469 DDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPefssrDPGELTKELQQHVKSVTAPYKYPR 548
Cdd:PRK13383 419 DDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHP-----GSGVDAAQLRDYLKDRVSRFEQPR 493
|
490 500
....*....|....*....|.
gi 529006476 549 KVEFVSELPKTITGKIKRSEL 569
Cdd:PRK13383 494 DINIVSSIPRNPTGKVLRKEL 514
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
42-576 |
2.52e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 118.14 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 42 DYDRPEEfNFASDVLDHWTQMEKEGKRSPNPALwwvndQGDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRV 121
Cdd:PRK12316 1991 DWDRTPE-AYPRGPGVHQRIAEQAARAPEAIAV-----VFGDQHLSYAELDSRANRLAHRLRAR-GVGPEVRVAIAAERS 2063
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 122 PEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVesvapecpSLKTKLLVSDHSREGWLdfrs 201
Cdd:PRK12316 2064 FELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERL--------PLPAGVARLPLDRDAEW---- 2131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 202 lvkSASPDHICIKSKTLDPMA-IFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDV---FWCLSDTGwilaALG 277
Cdd:PRK12316 2132 ---ADYPDTAPAVQLAGENLAyVIYTSGSTGLPKGVAVSHG-ALVAHCQAAGERYELSPADCelqFMSFSFDG----AHE 2203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 278 SLLEPWTAGSTVFAHHLPQFDPKVIIETFFKYPITqCLAAPSVYrmiLQQNYTSL----RFPTLEHCCTGGEALLPEEQE 353
Cdd:PRK12316 2204 QWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVT-ILDFPPVY---LQQLAEHAerdgRPPAVRVYCFGGEAVPAASLR 2279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 354 QWKRQT-GVLLYQAYGQSEAGIS-----CGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIG 427
Cdd:PRK12316 2280 LAWEALrPVYLFNGYGPTEAVVTpllwkCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLG-----GEG 2354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 428 LFMYYENNPEKTAEVECGD--------FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV 499
Cdd:PRK12316 2355 LARGYLNRPGLTAERFVPDpfsasgerLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVV 2434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006476 500 VSSpDPVRGEVVKAFIVlnpefsSRDPGE-LTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEFGQ 576
Cdd:PRK12316 2435 VAQ-DGASGKQLVAYVV------PDDAAEdLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQ 2505
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
87-569 |
3.26e-27 |
|
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: 114.27 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTd 166
Cdd:cd17652 14 TYAELNARANRLARLL-AARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLLTT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 tlapevesvapecpslktkllvsdhsregwldfrslvksasPDHiciksktldPMAIFFTSGTTGFPK--MAKHShgfAL 244
Cdd:cd17652 92 -----------------------------------------PDN---------LAYVIYTSGSTGRPKgvVVTHR---GL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 245 RSYFPACRKLLQLKMSDV---FWCLS-DtgwilAALGSLLEPWTAGSTVfahHLPQFDPKV----IIETFFKYPITQCLA 316
Cdd:cd17652 119 ANLAAAQIAAFDVGPGSRvlqFASPSfD-----ASVWELLMALLAGATL---VLAPAEELLpgepLADLLREHRITHVTL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 317 APSVYRMILQQNYTSLRfpTLehcCTGGEALLPEEQEQWKRqtGVLLYQAYGQSEAGIsCGT----LRGMKIKPgsMGKA 392
Cdd:cd17652 191 PPAALAALPPDDLPDLR--TL---VVAGEACPAELVDRWAP--GRRMINAYGPTETTV-CATmagpLPGGGVPP--IGRP 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 393 IPPFDIQIIDDKGNIQPPNTEGNIGIrikptRPIGLFMYYENNPEKTAE--VEC------GDFYNTGDRATIDEEGYFWF 464
Cdd:cd17652 261 VPGTRVYVLDARLRPVPPGVPGELYI-----AGAGLARGYLNRPGLTAErfVADpfgapgSRMYRTGDLARWRADGQLEF 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 465 LGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVlnpefSSRDPGELTKELQQHVKSVTAPY 544
Cdd:cd17652 336 LGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVV-----PAPGAAPTAAELRAHLAERLPGY 410
|
490 500
....*....|....*....|....*
gi 529006476 545 KYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd17652 411 MVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
126-572 |
4.55e-27 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 114.99 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 126 LVC-VGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVEsvapECPSLKTKLLVSDHSREGWLDFRSLVK 204
Cdd:PRK04813 66 LATfLGAVKAGHAYIPVDVSSPAERIEMIIEVAKPSLIIATEELPLEIL----GIPVITLDELKDIFATGNPYDFDHAVK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 205 SAspdhiciksktlDPMAIFFTSGTTGFPKMAKHSHGfALRSYfpacrkllqlkmsdVFWCLSDTG------WILAALGS 278
Cdd:PRK04813 142 GD------------DNYYIIFTSGTTGKPKGVQISHD-NLVSF--------------TNWMLEDFAlpegpqFLNQAPYS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 279 L------LEP-WTAGSTVFAhhLPQ---FDPKVIIETFFKYPITQCLAAPSVYRM-ILQQNYTSLRFPTLEH---CctgG 344
Cdd:PRK04813 195 FdlsvmdLYPtLASGGTLVA--LPKdmtANFKQLFETLPQLPINVWVSTPSFADMcLLDPSFNEEHLPNLTHflfC---G 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 345 EALLPEEQEQWK-RQTGVLLYQAYGQSEAgisCGTLRGMKI--------KPGSMGKAIPPFDIQIIDDKGNIQPPNTEGN 415
Cdd:PRK04813 270 EELPHKTAKKLLeRFPSATIYNTYGPTEA---TVAVTSIEItdemldqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 416 IGIrIKPTRPIGlfmyYENNPEKTAEVecgdF--------YNTGDRATIDEeGYFWFLGRSDDVINASGYRVGPAEVENA 487
Cdd:PRK04813 347 IVI-SGPSVSKG----YLNNPEKTAEA----FftfdgqpaYHTGDAGYLED-GLLFYQGRIDFQIKLNGYRIELEEIEQN 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 488 LAEHPAVAESAVVsspdPV-RGEVVK---AFIVLNPEFSSRDpGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 563
Cdd:PRK04813 417 LRQSSYVESAVVV----PYnKDHKVQyliAYVVPKEEDFERE-FELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGK 491
|
....*....
gi 529006476 564 IKRSELRKK 572
Cdd:PRK04813 492 IDRKALIEE 500
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
219-571 |
5.70e-27 |
|
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: 114.18 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKmsdvfwclSDTGWIL-------AALGSLLEPWTAGSTVFA 291
Cdd:cd05918 107 DAAYVIFTSGSTGKPKGVVIEHR-ALSTSALAHGRALGLT--------SESRVLQfasytfdVSILEIFTTLAAGGCLCI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 292 hhLPQFDPKVIIETFF-KYPITQCLAAPSVYRMILQQNytslrFPTLEHCCTGGEALLPEEQEQWkrQTGVLLYQAYGQS 370
Cdd:cd05918 178 --PSEEDRLNDLAGFInRLRVTWAFLTPSVARLLDPED-----VPSLRTLVLGGEALTQSDVDTW--ADRVRLINAYGPA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 371 EAGISC-GTLRGMKIKPGSMGKAIPpfDIQIIDDKGNIQPPntegnigirikptRPIG-----------LFMYYENNPEK 438
Cdd:cd05918 249 ECTIAAtVSPVVPSTDPRNIGRPLG--ATCWVVDPDNHDRL-------------VPIGavgelliegpiLARGYLNDPEK 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 439 TAEV---------ECGD-----FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVS--- 501
Cdd:cd05918 314 TAAAfiedpawlkQEGSgrgrrLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvk 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 502 -SPDPVRGEVVkAFIVLNPEFSSRDPG------------ELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSE 568
Cdd:cd05918 394 pKDGSSSPQLV-AFVVLDGSSSGSGDGdslflepsdefrALVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRA 472
|
...
gi 529006476 569 LRK 571
Cdd:cd05918 473 LRE 475
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-576 |
8.08e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.60 E-value: 8.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 40 WNDydRPEEFNFASDVLDHWtqmEKEGKRSPN-PALWWvndqgDEVKWSFREMTdltcRTANVLT---QTCGLQTGDRLA 115
Cdd:PRK12316 500 WNA--TAAEYPLQRGVHRLF---EEQVERTPEaPALAF-----GEETLDYAELN----RRANRLAhalIERGVGPDVLVG 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 116 LILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVesvapecpSLKTKLLVSDHSREG 195
Cdd:PRK12316 566 VAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKL--------PLAAGVQVLDLDRPA 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 196 -WLDFRSlvkSASPDhICIKSktLDPMAIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFwcLSDTGwiLA 274
Cdd:PRK12316 638 aWLEGYS---EENPG-TELNP--ENLAYVIYTSGSTGKPKGAGNRHR-ALSNRLCWMQQAYGLGVGDTV--LQKTP--FS 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 275 ALGSLLEPW----TAGSTVFAHHLPQFDPKVIIETFFKYPITQCLAAPSVYRMILQ----QNYTSLRfptleHCCTGGEA 346
Cdd:PRK12316 707 FDVSVWEFFwplmSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQdedvASCTSLR-----RIVCSGEA 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 347 L---LPEEQEQWKRQTGvlLYQAYGQSEAGI--SCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIK 421
Cdd:PRK12316 782 LpadAQEQVFAKLPQAG--LYNLYGPTEAAIdvTHWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGR 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 422 ptrpiGLFMYYENNPEKTAE-------VECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAV 494
Cdd:PRK12316 860 -----GLARGYHGRPGLTAErfvpspfVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWV 934
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 495 AESAVVSspdpVRGEVVKAFIVLnpefssRDPGELTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKE 573
Cdd:PRK12316 935 REAAVLA----VDGKQLVGYVVL------ESEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPE 1004
|
...
gi 529006476 574 FGQ 576
Cdd:PRK12316 1005 ASV 1007
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
63-571 |
8.37e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 116.60 E-value: 8.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 63 EKEGKRSPNPALWWVNDQgdevKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGT 142
Cdd:PRK12316 3064 EEQVERTPDAVALAFGEQ----RLSYAELNRRANRLAHRLIER-GVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLD 3138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 143 TQMKAKDILYRLQVSGAKAIVTTDTLApevesvAPECPSLKTKLLVSDHSREGWLDFRSLVksaSPDHICIksktldpma 222
Cdd:PRK12316 3139 PEYPEERLAYMLEDSGAQLLLSQSHLR------LPLAQGVQVLDLDRGDENYAEANPAIRT---MPENLAY--------- 3200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFWCLSDTGWILAALgSLLEPWTAGSTVFAHHLPQF-DPKV 301
Cdd:PRK12316 3201 VIYTSGSTGKPKGVGIRHS-ALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVE-ELFWPLMSGARVVLAGPEDWrDPAL 3278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 302 IIETFFKYPITQCLAAPSVYRMILQQNYTSlRFPTLEHCCTGGEALLPEEQEQWkrQTGVLLYQAYGQSEAGISCGTLRG 381
Cdd:PRK12316 3279 LVELINSEGVDVLHAYPSMLQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWQC 3355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 382 MKIKPGS--MGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAE-------VECGDFYNTGD 452
Cdd:PRK12316 3356 VEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGELYLG-----GEGLARGYHNRPGLTAErfvpdpfVPGERLYRTGD 3430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 453 RATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSspdpVRGEVVKAFIVlnpefSSRDPGELTKE 532
Cdd:PRK12316 3431 LARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLA----VDGRQLVAYVV-----PEDEAGDLREA 3501
|
490 500 510
....*....|....*....|....*....|....*....
gi 529006476 533 LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK12316 3502 LKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
111-569 |
4.06e-26 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 112.41 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 111 GDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVaPECPSLKTKLLVSD 190
Cdd:PRK05857 66 GSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAV-PEALHSIPVIAVDI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 191 HSREGWLdfrslvkSASPDHICIKSK----TLDPMAIFFTSGTTGFPKMAKhshgFALRSYFPACRKLLQLKMSDVFWCL 266
Cdd:PRK05857 145 AAVTRES-------EHSLDAASLAGNadqgSEDPLAMIFTSGTTGEPKAVL----LANRTFFAVPDILQKEGLNWVTWVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 267 SDTG-------------WILAAL--GSLLepWTAGSTVFAHHLPQFDPKVIietffkypiTQCLAAPSVYRMILQQNYTS 331
Cdd:PRK05857 214 GETTysplpathigglwWILTCLmhGGLC--VTGGENTTSLLEILTTNAVA---------TTCLVPTLLSKLVSELKSAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 332 LRFPTLEHCCTGGEALLPEEQeQWKRQTGVLLYQAYGQSEAGISCGTLRG-----MKIKPGSMGKAIPPFDIQIIDDKGN 406
Cdd:PRK05857 283 ATVPSLRLVGYGGSRAIAADV-RFIEATGVRTAQVYGLSETGCTALCLPTddgsiVKIEAGAVGRPYPGVDVYLAATDGI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 407 iqPPNTE--------GNIGIRiKPTRPIGlfmyYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYR 478
Cdd:PRK05857 362 --GPTAPgagpsasfGTLWIK-SPANMLG----YWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVN 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 479 VGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPK 558
Cdd:PRK05857 435 IAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPR 514
|
490
....*....|.
gi 529006476 559 TITGKIKRSEL 569
Cdd:PRK05857 515 TQSGKVMRASL 525
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
77-571 |
4.52e-26 |
|
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: 112.38 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 77 VNDQGDEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPR----VPEWWlvcvGCIRTGIIFMPGTTQM------- 145
Cdd:cd05906 31 IDADGSEEFQSYQDLLEDARRLAAGLRQL-GLRPGDSVILQFDDnedfIPAFW----ACVLAGFVPAPLTVPPtydepna 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 146 ---KAKDILyrlQVSGAKAIVTTDTLAPEVEsvapecpslktKLLVSDHSREGWLDFRSLVKSASPDHICIKSKTLDPMA 222
Cdd:cd05906 106 rlrKLRHIW---QLLGSPVVLTDAELVAEFA-----------GLETLSGLPGIRVLSIEELLDTAADHDLPQSRPDDLAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFwcLSdtgWI-LAALGSLLE-----PWTAGSTVFAH--HL 294
Cdd:cd05906 172 LMLTSGSTGFPKAVPLTHR-NILARSAGKIQHNGLTPQDVF--LN---WVpLDHVGGLVElhlraVYLGCQQVHVPteEI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 295 PQfDPKVIIETFFKYPITQCLAAPSVYRMILQQ---------NYTSLRFptlehCCTGGEAL-------LPEEQEQWKRQ 358
Cdd:cd05906 246 LA-DPLRWLDLIDRYRVTITWAPNFAFALLNDLleeiedgtwDLSSLRY-----LVNAGEAVvaktirrLLRLLEPYGLP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 359 TGVLLyQAYGQSE--AGI----SCGTL-RGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGlfmY 431
Cdd:cd05906 320 PDAIR-PAFGMTEtcSGViysrSFPTYdHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVR-GPVVTKG---Y 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 432 YeNNPEKTAEVECGD-FYNTGDRATIDEeGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAES--AVVSSPDPVRG 508
Cdd:cd05906 395 Y-NNPEANAEAFTEDgWFRTGDLGFLDN-GNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSftAAFAVRDPGAE 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529006476 509 EVVKAfIVLNPEFSSRDP-GELTKELQQHVK---SVTAPYKYPRKVEfvsELPKTITGKIKRSELRK 571
Cdd:cd05906 473 TEELA-IFFVPEYDLQDAlSETLRAIRSVVSrevGVSPAYLIPLPKE---EIPKTSLGKIQRSKLKA 535
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
219-569 |
6.03e-26 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 110.87 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHGFALrsyfpacrKLLQlkmsdvfWCLSDTG-----WILAALG-----SLLE---PWTA 285
Cdd:cd12115 106 DLAYVIYTSGSTGRPKGVAIEHRNAA--------AFLQ-------WAAAAFSaeelaGVLASTSicfdlSVFElfgPLAT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 286 GSTVF----AHHLPQF---DPKVIIETffkypitqclaAPSVYRMILQQNY--TSLRFPTLehcctGGEALLPE-EQEQW 355
Cdd:cd12115 171 GGKVVladnVLALPDLpaaAEVTLINT-----------VPSAAAELLRHDAlpASVRVVNL-----AGEPLPRDlVQRLY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 356 KRQTGVLLYQAYGQSEAGI-SCGTL--RGMKIKPgSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYY 432
Cdd:cd12115 235 ARLQVERVVNLYGPSEDTTySTVAPvpPGASGEV-SIGRPLANTQAYVLDRALQPVPLGVPGELYIG-----GAGVARGY 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 433 ENNPEKTAEVECGD-------FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDP 505
Cdd:cd12115 309 LGRPGLTAERFLPDpfgpgarLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDA 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529006476 506 VRGEVVKAFIVLNPEFSSrdpgeLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd12115 389 AGERRLVAYIVAEPGAAG-----LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
150-569 |
6.98e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 113.33 E-value: 6.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 150 ILYRLQVSGAKAIVTTDTLAPEVESVApecpslKTKLLVSDHSREgWLDFRSLVKSA---SPDHICIksktldpmaIFFT 226
Cdd:PRK12467 1663 LAYMIEDSGIELLLTQSHLQARLPLPD------GLRSLVLDQEDD-WLEGYSDSNPAvnlAPQNLAY---------VIYT 1726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 227 SGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDV---FWCLSDTGWILAALGSLLepwTAGSTVFAHHLPQFDPKVII 303
Cdd:PRK12467 1727 SGSTGRPKGAGNRHG-ALVNRLCATQEAYQLSAADVvlqFTSFAFDVSVWELFWPLI---NGARLVIAPPGAHRDPEQLI 1802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 304 ETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTG-VLLYQAYGQSEAGI-------S 375
Cdd:PRK12467 1803 QLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVdvthwtcR 1882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 376 CGTLRGMKIKPgsMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAE--------VECGDF 447
Cdd:PRK12467 1883 RKDLEGRDSVP--IGQPIANLSTYILDASLNPVPIGVAGELYLG-----GVGLARGYLNRPALTAErfvadpfgTVGSRL 1955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 448 YNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSpDPVRGEVVKAFIV-LNPEFSSRD- 525
Cdd:PRK12467 1956 YRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVpTDPGLVDDDe 2034
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 529006476 526 -PGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:PRK12467 2035 aQVALRAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKAL 2079
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
63-569 |
1.14e-25 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 109.95 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 63 EKEGKRSPNPALWWVNDQgdevKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGT 142
Cdd:cd17645 5 EEQVERTPDHVAVVDRGQ----SLTYKQLNEKANQLARHL-RGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 143 TQMKAKDILYRLQVSGAKAIVTtdtlapevesvapecpslktkllvsdhsregwldfrslvksaSPDhiciksktlDPMA 222
Cdd:cd17645 80 PDYPGERIAYMLADSSAKILLT------------------------------------------NPD---------DLAY 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPK--MAKHSHGFALRSYFPACRKLLQLKMSDVFWCLSDTGWILaalgSLLEPWTAGSTVfaHHLPQ---F 297
Cdd:cd17645 109 VIYTSGSTGLPKgvMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAW----EIFPHLTAGAAL--HVVPSerrL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 298 DPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFptlehCCTGGEALLPEEQEQWKrqtgvlLYQAYGQSEAGISCG 377
Cdd:cd17645 183 DLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSLRV-----LLTGGDKLKKIERKGYK------LVNNYGPTENTVVAT 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 378 TLrgmKIKPG----SMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAEVECGD------- 446
Cdd:cd17645 252 SF---EIDKPyaniPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGE-----GLARGYLNRPELTAEKFIVHpfvpger 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 447 FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFssrDP 526
Cdd:cd17645 324 MYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEI---PH 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 529006476 527 GELTKELQQhvksvTAP-YKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd17645 401 EELREWLKN-----DLPdYMIPTYFVHLKALPLTANGKVDRKAL 439
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
220-571 |
1.03e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 108.68 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 220 PMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLLQLKMSDVFWCLSDTGWI---LAALGSLlepwTAGSTVFAHHLPQ 296
Cdd:PTZ00237 256 PLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVsfhGFLYGSL----SLGNTFVMFEGGI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 297 FDPKVII----ETFFKYPITQCLAAPSVYRMILQQ--NYTSLR----FPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQA 366
Cdd:PTZ00237 332 IKNKHIEddlwNTIEKHKVTHTLTLPKTIRYLIKTdpEATIIRskydLSNLKEIWCGGEVIEESIPEYIENKLKIKSSRG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 367 YGQSEAGI----SCGTLrgmKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIkPTRPIGLFMYYENNpEKTAEV 442
Cdd:PTZ00237 412 YGQTEIGItylyCYGHI---NIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKL-PMPPSFATTFYKND-EKFKQL 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 443 --ECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPE 520
Cdd:PTZ00237 487 fsKFPGYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIGLLVLKQD 566
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 529006476 521 FSSR--DPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PTZ00237 567 QSNQsiDLNKLKNEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISK 619
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
87-569 |
1.54e-24 |
|
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: 106.62 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTd 166
Cdd:cd17643 14 TYGELDARANRLARTL-RAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLLTD- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 167 tlapevesvapecpslktkllvsdhsregwldfrslvksasPDhiciksktlDPMAIFFTSGTTGFPKMAKHSHGFALRs 246
Cdd:cd17643 92 -----------------------------------------PD---------DLAYVIYTSGSTGRPKGVVVSHANVLA- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 247 YFPACRKLLQLKMSDVFWCLSDTG-----W-ILAAL---GSLL--EPWTAGSTVFAHHLPQfDPKVIIetffkypITQcl 315
Cdd:cd17643 121 LFAATQRWFGFNEDDVWTLFHSYAfdfsvWeIWGALlhgGRLVvvPYEVARSPEDFARLLR-DEGVTV-------LNQ-- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 316 aAPSVYRMILQ------QNYTSLRFPTLehcctGGEALLPEEQEQWKRQTGV---LLYQAYGQSEAGI--SCGTLRGMKI 384
Cdd:cd17643 191 -TPSAFYQLVEaadrdgRDPLALRYVIF-----GGEALEAAMLRPWAGRFGLdrpQLVNMYGITETTVhvTFRPLDAADL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 385 KPGSM---GKAIPPFDIQIIDDKGNIQPPNTEGNIGIrikpTRPiGLFMYYENNPEKTAEVECGD--------FYNTGDR 453
Cdd:cd17643 265 PAAAAspiGRPLPGLRVYVLDADGRPVPPGVVGELYV----SGA-GVARGYLGRPELTAERFVANpfggpgsrMYRTGDL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 454 ATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEfssrdPGELTKEL 533
Cdd:cd17643 340 ARRLPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDG-----AAADIAEL 414
|
490 500 510
....*....|....*....|....*....|....*.
gi 529006476 534 QQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd17643 415 RALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
85-569 |
2.33e-24 |
|
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: 106.40 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 85 KWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVT 164
Cdd:cd17656 13 KLTYRELNERSNQLARFL-REKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 165 ----TDTLAPEVESVAPECPslktkllvsdhsregwldfrsLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPK--MAKH 238
Cdd:cd17656 92 qrhlKSKLSFNKSTILLEDP---------------------SISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKgvQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 SHGFAL----RSYFPACR--KLLQL-KMS-DVfwCLSDtgwILAAlgsllepWTAGSTVfahHLPQFDPKVIIETFF--- 307
Cdd:cd17656 151 KNMVNLlhfeREKTNINFsdKVLQFaTCSfDV--CYQE---IFST-------LLSGGTL---YIIREETKRDVEQLFdlv 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 308 -KYPITQCLAAPSVYRMILQQNYTSLRFPT-LEHCCTGGEAL-LPEEQEQWKRQTGVLLYQAYGQSEAGIscgtLRGMKI 384
Cdd:cd17656 216 kRHNIEVVFLPVAFLKFIFSEREFINRFPTcVKHIITAGEQLvITNEFKEMLHEHNVHLHNHYGPSETHV----VTTYTI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 385 KPGS-------MGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAEVECGD-------FYNT 450
Cdd:cd17656 292 NPEAeipelppIGKPISNTWIYILDQEQQLQPQGIVGELYIS-----GASVARGYLNRQELTAEKFFPDpfdpnerMYRT 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 451 GDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSsrdpgelT 530
Cdd:cd17656 367 GDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN-------I 439
|
490 500 510
....*....|....*....|....*....|....*....
gi 529006476 531 KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd17656 440 SQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
44-564 |
3.01e-24 |
|
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: 106.97 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 44 DRPEEF-----NFASDVLDHwtqmekegKRSPNPALWWVNDQGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALIL 118
Cdd:cd05943 60 PGARWFpgarlNYAENLLRH--------ADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL-RALGVKPGDRVAGYL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 119 PRVPEwwlVCVGCIRT---GIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDT---------LAPEVESVAPECPSLKTKL 186
Cdd:cd05943 131 PNIPE---AVVAMLATasiGAIWSSCSPDFGVPGVLDRFGQIEPKVLFAVDAytyngkrhdVREKVAELVKGLPSLLAVV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 187 LVSDHSREGWLDFRSLVKSASPDHICIKSKTL----------DPMAIFFTSGTTGFPKMAKHSHGFALRSYFPAcrKLLQ 256
Cdd:cd05943 208 VVPYTVAAGQPDLSKIAKALTLEDFLATGAAGelefeplpfdHPLYILYSSGTTGLPKCIVHGAGGTLLQHLKE--HILH 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 257 --LKMSDVFWCLSDTGWI-----LAALGSllepwtaGSTV----------FAHHLPQFDPKVIIeTFF----KYpITQCL 315
Cdd:cd05943 286 cdLRPGDRLFYYTTCGWMmwnwlVSGLAV-------GATIvlydgspfypDTNALWDLADEEGI-TVFgtsaKY-LDALE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 316 AAPSVYRmilqqnyTSLRFPTLEHCCTGGEALLPEEQEqW---KRQTGVLLYQAYGQSE-AGISCGTLRGMKIKPGSMGK 391
Cdd:cd05943 357 KAGLKPA-------ETHDLSSLRTILSTGSPLKPESFD-YvydHIKPDVLLASISGGTDiISCFVGGNPLLPVYRGEIQC 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 392 AIPPFDIQIIDDKGNIQPpnteGNIG----IRIKPTRPIGLF----------MYYENNPektaevecgDFYNTGDRATID 457
Cdd:cd05943 429 RGLGMAVEAFDEEGKPVW----GEKGelvcTKPFPSMPVGFWndpdgsryraAYFAKYP---------GVWAHGDWIEIT 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 458 EEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLnpefssRDPGELTKELQQHV 537
Cdd:cd05943 496 PRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKL------REGVELDDELRKRI 569
|
570 580 590
....*....|....*....|....*....|.
gi 529006476 538 KSVTA----PYKYPRKVEFVSELPKTITGKI 564
Cdd:cd05943 570 RSTIRsalsPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
62-577 |
2.55e-23 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 105.13 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 62 MEKEGKRSPN-PALwwvNDQGDEVkwSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMP 140
Cdd:PRK10252 464 VAQQAAKTPDaPAL---ADARYQF--SYREMREQVVALANLLRER-GVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLP 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 141 GTTQMKAKDILYRLQVSGAKAIVTTDTLA---PEVESVAPECPSlkTKLLVSDHsregwldfRSLVKSAsPDHicikskt 217
Cdd:PRK10252 538 LDTGYPDDRLKMMLEDARPSLLITTADQLprfADVPDLTSLCYN--APLAPQGA--------APLQLSQ-PHH------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 218 ldPMAIFFTSGTTGFPK--MAKHShgfA-------LRSYFP--ACRKLLQlKMS---DV-----FWclsdtgwilaalgs 278
Cdd:PRK10252 600 --TAYIIFTSGSTGRPKgvMVGQT---AivnrllwMQNHYPltADDVVLQ-KTPcsfDVsvwefFW-------------- 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 279 llePWTAGSTVF-----AHHlpqfDPKVIIETFFKYPITQCLAAPSvyrmILQQNYTSLRFPTLEHCC-------TGGEA 346
Cdd:PRK10252 660 ---PFIAGAKLVmaepeAHR----DPLAMQQFFAEYGVTTTHFVPS----MLAAFVASLTPEGARQSCaslrqvfCSGEA 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 347 LLPEEQEQWKRQTGVLLYQAYGQSEAGI------SCGT-LRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNI--- 416
Cdd:PRK10252 729 LPADLCREWQQLTGAPLHNLYGPTEAAVdvswypAFGEeLAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLylt 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 417 GIRikptrpigLFMYYENNPEKTAE-------VECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALA 489
Cdd:PRK10252 809 GIQ--------LAQGYLGRPDLTASrfiadpfAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQ 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 490 EHP----AVAESAVVSSPDPVRGEVVK--AFIVlnpefSSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGK 563
Cdd:PRK10252 881 ALPdveqAVTHACVINQAAATGGDARQlvGYLV-----SQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGK 955
|
570
....*....|....
gi 529006476 564 IKRSELRKKEFGQK 577
Cdd:PRK10252 956 LDRKALPLPELKAQ 969
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
99-571 |
6.43e-23 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 102.94 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 99 ANVLTQTCGLQTGDRLALILPRVPEWW--LVCVGCIrtGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVA 176
Cdd:PRK05620 52 AHALHDELGITGDQRVGSMMYNCAEHLevLFAVACM--GAVFNPLNKQLMNDQIVHIINHAEDEVIVADPRLAEQLGEIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 177 PECPSLKTKLLVSD--------HSREGW--LDFRSLVKSASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHgfalRS 246
Cdd:PRK05620 130 KECPCVRAVVFIGPsdadsaaaHMPEGIkvYSYEALLDGRSTVYDWPELDETTAAAICYSTGTTGAPKGVVYSH----RS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 247 YFPACrklLQLKMSDVF-------------------WCLSDTGWILAAlgSLLEPwtaGSTVFAHHLPQfdpkvIIETff 307
Cdd:PRK05620 206 LYLQS---LSLRTTDSLavthgesflccvpiyhvlsWGVPLAAFMSGT--PLVFP---GPDLSAPTLAK-----IIAT-- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 308 KYPiTQCLAAPSVY-------------RMILQQNYtslrfptlehccTGGEALLPEEQEQWKRQTGVLLYQAYGQSE--- 371
Cdd:PRK05620 271 AMP-RVAHGVPTLWiqlmvhylknppeRMSLQEIY------------VGGSAVPPILIKAWEERYGVDVVHVWGMTEtsp 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 --------AGISCGTLRGMKIkpgSMGKAIPPFDIQIIDDkGNIQPPN--TEGNIGIRikptRPIGLFMYYENNPEKTA- 440
Cdd:PRK05620 338 vgtvarppSGVSGEARWAYRV---SQGRFPASLEYRIVND-GQVMESTdrNEGEIQVR----GNWVTASYYHSPTEEGGg 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 441 --------EVECGD-------FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDP 505
Cdd:PRK05620 410 aastfrgeDVEDANdrftadgWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDD 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 529006476 506 VRGEVVKAFIVLNPEFSsrdPGELTKE-LQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK05620 490 KWGERPLAVTVLAPGIE---PTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
53-575 |
1.25e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 101.87 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 53 SDVLDHWTQmekegKRSPNPALwwvndQGDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCI 132
Cdd:PRK08279 40 GDVFEEAAA-----RHPDRPAL-----LFEDQSISYAELNARANRYAHWA-AARGVGKGDVVALLMENRPEYLAAWLGLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 133 RTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLKTKLLVSD---HSREGWLDFRSLVKSASPD 209
Cdd:PRK08279 109 KLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVAGGdtlDDPEGYEDLAAAAAGAPTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 210 HICIKSKTL--DPMAIFFTSGTTGFPKMAKHSHGFALRSY--FPAcrkLLQLKMSDVFWCL----SDTGwILAALGSLLe 281
Cdd:PRK08279 189 NPASRSGVTakDTAFYIYTSGTTGLPKAAVMSHMRWLKAMggFGG---LLRLTPDDVLYCClplyHNTG-GTVAWSSVL- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 282 pwTAGSTV-----FAhhLPQFDPKVIietffKYPITQClaapsVY-----RMILQQNYTSL-RFPTLEHCCtgGEALLPE 350
Cdd:PRK08279 264 --AAGATLalrrkFS--ASRFWDDVR-----RYRATAF-----QYigelcRYLLNQPPKPTdRDHRLRLMI--GNGLRPD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 351 EQEQWKRQTGVL-LYQAYGQSEAGISCGTLRGmkiKPGSMGK---------AIPPFDIQ----IIDDKGNIQPPNTeGNI 416
Cdd:PRK08279 328 IWDEFQQRFGIPrILEFYAASEGNVGFINVFN---FDGTVGRvplwlahpyAIVKYDVDtgepVRDADGRCIKVKP-GEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 417 GI---RIKPTRPiglFMYYeNNPEKTAEV------ECGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVEN 486
Cdd:PRK08279 404 GLligRITDRGP---FDGY-TDPEASEKKilrdvfKKGDaWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVEN 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 487 ALAEHPAVAESAV--VSSPDpVRGEVVKAFIVLN--PEFssrDPgeltKELQQHVKSVTAPYKYPRKVEFVSELPKTITG 562
Cdd:PRK08279 480 ALSGFPGVEEAVVygVEVPG-TDGRAGMAAIVLAdgAEF---DL----AALAAHLYERLPAYAVPLFVRLVPELETTGTF 551
|
570
....*....|...
gi 529006476 563 KIKRSELRKKEFG 575
Cdd:PRK08279 552 KYRKVDLRKEGFD 564
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
223-569 |
3.82e-22 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 99.43 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPK--------MAKHSHGFALRSYFPACRKLLQLkMSDVFwclsDtgwilAALGSLLEPWTAGST-VFAHH 293
Cdd:cd17644 111 VIYTSGSTGKPKgvmiehqsLVNLSHGLIKEYGITSSDRVLQF-ASIAF----D-----VAAEEIYVTLLSGATlVLRPE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 294 LPQFDPkviiETFFKYPITQCLAA----PSVYRM----ILQQNYTSLRFPTLehCCTGGEALLPEEQEQWKRQTG--VLL 363
Cdd:cd17644 181 EMRSSL----EDFVQYIQQWQLTVlslpPAYWHLlvleLLLSTIDLPSSLRL--VIVGGEAVQPELVRQWQKNVGnfIQL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 364 YQAYGQSEAGISC-----GTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEK 438
Cdd:cd17644 255 INVYGPTEATIAAtvcrlTQLTERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIG-----GVGLARGYLNRPEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 439 TAE---------VECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGE 509
Cdd:cd17644 330 TAEkfishpfnsSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNK 409
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 510 VVKAFIVLNPEFSSrdpgeLTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd17644 410 RLVAYIVPHYEESP-----STVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
50-564 |
4.39e-22 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 100.64 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 50 NFASDVLDHwtqmekegKRSPNPALWWVNDQGDEVKWSFREMTDLTCRTANVLTQtCGLQTGDRLALILPRVPEwwlvcv 129
Cdd:PRK03584 87 NYAENLLRH--------RRDDRPAIIFRGEDGPRRELSWAELRRQVAALAAALRA-LGVGPGDRVAAYLPNIPE------ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 130 gcirtGIIFMPGTT-----------QMKAKDILYRLQVSGAKAIVTTD---------TLAPEVESVAPECPSLKtKLLVS 189
Cdd:PRK03584 152 -----TVVAMLATAslgaiwsscspDFGVQGVLDRFGQIEPKVLIAVDgyryggkafDRRAKVAELRAALPSLE-HVVVV 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 190 DHSREG-----------WLDFRSLVKSASP-------DHiciksktldPMAIFFTSGTTGFPKMAKHSHGFALRSYFpac 251
Cdd:PRK03584 226 PYLGPAaaaaalpgallWEDFLAPAEAAELefepvpfDH---------PLWILYSSGTTGLPKCIVHGHGGILLEHL--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 252 rKLLQLKM----SDVFWCLSDTGWIL--AALGSLLEPWTA----GSTVFAHHLPQFDpkvIIE----TFF----KYpITQ 313
Cdd:PRK03584 294 -KELGLHCdlgpGDRFFWYTTCGWMMwnWLVSGLLVGATLvlydGSPFYPDPNVLWD---LAAeegvTVFgtsaKY-LDA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 314 CLAAPSVYRmilqqnyTSLRFPTLEHCCTGGEALLPEEQ----EQWKRqtGVLLyqaygqseAGISCGT------LRGMK 383
Cdd:PRK03584 369 CEKAGLVPG-------ETHDLSALRTIGSTGSPLPPEGFdwvyEHVKA--DVWL--------ASISGGTdicscfVGGNP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 384 IKP---GSM-----GKAIPPFDIQ---IIDDKGNI---QPpntegnigiriKPTRPIGL-------------FMYYENnp 436
Cdd:PRK03584 432 LLPvyrGEIqcrglGMAVEAWDEDgrpVVGEVGELvctKP-----------FPSMPLGFwndpdgsryrdayFDTFPG-- 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 437 ektaeVEC-GDFyntgdrATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFI 515
Cdd:PRK03584 499 -----VWRhGDW------IEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFV 567
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 529006476 516 VLnpefssRDPGELTKELQQHVKSV----TAPYKYPRKVEFVSELPKTITGKI 564
Cdd:PRK03584 568 VL------AEGVTLDDALRARIRTTirtnLSPRHVPDKIIAVPDIPRTLSGKK 614
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
223-574 |
8.44e-22 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 100.62 E-value: 8.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 223 IFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSD----------------VFWCLSDTGWILAALGSLLEPWTAG 286
Cdd:PRK12467 3242 VIYTSGSTGKPKGVGVRHG-ALANHLCWIAEAYELDANDrvllfmsfsfdgaqerFLWTLICGGCLVVRDNDLWDPEELW 3320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 287 STVFAHHLPqfdpkviietffkypiTQCLAaPSVYRMILQ----QNYTSLRfptleHCCTGGEALLPEEQEQWKRQTG-V 361
Cdd:PRK12467 3321 QAIHAHRIS----------------IACFP-PAYLQQFAEdaggADCASLD-----IYVFGGEAVPPAAFEQVKRKLKpR 3378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 362 LLYQAYGQSEAGI-----SCGTLRGMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNP 436
Cdd:PRK12467 3379 GLTNGYGPTEAVVtvtlwKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGV-----GLARGYHQRP 3453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 437 EKTAE-------VECGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSpDPVRG 508
Cdd:PRK12467 3454 SLTAErfvadpfSGSGGrLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGG 3532
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 529006476 509 EVVKAFIVLNPEfssrdPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEF 574
Cdd:PRK12467 3533 KQLVAYVVPADP-----QGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA 3593
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
82-569 |
9.01e-22 |
|
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: 98.31 E-value: 9.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:cd17650 9 ATRQLTYRELNERANQLARTLRGL-GVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTdtlapevesvaPEcpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPK--MAKHS 239
Cdd:cd17650 88 LLTQ-----------PE----------------------------------------DLAYVIYTSGTTGKPKgvMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 240 H----GFALRSYFPACRK---LLQL-KMS-DVFwclsdtgwilaaLGSLLEPWTAGSTVFAhhLPQ---FDPKVIIETFF 307
Cdd:cd17650 117 NvahaAHAWRREYELDSFpvrLLQMaSFSfDVF------------AGDFARSLLNGGTLVI--CPDevkLDPAALYDLIL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 308 KYPITQCLAAPSVYRMILQQNY-TSLRFPTLEHCCTGGEALLPEEQEQWKRQTG--VLLYQAYGQSEAGI-------SCG 377
Cdd:cd17650 183 KSRITLMESTPALIRPVMAYVYrNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGqgMRIINSYGVTEATIdstyyeeGRD 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 378 TLRGMKIKPgsMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAE-------VECGDFYNT 450
Cdd:cd17650 263 PLGDSANVP--IGRPLPNTAMYVLDERLQPQPVGVAGELYIGGA-----GVARGYLNRPELTAErfvenpfAPGERMYRT 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 451 GDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPvRGEV-VKAFIVLNpefSSRDPGEL 529
Cdd:cd17650 336 GDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDK-GGEArLCAYVVAA---ATLNTAEL 411
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 529006476 530 TKELQQHVKSVTAPYKYprkVEFVSeLPKTITGKIKRSEL 569
Cdd:cd17650 412 RAFLAKELPSYMIPSYY---VQLDA-LPLTPNGKVDRRAL 447
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
211-564 |
2.47e-20 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 95.76 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 211 ICIKSKTLD-PMAIFFTSGTTGFPKMAKHSHgFALRSYFPACRKLLQLKMSDVfwclsdtgwILAAL---------GSLL 280
Cdd:PRK08633 774 LYGPTFKPDdTATIIFSSGSEGEPKGVMLSH-HNILSNIEQISDVFNLRNDDV---------ILSSLpffhsfgltVTLW 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 281 EPWTAGSTVFAHHLPqFDPKVIIETFFKYPITQCLAAPSVYRMILQQN-YTSLRFPTLEHCCTGGEALLPEEQEQWKRQT 359
Cdd:PRK08633 844 LPLLEGIKVVYHPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKkLHPLMFASLRLVVAGAEKLKPEVADAFEEKF 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 360 GVLLYQAYGQSEAG--ISC--------GTLRGMKIKPGSMGKAIPPFDIQIID-DKGNIQPPNTEGNIGIRiKPTRPIGl 428
Cdd:PRK08633 923 GIRILEGYGATETSpvASVnlpdvlaaDFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIG-GPQVMKG- 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 429 fmyYENNPEKTAEV----ECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEhpAVAES----AVV 500
Cdd:PRK08633 1001 ---YLGDPEKTAEVikdiDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK--ALGGEevvfAVT 1075
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 529006476 501 SSPDPVRGEVvkafIVLNPEFSSRDPGELtkeLQQHVKSVTAPYKYPRKVEFVSELPKTITGKI 564
Cdd:PRK08633 1076 AVPDEKKGEK----LVVLHTCGAEDVEEL---KRAIKESGLPNLWKPSRYFKVEALPLLGSGKL 1132
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
85-574 |
3.07e-20 |
|
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: 94.03 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 85 KWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVT 164
Cdd:cd05939 3 HWTFRELNEYSNKVANFFQAQ-GYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 165 tdtlapevesvapecpSLKTKLLvsdhsregwldfrsLVKSASPDHICIKSKTlDPMAIFFTSGTTGFPKMAKHSHgfaL 244
Cdd:cd05939 82 ----------------NLLDPLL--------------TQSSTEPPSQDDVNFR-DKLFYIYTSGTTGLPKAAVIVH---S 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 245 RSYFPAC--RKLLQLKMSDVFW-CLS---DTGWILAALGSLLEpwtaGSTVfahhlpqfdpkVIIETF---------FKY 309
Cdd:cd05939 128 RYYRIAAgaYYAFGMRPEDVVYdCLPlyhSAGGIMGVGQALLH----GSTV-----------VIRKKFsasnfwddcVKY 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 310 PITQCLAAPSVYRMILQQNYtslRFPTLEHCC--TGGEALLPEEQEQWKRQTGVL-LYQAYGQSEAGISCGTLRGmkiKP 386
Cdd:cd05939 193 NCTIVQYIGEICRYLLAQPP---SEEEQKHNVrlAVGNGLRPQIWEQFVRRFGIPqIGEFYGATEGNSSLVNIDN---HV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 387 GSMG--KAIPPF--DIQII-----------DDKGNIQP--PNTEGNIGIRIKPTRPIGLFMYYENNPEKTAEV-----EC 444
Cdd:cd05939 267 GACGfnSRILPSvyPIRLIkvdedtgelirDSDGLCIPcqPGEPGLLVGKIIQNDPLRRFDGYVNEGATNKKIardvfKK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 445 GD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV--VSSPDpVRGEVVKAFIVlNPEf 521
Cdd:cd05939 347 GDsAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPG-VEGRAGMAAIV-DPE- 423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 529006476 522 SSRDPGELTKELQqhvkSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEF 574
Cdd:cd05939 424 RKVDLDRFSAVLA----KSLPPYARPQFIRLLPEVDKTGTFKLQKTDLQKEGY 472
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
87-574 |
1.16e-19 |
|
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: 92.35 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTG--IIFMPgtTQMKAKDILYRLQVSGAKAIVT 164
Cdd:cd05938 7 TYRDVDRRSNQAARALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLN--TNIRSKSLLHCFRCCGAKVLVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 165 tdtlAPE-VESVAPECPSLKTK-----LLVSDHSREGWLDFRSLVKSASPD--------HICIKSktldPMAIFFTSGTT 230
Cdd:cd05938 85 ----APElQEAVEEVLPALRADgvsvwYLSHTSNTEGVISLLDKVDAASDEpvpaslraHVTIKS----PALYIYTSGTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 231 GFPKMAKHSHGFALrsyfpACRKLLQL---KMSDVFW-CLS---DTGWILAALGSLlepwTAGSTVFahhlpqFDPKVII 303
Cdd:cd05938 157 GLPKAARISHLRVL-----QCSGFLSLcgvTADDVIYiTLPlyhSSGFLLGIGGCI----ELGATCV------LKPKFSA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 304 ETFF----KYPITQCLAAPSVYRMILQQNytslrfPTLEHC-----CTGGEALLPEEQEQWKRQTG-VLLYQAYGQSEAG 373
Cdd:cd05938 222 SQFWddcrKHNVTVIQYIGELLRYLCNQP------QSPNDRdhkvrLAIGNGLRADVWREFLRRFGpIRIREFYGSTEGN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 374 ISCGTLRGmkiKPGSMGKA------IPPFD-IQIIDDKGniQPPNTEGNIGIRIKPTRPiGL----------FMYYENNP 436
Cdd:cd05938 296 IGFFNYTG---KIGAVGRVsylyklLFPFElIKFDVEKE--EPVRDAQGFCIPVAKGEP-GLlvakitqqspFLGYAGDK 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 437 EKT-----AEV-ECGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV--VSSPDpVR 507
Cdd:cd05938 370 EQTekkllRDVfKKGDvYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVygVTVPG-HE 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 529006476 508 GEVVKAFIVLnpefssRDPGELT-KELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEF 574
Cdd:cd05938 449 GRIGMAAVKL------KPGHEFDgKKLYQHVREYLPAYARPRFLRIQDSLEITGTFKQQKVRLVEEGF 510
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
85-520 |
2.02e-19 |
|
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: 91.72 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 85 KWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVT 164
Cdd:cd17641 11 EFTWADYADRVRAFALGL-LALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 165 TDT-LAPEVESVAPECPSLKtKLLVSD--------HSREGWLD----------------FRSLVKSASPDHICIKSktld 219
Cdd:cd17641 90 EDEeQVDKLLEIADRIPSVR-YVIYCDprgmrkydDPRLISFEdvvalgraldrrdpglYEREVAAGKGEDVAVLC---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 220 pmaifFTSGTTGFPKMAKHSHGFALRSyfpaCRKLLQ---LKMSDVFWCLSDTGWILAALGSLLEPWTAGSTVfahHLP- 295
Cdd:cd17641 165 -----TTSGTTGKPKLAMLSHGNFLGH----CAAYLAadpLGPGDEYVSVLPLPWIGEQMYSVGQALVCGFIV---NFPe 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 296 -----QFDPKVIIETFFkypitqcLAAPSVYRMILQQN------------------------------------------ 328
Cdd:cd17641 233 epetmMEDLREIGPTFV-------LLPPRVWEGIAADVrarmmdatpfkrfmfelgmklglraldrgkrgrpvslwlrla 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 329 --------YTSLR----FPTLEHCCTGGEALLPEeQEQWKRQTGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPPF 396
Cdd:cd17641 306 swladallFRPLRdrlgFSRLRSAATGGAALGPD-TFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 397 DIQIiDDKGNIQppntegnigirikpTRPIGLFMYYENNPEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDDVIN-A 474
Cdd:cd17641 385 EVRI-DEVGEIL--------------VRSPGVFVGYYKNPEATAEDFDEDgWLHTGDAGYFKENGHLVVIDRAKDVGTtS 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 529006476 475 SGYRVGPAEVENALAEHPAVAESAVVSSPDPvrgeVVKAFIVLNPE 520
Cdd:cd17641 450 DGTRFSPQFIENKLKFSPYIAEAVVLGAGRP----YLTAFICIDYA 491
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
388-571 |
6.96e-19 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 89.67 E-value: 6.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 388 SMGKAIPPFDIQIiddkgniqPPNTEGNIGIRIKptrpiGLFM-YYENNPEKTAEVEcgdfynTGDRATIDEEGYFWFLG 466
Cdd:PRK07445 284 SSGQVLPHAQITI--------PANQTGNITIQAQ-----SLALgYYPQILDSQGIFE------TDDLGYLDAQGYLHILG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 467 RSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRDpgeltkELQQHVKSVTAPYKY 546
Cdd:PRK07445 345 RNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLE------ELKTAIKDQLSPFKQ 418
|
170 180
....*....|....*....|....*
gi 529006476 547 PRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK07445 419 PKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
85-575 |
1.74e-18 |
|
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: 88.18 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 85 KWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVt 164
Cdd:cd05940 3 ALTYAELDAMANRYARWLKSL-GLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 165 tdtlapevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktLDPMAIFFTSGTTGFPKMAKHSHGFAL 244
Cdd:cd05940 81 -----------------------------------------------------VDAALYIYTSGTTGLPKAAIISHRRAW 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 245 RSYFPACRKLLQLKmSDVFW-CLS---DTGWILAALGSLLepwtAGSTV-----FAHHlpQFDPKVIIE--TFFKYPITQ 313
Cdd:cd05940 108 RGGAFFAGSGGALP-SDVLYtCLPlyhSTALIVGWSACLA----SGATLvirkkFSAS--NFWDDIRKYqaTIFQYIGEL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 314 C---LAAPSV-------YRMILqqnytslrfptlehcctgGEALLPEEQEQWKRQTGVL-LYQAYGQSEAGISCGTLRGm 382
Cdd:cd05940 181 CrylLNQPPKpterkhkVRMIF------------------GNGLRPDIWEEFKERFGVPrIAEFYAATEGNSGFINFFG- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 383 kiKPGSMGKA----IPPFDIQIID---DKGN-IQPPN------TEGNIGIRIKPTRPIGLFMYYENNPEKTAEV-----E 443
Cdd:cd05940 242 --KPGAIGRNpsllRKVAPLALVKydlESGEpIRDAEgrcikvPRGEPGLLISRINPLEPFDGYTDPAATEKKIlrdvfK 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 444 CGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV--VSSPDpVRGEVVKAFIVLNPE 520
Cdd:cd05940 320 KGDaWFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPG-TDGRAGMAAIVLQPN 398
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 529006476 521 fssrDPGELTKeLQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEFG 575
Cdd:cd05940 399 ----EEFDLSA-LAAHLEKNLPGYARPLFLRLQPEMEITGTFKQQKVDLRNEGFD 448
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
432-576 |
8.57e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 85.10 E-value: 8.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 432 YENNPEKTAEVECGDFyNTGDRATIDEeGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVV 511
Cdd:PRK07824 221 YRNPVDPDPFAEPGWF-RTDDLGALDD-GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRV 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529006476 512 KAFIVLNPEfssrdPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKeFGQ 576
Cdd:PRK07824 299 VAAVVGDGG-----PAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR-FAG 357
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
83-564 |
1.01e-17 |
|
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: 85.91 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRvPEWWLVCV-GCIRTGIIFMPGTTQMKAKDILYRLQVSGAKA 161
Cdd:cd17648 10 DKRLTYRELNERANRLAHYLLSVAEIRPDDLVGLVLDK-SELMIIAIlAVWKAGAAYVPIDPSYPDERIQFILEDTGARV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 162 IVTTDTlapevesvapecpslktkllvsdhsregwldfrslvksaspdhiciksktlDPMAIFFTSGTTGFPKMAKHSHG 241
Cdd:cd17648 89 VITNST---------------------------------------------------DLAYAIYTSGTTGKPKGVLVEHG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 242 FALRSYFPACRKllqlkmsdvfWCLSDTGWILAALGSllepwtagSTVFAHHLPQ-------------------FDPKVI 302
Cdd:cd17648 118 SVVNLRTSLSER----------YFGRDNGDEAVLFFS--------NYVFDFFVEQmtlallngqklvvppdemrFDPDRF 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 303 IETFFKYPITQCLAAPSVyrmiLQQnYTSLRFPTLEHCCTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGISC--GTLR 380
Cdd:cd17648 180 YAYINREKVTYLSGTPSV----LQQ-YDLARLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNhkRFFP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 381 GMKIKPGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAEV---------------ECG 445
Cdd:cd17648 255 GDQRFDKSLGRPVRNTKCYVLNDAMKRVPVGAVGELYLG-----GDGVARGYLNRPELTAERflpnpfqteqerargRNA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 446 DFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRG-EVVKAFIVlnpEFSSR 524
Cdd:cd17648 330 RLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAqSRIQKYLV---GYYLP 406
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 529006476 525 DPGELTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKI 564
Cdd:cd17648 407 EPGHVPEsDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKL 447
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
86-572 |
1.21e-16 |
|
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: 82.87 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 86 WSFREMTDLTCRTANVLTQTCGLQTGDRLALILPRVPEW---W--LVCVGCIRTGIifmpgTTQMKAKDILYRLQVSGAK 160
Cdd:cd05937 6 WTYSETYDLVLRYAHWLHDDLGVQAGDFVAIDLTNSPEFvflWlgLWSIGAAPAFI-----NYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 aivttdtlapevesvapecpslktkLLVSDhsregwldfrslvksasPDhiciksktlDPMAIFFTSGTTGFPKMAKHSH 240
Cdd:cd05937 81 -------------------------FVIVD-----------------PD---------DPAILIYTSGTTGLPKAAAISW 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 GFALRSYFPACRKLLQLKMSDVFWCLS---DTGWILAALGSLLepwtAGSTV-----FAHHlpQFDPKVIIE--TFFKYP 310
Cdd:cd05937 110 RRTLVTSNLLSHDLNLKNGDRTYTCMPlyhGTAAFLGACNCLM----SGGTLalsrkFSAS--QFWKDVRDSgaTIIQYV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 311 ITQC---LAAP-SVYrmilQQNYtSLRfptlehcCTGGEALLPEEQEQWKRQTGV-LLYQAYGQSEA------------G 373
Cdd:cd05937 184 GELCrylLSTPpSPY----DRDH-KVR-------VAWGNGLRPDIWERFRERFNVpEIGEFYAATEGvfaltnhnvgdfG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 374 ISC----GTLRGMKIKPGSMGKAIPPFDIQIIDDKGN----IQPPNTEGNIGIRIkPTRPIGLFMYYENNPEKTAE---- 441
Cdd:cd05937 252 AGAighhGLIRRWKFENQVVLVKMDPETDDPIRDPKTgfcvRAPVGEPGEMLGRV-PFKNREAFQGYLHNEDATESklvr 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 442 --VECGD-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDP-VRGEVVKAFIVL 517
Cdd:cd05937 331 dvFRKGDiYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPgHDGRAGCAAITL 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 529006476 518 NPEfsSRDPGELTK-ELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:cd05937 411 EES--SAVPTEFTKsLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLRDE 464
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
72-571 |
2.32e-16 |
|
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: 82.29 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 72 PALWWVNDQ-GDEVKWSFREMTDLTCRTANVLTQTCGlqTGDRLALILPRVPEwwLVC--VGCIRTGIIF--MPGTTQMK 146
Cdd:cd05931 10 PAYTFLDDEgGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLD--FVAafLGCLYAGAIAvpLPPPTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 147 -AKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPSLktkllvsdhsREGWLDFRSLVKSASPDHICIKSKTLDPMAIF- 224
Cdd:cd05931 86 hAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAA----------GTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLq 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 225 FTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSD--VFWcLS---DTGWIlaalGSLLEPWTAGST-VFAHhlPQ-F 297
Cdd:cd05931 156 YTSGSTGTPKGVVVTHR-NLLANVRQIRRAYGLDPGDvvVSW-LPlyhDMGLI----GGLLTPLYSGGPsVLMS--PAaF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 298 --DPKVIIETFFKYPITqCLAAPS-----VYRMILQQNYTSLRFPTLEHCCTGGEALLPEEQEQW---------KRQTgv 361
Cdd:cd05931 228 lrRPLRWLRLISRYRAT-ISAAPNfaydlCVRRVRDEDLEGLDLSSWRVALNGAEPVRPATLRRFaeafapfgfRPEA-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 362 lLYQAYGQSEA-----GISCGT-----------LRGMKIKPG----------SMGKAIPPFDIQIIDDKGNIqpPNTEGN 415
Cdd:cd05931 305 -FRPSYGLAEAtlfvsGGPPGTgpvvlrvdrdaLAGRAVAVAaddpaarelvSCGRPLPDQEVRIVDPETGR--ELPDGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 416 IG-IRIK-PTRPIGlfmyYENNPEKTAEVEC-------GDFYNTGDRATIDEeGYFWFLGRSDDVINASGYRVGPAEVEN 486
Cdd:cd05931 382 VGeIWVRgPSVASG----YWGRPEATAETFGalaatdeGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 487 ALAE-HPAVAES--AVVSSPDPVRGEVVkAFIVLNPEFSSRDPGELTKELQQHVKS---VTapykyPRKVEFVS--ELPK 558
Cdd:cd05931 457 TAEEaHPALRPGcvAAFSVPDDGEERLV-VVAEVERGADPADLAAIAAAIRAAVARehgVA-----PADVVLVRpgSIPR 530
|
570
....*....|...
gi 529006476 559 TITGKIKRSELRK 571
Cdd:cd05931 531 TSSGKIQRRACRA 543
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
81-535 |
3.94e-16 |
|
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: 81.25 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 81 GDEVKWSFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:cd17640 1 KPPKRITYKDLYQEILDFAAGL-RSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVttdtlapeVESvapecpslktkllvsdhsregwldfrslvksaSPDhiciksktlDPMAIFFTSGTTGFPKMAKHSH 240
Cdd:cd17640 80 ALV--------VEN--------------------------------DSD---------DLATIIYTSGTTGNPKGVMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 G---FALRSYFpacrKLLQLKMSDVFWclsdtgwilaalgSLLEPW------------TAGST-------VFAHHLPQFD 298
Cdd:cd17640 111 AnllHQIRSLS----DIVPPQPGDRFL-------------SILPIWhsyersaeyfifACGCSqaytsirTLKDDLKRVK 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 299 PKVII------ETFFKYPITQCLAAPSVYRMILQqnyTSLRFPTLEHCCTGGEALlPEEQEQWKRQTGVLLYQAYGQSEA 372
Cdd:cd17640 174 PHYIVsvprlwESLYSGIQKQVSKSSPIKQFLFL---FFLSGGIFKFGISGGGAL-PPHVDTFFEAIGIEVLNGYGLTET 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 373 G--ISCGTLRGMKIkpGSMGKAIPPFDIQIIDDKGN-IQPPNTEGNIGIRIKPtrpigLFMYYENNPEKTAEVECGD-FY 448
Cdd:cd17640 250 SpvVSARRLKCNVR--GSVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQ-----VMKGYYKNPEATSKVLDSDgWF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 449 NTGDRATIDEEGYFWFLGRSDDVINAS-GYRVGPAEVENALAEHPAVaESAVVSSPDPVRgevVKAFIVLNPEfssrdpg 527
Cdd:cd17640 323 NTGDLGWLTCGGELVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFI-EQIMVVGQDQKR---LGALIVPNFE------- 391
|
....*...
gi 529006476 528 ELTKELQQ 535
Cdd:cd17640 392 ELEKWAKE 399
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
219-571 |
5.47e-16 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 81.94 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHGFALRSYFPACRKLlQLKMSD-------VFWCLSDTGwilaalGSLLePWTAGstvfa 291
Cdd:PRK06814 794 DPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARI-DFSPEDkvfnalpVFHSFGLTG------GLVL-PLLSG----- 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 292 hhlpqfdpkviIETFFkYPitqclaAPSVYR----MILQQNYTSL-----------------RFPTLEHCCTGGEALLPE 350
Cdd:PRK06814 861 -----------VKVFL-YP------SPLHYRiipeLIYDTNATILfgtdtflngyaryahpyDFRSLRYVFAGAEKVKEE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 351 EQEQWKRQTGVLLYQAYGQSEAG--ISCGTlrGMKIKPGSMGKAIPPFDIQI-----IDDKGN--IQPPNtegnigirik 421
Cdd:PRK06814 923 TRQTWMEKFGIRILEGYGVTETApvIALNT--PMHNKAGTVGRLLPGIEYRLepvpgIDEGGRlfVRGPN---------- 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 422 ptrpIGLFMYYENNPeKTAEVECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVS 501
Cdd:PRK06814 991 ----VMLGYLRAENP-GVLEPPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAAVS 1065
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529006476 502 SPDPVRGEVvkafIVLnpeFSSRDPGElTKELQQHVKSVTAPYKY-PRKVEFVSELPKTITGKIKRSELRK 571
Cdd:PRK06814 1066 IPDARKGER----IIL---LTTASDAT-RAAFLAHAKAAGASELMvPAEIITIDEIPLLGTGKIDYVAVTK 1128
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
200-569 |
2.42e-15 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 78.67 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 200 RSLVKSASPDHICIKSKTLDPMA-IFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFWCLSdtgwILAALGS 278
Cdd:cd17654 99 DNAPLSFTPEHRHFNIRTDECLAyVIHTSGTTGTPKIVAVPHK-CILPNIQHFRSLFNITSEDILFLTS----PLTFDPS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 279 LLEPWTA----GSTVFAHHLPQFDPKVIIETFFKYPITQCL-AAPSVYRMILQQNY--------TSLRFPTLehcctGGE 345
Cdd:cd17654 174 VVEIFLSlssgATLLIVPTSVKVLPSKLADILFKRHRITVLqATPTLFRRFGSQSIkstvlsatSSLRVLAL-----GGE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 346 ALlPE--EQEQW-KRQTGVLLYQAYGQSEagISC-GTLRGMKIK--PGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIR 419
Cdd:cd17654 249 PF-PSlvILSSWrGKGNRTRIFNIYGITE--VSCwALAYKVPEEdsPVQLGSPLLGTVIEVRDQNGSEGTGQVFLGGLNR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 420 IKPTRPiglfmyYENNPEktaevecGDFYNTGDRATIdEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAV 499
Cdd:cd17654 326 VCILDD------EVTVPK-------GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAV 391
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 500 VSSPDpvrgEVVKAFIVLnPEFSSRdpgeLTKELQQHVKSvtaPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd17654 392 TLSDQ----QRLIAFIVG-ESSSSR----IHKELQLTLLS---SHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
62-576 |
7.53e-15 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 77.81 E-value: 7.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 62 MEKEGKRSPNPALWWVNDQGDEVKWSFREMTDL---TCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIF 138
Cdd:PLN03052 182 TPKPSKTDDSIAIIWRDEGSDDLPVNRMTLSELrsqVSRVANAL-DALGFEKGDAIAIDMPMNVHAVIIYLAIILAGCVV 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 139 MPGTTQMKAKDILYRLQVSGAKAIVTTDTL----------APEVESVAPEC---P----SLKTKLLVSDHSregWLDFRS 201
Cdd:PLN03052 261 VSIADSFAPSEIATRLKISKAKAIFTQDVIvrggksiplySRVVEAKAPKAivlPadgkSVRVKLREGDMS---WDDFLA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 202 LVK-SASPDHICIKSKTLDP-MAIFFTSGTTGFPKMAKHSHGFALRSYFPAcrkllqlkmsdvfWCLSDT--GWILA--- 274
Cdd:PLN03052 338 RANgLRRPDEYKAVEQPVEAfTNILFSSGTTGEPKAIPWTQLTPLRAAADA-------------WAHLDIrkGDIVCwpt 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 275 ALGSLLEPWTA------GSTVFAHHLPQFDPkviieTFFKY----PITQCLAAPSVYRMILQQNYTS-LRFPTLEHCCTG 343
Cdd:PLN03052 405 NLGWMMGPWLVyasllnGATLALYNGSPLGR-----GFAKFvqdaKVTMLGTVPSIVKTWKNTNCMAgLDWSSIRCFGST 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 344 GEALLPEEqEQWkrqtgvLLYQAY--------GQSEagISCGTLRGMKIKPGSMGKAIPP---FDIQIIDDKGNIQPPNT 412
Cdd:PLN03052 480 GEASSVDD-YLW------LMSRAGykpiieycGGTE--LGGGFVTGSLLQPQAFAAFSTPamgCKLFILDDSGNPYPDDA 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 413 EGnigirikpTRPIGLF-----------------MYYENNPektaevecgdFYNT------GDRATIDEEGYFWFLGRSD 469
Cdd:PLN03052 551 PC--------TGELALFplmfgasstllnadhykVYFKGMP----------VFNGkilrrhGDIFERTSGGYYRAHGRAD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 470 DVINASGYRVGPAEVENAL-AEHPAVAESAVVSSPDPVRG--EVVKAFIVLNPEFSSRDPGELTKELQQHVKSVTAPYKY 546
Cdd:PLN03052 613 DTMNLGGIKVSSVEIERVCnAADESVLETAAIGVPPPGGGpeQLVIAAVLKDPPGSNPDLNELKKIFNSAIQKKLNPLFK 692
|
570 580 590
....*....|....*....|....*....|
gi 529006476 547 PRKVEFVSELPKTITGKIKRSELRkKEFGQ 576
Cdd:PLN03052 693 VSAVVIVPSFPRTASNKVMRRVLR-QQLAQ 721
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
61-569 |
1.02e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 77.90 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 61 QMEKEGKRSP-NPALWWVNDQGDevkwsFREMTDLTCRTANVLtQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFM 139
Cdd:PRK05691 1136 LLNEQARQTPeRIALVWDGGSLD-----YAELHAQANRLAHYL-RDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYV 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 140 PGTTQMKAKDILYRLQVSGAKAIVTTDTLAPEVESVAPECPslktkllvsdhsregwLDFRSLVKSASPDHICIKSKTLD 219
Cdd:PRK05691 1210 PLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSA----------------IALDSLHLDSWPSQAPGLHLHGD 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 220 PMA-IFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDV----------------FWCLSdTG--WILAALGSLL 280
Cdd:PRK05691 1274 NLAyVIYTSGSTGQPKGVGNTHA-ALAERLQWMQATYALDDSDVlmqkapisfdvsvwecFWPLI-TGcrLVLAGPGEHR 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 281 EPWTAGSTVFAHHLP--QFDPKvIIETFFKYPitqclaapsvyrmiLQQNYTSLRfptleHCCTGGEALLPEEQEQ-WKR 357
Cdd:PRK05691 1352 DPQRIAELVQQYGVTtlHFVPP-LLQLFIDEP--------------LAAACTSLR-----RLFSGGEALPAELRNRvLQR 1411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 358 QTGVLLYQAYGQSEAGIS-----CGTLRGMKikpGSMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYY 432
Cdd:PRK05691 1412 LPQVQLHNRYGPTETAINvthwqCQAEDGER---SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIG-----GAGLARGY 1483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 433 ENNPEKTAEVECGD--------FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPD 504
Cdd:PRK05691 1484 LGRPALTAERFVPDplgedgarLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREG 1563
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 529006476 505 PVRGEVVKAFIvlnpefSSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:PRK05691 1564 AAGAQLVGYYT------GEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
206-544 |
1.69e-14 |
|
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: 75.96 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 206 ASPDHICIKSKTLDPMAIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVfwclsdtgwILAA--LGSLLEPW 283
Cdd:cd05910 73 AEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHG-TFAAQIDALRQLYGIRPGEV---------DLATfpLFALFGPA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 284 TAGSTVFA---HHLP-QFDPKVIIETFFKYPITQCLAAPSVYRMI----LQQNYTslrFPTLEHCCTGGEALLPEEQEQW 355
Cdd:cd05910 143 LGLTSVIPdmdPTRPaRADPQKLVGAIRQYGVSIVFGSPALLERVarycAQHGIT---LPSLRRVLSAGAPVPIALAARL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 356 KR--QTGVLLYQAYGQSEA----GISCGTLRGMKIKPGS------MGKAIPPFDIQII--DDKGNIQPPNT----EGNIG 417
Cdd:cd05910 220 RKmlSDEAEILTPYGATEAlpvsSIGSRELLATTTAATSggagtcVGRPIPGVRVRIIeiDDEPIAEWDDTlelpRGEIG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 418 iRIKPTRPIGLFMYYeNNPEKTAEVECGD-----FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHP 492
Cdd:cd05910 300 -EITVTGPTVTPTYV-NRPVATALAKIDDnsegfWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHP 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 529006476 493 AVAESAVVSSPDPVRGEVVkafIVLNPEFSSRDPgelTKELQQHVKSVTAPY 544
Cdd:cd05910 378 GVRRSALVGVGKPGCQLPV---LCVEPLPGTITP---RARLEQELRALAKDY 423
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
87-536 |
2.00e-14 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 76.09 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 87 SFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFM---PGttqMKAKDILYRLQVSGAKAIV 163
Cdd:PRK09274 43 SFAELDARSDAIAHGLNAA-GIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVlvdPG---MGIKNLKQCLAEAQPDAFI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 164 TTdTLApeveSVA-----PECPSLKTKLLVSDhsREGW----LDFRSLVKSASPdHICIKSKTLDPMAIFFTSGTTGFPK 234
Cdd:PRK09274 119 GI-PKA----HLArrlfgWGKPSVRRLVTVGG--RLLWggttLATLLRDGAAAP-FPMADLAPDDMAAILFTSGSTGTPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 235 MAKHSHG-F-----ALRSYFPACRKLLQLKMSDVFwclsdtgwilaalgSLLEPWTAGSTV-----FAHhlP-QFDPKVI 302
Cdd:PRK09274 191 GVVYTHGmFeaqieALREDYGIEPGEIDLPTFPLF--------------ALFGPALGMTSVipdmdPTR--PaTVDPAKL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 303 IETFFKYPITQCLAAPSVYRMILQQNYTS-LRFPTLEHCCTGG-----------EALLPEeqeqwkrqtGVLLYQAYGQS 370
Cdd:PRK09274 255 FAAIERYGVTNLFGSPALLERLGRYGEANgIKLPSLRRVISAGapvpiavierfRAMLPP---------DAEILTPYGAT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 371 EA-GISCGTLRGMKIKPGSM---------GKAIPPFDIQIIDdkgnIqppnTEGNI----GIRIKPTRPIGLFM------ 430
Cdd:PRK09274 326 EAlPISSIESREILFATRAAtdngagicvGRPVDGVEVRIIA----I----SDAPIpewdDALRLATGEIGEIVvagpmv 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 431 ---YYeNNPEKTAEV----ECGDFYN-TGDRATIDEEGYFWFLGR-SDDVINASGyRVGPAEVENALAEHPAVAESAVVS 501
Cdd:PRK09274 398 trsYY-NRPEATRLAkipdGQGDVWHrMGDLGYLDAQGRLWFCGRkAHRVETAGG-TLYTIPCERIFNTHPGVKRSALVG 475
|
490 500 510
....*....|....*....|....*....|....*.
gi 529006476 502 SPDPvrGEVVKAFIV-LNPEfSSRDPGELTKELQQH 536
Cdd:PRK09274 476 VGVP--GAQRPVLCVeLEPG-VACSKSALYQELRAL 508
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
225-569 |
6.41e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 75.59 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 225 FTSGTTGFPKMAKHSHG-FALRsyfpaCRKLLQ---LKMSDV---FWCLSdtgwILAALGSLLEPWTAGSTVFAHHLPQF 297
Cdd:PRK05691 2340 YTSGSTGKPKGVVVSHGeIAMH-----CQAVIErfgMRADDCelhFYSIN----FDAASERLLVPLLCGARVVLRAQGQW 2410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 298 DPKVIIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCTGGEALLPEeqeQWKRQTGV----LLYQAYGQSE-- 371
Cdd:PRK05691 2411 GAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGE---HLQRIRQAfapqLFFNAYGPTEtv 2487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 372 ----AGISCGTLR-GMKIKPgsMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNPEKTAE----- 441
Cdd:PRK05691 2488 vmplACLAPEQLEeGAASVP--IGRVVGARVAYILDADLALVPQGATGELYVGGA-----GLAQGYHDRPGLTAErfvad 2560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 442 ---VECGDFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLN 518
Cdd:PRK05691 2561 pfaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAV 2640
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 529006476 519 PEFSSRDPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSEL 569
Cdd:PRK05691 2641 AGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL 2691
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
83-576 |
1.09e-13 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.82 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 83 EVKWSFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAI 162
Cdd:PRK05691 3743 DQQWSYAELNRAANRLGHALRAA-GVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVL 3821
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 163 VTTDTLAPEVESVAPECP-SLKTKLLVsdhsregWLDFRSlvkSASPDHICIKSKTLDPMA-IFFTSGTTGFPK--MAKH 238
Cdd:PRK05691 3822 VCSAACREQARALLDELGcANRPRLLV-------WEEVQA---GEVASHNPGIYSGPDNLAyVIYTSGSTGLPKgvMVEQ 3891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 239 shgfalrsyfpacRKLLQLKMSDVFWCLSDTGWILAALGS----------LLEPWTAGSTVFAHHLPQFDPKVIIETFFK 308
Cdd:PRK05691 3892 -------------RGMLNNQLSKVPYLALSEADVIAQTASqsfdisvwqfLAAPLFGARVEIVPNAIAHDPQGLLAHVQA 3958
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 309 YPITQCLAAPSVYRMIL---QQNYTSLRF--PTlehcctgGEALLPEEQEQW-KRQTGVLLYQAYGQSEAG-------IS 375
Cdd:PRK05691 3959 QGITVLESVPSLIQGMLaedRQALDGLRWmlPT-------GEAMPPELARQWlQRYPQIGLVNAYGPAECSddvaffrVD 4031
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 376 CGTLRGMKIKPGSmgkaipPFD---IQIIDDKGNIQPPNTEGNIGIRikptrPIGLFMYYENNPEKTAEV-------ECG 445
Cdd:PRK05691 4032 LASTRGSYLPIGS------PTDnnrLYLLDEALELVPLGAVGELCVA-----GTGVGRGYVGDPLRTALAfvphpfgAPG 4100
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 446 D-FYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSpDPVRGEVVKAFIVlnPEFSSR 524
Cdd:PRK05691 4101 ErLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ-EGVNGKHLVGYLV--PHQTVL 4177
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 529006476 525 DPGELTKELQQHVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELRKKEFGQ 576
Cdd:PRK05691 4178 AQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQ 4229
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
118-570 |
3.57e-12 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 68.69 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 118 LPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVTTDTLA------PEVESVAPECPSLKTKLLVSDH 191
Cdd:PLN03051 1 MPMTVDAVIIYLAIVLAGCVVVSVADSFSAKEIATRLDISGAKGVFTQDVVLrggralPLYSKVVEAAPAKAIVLPAAGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 192 S-----REG---WLDF-RSLVKSASPDHICIKSKTLD---PMAIFFTSGTTGFPKMAKHSHGFALRSyfpAC--RKLLQL 257
Cdd:PLN03051 81 PvavplREQdlsWCDFlGVAAAQGSVGGNEYSPVYAPvesVTNILFSSGTTGEPKAIPWTHLSPLRC---ASdgWAHMDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 258 KMSDVFWCLSDTGWILaalGSLL--EPWTAGSTVFAHHLPQFDPKviietFFKY----PITQCLAAPSVYRMILQQNYTS 331
Cdd:PLN03051 158 QPGDVVCWPTNLGWMM---GPWLlySAFLNGATLALYGGAPLGRG-----FGKFvqdaGVTVLGLVPSIVKAWRHTGAFA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 332 LRFPTLEHC---CTGGEALLPEEqEQWkrqtgVLLYQAY--------GQSEagISCGTLRGMKIKP---GSMGKAIPPFD 397
Cdd:PLN03051 230 MEGLDWSKLrvfASTGEASAVDD-VLW-----LSSVRGYykpvieycGGTE--LASGYISSTLLQPqapGAFSTASLGTR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 398 IQIIDDKGniQPPNTEGNIgirikpTRPIGLFM-----------------YYENNPekTAEVECGDFYNTGDRATIDEEG 460
Cdd:PLN03051 302 FVLLNDNG--VPYPDDQPC------VGEVALAPpmlgasdrllnadhdkvYYKGMP--MYGSKGMPLRRHGDIMKRTPGG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 461 YFWFLGRSDDVINASGYRVGPAEVENALAE-HPAVAESAVVSSPDPVRGE----VVKAFIVLNPEFSSRDPGELTKELQQ 535
Cdd:PLN03051 372 YFCVQGRADDTMNLGGIKTSSVEIERACDRaVAGIAETAAVGVAPPDGGPellvIFLVLGEEKKGFDQARPEALQKKFQE 451
|
490 500 510
....*....|....*....|....*....|....*
gi 529006476 536 HVKSVTAPYKYPRKVEFVSELPKTITGKIKRSELR 570
Cdd:PLN03051 452 AIQTNLNPLFKVSRVKIVPELPRNASNKLLRRVLR 486
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
213-563 |
1.19e-10 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 64.35 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 213 IKSKTLDPMAIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFwclsdtgwiLAALG---------SLLEPW 283
Cdd:PRK08043 360 VKQQPEDAALILFTSGSEGHPKGVVHSHK-SLLANVEQIKTIADFTPNDRF---------MSALPlfhsfgltvGLFTPL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 284 TAGSTVFAhhlpqfdpkviietffkYPitqclaAPSVYRMILQ----QNYTSL-----------------RFPTLEHCCT 342
Cdd:PRK08043 430 LTGAEVFL-----------------YP------SPLHYRIVPElvydRNCTVLfgtstflgnyarfanpyDFARLRYVVA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 343 GGEALLPEEQEQWKRQTGVLLYQAYGQSEAGISCGTLRGMKIKPGSMGKAIPPFDIQI-----IDDKGNIQ--PPNTEgN 415
Cdd:PRK08043 487 GAEKLQESTKQLWQDKFGLRILEGYGVTECAPVVSINVPMAAKPGTVGRILPGMDARLlsvpgIEQGGRLQlkGPNIM-N 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 416 IGIRIKptRPIGLFMYYENNPEktAEVECGdFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVEN-ALAEHPAv 494
Cdd:PRK08043 566 GYLRVE--KPGVLEVPTAENAR--GEMERG-WYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPD- 639
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 529006476 495 AESAVVSSPDPVRGEVVKAFivlnpefsSRDPgELTKE-LQQHVKSVTAP-YKYPRKVEFVSELPKTITGK 563
Cdd:PRK08043 640 KQHATAIKSDASKGEALVLF--------TTDS-ELTREkLQQYAREHGVPeLAVPRDIRYLKQLPLLGSGK 701
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
388-572 |
1.41e-10 |
|
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: 63.66 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 388 SMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTRPiglfMYYeNNPEKTAEVECGD-FYNTGDRATIdEEGYFWFLG 466
Cdd:cd05908 315 EVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTP----GYY-NNPEATAKVFTDDgWLKTGDLGFI-RNGRLVITG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 467 RSDDVINASGYRVGPAEVENALAEHPAVAESAVVS---SPDPVRGEVVKAFIVLNPefSSRDPGELTKELQQHVKSVTAp 543
Cdd:cd05908 389 REKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNKRGG- 465
|
170 180
....*....|....*....|....*....
gi 529006476 544 yKYPRKVEFVSELPKTITGKIKRSELRKK 572
Cdd:cd05908 466 -WQINEVLPIRRIPKTTSGKVKRYELAQR 493
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
82-569 |
1.07e-09 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 61.08 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 82 DEVKW-SFREMTDLTCRTANVLTQTcGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAK 160
Cdd:cd17639 1 GEYKYmSYAEVWERVLNFGRGLVEL-GLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 161 AIVTtdtlapevesvapecpslktkllvsdhsregwldfrslvkSASPDHICIksktldpmaIFFTSGTTGFPKMAKHSH 240
Cdd:cd17639 80 AIFT----------------------------------------DGKPDDLAC---------IMYTSGSTGNPKGVMLTH 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 241 --------GFALR------------SYFPACRKLlqlKMSDVFWCLSDTGWIlaALGSllePWTAGSTVFAH---HLPQF 297
Cdd:cd17639 111 gnlvagiaGLGDRvpellgpddrylAYLPLAHIF---ELAAENVCLYRGGTI--GYGS---PRTLTDKSKRGckgDLTEF 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 298 DPKV------IIETFFKYPITQCLAAPSVYRMILQQNYTSLRFPTLEHCCT------------------------GGEAL 347
Cdd:cd17639 183 KPTLmvgvpaIWDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGTplldelvfkkvraalggrlrymlsGGAPL 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 348 LPEEQEQWKRQTGVLLyQAYGQSEaGISCGT-LRGMKIKPGSMGKAIPPFDIQIID-DKGNIQP--PNTEGNIGIRIKPt 423
Cdd:cd17639 263 SADTQEFLNIVLCPVI-QGYGLTE-TCAGGTvQDPGDLETGRVGPPLPCCEIKLVDwEEGGYSTdkPPPRGEILIRGPN- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 424 rpigLFMYYENNPEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDD-VINASGYRVGPAEVENALAEHPAVAESAVVS 501
Cdd:cd17639 340 ----VFKGYYKNPEKTKEAFDGDgWFHTGDIGEFHPDGTLKIIDRKKDlVKLQNGEYIALEKLESIYRSNPLVNNICVYA 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 502 SPDPVRgevVKAFIVLNPEF-----------SSRDP---------GELTKELQQHVKSVT-APYKYPRKVEFVSEL--PK 558
Cdd:cd17639 416 DPDKSY---PVAIVVPNEKHltklaekhgviNSEWEelcedkklqKAVLKSLAETARAAGlEKFEIPQGVVLLDEEwtPE 492
|
570
....*....|....*
gi 529006476 559 ----TITGKIKRSEL 569
Cdd:cd17639 493 nglvTAAQKLKRKEI 507
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
85-500 |
1.57e-08 |
|
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: 57.37 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 85 KWSFREMTDLtCRTANVLTQTCGLQTGDRLALILPRVPEWWLVCVGCIRTGIIFMPGTTQMKAKDILYRLQVSGAKAIVT 164
Cdd:cd05933 8 TLTYKEYYEA-CRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 165 -TDTLAPEVESVAPECPSLKTKLLVSDHSRE------GWLDFRSLVKSASPDHICIKSKTLDP---MAIFFTSGTTGFPK 234
Cdd:cd05933 87 eNQKQLQKILQIQDKLPHLKAIIQYKEPLKEkepnlySWDEFMELGRSIPDEQLDAIISSQKPnqcCTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 235 --MAKH----------SHGFALR----------SYFPACRKLLQlkMSDVFWCLSDTGWI----LAAL-GSLLE------ 281
Cdd:cd05933 167 gvMLSHdnitwtakaaSQHMDLRpatvgqesvvSYLPLSHIAAQ--ILDIWLPIKVGGQVyfaqPDALkGTLVKtlrevr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 282 -------PWT------------AGSTVFAHHLPQFDPKVIIETFFKY-------PITQCLAAPSVYRMILQqnytslrFP 335
Cdd:cd05933 245 ptafmgvPRVwekiqekmkavgAKSGTLKRKIASWAKGVGLETNLKLmggespsPLFYRLAKKLVFKKVRK-------AL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 336 TLEHC--CTGGEALLPEEQEQWKRQTGVLLYQAYGQSEAGiSCGTLRGMK-IKPGSMGKAIPPFDIQII--DDKGNiqpp 410
Cdd:cd05933 318 GLDRCqkFFTGAAPISRETLEFFLSLNIPIMELYGMSETS-GPHTISNPQaYRLLSCGKALPGCKTKIHnpDADGI---- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 411 nteGNIGIRikpTRPIglFMYYENNPEKTAE-VECGDFYNTGDRATIDEEGYFWFLGRSDD-VINASGYRVGPAEVENAL 488
Cdd:cd05933 393 ---GEICFW---GRHV--FMGYLNMEDKTEEaIDEDGWLHSGDLGKLDEDGFLYITGRIKElIITAGGENVPPVPIEDAV 464
|
490
....*....|...
gi 529006476 489 -AEHPAVAESAVV 500
Cdd:cd05933 465 kKELPIISNAMLI 477
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
440-571 |
1.69e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 54.00 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 440 AEVECGDFYNTGDRATIDEEGYFwFLGRSDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGevVKAFIVLNP 519
Cdd:PRK05851 390 APIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGS--ARPGLVIAA 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 529006476 520 EFSSRDPGELTKELQQHVKSVTApyKYPRKVEFVS--ELPKTITGKIKRSELRK 571
Cdd:PRK05851 467 EFRGPDEAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRRLAVKR 518
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
388-568 |
2.39e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 53.46 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 388 SMGKAIPPFDIQIIDDKGNIQPPNTEGNIGIRIKPTRPiglfmYYENNPEKTAEVECGDFYNTGDRATIDEEGYFWFLGR 467
Cdd:PRK07768 361 TLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTP-----GYLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGR 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 468 SDDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPvRGEVVKAFIVLNPEFSSRDPGELTKELQQHVKSVTAPYKY- 546
Cdd:PRK07768 436 VKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD-AGHSREGFAVAVESNAFEDPAEVRRIRHQVAHEVVAEVGVr 514
|
170 180
....*....|....*....|....
gi 529006476 547 PRKVEFVS--ELPKTITGKIKRSE 568
Cdd:PRK07768 515 PRNVVVLGpgSIPKTPSGKLRRAN 538
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
219-491 |
4.94e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 52.51 E-value: 4.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 219 DPMAIFFTSGTTGFPKMAKHSHGfALRSYFPACRKLLQLKMSDVFWC----LSDTGWILAALGSLLepwtAG-STVFAHH 293
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHA-NLLANQRACLKFFSPKEDDVMMSflppFHAYGFNSCTLFPLL----SGvPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 294 LPQfdPKVIIETFFKYPITQCLAAPSVYRMIL---QQNYTSLrfPTLEHCCTGGEAL---LPEEQEqwKRQTGVLLYQAY 367
Cdd:PRK06334 259 PLY--PKKIVEMIDEAKVTFLGSTPVFFDYILktaKKQESCL--PSLRFVVIGGDAFkdsLYQEAL--KTFPHIQLRQGY 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 368 GQSEAG--ISCGTLRGMKIKpGSMGKAIPPFDIQIIDDKGNIqpPNTEGNIGIRIkpTRPIGLFMYYENNPEKTAEVECG 445
Cdd:PRK06334 333 GTTECSpvITINTVNSPKHE-SCVGMPIRGMDVLIVSEETKV--PVSSGETGLVL--TRGTSLFSGYLGEDFGQGFVELG 407
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 529006476 446 --DFYNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENALAEH 491
Cdd:PRK06334 408 geTWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
390-571 |
4.98e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 49.23 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 390 GKAIPPFDIQIIDDKGNIQPPNTEGNIGIRiKPTRPIGLFmyyeNNPEKTAEVECGDFYNTGDRATIdEEGYFWFLGRSD 469
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVR-GPSLMSGYF----RDEESQDVLAADGWLDTGDLGYL-LDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 470 DVINASGYRVGPAEVENALAEHPAV--AESAVVSSPDPvRGEVVKAFI---VLNPEfssrDPGELTKELQQHVKSVTApy 544
Cdd:PRK09192 462 DLIIINGRNIWPQDIEWIAEQEPELrsGDAAAFSIAQE-NGEKIVLLVqcrISDEE----RRGQLIHALAALVRSEFG-- 534
|
170 180
....*....|....*....|....*....
gi 529006476 545 kYPRKVEFVS--ELPKTITGKIKRSELRK 571
Cdd:PRK09192 535 -VEAAVELVPphSLPRTSSGKLSRAKAKK 562
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
343-566 |
1.81e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 47.45 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 343 GGEALLPEEQEQWKRQTGVLLYQAYGQSEAG----ISCGTLRGMKIKPGSMgkaIPpfdiQIIDdkgniqpPNT-----E 413
Cdd:COG1541 211 GGEPWSEEMRKEIEERWGIKAYDIYGLTEVGpgvaYECEAQDGLHIWEDHF---LV----EIID-------PETgepvpE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 414 GNIG--------------IRikptrpiglfmyyennpektaevecgdfYNTGDRATIDEE-----------GYfwFLGRS 468
Cdd:COG1541 277 GEEGelvvttltkeamplIR----------------------------YRTGDLTRLLPEpcpcgrthpriGR--ILGRA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 469 DDVINASGYRVGPAEVENALAEHPAVAESAVVSSPDPVRGEVVKAFIVLNPEFSSRdpgELTKELQQHVKSVTapyKYPR 548
Cdd:COG1541 327 DDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPGASLE---ALAEAIAAALKAVL---GLRA 400
|
250 260
....*....|....*....|
gi 529006476 549 KVEFVS--ELPKTiTGKIKR 566
Cdd:COG1541 401 EVELVEpgSLPRS-EGKAKR 419
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
225-569 |
3.10e-05 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 46.74 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 225 FTSGTTGFPKMAKHSHgFALRSYFPACRKLLQLKMSDVFWCLSdtgwilaalG--------SLLEPWTAGSTVFahhLPQ 296
Cdd:cd17647 116 FTSGSEGIPKGVLGRH-FSLAYYFPWMAKRFNLSENDKFTMLS---------GiahdpiqrDMFTPLFLGAQLL---VPT 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 297 FD----PKVIIETFFKYPITQCLAAPSVYRMILQQNYTSlrFPTLEHCCTGGEALLpeEQEQWKRQT---GVLLYQAYGQ 369
Cdd:cd17647 183 QDdigtPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTP--FPKLHHAFFVGDILT--KRDCLRLQTlaeNVRIVNMYGT 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 370 SEA--GISCGTLRGMKIKPG---SMGKAIPP----FDIQII----DDKGNIQPPNTEGNIGIRIKptrpiGLFMYYENNP 436
Cdd:cd17647 259 TETqrAVSYFEVPSRSSDPTflkNLKDVMPAgrgmLNVQLLvvnrNDRTQICGIGEVGEIYVRAG-----GLAEGYRGLP 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 437 EKTAE-------VECGDF----------------------YNTGDRATIDEEGYFWFLGRSDDVINASGYRVGPAEVENA 487
Cdd:cd17647 334 ELNKEkfvnnwfVEPDHWnyldkdnnepwrqfwlgprdrlYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTH 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 488 LAEHPAVAES------------AVVS--SPDPVRGEVVKAFIVLNPEFSSRDP--------GELTKELQQHVKSVTAPYK 545
Cdd:cd17647 414 ISQHPLVRENitlvrrdkdeepTLVSyiVPRFDKPDDESFAQEDVPKEVSTDPivkgligyRKLIKDIREFLKKRLASYA 493
|
410 420
....*....|....*....|....
gi 529006476 546 YPRKVEFVSELPKTITGKIKRSEL 569
Cdd:cd17647 494 IPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
360-571 |
4.16e-05 |
|
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: 46.44 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 360 GVLLYQAYGQSE-AGISCGTLRGMKIkPGSMGKAIPPFDIQIID--DKG-NIQPPNTEGNIGIRIKptrpiGLFMYYENN 435
Cdd:cd05927 299 GCPVLEGYGQTEcTAGATLTLPGDTS-VGHVGGPLPCAEVKLVDvpEMNyDAKDPNPRGEVCIRGP-----NVFSGYYKD 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 436 PEKTAEVECGD-FYNTGDRATIDEEGYFWFLGRSDDVIN-ASGYRVGPAEVENALAEHPAVAES------------AVVs 501
Cdd:cd05927 373 PEKTAEALDEDgWLHTGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPFVAQIfvygdslksflvAIV- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 502 SPDP--------VRGEVVKAFIVL--NPEFSSR---DPGELTKELQQHvksvtaPYKYPRKVEFVSELPK------TITG 562
Cdd:cd05927 452 VPDPdvlkewaaSKGGGTGSFEELckNPEVKKAileDLVRLGKENGLK------GFEQVKAIHLEPEPFSvengllTPTF 525
|
....*....
gi 529006476 563 KIKRSELRK 571
Cdd:cd05927 526 KLKRPQLKK 534
|
|
| PRK09188 |
PRK09188 |
serine/threonine protein kinase; Provisional |
466-569 |
2.93e-03 |
|
serine/threonine protein kinase; Provisional
Pssm-ID: 236400 [Multi-domain] Cd Length: 365 Bit Score: 40.13 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529006476 466 GRSDDVINasgyrVGPAEVEnALAEHPAVAESAVVSSPDPVRGEVVKAFIvlnpefsSRDPGELTKELQQHVKSVTAPyK 545
Cdd:PRK09188 233 GTGDRIDN-----EAPAIQA-ALKSDPAVSDVAIALFSLPAKGVGLYAFV-------EAELPADEKSLRARLAGAKPP-K 298
|
90 100
....*....|....*....|....
gi 529006476 546 YPRKVEFVSELPKTITGKIkRSEL 569
Cdd:PRK09188 299 PPEHIQPVAALPRDADGTV-RDDI 321
|
|
| |
