|
Name |
Accession |
Description |
Interval |
E-value |
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
10-678 |
6.77e-161 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 496.87 E-value: 6.77e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 10 LELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQ-FGCDLDAFELAF 88
Cdd:PRK10252 8 LPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQwVDPALTFPLPEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 89 IDASGDADPFAACWNAMQAESDRPYDLLSSK-LFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQ 167
Cdd:PRK10252 88 IDLRTQPDPHAAAQALMQADLQQDLRVDSGKpLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 168 PVPDSDFGPIEPMTNGDRAYRSSSRYVTDRRYWQDYVAALPATETLAGT--AARASGA-FRRASAPLPVPFVEQLDTiEA 244
Cdd:PRK10252 168 PTPASPFTPFADVVEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAplPGRSASAdILRLKLEFTDGAFRQLAA-QA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 245 RIAKWPLVLTAIVAAYLYRMSNGRITVFDFPVSART-KETRTLPGMFANILPMRLPITPRTTLAELTRQVGAEVFAHMKH 323
Cdd:PRK10252 247 SGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLgSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRH 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 324 QQFRVKEIKQMRGAFAG--PVFGPRINIVAYDNRWEFGGSLATLHALANGLVNDFAVTVTGNPrDPGCTLHVDGNAELYD 401
Cdd:PRK10252 327 QRYDAEQIVRDSGRAAGdePLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLELALFPDE-HGGLSIEILANPQRYD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 402 GADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRlLLHTWNATEAAYPEhQRVHELVEAQARQMPEAVALVAEHEQ 481
Cdd:PRK10252 406 EATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYA-QLAQVNATAVEIPE-TTLSALVAQQAAKTPDAPALADARYQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 482 LSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPpvvlvdp 561
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARP------- 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 562 vgrKALADALGDAHRATHALVDVTAG--SPPWDALPPDNLSSHsreltSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVT 639
Cdd:PRK10252 557 ---SLLITTADQLPRFADVPDLTSLCynAPLAPQGAAPLQLSQ-----PHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLL 628
|
650 660 670
....*....|....*....|....*....|....*....
gi 1939408627 640 WHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK10252 629 WMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKL 667
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
6-678 |
7.64e-148 |
|
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: 463.17 E-value: 7.64e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 6 PQEILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDA--FEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDA 83
Cdd:COG1020 14 AAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAAllLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 84 FELAFIDASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSL 163
Cdd:COG1020 94 LPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 164 LRQQPVPdsdfGPIEPMTNGDRAY-----RSSSRYVTDRRYWQDYVAALPATETL---AGTAARASGAFRRASAPLPVPF 235
Cdd:COG1020 174 YAGAPLP----LPPLPIQYADYALwqrewLQGEELARQLAYWRQQLAGLPPLLELptdRPRPAVQSYRGARVSFRLPAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 236 VEQLDTIEARI-AKWPLVLTAIVAAYLYRMSNGRITVFDFPVSART-KETRTLPGMFANILPMRLPITPRTTLAELTRQV 313
Cdd:COG1020 250 TAALRALARRHgVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPrPELEGLVGFFVNTLPLRVDLSGDPSFAELLARV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 314 GAEVFAHMKHQQFR----VKEIKQMRGAFAGPVFGPRINIVAYD-NRWEFGGSLATLHALANGLVNdFAVTVTGNPRDPG 388
Cdd:COG1020 330 RETLLAAYAHQDLPferlVEELQPERDLSRNPLFQVMFVLQNAPaDELELPGLTLEPLELDSGTAK-FDLTLTVVETGDG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 389 CTLHVDGNAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEAAYPEHQRVHELVEAQARQ 468
Cdd:COG1020 409 LRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAAR 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 469 MPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHV 548
Cdd:COG1020 489 TPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYM 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 549 LDDAKPPVVLVDPvgrkALADALGDaHRATHALVDvtagSPPWDALPPDNLSShsrELTSHHLAYVIYTSGSTGVPKGVM 628
Cdd:COG1020 569 LEDAGARLVLTQS----ALAARLPE-LGVPVLALD----ALALAAEPATNPPV---PVTPDDLAYVIYTSGSTGRPKGVM 636
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1939408627 629 VEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:COG1020 637 VEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATL 686
|
|
| NRPS_MxcG |
NF038078 |
myxochelin non-ribosomal peptide synthetase MxcG; |
7-678 |
4.04e-138 |
|
myxochelin non-ribosomal peptide synthetase MxcG;
Pssm-ID: 468336 [Multi-domain] Cd Length: 1444 Bit Score: 439.16 E-value: 4.04e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 7 QEILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFEL 86
Cdd:NF038078 2 EARWPLSAAQHGIWLGQQLDLASPVYNAGECIEIRGPVDPAVFEAALRQAVGEAEALHMRFVPGEEGPRQLLDPSADWPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 87 AFIDASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQ 166
Cdd:NF038078 82 HRVDVSGTPDPWAAAQAWMREDLARTVDLSRGPLFAEALFKAAPDRFFWYQRAHHIALDGFGFSLLARRVAELYTARVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 167 QPVPDSdFGPIEPMTNGDRAYRSSSRYVTDRRYWQDYVAALPATETLAGtAARASGAFRRASAPLPVPFVEQLDTIEARI 246
Cdd:NF038078 162 RPATGG-FGSLRAVLDEDAAYRAGPQCELDRAFWMERFADRPTPVSLAE-PAPMSRSFVRQTRHLSPSEMERLQAVARQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 247 -AKWPLVLTAIVAAYLYRMSNGRITVFDFPVSARTKETR-TLPGMFANILPMRLPITPRTTLAELTRQVGAEVFAHMKHQ 324
Cdd:NF038078 240 gLSWPDLVLAATAAWLHRRTGAPEVVLGLPVMGRLGSAAlRVPCMAMNIVPLRVPVRPGAGLLALARGVAAELRAIRPHL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 325 QFRVKEIKQMRGAFAGP--VFGPRINIVAYDNRWEFGGSLATLHALANGLVNDFAVTVTGNPRDPGCTLHVDGNAELYDG 402
Cdd:NF038078 320 RYRYEQLRRDLKLVGGQrrLFGPVVNIMPFDYALRFAGMPAIAHNISAGPVEDLSIGVYARSDGRGPRVDFDANPACYSA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 403 ADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEAAYP---EHQRVHELVEAQARQMPEAVALVAEH 479
Cdd:NF038078 400 DELDAHQREFLQLLEALLAAPEQAVARALIPGAAAPAPAASRPGSLLDGGPlpaPARPVLELIAERAREQPDAIAVEHGP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKpPVVLV 559
Cdd:NF038078 480 RRMTYRELLLAARALAARLVAAGARPDTLVAVMLPRSIDAIVASLGVLFSGAGYLPLDPFGPSSRTAAILADAA-PALIV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 560 DPVGRKALADALGDAHRatHALVDVTAGSPPWDALPPDNLSSHSreltshHLAYVIYTSGSTGVPKGVMVEHRQLVNLVT 639
Cdd:NF038078 559 TSSEHAPTAKAGPQAPG--ALVVRRLEEAVPSPAPEAPPRPADE------RLAYVIYTSGSTGQPNGVQISRGALAHFVA 630
|
650 660 670
....*....|....*....|....*....|....*....
gi 1939408627 640 WHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:NF038078 631 GATQRYGVRRDDRVLQFAPLHFDASVEEIFLTLCAGARL 669
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
10-423 |
4.01e-111 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380456 [Multi-domain] Cd Length: 419 Bit Score: 341.66 E-value: 4.01e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 10 LELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFI 89
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 90 DASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQPV 169
Cdd:cd19533 82 DLSGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 170 PDSDFGPIEPMTNGDRAYRSSSRYVTDRRYWQDYVAALPATETLAGTAARASGAFRRASAPLPVPFVEQL-DTIEARIAK 248
Cdd:cd19533 162 PPAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELTRTLlEAAEAHGAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 249 WPLVLTAIVAAYLYRMSNGRITVFDFPVSART-KETRTLPGMFANILPMRLPITPRTTLAELTRQVGAEVFAHMKHQQFR 327
Cdd:cd19533 242 WPSFFIALVAAYLHRLTGANDVVLGVPVMGRLgAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 328 VKEIKQMRGAFAG--PVFGPRINIVAYDNRWEFGGSLATLHALANGLVNDFAVTVTGNPRDPGCTLHVDGNAELYDGADV 405
Cdd:cd19533 322 YEDLRRDLGLTGElhPLFGPTVNYMPFDYGLDFGGVVGLTHNLSSGPTNDLSIFVYDRDDESGLRIDFDANPALYSGEDL 401
|
410
....*....|....*...
gi 1939408627 406 QAHRKRLLHFIEAALADP 423
Cdd:cd19533 402 ARHQERLLRLLEEAAADP 419
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
6-678 |
4.02e-95 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 323.06 E-value: 4.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 6 PQEILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFE 85
Cdd:PRK12316 46 SAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 86 LAFIDASGDADP--FAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSL 163
Cdd:PRK12316 126 VEFEDCSGLPEAeqEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 164 LRQQ-------PVPDSDFGPIEpmtngdRAYRSSSRYVTDRRYWQdyvAAL----PATETLAGTAARASGAFR--RASAP 230
Cdd:PRK12316 206 ATGAepglpalPIQYADYALWQ------RSWLEAGEQERQLEYWR---AQLgeehPVLELPTDHPRPAVPSYRgsRYEFS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 231 LPVPFVEQLDTIEAR--IAKWPLVLTAiVAAYLYRMSNG---RITVfdfPVSART-KETRTLPGMFANILPMRLPITPRT 304
Cdd:PRK12316 277 IDPALAEALRGTARRqgLTLFMLLLGA-FNVLLHRYSGQtdiRVGV---PIANRNrAEVEGLIGFFVNTQVLRSVFDGRT 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 305 TLAELTRQVGAEVFAHMKHQQFR----VKEIKQMRGAFAGPVFGPRINivaYDNRWEFGGSLATLHALANGLVNDFAVT- 379
Cdd:PRK12316 353 RVATLLAGVKDTVLGAQAHQDLPferlVEALKVERSLSHSPLFQVMYN---HQPLVADIEALDTVAGLEFGQLEWKSRTt 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 380 ---VTGNPRDPGCTLHVDGN--AELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEAAYPE 454
Cdd:PRK12316 430 qfdLTLDTYEKGGRLHAALTyaTDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPL 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 455 HQRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYL 534
Cdd:PRK12316 510 QRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYV 589
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 535 PVDPAYSSARLAHVLDDAKPPVVLVDpvgrKALADALGDAHRATHALVDvtAGSPPWDALPPDNLSSHsreLTSHHLAYV 614
Cdd:PRK12316 590 PLDPEYPAERLAYMLEDSGVQLLLSQ----SHLGRKLPLAAGVQVLDLD--RPAAWLEGYSEENPGTE---LNPENLAYV 660
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939408627 615 IYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK12316 661 IYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARL 724
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
10-678 |
2.29e-93 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 317.87 E-value: 2.29e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 10 LELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFI 89
Cdd:PRK12467 1117 LPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEP 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 90 DASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQ-- 167
Cdd:PRK12467 1197 LLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQsl 1276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 168 -----PVPDSDFG--PIEPMTNGDRAYRSSsrYVTDRRYWQDYVAALPATEtlagtAARASGAFR--RASAPLPVPFVEQ 238
Cdd:PRK12467 1277 qlpalPIQYADYAvwQRQWMDAGERARQLA--YWKAQLGGEQPVLELPTDR-----PRPAVQSHRgaRLAFELPPALAEG 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 239 LDTIEARI-AKWPLVLTAIVAAYLYRMSNGRITVFDFPVSARTK-ETRTLPGMFANILPMRLPITPRTTLAELTRQVGAE 316
Cdd:PRK12467 1350 LRALARREgVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRaETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQA 1429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 317 VFAHMKHQQFR----VKEIKQMRGAFAGPVFGpriniVAYDNRWEFGGSLATLHALA-NGLVND-----FAVTVTGNPRD 386
Cdd:PRK12467 1430 ALEAQAHQDLPfeqlVEALQPERSLSHSPLFQ-----VMFNHQRDDHQAQAQLPGLSvESLSWEsqtaqFDLTLDTYESS 1504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 387 PGCTLHVDGNAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEAAYPEHQRVHELVEAQA 466
Cdd:PRK12467 1505 EGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQA 1584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 467 RQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLA 546
Cdd:PRK12467 1585 AATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLA 1664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 547 HVLDDAKPPVVLVD---------PVGRKALADALGDAHRATHALVDvtagspPWDALPPDNlsshsreltshhLAYVIYT 617
Cdd:PRK12467 1665 YMIEDSGIELLLTQshlqarlplPDGLRSLVLDQEDDWLEGYSDSN------PAVNLAPQN------------LAYVIYT 1726
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939408627 618 SGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK12467 1727 SGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARL 1787
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
8-678 |
1.66e-92 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 315.18 E-value: 1.66e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 8 EILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELA 87
Cdd:PRK12467 48 ERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 88 FIDASGDADPFAACW--NAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLR 165
Cdd:PRK12467 128 LDDLANEQGRARESQieAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 166 QQPVPDSDFgPIEP----------MTNGDRAYRsssryvtdRRYWQDYVAALPATETLAGTAAR-ASGAFR--RASAPLP 232
Cdd:PRK12467 208 GREPSLPAL-PIQYadyaiwqrswLEAGERERQ--------LAYWQEQLGGEHTVLELPTDRPRpAVPSYRgaRLRVDLP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 233 VPFVEQLDTIEARIAKWP-LVLTAIVAAYLYRMSNGRITVFDFPVSARTK-ETRTLPGMFANILPMRLPITPRTTLAELT 310
Cdd:PRK12467 279 QALSAGLKALAQREGVTLfMVLLASFQTLLHRYSGQSDIRIGVPNANRNRvETERLIGFFVNTQVLKAEVDPQASFLELL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 311 RQVGAEVFAHMKHQQFR----VKEIKQMRGAFAGPVFGPRINivaydnrwefggslatLHALANGLVNDFAVTVTG---N 383
Cdd:PRK12467 359 QQVKRTALGAQAHQDLPfeqlVEALQPERSLSHSPLFQVMFN----------------HQNTATGGRDREGAQLPGltvE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 384 PRDPGC-TLHVDGN-----------------AELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTW 445
Cdd:PRK12467 423 ELSWARhTAQFDLAldtyesaqglwaaftyaTDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRW 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 446 NATEAAYPEHQrVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLA 525
Cdd:PRK12467 503 NAPATEYAPDC-VHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLA 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 526 VLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDPVGRKALADALGDAHRATHALVDVTAGSP---PWDALPPDNlssh 602
Cdd:PRK12467 582 VLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPADLLCGYSghnPEVALDPDN---- 657
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939408627 603 sreltshhLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK12467 658 --------LAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATL 725
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-678 |
3.09e-89 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 305.73 E-value: 3.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 10 LELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFI 89
Cdd:PRK12316 2603 LPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLE 2682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 90 DASGDADpfAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQPV 169
Cdd:PRK12316 2683 DCAGVAD--AAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQP 2760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 170 PDsdfgPIEPMTNGD-----RAYRSSSRYVTDRRYWQDYVAALPATETLAGTAAR---ASGAFRRASAPLPVPFVEQLDT 241
Cdd:PRK12316 2761 TL----PPLPLQYADyaawqRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRpalQSHRGARLDVALDVALSRELLA 2836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 242 IEARIAKWP-LVLTAIVAAYLYRMSNGRITVFDFPVSARTK-ETRTLPGMFANILPMRLPITPRTTLAELTRQVGAEVFA 319
Cdd:PRK12316 2837 LARREGVTLfMLLLASFQVLLHRYSGQSDIRVGVPIANRNRaETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALG 2916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 320 HMKHQQF----RVKEIKQMRGAFAGPVFGPRINIVAYDNRWEFGGSLATLHALANGLVNDFAVTVTGNPRDPGCTLHVDG 395
Cdd:PRK12316 2917 AQAHQDLpfeqLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTY 2996
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 396 NAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEAAYPEHQRVHELVEAQARQMPEAVAL 475
Cdd:PRK12316 2997 ATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVAL 3076
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 476 VAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPP 555
Cdd:PRK12316 3077 AFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQ 3156
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 556 VVLVDPVGRKALADAlgdahrathalVDVTAGSPPWDALPPDNLSSHsreLTSHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK12316 3157 LLLSQSHLRLPLAQG-----------VQVLDLDRGDENYAEANPAIR---TMPENLAYVIYTSGSTGKPKGVGIRHSALS 3222
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1939408627 636 NLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK12316 3223 NHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARV 3265
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-678 |
1.58e-86 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 297.64 E-value: 1.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 7 QEILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGaIDRDAFEMALRRFIEEARSLHFRFVETSTG--PMQFGCDLDAF 84
Cdd:PRK12316 4100 EDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGELgrPLQVVHKQVSL 4178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 85 ELAFIDASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSll 164
Cdd:PRK12316 4179 PFAELDWRGRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSG-- 4256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 165 rqQPVPDSDFGPIEPMTNGDRAYRSSSRyvtdrRYWQDYVAALPATETLAGTAARASGAFRRASAPLPVPFVEQLDTIEA 244
Cdd:PRK12316 4257 --RPPAQPGGRYRDYIAWLQRQDAAASE-----AFWREQLAALDEPTRLAQAIARADLRSANGYGEHVRELDATATARLR 4329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 245 RIAK-----WPLVLTAIVAAYLYRMSNGRITVFDFPVSART---KETRTLPGMFANILPMRLPITPRTTLAELTRQVGAE 316
Cdd:PRK12316 4330 EFARtqrvtLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPaelPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQ 4409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 317 VFAHMKHQQFRVKEIKQMRGAFAGPVFGpriNIVAYDNrweFGGSLATLHALANGLVNDfAVTVTGNPRDPgCTLHVDG- 395
Cdd:PRK12316 4410 NLALREHEHTPLYEIQRWAGQGGEALFD---SLLVFEN---YPVSEALQQGAPGGLRFG-EVTNHEQTNYP-LTLAVGLg 4481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 396 ---------NAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEAAYPEHQRVHELVEAQA 466
Cdd:PRK12316 4482 etlslqfsyDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERA 4561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 467 RQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLA 546
Cdd:PRK12316 4562 RMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLA 4641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 547 HVLDDAKPPVVLVdpvgRKALADALGDAHRATHALVDVTAgspPWDALPPDNlssHSRELTSHHLAYVIYTSGSTGVPKG 626
Cdd:PRK12316 4642 YMMEDSGAALLLT----QSHLLQRLPIPDGLASLALDRDE---DWEGFPAHD---PAVRLHPDNLAYVIYTSGSTGRPKG 4711
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1939408627 627 VMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK12316 4712 VAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV 4763
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-678 |
5.53e-82 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 284.37 E-value: 5.53e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 7 QEILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFEL 86
Cdd:PRK05691 673 GQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFAL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 87 AFIDASG--DADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLL 164
Cdd:PRK05691 753 QRIDLSDlpEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAC 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 165 RQQPVpdsDFGPIePMTNGD-----RAYRSSSRYVTDRRYWQDYVAALPATETLA----GTAARASGAfRRASAPLPVPF 235
Cdd:PRK05691 833 QGQTA---ELAPL-PLGYADygawqRQWLAQGEAARQLAYWKAQLGDEQPVLELAtdhpRSARQAHSA-ARYSLRVDASL 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 236 VEQL-DTIEARIAKWPLVLTAIVAAYLYRMSNGRITVFDFPVSARTK-ETRTLPGMFANILPMRLPITPRTTLAELTRQV 313
Cdd:PRK05691 908 SEALrGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRlETQGLVGFFINTQVLRAQLDGRLPFTALLAQV 987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 314 GAEVFAHMKHQQFrvkEIKQMRGAFA-GPVFGPRINIVAYDNRwefggSLATLHALANGLVND---------FAVTVTGN 383
Cdd:PRK05691 988 RQATLGAQAHQDL---PFEQLVEALPqAREQGLFQVMFNHQQR-----DLSALRRLPGLLAEElpwhsreakFDLQLHSE 1059
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 384 PRDPG-CTLHVDGNAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLlHTWNATEAAyPEHQRVHELV 462
Cdd:PRK05691 1060 EDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQL-AQWGQAPCA-PAQAWLPELL 1137
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 463 EAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSS 542
Cdd:PRK05691 1138 NEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPA 1217
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 543 ARLAHVLDDAKPPVVLvdpvGRKALADALGDAHRAThalvdvtagSPPWDALPPDNLSSHSR--ELTSHHLAYVIYTSGS 620
Cdd:PRK05691 1218 ERLAYMLADSGVELLL----TQSHLLERLPQAEGVS---------AIALDSLHLDSWPSQAPglHLHGDNLAYVIYTSGS 1284
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1939408627 621 TGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK05691 1285 TGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRL 1342
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-678 |
3.45e-81 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 282.05 E-value: 3.45e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 7 QEILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGaIDRDAFEMALRRFIEEARSLHFRFVETS--TGPMQFGCDLDAF 84
Cdd:PRK12467 2644 EDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGelEEPLQVVYKQARL 2722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 85 ELAFIDASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRY--IWYQryHHIVMDGASIPLATRRVARIYTS 162
Cdd:PRK12467 2723 PFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHhlIYTN--HHILMDGWSGSQLLGEVLQRYFG 2800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 163 llrqqpvpdsdfgpiEPMTNGDRAYR-------SSSRYVTDRrYWQDYVAALPATETLAgtaarasgafrRASAPLPVPF 235
Cdd:PRK12467 2801 ---------------QPPPAREGRYRdyiawlqAQDAEASEA-FWKEQLAALEEPTRLA-----------RALYPAPAEA 2853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 236 VE-------QLD-TIEARIAKWP-----LVLTAIVAAYLYRMS--NGRITV-FDFPVSARTKETR---TLPGMFANILPM 296
Cdd:PRK12467 2854 VAghgahylHLDaTQTRQLIEFArrhrvTLNTLVQGAWLLLLQrfTGQDTVcFGATVAGRPAQLRgaeQQLGLFINTLPV 2933
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 297 RLPITPRTTLAELTRQVGAEVFAHMKHQQFRVKEIKQMRGAFAGPVFGpriNIVAYDNR------WEFGGSLATLHALAN 370
Cdd:PRK12467 2934 IASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEALFD---SILVFENYpisealKQGAPSGLRFGAVSS 3010
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 371 GLVNDFAVTVTGNPRDPgCTLHVDGNAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEA 450
Cdd:PRK12467 3011 REQTNYPLTLAVGLGDT-LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAA 3089
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 451 AYPEHQRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAG 530
Cdd:PRK12467 3090 AYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAG 3169
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 531 GAYLPVDPAYSSARLAHVLDDAKPPVVLVdpvgRKALADALGDAHRATHALVDVTAgsppWDALPPDNLSSHsreLTSHH 610
Cdd:PRK12467 3170 GAYVPLDPEYPRERLAYMIEDSGVKLLLT----QAHLLEQLPAPAGDTALTLDRLD----LNGYSENNPSTR---VMGEN 3238
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939408627 611 LAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK12467 3239 LAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCL 3306
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
462-678 |
3.08e-76 |
|
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: 252.65 E-value: 3.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 462 VEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYS 541
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 542 SARLAHVLDDAKPPVVLVDPvgrkaladalGDAHRATHALVDVTAGSPPWDALPPDNlsSHSRELTSHHLAYVIYTSGST 621
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHP----------ALAGELAVELVAVTLLDQPGAAAGADA--EPDPALDADDLAYVIYTSGST 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939408627 622 GVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17651 149 GRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATL 205
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
8-678 |
3.03e-75 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 264.51 E-value: 3.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 8 EILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGaIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELA 87
Cdd:PRK12316 1555 DIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQVIHKQVELP 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 88 FI--DASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLR 165
Cdd:PRK12316 1634 FAelDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPV 1713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 166 QQPVPD-SDFgpIEPMTNGDRAyrsssryvTDRRYWQDYVAALPATETLAGTAARASGAFRRAS--APLPVPFVEQLDTI 242
Cdd:PRK12316 1714 AAPGGRyRDY--IAWLQRQDAA--------ASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDhqQLLDPAQTRALAEF 1783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 243 eARIAKWPLVlTAIVAAY---LYRMSNGRITVFDFPVSARTKEtrtLPG------MFANILPMRLPITPRTTLAELTRQV 313
Cdd:PRK12316 1784 -ARAQKVTLN-TLVQAAWlllLQRYTGQETVAFGATVAGRPAE---LPGieqqigLFINTLPVIAAPRPDQSVADWLQEV 1858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 314 GAEVFAHMKHQQFRVKEIKQMRGAFAGPVFGpriNIVAYDNrweFGGSLATLHALANGLV---------NDFAVTVTGNP 384
Cdd:PRK12316 1859 QALNLALREHEHTPLYDIQRWAGQGGEALFD---SLLVFEN---YPVAEALKQGAPAGLVfgrvsnheqTNYPLTLAVTL 1932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 385 RDPgCTLHVDGNAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEAAYPEHQRVHELVEA 464
Cdd:PRK12316 1933 GET-LSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAE 2011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 465 QARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSAR 544
Cdd:PRK12316 2012 QAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 545 LAHVLDDAKPPVVLVDpvgrKALADALGDAHRATHALVDVTAGSPPWDALPPDNlsshsrELTSHHLAYVIYTSGSTGVP 624
Cdd:PRK12316 2092 LAYMLEDSGAALLLTQ----RHLLERLPLPAGVARLPLDRDAEWADYPDTAPAV------QLAGENLAYVIYTSGSTGLP 2161
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1939408627 625 KGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV 2215
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
470-678 |
2.67e-74 |
|
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: 246.29 E-value: 2.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltsHHLAYVIYTSGSTGVPKGVMV 629
Cdd:cd05930 81 EDSGAKLVLTDP-----------------------------------------------DDLAYVIYTSGSTGKPKGVMV 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1939408627 630 EHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd05930 114 EHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATL 162
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
12-676 |
3.80e-74 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 261.26 E-value: 3.80e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFIDA 91
Cdd:PRK05691 1731 LSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDF 1810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 92 SgdADPFAACWNAMQAESDR----PYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQ 167
Cdd:PRK05691 1811 S--ALPADARQQRLQQLADSeahqPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDR 1888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 168 PvpdsdfGPIEPM-------TNGDRAYRSSSRYVTDRRYWQDY------VAALPATETLAGTAARASGAFRRASAPLPVP 234
Cdd:PRK05691 1889 E------SPLEPLpvqyldySVWQRQWLESGERQRQLDYWKAQlgnehpLLELPADRPRPPVQSHRGELYRFDLSPELAA 1962
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 235 FVEQLDTieARIAKWPLVLTAIVAAYLYRMSNGRITVFDFPVSARTK-ETRTLPGMFANILPMRLPITPRTTLAELTRQV 313
Cdd:PRK05691 1963 RVRAFNA--QRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRpESEGLIGAFLNTQVLRCQLDGQMSVSELLEQV 2040
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 314 GAEVFAHMKHQQFR----VKEIKQMRGAFAGPVFGPRINIvaydNRWEFGGSLATLHALANGLVNDFAVT-------VTG 382
Cdd:PRK05691 2041 RQTVIEGQSHQDLPfdhlVEALQPPRSAAYNPLFQVMCNV----QRWEFQQSRQLAGMTVEYLVNDARATkfdlnleVTD 2116
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 383 NPRDPGCTLHVdgNAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLLHTWNATEAAYPEHQRVHELV 462
Cdd:PRK05691 2117 LDGRLGCCLTY--SRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLF 2194
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 463 EAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSS 542
Cdd:PRK05691 2195 AAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPL 2274
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 543 ARLAHVLDDAKPPVVLvdpvGRKALADALGD--AHRATHALVDVTAGSPPWDALPPDNLSshsrelTSHHLAYVIYTSGS 620
Cdd:PRK05691 2275 ERLHYMIEDSGIGLLL----SDRALFEALGElpAGVARWCLEDDAAALAAYSDAPLPFLS------LPQHQAYLIYTSGS 2344
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939408627 621 TGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGA 676
Cdd:PRK05691 2345 TGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGA 2400
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
483-678 |
4.83e-72 |
|
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: 239.09 E-value: 4.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 483 SYGELNARANRLARYLV-TLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDP 561
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 562 VGRKALADAlgdahRATHALVDVTAGSPPWDALPPDNLSSHSReltSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWH 641
Cdd:TIGR01733 81 ALASRLAGL-----VLPVILLDPLELAALDDAPAPPPPDAPSG---PDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWL 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1939408627 642 IGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:TIGR01733 153 ARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATL 189
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
459-678 |
1.44e-66 |
|
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: 226.77 E-value: 1.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDP 538
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 539 AYSSARLAHVLDDAKPPVVLVDPvgrkALADALGDAHRATHALVDVTA---GSPPWDALPPDNlsshsreltshhLAYVI 615
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTA----DLAARLPAGGDVALLGDEALAappATPPLVPPRPDN------------LAYVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939408627 616 YTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17646 145 YTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARL 207
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
460-678 |
3.96e-65 |
|
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: 222.97 E-value: 3.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 460 ELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPA 539
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 540 YSSARLAHVLDDAKPPVVLVDpvgrKALadALGDAHRATHALVDV-TAGSPPWDALPPDNLSShsreltshHLAYVIYTS 618
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQ----SHL--QPPIAFIGLIDLLDEdTIYHEESENLEPVSKSD--------DLAYVIYTS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 619 GSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17655 147 GSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTL 206
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
460-678 |
1.18e-64 |
|
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: 221.69 E-value: 1.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 460 ELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPA 539
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 540 YSSARLAHVLDDAKPPVVLVDPvgrkaladALGDAHRATHALVDVTAGSPPWDALPPDnlsshsRELTSHHLAYVIYTSG 619
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDR--------SLAGRAGGLEVAVVIDEALDAGPAGNPA------VPVSPDDLAYVMYTSG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939408627 620 STGVPKGVMVEHRQLVNLV--TWHIgrfELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd12117 147 STGRPKGVAVTHRGVVRLVknTNYV---TLGPDDRVLQTSPLAFDASTFEIWGALLNGARL 204
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
470-678 |
2.69e-62 |
|
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: 214.04 E-value: 2.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVDPVgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltshHLAYVIYTSGSTGVPKGVMV 629
Cdd:cd17652 81 ADARPALLLTTPD-----------------------------------------------NLAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1939408627 630 EHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17652 114 THRGLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATL 162
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
458-676 |
3.44e-60 |
|
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: 209.32 E-value: 3.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVD 537
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 538 PAYSSARLAHVLDDAKPPVVLVDpvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsrelTSHHLAYVIYT 617
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTS----------------------------------------------SPSDAAYVIFT 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939408627 618 SGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGA 676
Cdd:cd05918 115 SGSTGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGG 173
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
7-442 |
2.05e-59 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 206.80 E-value: 2.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 7 QEILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTG-PMQFGCDLDAFE 85
Cdd:pfam00668 2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGePVQVILEERPFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 86 LAFIDASGDA--DPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSL 163
Cdd:pfam00668 82 LEIIDISDLSesEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 164 LRQQPVPDSDFGPIEPMTNGDRAYRSSSRYVTDRRYWQDYVAALPATETLAGTAAR-ASGAFR--RASAPLPVPFVEQL- 239
Cdd:pfam00668 162 LKGEPLPLPPKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARpADRSFKgdRLSFTLDEDTEELLr 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 240 DTIEARIAKWPLVLTAIVAAYLYRMSNGRITVFDFPVSARTKET-RTLPGMFANILPMRLPITPRTTLAELTRQVGAEVF 318
Cdd:pfam00668 242 KLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDiERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 319 AHMKHQQFR----VKEIKQMRGAFAGPVFGPRINIVAYD------NRWEFGGSLATLHALANGlVNDFAVTVTGNPRDPG 388
Cdd:pfam00668 322 SAEPHQGYPfgdlVNDLRLPRDLSRHPLFDPMFSFQNYLgqdsqeEEFQLSELDLSVSSVIEE-EAKYDLSLTASERGGG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1939408627 389 CTLHVDGNAELYDGADVQAHRKRLLHFIEAALADPEQPIGQIDLLDADERRLLL 442
Cdd:pfam00668 401 LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
470-678 |
3.72e-57 |
|
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: 200.23 E-value: 3.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltsHHLAYVIYTSGSTGVPKGVMV 629
Cdd:cd17643 81 ADSGPSLLLTDP-----------------------------------------------DDLAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1939408627 630 EHRQLVNLVtWHIGR-FELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17643 114 SHANVLALF-AATQRwFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRL 162
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
458-676 |
6.62e-57 |
|
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: 199.47 E-value: 6.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVD 537
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 538 PAYSSARLAHVLDDAKPPVVLVDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltsHHLAYVIYT 617
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDP-----------------------------------------------DDLAYVIYT 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939408627 618 SGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGA 676
Cdd:cd12115 114 SGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGG 172
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
470-678 |
8.60e-57 |
|
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: 199.82 E-value: 8.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVDPvgrkALADALgdahratHALVDVTAGSPPWDALPPDNLsshSRELTSHHLAYVIYTSGSTGVPKGVMV 629
Cdd:cd12116 81 EDAEPALVLTDD----ALPDRL-------PAGLPVLLLALAAAAAAPAAP---RTPVSPDDLAYVIYTSGSTGRPKGVVV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1939408627 630 EHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd12116 147 SHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARV 195
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
462-678 |
1.26e-56 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 197.92 E-value: 1.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 462 VEAQARQMPEAVAL-VAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAY 540
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 541 SSARLAHVLDDAKPPVVLVDPVGR--KALADALGDAHRATHALVDVTAGSP----PWDALPPDNLSSHSRELTSHHLAYV 614
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKleELLEALGKLEVVKLVLVLDRDPVLKeeplPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939408627 615 IYTSGSTGVPKGVMVEHRQLVNLVTWHIG----RFELHAGSRVPATASLAFDASV-WEIWSALCAGAAL 678
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvrprGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATV 229
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
458-678 |
7.96e-56 |
|
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: 197.27 E-value: 7.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVD 537
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 538 PAYSSARLAHVLDDAKPPVVLVDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltsHHLAYVIYT 617
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQP-----------------------------------------------ENLAYVIYT 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939408627 618 SGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17644 115 SGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATL 175
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
470-678 |
1.92e-49 |
|
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: 179.77 E-value: 1.92e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVDpvgrkaLADALGDAHRATHALVDVTAGSPPwdALPPdnlsshSRELTSHHLAYVIYTSGSTGVPKGVMV 629
Cdd:cd12114 81 ADAGARLVLTD------GPDAQLDVAVFDVLILDLDALAAP--APPP------PVDVAPDDLAYVIFTSGSTGTPKGVMI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1939408627 630 EHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd12114 147 SHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATL 195
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
470-678 |
2.53e-49 |
|
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: 179.59 E-value: 2.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVdpvgRKALADALGDAHRATHalvdvtagsPPWDALPPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMV 629
Cdd:cd17656 82 LDSGVRVVLT----QRHLKSKLSFNKSTIL---------LEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1939408627 630 EHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17656 149 EHKNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTL 197
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
459-678 |
5.91e-49 |
|
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: 177.75 E-value: 5.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDP 538
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 539 AYSSARLAHVLDDAKPPVVLVDPvgrkaladalGDahrathalvdvtagsppwdalppdnlsshsreltshhLAYVIYTS 618
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNP----------DD-------------------------------------LAYVIYTS 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 619 GSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17645 114 GSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAAL 173
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
470-676 |
1.12e-48 |
|
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: 177.18 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVlvdpvgrkaladalgdahrathalvdvtagsppwdalppdnLSSHSReltshHLAYVIYTSGSTGVPKGVMV 629
Cdd:cd17649 81 EDSGAGLL-----------------------------------------LTHHPR-----QLAYVIYTSGSTGTPKGVAV 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1939408627 630 EHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGA 676
Cdd:cd17649 115 SHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGA 161
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-676 |
5.28e-46 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 177.28 E-value: 5.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 7 QEILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPM-QFGCDLDAFE 85
Cdd:PRK05691 3255 EDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMlQVIHKPGRTP 3334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 86 LAFIDASGDADpfAACWNAMQA----ESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYT 161
Cdd:PRK05691 3335 IDYLDWRGLPE--DGQEQRLQAlhkqEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYT 3412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 162 SLLR----QQPVPdsdfgpiePMTNGDRAYRSSSRYVTDRRYWQDYVA------ALPATETLAGTAARASGA------FR 225
Cdd:PRK05691 3413 ALGEgreaQLPVP--------PRYRDYIGWLQRQDLAQARQWWQDNLRgferptPIPSDRPFLREHAGDSGGmvvgdcYT 3484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 226 RASAPLPVPFVE-----QLDTIEARIAKWPLVLTaivaaylyRMSNGRITVFDFPVSARTKE----TRTLpGMFANILPM 296
Cdd:PRK05691 3485 RLDAADGARLRElaqahQLTVNTFAQAAWALVLR--------RYSGDRDVLFGVTVAGRPVSmpqmQRTV-GLFINSIAL 3555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 297 R--LP-ITPRTTLAELTRQVGAEVFAHMKHQQFRVKEIKQMRGAFAG-PVF--------GPrINIVAYDNRWEFGGSLAT 364
Cdd:PRK05691 3556 RvqLPaAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGqPLFdslfvfenAP-VEVSVLDRAQSLNASSDS 3634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 365 LHALANglvndFAVTVTGNPRDpGCTLHVDGNAELYDGADVQ---AHRKRLLhfieAALADP-EQPIGQIDLLDADERRL 440
Cdd:PRK05691 3635 GRTHTN-----FPLTAVCYPGD-DLGLHLSYDQRYFDAPTVErllGEFKRLL----LALVQGfHGDLSELPLLGEQERDF 3704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 441 LLHTWNATEAAYPEHQRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMV 520
Cdd:PRK05691 3705 LLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLL 3784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 521 VSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDPVGR---KALADALGDAHRAtHALVdvtagsppWDALPPD 597
Cdd:PRK05691 3785 GMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACReqaRALLDELGCANRP-RLLV--------WEEVQAG 3855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 598 NLSSHSRELTS--HHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAG 675
Cdd:PRK05691 3856 EVASHNPGIYSgpDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFG 3935
|
.
gi 1939408627 676 A 676
Cdd:PRK05691 3936 A 3936
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
460-678 |
1.62e-45 |
|
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: 167.87 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 460 ELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPA 539
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 540 YSSARLAHVLDDAkppvvlvdpvgRKALAdalgdahrathalvdVTAGSPpwdalppdnlsshsreltsHHLAYVIYTSG 619
Cdd:cd17653 81 LPSARIQAILRTS-----------GATLL---------------LTTDSP-------------------DDLAYIIFTSG 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939408627 620 STGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17653 116 STGIPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTL 174
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
470-678 |
5.21e-42 |
|
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: 158.40 E-value: 5.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltsHHLAYVIYTSGSTGVPKGVMV 629
Cdd:cd17650 81 EDSGAKLLLTQP-----------------------------------------------EDLAYVIYTSGTTGKPKGVMV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1939408627 630 EHRQLVNLV-TWHiGRFELHAGS-RVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17650 114 EHRNVAHAAhAWR-REYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTL 163
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
466-678 |
1.67e-40 |
|
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: 153.94 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 466 ARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARL 545
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 546 AHVLDDAKPPVVLVDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltsHHLAYVIYTSGSTGVPK 625
Cdd:cd05945 81 REILDAAKPALLIADG-----------------------------------------------DDNAYIIFTSGSTGRPK 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1939408627 626 GVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd05945 114 GVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATL 166
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
12-423 |
3.20e-40 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380453 [Multi-domain] Cd Length: 427 Bit Score: 152.95 E-value: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQ-FGCDLDAFELAFID 90
Cdd:cd19066 4 LSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQvVLDKTVRFRIEIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 91 ASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQPVP 170
Cdd:cd19066 84 LRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKPTL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 171 DSDFGPIEPMTNGDRAYRSSSRYVTDRRYWQDYVAALPATETLAG---TAARASGAFRRASAPLPVPFVEQL-DTIEARI 246
Cdd:cd19066 164 PPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKakrPSQVASYEVLTLEFFLRSEETKRLrEVARESG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 247 AKWPLVLTAIVAAYLYRMSNGRITVFDFPVSARTKE--TRTLpGMFANILPMRLPITPRTTLAELTRQVGAEVFAHMKHQ 324
Cdd:cd19066 244 TTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEavEDTI-GLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 325 QF----RVKEIKQMRGAFAGPVFGPRINIVAYDNRWEFGGSLAT---LHALANGLVNDFAVTVTGNPrDPGCTLHVDGNA 397
Cdd:cd19066 323 RVpfieLVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFttpVYTSSEGTVFDLDLEASEDP-DGDLLLRLEYSR 401
|
410 420
....*....|....*....|....*.
gi 1939408627 398 ELYDGADVQAHRKRLLHFIEAALADP 423
Cdd:cd19066 402 GVYDERTIDRFAERYMTALRQLIENP 427
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
458-678 |
4.14e-39 |
|
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: 150.35 E-value: 4.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVD 537
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 538 PAYSSARLAHVLDDAKPPVVLVdpvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltshhlAYVIYT 617
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT----------------------------------------------------ALILYT 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939408627 618 SGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDAS-VWEIWSALCAGAAL 678
Cdd:COG0318 109 SGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATL 170
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
470-678 |
2.95e-33 |
|
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: 133.29 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVG-PDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHV 548
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 549 LDDAKPPVVLVDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltsHHLAYVIYTSGSTGVPKGVM 628
Cdd:cd17648 81 LEDTGARVVITNS-----------------------------------------------TDLAYAIYTSGTTGKPKGVL 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1939408627 629 VEHRQLVNLVTWHIGRFEL--HAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17648 114 VEHGSVVNLRTSLSERYFGrdNGDEAVLFFSNYVFDFFVEQMTLALLNGQKL 165
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
460-678 |
4.74e-30 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 124.62 E-value: 4.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 460 ELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPA 539
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 540 YSSARLAHVLDDAKPPVVLvdpvgrkALADA-LGDAHRATHALVDVTagsppwDALPPDNLSSHSRELTSHHLAYVIYTS 618
Cdd:PRK04813 86 SPAERIEMIIEVAKPSLII-------ATEELpLEILGIPVITLDELK------DIFATGNPYDFDHAVKGDDNYYIIFTS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 619 GSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:PRK04813 153 GTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTL 212
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
458-678 |
4.25e-29 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 121.81 E-value: 4.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVD 537
Cdd:TIGR03098 2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 538 PAYSSARLAHVLDDAKPPVVLVDPVGRKALADALGDAHRATHAL-VDVTAGSPP---------WDALP--PDNLSSHSRe 605
Cdd:TIGR03098 82 PLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPGCHDLRTLIiVGDPAHASEghpgeepasWPKLLalGDADPPHPV- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939408627 606 lTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:TIGR03098 161 -IDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV 232
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
12-234 |
9.11e-29 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 115.14 E-value: 9.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFsqqLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFIDA 91
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 92 SG--DADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQPV 169
Cdd:COG4908 78 SAlpEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939408627 170 PDSDF-GPIEPMTNGDRAYRSSSRYVTDRRYWQDYVAALPATETLAGTAAR-ASGAFRRASAPLPVP 234
Cdd:COG4908 158 PLPELpIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRpAVQTFRGATLSFTLP 224
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
9-423 |
2.47e-28 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 118.07 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 9 ILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTG-PMQFgcdLDA---F 84
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGePLQV---VLKdrkL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 85 ELAFIDASGDADPFAACWNAMQAESDR--PYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTS 162
Cdd:cd19543 78 PWRELDLSHLSEAEQEAELEALAEEDRerGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 163 LLRQQPVPDSDfgpiepmtngDRAYRSSSRYVTDR------RYWQDYVAALPATETL-AGTAARASGAFRR--ASAPLPV 233
Cdd:cd19543 158 LGEGQPPSLPP----------VRPYRDYIAWLQRQdkeaaeAYWREYLAGFEEPTPLpKELPADADGSYEPgeVSFELSA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 234 PFVEQLDTIeARIAKWPL--VLTAIVAAYLYRMSNGRITVFDFPVSARTKEtrtLP------GMFANILPMRLPITPRTT 305
Cdd:cd19543 228 ELTARLQEL-ARQHGVTLntVVQGAWALLLSRYSGRDDVVFGTTVSGRPAE---LPgietmvGLFINTLPVRVRLDPDQT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 306 LAELTRQVGAEVFAHMKHQQFRVKEIkQMRGAFAGPVFGpriNIVAYDN-------RWEFGGSLATLHALANGLVNDFAV 378
Cdd:cd19543 304 VLELLKDLQAQQLELREHEYVPLYEI-QAWSEGKQALFD---HLLVFENypvdeslEEEQDEDGLRITDVSAEEQTNYPL 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1939408627 379 TVTGNPRDpGCTLHVDGNAELYDGADVQAHRKRLLHFIEAALADP 423
Cdd:cd19543 380 TVVAIPGE-ELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
252-678 |
2.06e-26 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 115.93 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 252 VLTAIVAAYLYRMSNGRitvfDFPVSARTKETrtlpgmfANILPMRLPITPRTTLAELTRQVgAEVFAHMKHQQFR---- 327
Cdd:TIGR03443 51 ILLAAFAALVYRLTGDE----DIVLGTSSNKS-------GRPFVLRLNITPELSFLQLYAKV-SEEEKEGASDIGVpfde 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 328 -VKEIKQMRGAFAGPVFgprINIVAYDNrwefggSLATLHALANGLVNDFAVTVTGNPRDPGCTLHVdgNAELYDGADVQ 406
Cdd:TIGR03443 119 lSEHIQAAKKLERTPPL---FRLAFQDA------PDNQQTTYSTGSTTDLTVFLTPSSPELELSIYY--NSLLFSSDRIT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 407 AHRKRLLHFIEAALADPEQPIGQIDLLDADERRLL------LHtWNATEAAypehqrVHELVEAQARQMPEAVALV---- 476
Cdd:TIGR03443 188 IVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLpdptkdLD-WSGFRGA------IHDIFADNAEKHPDRTCVVetps 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 477 -----AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDD 551
Cdd:TIGR03443 261 fldpsSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 552 AKPPVVLV-------DPVGRKALADALGDAHRATH-ALVD---VTAGSPPWDAlppDNLSSHSRELTSHHLAYVI----- 615
Cdd:TIGR03443 341 AKPRALIViekagtlDQLVRDYIDKELELRTEIPAlALQDdgsLVGGSLEGGE---TDVLAPYQALKDTPTGVVVgpdsn 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939408627 616 ----YTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:TIGR03443 418 ptlsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL 484
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
451-635 |
1.24e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 111.43 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 451 AYPEHQRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAG 530
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 531 GAYLPVDPAYSSARLAHVLDDAKPPVVLVDPVGRKALADALGDAHRATHALVdvtAGSPPWDALPPDN------LSSHSR 604
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQLPTVRTVIV---EGDGPAAPLAPEVgeyeelLAAASD 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1939408627 605 ELTSHH-----LAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK06187 158 TFDFPDidendAAAMLYTSGTTGHPKGVVLSHRNLF 193
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
460-634 |
1.82e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 107.68 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 460 ELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPA 539
Cdd:PRK07656 9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 540 YSSARLAHVLDDAKPPVVLVdpvgrkaLADALGDAHRATHAL--------------VDVTAGSPPWDA-LPPDNLSSHSR 604
Cdd:PRK07656 89 YTADEAAYILARGDAKALFV-------LGLFLGVDYSATTRLpalehvviceteedDPHTEKMKTFTDfLAAGDPAERAP 161
|
170 180 190
....*....|....*....|....*....|
gi 1939408627 605 ELTSHHLAYVIYTSGSTGVPKGVMVEHRQL 634
Cdd:PRK07656 162 EVDPDDVADILFTSGTTGRPKGAMLTHRQL 191
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
459-678 |
5.83e-24 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 106.35 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQARQMPEAVALVAEHE-----QLSYGELNARANRLARYLVTLGVGP-DVpVAVCAERSISMVVSLLAVLKAGGA 532
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEdgeerTLTYAELRREVNRFANALRALGVKKgDR-VAIYLPNIPEAVIAMLACARIGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 533 YLPVDPAYSSARLAHVLDDAKPPVVLVD--------PVGRKALAD-ALGDAHRATHALV-------DVTAGSPPWDALpp 596
Cdd:COG0365 91 HSPVFPGFGAEALADRIEDAEAKVLITAdgglrggkVIDLKEKVDeALEELPSLEHVIVvgrtgadVPMEGDLDWDEL-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 597 dnLSSHSRELT-----SHHLAYVIYTSGSTGVPKGVMveHRQ---LVNLVTWHIGRFELHAGSRVPATASLAFDASVW-E 667
Cdd:COG0365 169 --LAAASAEFEpeptdADDPLFILYTSGTTGKPKGVV--HTHggyLVHAATTAKYVLDLKPGDVFWCTADIGWATGHSyI 244
|
250
....*....|.
gi 1939408627 668 IWSALCAGAAL 678
Cdd:COG0365 245 VYGPLLNGATV 255
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
10-320 |
8.68e-24 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 104.74 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 10 LELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIeeAR--SLHFRFVETSTGPMQFGCDLDAFELA 87
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELV--ARheALRTTFVEVDGEPVQVILPPLPLPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 88 FIDASG--DADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLR 165
Cdd:cd19531 80 VVDLSGlpEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 166 QQPVPDSDfgpiEPMTNGD-----RAYRSSSRYVTDRRYWQDYVAALPATETLAGTAAR-ASGAFR--RASAPLPVPFVE 237
Cdd:cd19531 160 GRPSPLPP----LPIQYADyavwqREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRpAVQSFRgaRVRFTLPAELTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 238 QLDTIeARIAKWPL--VLTAIVAAYLYRMSNGRitvfDF----PVSART-KETRTLPGMFANILPMRLPITPRTTLAELT 310
Cdd:cd19531 236 ALRAL-ARREGATLfmTLLAAFQVLLHRYSGQD----DIvvgtPVAGRNrAELEGLIGFFVNTLVLRTDLSGDPTFRELL 310
|
330
....*....|...
gi 1939408627 311 RQVGAEV---FAH 320
Cdd:cd19531 311 ARVRETAleaYAH 323
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
447-653 |
8.94e-24 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 106.34 E-value: 8.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 447 ATEAAYPEHQRVHELVEAQARQMPEAVALVAEH----EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVS 522
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 523 LLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLV-DPVGRKALADALGDAHRATHALVDVTAGSP------PWDAL- 594
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELPSLRHIVVLDPRGLRddprllSLDELl 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939408627 595 -------PPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRV 653
Cdd:COG1022 162 algrevaDPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRT 227
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
462-632 |
2.46e-23 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 104.96 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 462 VEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGP-DVpVAVCAERSISMVVSLLAVLKAGGAYLPVDPAY 540
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKgDV-VALLMENRPEYLAAWLGLAKLGAVVALLNTQQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 541 SSARLAHVLDDAKPPVVLVDPVGRKALADALGDAHRATHALV--DVTAGSPP-WDAL-------PPDNLSSHSReLTSHH 610
Cdd:PRK08279 122 RGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRLWVagGDTLDDPEgYEDLaaaaagaPTTNPASRSG-VTAKD 200
|
170 180
....*....|....*....|..
gi 1939408627 611 LAYVIYTSGSTGVPKGVMVEHR 632
Cdd:PRK08279 201 TAFYIYTSGTTGLPKAAVMSHM 222
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
460-635 |
2.91e-23 |
|
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: 103.41 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 460 ELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPA 539
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 540 YSSARLAHVLDDAKPPVVLVDpvgrkaladalgdahratHALVDVTAGSPPWDALPpdnlsshsrELTSHHLAYVIYTSG 619
Cdd:cd05936 83 YTPRELEHILNDSGAKALIVA------------------VSFTDLLAAGAPLGERV---------ALTPEDVAVLQYTSG 135
|
170
....*....|....*.
gi 1939408627 620 STGVPKGVMVEHRQLV 635
Cdd:cd05936 136 TTGVPKGAMLTHRNLV 151
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
481-662 |
4.72e-23 |
|
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: 103.06 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 481 QLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVD 560
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 561 PVGRKALADALgdAHRATHALVDVTAGSPPWDALPPDNLSSHS----------RELTSHHLAYVIYTSGSTGVPKGVMVE 630
Cdd:cd05911 90 PDGLEKVKEAA--KELGPKDKIIVLDDKPDGVLSIEDLLSPTLgeededlpppLKDGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1939408627 631 HRqlvNLVTWH---IGRFELHAGSRVPATASLAFD 662
Cdd:cd05911 168 HR---NLIANLsqvQTFLYGNDGSNDVILGFLPLY 199
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
461-628 |
5.97e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 103.04 E-value: 5.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 461 LVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAY 540
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 541 SSARLAHVLDDAKPPVVLVDPVGRKALADALGDAHRATHALV--D----------------VTAGSPPWDALP--PDNLs 600
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFAPRVAEVLPRLPKLRTLVVveDgsgndllpgavdyedaLAAGSPERDFGErsPDDL- 166
|
170 180
....*....|....*....|....*...
gi 1939408627 601 shsreltshhlaYVIYTSGSTGVPKGVM 628
Cdd:PRK07798 167 ------------YLLYTGGTTGMPKGVM 182
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
470-634 |
4.13e-22 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 100.34 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQ-LSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHV 548
Cdd:PRK07514 16 RDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 549 LDDAKPPVVLVDPVGR---KALADALGDAH------RATHALVDVTAGSPP-WDALP--PDNlsshsreltshhLAYVIY 616
Cdd:PRK07514 96 IGDAEPALVVCDPANFawlSKIAAAAGAPHvetldaDGTGSLLEAAAAAPDdFETVPrgADD------------LAAILY 163
|
170
....*....|....*...
gi 1939408627 617 TSGSTGVPKGVMVEHRQL 634
Cdd:PRK07514 164 TSGTTGRSKGAMLSHGNL 181
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
466-635 |
1.93e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 98.47 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 466 ARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARL 545
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 546 AHVLDDAKPPVVLVDPVGRKALADALGDAHRATHALVDVTAGSPP---W----DALPPDNLSSHSRELTSHHLAYVIYTS 618
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREApggWldfaDWAEAGSVAEPDVELADDDLAQILYTS 180
|
170
....*....|....*..
gi 1939408627 619 GSTGVPKGVMVEHRQLV 635
Cdd:PRK08316 181 GTESLPKGAMLTHRALI 197
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
466-652 |
7.16e-20 |
|
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: 92.67 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 466 ARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARL 545
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 546 AHVLDDAKPPVVLVDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltshhlAYVIYTSGSTGVPK 625
Cdd:cd17631 85 AYILADSGAKVLFDDL--------------------------------------------------ALLMYTSGTTGRPK 114
|
170 180
....*....|....*....|....*..
gi 1939408627 626 GVMVEHRQLVNLVTWHIGRFELHAGSR 652
Cdd:cd17631 115 GAMLTHRNLLWNAVNALAALDLGPDDV 141
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
466-653 |
8.14e-20 |
|
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: 93.46 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 466 ARQMPEAVALV------AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAErSISMVVSLLAVLKAGG----AYLP 535
Cdd:cd05931 3 AAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVGKPGDRVLLLAPP-GLDFVAAFLGCLYAGAiavpLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 536 VDPAYSsARLAHVLDDAKPPVVLVDPvgrKALADALGDAHRATHALVDVTAGSPPWDALPPDnlSSHSRELTSHHLAYVI 615
Cdd:cd05931 82 TPGRHA-ERLAAILADAGPRVVLTTA---AALAAVRAFAASRPAAGTPRLLVVDLLPDTSAA--DWPPPSPDPDDIAYLQ 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1939408627 616 YTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRV 653
Cdd:cd05931 156 YTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVV 193
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
451-634 |
1.14e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 93.19 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 451 AYPEHqrVHELVEAQARQMPEAVALV---AEH---EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLL 524
Cdd:PRK12582 46 PYPRS--IPHLLAKWAAEAPDRPWLAqrePGHgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 525 AVLKAGGAYLPVDPAYSS-----ARLAHVLDDAKPPVVLVDPVGRKALADALGDAHRATHALVDVTA---GSPPWDAL-- 594
Cdd:PRK12582 124 AAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGAPFARALAALDLLDVTVVHVTGPGegiASIAFADLaa 203
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1939408627 595 -PPDNLSSHSRELTSHH-LAYVIYTSGSTGVPKGVMVEHRQL 634
Cdd:PRK12582 204 tPPTAAVAAAIAAITPDtVAKYLFTSGSTGMPKAVINTQRMM 245
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
450-634 |
6.12e-19 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 91.09 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 450 AAYPehQRVHELVEAQARQMPEAVALV-----AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLL 524
Cdd:PRK08180 35 GDYP--RRLTDRLVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 525 AVLKAGGAYLPVDPAYSS-----ARLAHVLDDAKPPVVLVDPVGRKALA-DALGDAHRATHALVDVTAGSP--PWDAL-- 594
Cdd:PRK08180 113 AAMYAGVPYAPVSPAYSLvsqdfGKLRHVLELLTPGLVFADDGAAFARAlAAVVPADVEVVAVRGAVPGRAatPFAALla 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1939408627 595 --PPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQL 634
Cdd:PRK08180 193 tpPTAAVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRML 234
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
470-644 |
9.71e-19 |
|
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: 89.68 E-value: 9.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVA--EHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAH 547
Cdd:cd05926 1 PDAPALVVpgSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 548 VLDDAKPPVVLVDPVGRKALADAlgdAHRATHALVDVT------AGSPPWDALPP-DNLSSHSRELTSHH---LAYVIYT 617
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRA---ASKLGLAILELAldvgvlIRAPSAESLSNlLADKKNAKSEGVPLpddLALILHT 157
|
170 180
....*....|....*....|....*..
gi 1939408627 618 SGSTGVPKGVMVEHRQLVNLVTwHIGR 644
Cdd:cd05926 158 SGTTGRPKGVPLTHRNLAASAT-NITN 183
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
453-638 |
6.18e-18 |
|
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: 87.29 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 453 PEHQRVHELVEAQARQMPEAVALV--AEHEQLSYGELNARANRLARYLVTLGVGP-DVpVAVCAERSISMVVSLLAVLKA 529
Cdd:cd05904 2 PTDLPLDSVSFLFASAHPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKgDV-VLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 530 GGAYLPVDPAYSSARLAHVLDDAKPPVVLVDPvgrkALADALGDAHRAThalvdVTAGSPPWDALPPDNLSSHSRE---- 605
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA----ELAEKLASLALPV-----VLLDSAEFDSLSFSDLLFEADEaepp 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 1939408627 606 ---LTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLV 638
Cdd:cd05904 152 vvvIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMV 187
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
11-406 |
5.47e-17 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 83.66 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 11 ELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIE--EArslhFR---FVETSTG-PMQFGCDLDAF 84
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQrhEA----LRtcfFTDPEDGePMQGVLASSPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 85 ELAFIDASGDADpFAACWNAMQaesDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLL 164
Cdd:cd19532 79 RLEHVQISDEAE-VEEEFERLK---NHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 165 RQQPVPD-SDFgpiepmTNGDRAYRSSSRYVTDRRYWQDYVAALPatETL-----AGTAAR---ASGAFRRASAPLPVPF 235
Cdd:cd19532 155 LLPPPLQyLDF------AARQRQDYESGALDEDLAYWKSEFSTLP--EPLpllpfAKVKSRpplTRYDTHTAERRLDAAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 236 VEQLDTIeARIAKwplvLT------AIVAAYLYRMSNGR---ITVFDfpvSART--KETRTLpGMFANILPMRLPITPRT 304
Cdd:cd19532 227 AARIKEA-SRKLR----VTpfhfylAALQVLLARLLDVDdicIGIAD---ANRTdeDFMETI-GFFLNLLPLRFRRDPSQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 305 TLAELTRQVGAEVFAHMKHQQ--FRV--KEIKQMRGAFAGPVFGpriniVAYDNRWE------FGGSLATLHALANG-LV 373
Cdd:cd19532 298 TFADVLKETRDKAYAALAHSRvpFDVllDELGVPRSATHSPLFQ-----VFINYRQGvaesrpFGDCELEGEEFEDArTP 372
|
410 420 430
....*....|....*....|....*....|...
gi 1939408627 374 NDFAVTVTGNPRDpGCTLHVDGNAELYDGADVQ 406
Cdd:cd19532 373 YDLSLDIIDNPDG-DCLLTLKVQSSLYSEEDAE 404
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
435-635 |
8.05e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 84.32 E-value: 8.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 435 ADERRLLLHTWNA---TEAAYPEHQR-VHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVA 510
Cdd:PRK06178 8 AELRALQQAAWPAgipREPEYPHGERpLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 511 VCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLV-D---PVGRK-------------ALAD---- 569
Cdd:PRK06178 88 VFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLAlDqlaPVVEQvraetslrhvivtSLADvlpa 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 570 ----ALGDAHRATHALVDVTAGSPPWDALPPDNLSSHSRELTShhLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK06178 168 eptlPLPDSLRAPRLAAAGAIDLLPALRACTAPVPLPPPALDA--LAALNYTGGTTGMPKGCEHTQRDMV 235
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
461-628 |
2.70e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 82.28 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 461 LVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAY 540
Cdd:PRK07788 54 LVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 541 SSARLAHVLDDAKPPVVLVDPVGRKALADALGDAHRAtHALVDVTAGSPPWDALPP--DNLSSHSRE----LTSHHLAYV 614
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRL-RAWGGNPDDDEPSGSTDEtlDDLIAGSSTaplpKPPKPGGIV 212
|
170
....*....|....
gi 1939408627 615 IYTSGSTGVPKGVM 628
Cdd:PRK07788 213 ILTSGTTGTPKGAP 226
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
9-421 |
2.97e-16 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 81.20 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 9 ILELTAAQMEMWFSQQLEPDSPLFDSrgYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAF 88
Cdd:cd19542 1 IYPCTPMQEGMLLSQLRSPGLYFNHF--VFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSLDPPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 89 IDASGDADPFAACwnaMQAESDRPydLLSSKLFSQ-TLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQ 167
Cdd:cd19542 79 EEVETDEDSLDAL---TRDLLDDP--TLFGQPPHRlTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 168 PVPDSDFgpIepmtngdrAYRSSSRYVTDRRYWQDYVA-----ALPaTETLAGTAARASGAFRRASAPLpvpfVEQLDTI 242
Cdd:cd19542 154 APPFSDY--I--------SYLQSQSQEESLQYWRKYLQgaspcAFP-SLSPKRPAERSLSSTRRSLAKL----EAFCASL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 243 EARIAkwpLVLTAIVAAYLYRMSNGRITVFDFPVSART---KETRTLPGMFANILPMRLPITPRTTLAELTRQVGAEVFA 319
Cdd:cd19542 219 GVTLA---SLFQAAWALVLARYTGSRDVVFGYVVSGRDlpvPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 320 HMKHQQFRVKEIKQMRG-AFAGPVFGPRINIVAYDNRWEFGGSLATL-HALANGLVNDFAVTVTGNPRDPGCTLHVDGNA 397
Cdd:cd19542 296 SLPHQHLSLREIQRALGlWPSGTLFNTLVSYQNFEASPESELSGSSVfELSAAEDPTEYPVAVEVEPSGDSLKVSLAYST 375
|
410 420
....*....|....*....|....
gi 1939408627 398 ELYDGADVQahrkRLLHFIEAALA 421
Cdd:cd19542 376 SVLSEEQAE----ELLEQFDDILE 395
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
458-632 |
3.35e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 81.93 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLV-TLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPV 536
Cdd:PRK08314 12 LFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 537 DPAYSSARLAHVLDD--AKPPVVLVDPVGR-KALADALGDAHRATHALVDVTAGSPPwDALPPDNLSSHSRELTSHH--- 610
Cdd:PRK08314 92 NPMNREEELAHYVTDsgARVAIVGSELAPKvAPAVGNLRLRHVIVAQYSDYLPAEPE-IAVPAWLRAEPPLQALAPGgvv 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1939408627 611 ---------------------LAYVIYTSGSTGVPKGVMVEHR 632
Cdd:PRK08314 171 awkealaaglappphtagpddLAVLPYTSGTTGVPKGCMHTHR 213
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
480-678 |
5.11e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 80.80 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLV 559
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 560 DPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltshhlAYVIYTSGSTGVPKGVMVEHRQLVNLVT 639
Cdd:cd05934 82 DP--------------------------------------------------ASILYTSGTTGPPKGVVITHANLTFAGY 111
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1939408627 640 WHIGRFELHAGSRVPATASLaF--DASVWEIWSALCAGAAL 678
Cdd:cd05934 112 YSARRFGLGEDDVYLTVLPL-FhiNAQAVSVLAALSVGATL 151
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
12-325 |
1.72e-15 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 79.23 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFIDA 91
Cdd:cd20483 4 MSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVIDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 92 SGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQP--- 168
Cdd:cd20483 84 SEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRDlat 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 169 VPD-----SDFgpiepmTNGDRAYRSSSRYVTDRRYWQDYVAALPATETL---AGTAARASGAFRRA--SAPLPVPFVEQ 238
Cdd:cd20483 164 VPPppvqyIDF------TLWHNALLQSPLVQPLLDFWKEKLEGIPDASKLlpfAKAERPPVKDYERStvEATLDKELLAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 239 LDTIEARIAKWPL-VLTAIVAAYLYRMSNGR---ITVFDfpvSARTK-ETRTLPGMFANILPMRLPITPRTTLAELTRQV 313
Cdd:cd20483 238 MKRICAQHAVTPFmFLLAAFRAFLYRYTEDEdltIGMVD---GDRPHpDFDDLVGFFVNMLPIRCRMDCDMSFDDLLEST 314
|
330
....*....|..
gi 1939408627 314 GAEVFAHMKHQQ 325
Cdd:cd20483 315 KTTCLEAYEHSA 326
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
12-354 |
1.77e-15 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 79.28 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFV-ETSTGPMQFGCDLDAFELAFID 90
Cdd:cd19547 4 LAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDDLAPPWALLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 91 ASG-DADPFAACWNAMQAEsDRP--YDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQ 167
Cdd:cd19547 84 WSGeDPDRRAELLERLLAD-DRAagLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 168 pvpdsdfgpiEPMTNGDRAYRSSSRYVTDR--------RYWQDYVAALPATETLAGTAARaSGAFRRASAPLPvpfvEQL 239
Cdd:cd19547 163 ----------EPQLSPCRPYRDYVRWIRARtaqseeseRFWREYLRDLTPSPFSTAPADR-EGEFDTVVHEFP----EQL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 240 DTIEARIAKWPLVLTAIVAAYLYRM-----SNGRITVFDFPVSARTKE---TRTLPGMFANILPMRLPITPRTTLAELTR 311
Cdd:cd19547 228 TRLVNEAARGYGVTTNAISQAAWSMllalqTGARDVVHGLTIAGRPPElegSEHMVGIFINTIPLRIRLDPDQTVTGLLE 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1939408627 312 QVGAEVFAHMKHQQFRVKEIKQMRGA---FAGPVFGpriNIVAYDN 354
Cdd:cd19547 308 TIHRDLATTAAHGHVPLAQIKSWASGerlSGGRVFD---NLVAFEN 350
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
471-639 |
2.10e-15 |
|
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: 78.87 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 471 EAVALVAEHEQLSYGELNARANRLARYLVTLG-VGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLvDPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltshhlAYVIYTSGSTGVPKGVMV 629
Cdd:cd05941 81 TDSEPSLVL-DP--------------------------------------------------ALILYTSGTTGRPKGVVL 109
|
170
....*....|
gi 1939408627 630 EHRQLVNLVT 639
Cdd:cd05941 110 THANLAANVR 119
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
482-653 |
2.72e-15 |
|
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: 78.58 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 482 LSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDP 561
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 562 VGRKALADALGDAhrathalvdvtagsppwdalppdnlsshsreltshhLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWH 641
Cdd:cd05903 82 RFRQFDPAAMPDA------------------------------------VALLLFTSGTTGEPKGVMHSHNTLSASIRQY 125
|
170
....*....|..
gi 1939408627 642 IGRFELHAGSRV 653
Cdd:cd05903 126 AERLGLGPGDVF 137
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
489-678 |
4.65e-15 |
|
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: 78.25 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 489 ARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGA----YLPVDPAYSSARLAHVLDDAKPPVVLVDPVGR 564
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 565 KALADALGDAHRAThALVDVtagsppwDALPPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGR 644
Cdd:cd05922 81 DRLRDALPASPDPG-TVLDA-------DGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY 152
|
170 180 190
....*....|....*....|....*....|....
gi 1939408627 645 FELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd05922 153 LGITADDRALTVLPLSYDYGLSVLNTHLLRGATL 186
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
12-324 |
5.90e-15 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 77.42 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTG-PMQFGCDLDAFELAFID 90
Cdd:cd19539 4 LSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGvPRQEILPPGPAPLEVRD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 91 AS-GDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSlLRQQPV 169
Cdd:cd19539 84 LSdPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAA-RRKGPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 170 PDsdfgpiEPMTNG--------DRAYRSSSRYVTDRRYWQDYVAALPATEtLAGTAARASGAFRRA---SAPLPVPFVEQ 238
Cdd:cd19539 163 AP------LPELRQqykeyaawQREALAAPRAAELLDFWRRRLRGAEPTA-LPTDRPRPAGFPYPGadlRFELDAELVAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 239 LDTIEARIAKWP-LVLTAIVAAYLYRMSNGRITVFDFPVSARTK-ETRTLPGMFANILPMRLPITPRTTLAELTRQVGAE 316
Cdd:cd19539 236 LRELAKRARSSLfMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHpRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKA 315
|
....*...
gi 1939408627 317 VFAHMKHQ 324
Cdd:cd19539 316 LVDAQRHQ 323
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
482-678 |
6.09e-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: 77.51 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 482 LSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKppvvlvdp 561
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCH-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 562 VGRKALADALGDAHRATHalvdvtagsppwdalppdNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWH 641
Cdd:cd17654 89 VSYLLQNKELDNAPLSFT------------------PEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHF 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1939408627 642 IGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17654 151 RSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATL 187
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
9-423 |
1.27e-14 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 76.33 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 9 ILELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTG-PMQFGCDLDAFELA 87
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGqPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 88 FIDASGDADPFAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDD-RYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQ 166
Cdd:cd19536 81 ELDLTPLEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDEReRFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 167 QPVPdsdfgpiEPMTNGDRAYRSSSRYVTDR----RYWQDYVAALPATETLAGTAARASGAFRRASAPLPVPfveqLDTI 242
Cdd:cd19536 161 KPLS-------LPPAQPYRDFVAHERASIQQaaseRYWREYLAGATLATLPALSEAVGGGPEQDSELLVSVP----LPVR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 243 EARIAK---WPL--VLTAIVAAYLYRMSNGRITVFDFPVSARTKET---RTLPGMFANILPMRLPItPRTTLAELTRQVG 314
Cdd:cd19536 230 SRSLAKrsgIPLstLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETtgaERLLGLFLNTLPLRVTL-SEETVEDLLKRAQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 315 AEVFAHMKHQQFRVKEIKqmRGAFAGPVFGPRINIVAYD----NRWEFGGSLATLHALANGLVNDFAVTVTGNPRDPGCT 390
Cdd:cd19536 309 EQELESLSHEQVPLADIQ--RCSEGEPLFDSIVNFRHFDldfgLPEWGSDEGMRRGLLFSEFKSNYDVNLSVLPKQDRLE 386
|
410 420 430
....*....|....*....|....*....|...
gi 1939408627 391 LHVDGNAELYDGADVQAHRKRLLHFIEAALADP 423
Cdd:cd19536 387 LKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
465-635 |
1.39e-14 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 77.10 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 465 QARQMPEAVALVAEH-EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSA 543
Cdd:PRK06087 32 TARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 544 RLAHVLDDAKPPVVL--------------------VDPVGRKALADALGDAHrATHALVDVTAGSPPWDALPPdnlsshs 603
Cdd:PRK06087 112 ELVWVLNKCQAKMFFaptlfkqtrpvdlilplqnqLPQLQQIVGVDKLAPAT-SSLSLSQIIADYEPLTTAIT------- 183
|
170 180 190
....*....|....*....|....*....|..
gi 1939408627 604 reLTSHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK06087 184 --THGDELAAVLFTSGTEGLPKGVMLTHNNIL 213
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
432-651 |
2.18e-14 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 76.25 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 432 LLDADERRLllhtwnATEAAYPEHQRVHELVEAQARQMPEAVALVA------EHEQLSYGELNARANRLARYLVTLGVGP 505
Cdd:PRK13295 6 VLLPPRRAA------SIAAGHWHDRTINDDLDACVASCPDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 506 DVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDPVGRK----ALADALGDAHRATHAL 581
Cdd:PRK13295 80 GDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRGfdhaAMARRLRPELPALRHV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 582 VDVTAG----------SPPWDALPPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGS 651
Cdd:PRK13295 160 VVVGGDgadsfealliTPAWEQEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADD 239
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
465-634 |
2.59e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 76.00 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 465 QARQMPEAVALV--AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSS 542
Cdd:PRK09088 4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 543 ARLAHVLDDAKPPVVLVDpvgrkalaDALGDAHRATHALVDVTAGSppwDALPPDNLSSHSRELTShhlaYVIYTSGSTG 622
Cdd:PRK09088 84 SELDALLQDAEPRLLLGD--------DAVAAGRTDVEDLAAFIASA---DALEPADTPSIPPERVS----LILFTSGTSG 148
|
170
....*....|..
gi 1939408627 623 VPKGVMVEHRQL 634
Cdd:PRK09088 149 QPKGVMLSERNL 160
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
477-678 |
5.93e-14 |
|
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: 74.86 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 477 AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPV 556
Cdd:cd17647 16 SKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 557 VLVdpvgrkaLADAlgdahrathalvDVTAGsppwdalpPDNLSSHSreltshhlayviYTSGSTGVPKGVMVEHRQLVN 636
Cdd:cd17647 96 LIV-------IRAA------------GVVVG--------PDSNPTLS------------FTSGSEGIPKGVLGRHFSLAY 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1939408627 637 LVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd17647 137 YFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL 178
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
474-634 |
7.00e-14 |
|
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: 74.71 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 474 ALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAK 553
Cdd:cd05959 22 AFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 554 PPVVLVDPVGRKALADALGDAhRATHALVDVTAGSPPWDALP--PDNLSSHSRELTS-----HHLAYVIYTSGSTGVPKG 626
Cdd:cd05959 102 ARVVVVSGELAPVLAAALTKS-EHTLVVLIVSGGAGPEAGALllAELVAAEAEQLKPaathaDDPAFWLYSSGSTGRPKG 180
|
....*...
gi 1939408627 627 VMVEHRQL 634
Cdd:cd05959 181 VVHLHADI 188
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
461-635 |
1.24e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 74.16 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 461 LVEAqARQMPEAVALVAEH----------EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAG 530
Cdd:PRK09274 12 LPRA-AQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 531 GAYLPVDPAYSSARLAHVLDDAKPPVVLVDP---VGRKALADALGDAHRAthalvdVTAGSPP-WDALPPDNLSSHS--- 603
Cdd:PRK09274 91 AVPVLVDPGMGIKNLKQCLAEAQPDAFIGIPkahLARRLFGWGKPSVRRL------VTVGGRLlWGGTTLATLLRDGaaa 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1939408627 604 ----RELTSHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK09274 165 pfpmADLAPDDMAAILFTSGSTGTPKGVVYTHGMFE 200
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
455-636 |
1.49e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 73.69 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 455 HQRVHELVEAQARQMPEAVALVAEHEQL--SYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGA 532
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 533 YLPVDPAYSSARLAHVLDDakppvvlvdpVGRKALADAlgDAHRATH--------------------------ALVDV-- 584
Cdd:PRK08315 95 LVTINPAYRLSELEYALNQ----------SGCKALIAA--DGFKDSDyvamlyelapelatcepgqlqsarlpELRRVif 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939408627 585 -----TAGSPPWDAL-------PPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVN 636
Cdd:PRK08315 163 lgdekHPGMLNFDELlalgravDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILN 226
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
472-627 |
1.81e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 73.40 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 472 AVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDD 551
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 552 AKPPVVLVDPVGRKALADALGDAHRATHALVDVTAGSPPW-------DALPPDNLSSHSREltshhlAYVIYTSGSTGVP 624
Cdd:PRK08276 82 SGAKVLIVSAALADTAAELAAELPAGVPLLLVVAGPVPGFrsyeealAAQPDTPIADETAG------ADMLYSSGTTGRP 155
|
...
gi 1939408627 625 KGV 627
Cdd:PRK08276 156 KGI 158
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
12-423 |
2.07e-13 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 72.84 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQ--FGCDLDAFELAFI 89
Cdd:cd19540 4 LSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQvvLPAAEARPDLTVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 90 DASGDADPfaacwNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLRQQ-- 167
Cdd:cd19540 84 DVTEDELA-----ARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRap 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 168 -----PVPDSDF---------GPIEPmtngdrayrsSSRYVTDRRYWQDYVAALPATETLAGT---AARASGAFRRASAP 230
Cdd:cd19540 159 dwaplPVQYADYalwqrellgDEDDP----------DSLAARQLAYWRETLAGLPEELELPTDrprPAVASYRGGTVEFT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 231 LPVPFVEQLDTI-EARIAKWPLVLTAIVAAYLYRMSNGRITVFDFPVSARTKETRT-LPGMFANILPMRLPITPRTTLAE 308
Cdd:cd19540 229 IDAELHARLAALaREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDdLVGMFVNTLVLRTDVSGDPTFAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 309 LTRQVGAEVFAHMKHQQF---R-VKEIKQMRGAFAGPVFGPrinIVAYDN----RWEFGGSLATLHALANGLVN-DFAVT 379
Cdd:cd19540 309 LLARVRETDLAAFAHQDVpfeRlVEALNPPRSTARHPLFQV---MLAFQNtaaaTLELPGLTVEPVPVDTGVAKfDLSFT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1939408627 380 VTGNPRDPGCTLHVDG----NAELYDGADVQAHRKRLLHFIEAALADP 423
Cdd:cd19540 386 LTERRDADGAPAGLTGeleyATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
449-625 |
2.77e-13 |
|
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: 72.87 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 449 EAAYPEHQRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAV----CAErsisMVVSLL 524
Cdd:COG1021 18 EAGYWRGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVqlpnVAE----FVIVFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 525 AVLKAGGayLPVD--PAYSSARLAHVLDDAKPPVVLVDPVGRK----ALADALGDAHRA-THALVDVTAGSP-PWDALPP 596
Cdd:COG1021 94 ALFRAGA--IPVFalPAHRRAEISHFAEQSEAVAYIIPDRHRGfdyrALARELQAEVPSlRHVLVVGDAGEFtSLDALLA 171
|
170 180
....*....|....*....|....*....
gi 1939408627 597 DNLSSHSRELTSHHLAYVIYTSGSTGVPK 625
Cdd:COG1021 172 APADLSEPRPDPDDVAFFQLSGGTTGLPK 200
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
459-659 |
3.01e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 72.71 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQARQmPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAV----CAERSISMVVSLLAvlkaGGAYL 534
Cdd:PRK06188 16 HLLVSALKRY-PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlslnRPEVLMAIGAAQLA----GLRRT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 535 PVDPAYSSARLAHVLDDAKPPVVLVDPV-----GRKALADALGDAHRATHA----LVDVTAGSppwDALPPDNLSSHSRE 605
Cdd:PRK06188 91 ALHPLGSLDDHAYVLEDAGISTLIVDPApfverALALLARVPSLKHVLTLGpvpdGVDLLAAA---AKFGPAPLVAAALP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1939408627 606 LTSHHLAyviYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASL 659
Cdd:PRK06188 168 PDIAGLA---YTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPL 218
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
461-633 |
3.12e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 72.85 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 461 LVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAY 540
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 541 SSARLAHVLDDAKPPVVLVDPVGRK-----ALADALGDAHRATHALVDVTAGSP----PWDALPPDNLSSHSRELTS--- 608
Cdd:PRK06164 95 RSHEVAHILGRGRARWLVVWPGFKGidfaaILAAVPPDALPPLRAIAVVDDAADatpaPAPGARVQLFALPDPAPPAaag 174
|
170 180 190
....*....|....*....|....*....|.
gi 1939408627 609 ------HHLAYVIYTSGSTGVPKGVMveHRQ 633
Cdd:PRK06164 175 eraadpDAGALLFTTSGTTSGPKLVL--HRQ 203
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
462-634 |
3.24e-13 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 72.85 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 462 VEAQARQMPEAVALvAEHE------QLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLP 535
Cdd:cd05921 1 LAHWARQAPDRTWL-AEREgnggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 536 VDPAYSS-----ARLAHVLDDAKPPVVLVD--PVGRKALA----------------DALGDAHRATHALVDVTAGSPP-W 591
Cdd:cd05921 80 VSPAYSLmsqdlAKLKHLFELLKPGLVFAQdaAPFARALAaifplgtplvvsrnavAGRGAISFAELAATPPTAAVDAaF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1939408627 592 DALPPDNlsshsreltshhLAYVIYTSGSTGVPKGVMVEHRQL 634
Cdd:cd05921 160 AAVGPDT------------VAKFLFTSGSTGLPKAVINTQRML 190
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
466-633 |
3.30e-13 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 72.21 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 466 ARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARL 545
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 546 AHVLDDAKPPVVLVDpvgrkaladalgDAHRATHALVDVTAGSPPWdalppdnlsSHSRELTSHHLAYVIYTSGSTGVPK 625
Cdd:PRK09029 93 EELLPSLTLDFALVL------------EGENTFSALTSLHLQLVEG---------AHAVAWQPQRLATMTLTSGSTGLPK 151
|
....*...
gi 1939408627 626 GVMVEHRQ 633
Cdd:PRK09029 152 AAVHTAQA 159
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
456-632 |
5.54e-13 |
|
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: 71.77 E-value: 5.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 456 QRVHELVEAQARQMPEAVALV--AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAY 533
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 534 LPVDPAYSSARLAHVL--DDAKPPVVLVDPVGRKALADALGDAHRAThalVDVTAGSPPWDA-LPPDnlsshsRELTSHH 610
Cdd:cd05923 81 ALINPRLKAAELAELIerGEMTAAVIAVDAQVMDAIFQSGVRVLALS---DLVGLGEPESAGpLIED------PPREPEQ 151
|
170 180
....*....|....*....|..
gi 1939408627 611 LAYVIYTSGSTGVPKGVMVEHR 632
Cdd:cd05923 152 PAFVFYTSGTTGLPKGAVIPQR 173
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
462-626 |
8.18e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 71.04 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 462 VEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLV-TLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAY 540
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 541 SSARLAHVLDDAKPPVVLVDPvgrkaladalgdAHRATHALVDVTAG-SPPWDALPPDNLSSHSR---ELTSHHLAYVI- 615
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEK------------TFQNMALSMQKVSYvQRVISITSLKEIEDRKIdnfVEKNESASFIIc 155
|
170
....*....|.
gi 1939408627 616 YTSGSTGVPKG 626
Cdd:PRK06839 156 YTSGTTGKPKG 166
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
478-635 |
8.61e-13 |
|
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: 71.12 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 478 EHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVV 557
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 558 LVDPVGRKALADALGDAHRATHalVDVTAGSPPWDALPPDNLSSHSRELTSH-----------HLAYVI-YTSGSTGVPK 625
Cdd:cd12119 102 FVDRDFLPLLEAIAPRLPTVEH--VVVMTDDAAMPEPAGVGVLAYEELLAAEspeydwpdfdeNTAAAIcYTSGTTGNPK 179
|
170
....*....|
gi 1939408627 626 GVMVEHRQLV 635
Cdd:cd12119 180 GVVYSHRSLV 189
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
10-423 |
9.46e-13 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 70.59 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 10 LELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALR-----------RFIEEARSLHFRFVETSTGPMqfg 78
Cdd:cd19546 5 VPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGdvaarheilrtTFPGDGGDVHQRILDADAARP--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 79 cdldafELAFIDASGDADPfaacwNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVAR 158
Cdd:cd19546 82 ------ELPVVPATEEELP-----ALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 159 IYTSLLRQQ-------PVPDSDFGPIE-PMTNGDRAYRSssrYVTDR-RYWQDYVAALPATETLAGTAARASGAFRRA-S 228
Cdd:cd19546 151 AYGARREGRaperaplPLQFADYALWErELLAGEDDRDS---LIGDQiAYWRDALAGAPDELELPTDRPRPVLPSRRAgA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 229 APLPVP---FVEQLDTIEARIAKWPLVLTAIVAAYLYRMSNGRITVFDFPVSARTKETRTLP--GMFANILPMRLPITPR 303
Cdd:cd19546 228 VPLRLDaevHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEGDLEGmvGPFARPLALRTDLSGD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 304 TTLAEL---TRQVGAEVFAHMKHQQFRVKEIKQMRGAFA-GPVFGPRINIVAYDNR----WEFGG---SLATLHALANGL 372
Cdd:cd19546 308 PTFRELlgrVREAVREARRHQDVPFERLAELLALPPSADrHPVFQVALDVRDDDNDpwdaPELPGlrtSPVPLGTEAMEL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1939408627 373 vnDFAVTVTGNPRDPGCTLHVDGN----AELYDGADVQAHRKRLLHFIEAALADP 423
Cdd:cd19546 388 --DLSLALTERRNDDGDPDGLDGSlryaADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
482-632 |
9.89e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 70.79 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 482 LSYGELNARANRLARYLVTLGvgpdvPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDP 561
Cdd:PRK07787 26 LSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939408627 562 vgrkalADALGDAHRAThalVDVTAGSppWDALP-PDNLSShsreltshhlAYVIYTSGSTGVPKGVMVEHR 632
Cdd:PRK07787 101 ------PDDPAGLPHVP---VRLHARS--WHRYPePDPDAP----------ALIVYTSGTTGPPKGVVLSRR 151
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
478-653 |
1.03e-12 |
|
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: 70.70 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 478 EHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVV 557
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 558 LVDPvgrkaladalgdahrathalvdvtagsppwdalpPDnlsshsreltshHLAYVIYTSGSTGVPKGVMVEHRQLVNL 637
Cdd:cd05907 82 FVED----------------------------------PD------------DLATIIYTSGTTGRPKGVMLSHRNILSN 115
|
170
....*....|....*.
gi 1939408627 638 VTWHIGRFELHAGSRV 653
Cdd:cd05907 116 ALALAERLPATEGDRH 131
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
456-636 |
1.37e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 70.57 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 456 QRVHELVEAQARQMPEAVALVAEHEQL--SYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAY 533
Cdd:PRK12583 18 QTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 534 LPVDPAYSSARLAHVLDDAKPPVVLVDPVGRK--------ALADALGDAHRATHAL--------VDVTAGSPP-----WD 592
Cdd:PRK12583 98 VNINPAYRASELEYALGQSGVRWVICADAFKTsdyhamlqELLPGLAEGQPGALACerlpelrgVVSLAPAPPpgflaWH 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1939408627 593 AL-------PPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVN 636
Cdd:PRK12583 178 ELqargetvSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILN 228
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
445-634 |
3.15e-12 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 69.40 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 445 WNATEAAYPEHQRV-HELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSL 523
Cdd:PRK06155 9 AARAVDPLPPSERTlPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 524 LAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDPVGRKAL--ADALGDAHRATHALVDVTAGSPP--WDA--LPPD 597
Cdd:PRK06155 89 LGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeaADPGDLPLPAVWLLDAPASVSVPagWSTapLPPL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1939408627 598 NLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQL 634
Cdd:PRK06155 169 DAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQF 205
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
470-640 |
3.41e-12 |
|
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: 69.25 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVDpvgRKALADALgdahrathalvdVTAGSPPWDALPPDNlsshsrELTSHHLAyviYTSGSTGVPKGVMV 629
Cdd:cd12118 98 RHSEAKVLFVD---REFEYEDL------------LAEGDPDFEWIPPAD------EWDPIALN---YTSGTTGRPKGVVY 153
|
170
....*....|....*.
gi 1939408627 630 EHR-----QLVNLVTW 640
Cdd:cd12118 154 HHRgaylnALANILEW 169
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
464-627 |
4.94e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.95 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 464 AQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSA 543
Cdd:PRK13391 7 AQTTPDKPAVIMASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 544 RLAHVLDDAKPPVVLVDPVGRKALADALGDAHRATHALV-DVTAGSPPWD-------ALPPDNLSSHSREltshhlAYVI 615
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVARALLKQCPGVRHRLVlDGDGELEGFVgyaeavaGLPATPIADESLG------TDML 160
|
170
....*....|..
gi 1939408627 616 YTSGSTGVPKGV 627
Cdd:PRK13391 161 YSSGTTGRPKGI 172
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
460-636 |
5.08e-12 |
|
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: 68.85 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 460 ELVEAQARQMPEA----VALVAEHEQLSYGELNARANRLARYLVTLGVGP-DVPVAVCAERSISMVVsLLAVLKAGG--A 532
Cdd:cd05906 14 ELLLRAAERGPTKgityIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPgDSVILQFDDNEDFIPA-FWACVLAGFvpA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 533 YLPVDPAYSSAR-----LAHVLDDAKPPVVLVDPVGRKALADALGDAHRathalvdvtagsPPWDALPPDNLSSHSRELT 607
Cdd:cd05906 93 PLTVPPTYDEPNarlrkLRHIWQLLGSPVVLTDAELVAEFAGLETLSGL------------PGIRVLSIEELLDTAADHD 160
|
170 180 190
....*....|....*....|....*....|....
gi 1939408627 608 SHH-----LAYVIYTSGSTGVPKGVMVEHRQLVN 636
Cdd:cd05906 161 LPQsrpddLALLMLTSGSTGFPKAVPLTHRNILA 194
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
480-640 |
6.92e-12 |
|
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: 68.15 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLV 559
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 560 DPvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsreltshhlAYVIYTSGSTGVPKGVMVEHRQLVNLVT 639
Cdd:cd05940 82 DA--------------------------------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGA 111
|
.
gi 1939408627 640 W 640
Cdd:cd05940 112 F 112
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
479-635 |
6.96e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 68.43 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 479 HEQLSYGELNARANRLARYLVTLGVGPDvPVAVCAERSISMVVSLLAVLKAG--GAYLPVdPAYSSA--RLAHVLDDAKP 554
Cdd:PRK05850 33 AETLTWSQLYRRTLNVAEELRRHGSTGD-RAVILAPQGLEYIVAFLGALQAGliAVPLSV-PQGGAHdeRVSAVLRDTSP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 555 PVVL-----VDPVGRKALADALGdahrATHALVDVTA---GSPPWDALPPDNLSShsreltshhLAYVIYTSGSTGVPKG 626
Cdd:PRK05850 111 SVVLttsavVDDVTEYVAPQPGQ----SAPPVIEVDLldlDSPRGSDARPRDLPS---------TAYLQYTSGSTRTPAG 177
|
....*....
gi 1939408627 627 VMVEHRQLV 635
Cdd:PRK05850 178 VMVSHRNVI 186
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
466-643 |
7.06e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 68.14 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 466 ARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARL 545
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 546 AHVLDDAKPPVVLVDPVGRKALADALGDAHRATHALVDVTA-GSPPWDALPPDNLSSHSRELTSHH--LAYVIYTSGSTG 622
Cdd:PRK07470 97 AYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGArAGLDYEALVARHLGARVANAAVDHddPCWFFFTSGTTG 176
|
170 180
....*....|....*....|.
gi 1939408627 623 VPKGVMVEHRQLVNLVTWHIG 643
Cdd:PRK07470 177 RPKAAVLTHGQMAFVITNHLA 197
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
454-635 |
7.44e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 68.51 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 454 EHQRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAY 533
Cdd:PRK07059 21 QYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 534 LPVDPAYSSARLAHVLDD--AKPPVVL------VDPVGRKA-----LADALGDAHRATHALVD-----VTAGSPPWdALP 595
Cdd:PRK07059 101 VNVNPLYTPRELEHQLKDsgAEAIVVLenfattVQQVLAKTavkhvVVASMGDLLGFKGHIVNfvvrrVKKMVPAW-SLP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1939408627 596 -----PDNLSSHSR------ELTSHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK07059 180 ghvrfNDALAEGARqtfkpvKLGPDDVAFLQYTGGTTGVSKGATLLHRNIV 230
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
452-636 |
8.14e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 68.14 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 452 YPEH---------QRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVS 522
Cdd:PRK06710 11 YPEEipstisydiQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 523 LLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVL-VDPVGRKALadALGDAHRATHALVDVTAgsppwDALP-PDNL- 599
Cdd:PRK06710 91 YYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILcLDLVFPRVT--NVQSATKIEHVIVTRIA-----DFLPfPKNLl 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 600 ----------------SSHSREL-----------------TSHHLAYVIYTSGSTGVPKGVMVEHRQLVN 636
Cdd:PRK06710 164 ypfvqkkqsnlvvkvsESETIHLwnsvekevntgvevpcdPENDLALLQYTGGTTGFPKGVMLTHKNLVS 233
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
457-627 |
1.09e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 67.60 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 457 RVHELVEAQARQMPEAVALV--AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYL 534
Cdd:PRK05852 17 RIADLVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 535 PVDPAYSSARLAHVLDDAKPPVVLVDPVGRKALADAlgdAHRATHALVDVTAGSPPWDALPPDNLSS----HSRELTSHH 610
Cdd:PRK05852 97 PLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEP---TTRWWPLTVNVGGDSGPSGGTLSVHLDAatepTPATSTPEG 173
|
170 180
....*....|....*....|.
gi 1939408627 611 L----AYVIYTSGSTGVPKGV 627
Cdd:PRK05852 174 LrpddAMIMFTGGTTGLPKMV 194
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
610-678 |
1.53e-11 |
|
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: 66.15 E-value: 1.53e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939408627 610 HLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWSALCAGAAL 678
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTV 69
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
466-628 |
2.15e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 66.83 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 466 ARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARL 545
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 546 AHVLDDAKPPVVLVD-----PVG---RKALADAlgdahratHALVDVTAGSPPWDALPPDNLSSHSreltshHLAYVIYT 617
Cdd:PRK06145 92 AYILGDAGAKLLLVDeefdaIVAletPKIVIDA--------AAQADSRRLAQGGLEIPPQAAVAPT------DLVRLMYT 157
|
170
....*....|.
gi 1939408627 618 SGSTGVPKGVM 628
Cdd:PRK06145 158 SGTTDRPKGVM 168
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
474-661 |
2.16e-11 |
|
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: 66.33 E-value: 2.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 474 ALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAK 553
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 554 PPVVLVDpvgrkalADAlgdahrathalvdvtagsppwdalppdnlsshsreltshhLAYVIYTSGSTGVPKGVMVEHRQ 633
Cdd:cd05919 83 ARLVVTS-------ADD----------------------------------------IAYLLYSSGTTGPPKGVMHAHRD 115
|
170 180
....*....|....*....|....*....
gi 1939408627 634 LVNLV-TWHIGRFELHAGSRVPATASLAF 661
Cdd:cd05919 116 PLLFAdAMAREALGLTPGDRVFSSAKMFF 144
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
444-635 |
2.59e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 66.56 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 444 TWNATEAAYPEHQRVHeLVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSL 523
Cdd:PRK05605 21 PWTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 524 LAVLKAGGAYLPVDPAYSSARLAHVLDD--AK---------------------PPVVLVD------PVGRKALADALGDA 574
Cdd:PRK05605 100 YAVLRLGAVVVEHNPLYTAHELEHPFEDhgARvaivwdkvaptverlrrttplETIVSVNmiaampLLQRLALRLPIPAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939408627 575 HRATHALVDVTAGSPPWDAL-----PPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK05605 180 RKARAALTGPAPGTVPWETLvdaaiGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLF 245
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
458-631 |
2.71e-11 |
|
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: 66.74 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEHEQ-----LSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGA 532
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 533 YLPVDPAYSSARLAHVLDDAKPPVVLV--------DPVGRKALADALGDA---------HRATHALVDVTAGSPPWDALP 595
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITadgftrrgREVNLKEEADKACAQcptvekvvvVRHLGNDFTPAKGRDLSYDEE 222
|
170 180 190
....*....|....*....|....*....|....*.
gi 1939408627 596 PDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEH 631
Cdd:cd05968 223 KETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVH 258
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
12-423 |
4.60e-11 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 65.36 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFIDA 91
Cdd:cd19538 4 LSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 92 SGDADPFAAcwnAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASI-PLaTRRVARIYTSLLRQQ--- 167
Cdd:cd19538 84 EVDEEELES---EINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLaPL-TRDLSKAYRARCKGEape 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 168 ----PVPDSDFGpIEPMTNGDRAYRSSSRYVTDRRYWQDYVAALPATETLAGTAAR-ASGAFRRASAPLPVP--FVEQLD 240
Cdd:cd19538 160 laplPVQYADYA-LWQQELLGDESDPDSLIARQLAYWKKQLAGLPDEIELPTDYPRpAESSYEGGTLTFEIDseLHQQLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 241 TIeARIAKWPL--VLTAIVAAYLYRMSNGRITVFDFPVSARTKE-TRTLPGMFANILPMRLPITPRTTLAELTRQVGAEV 317
Cdd:cd19538 239 QL-AKDNNVTLfmVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDsLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 318 FAHMKHQQ--FR--VKEIKQMRGAFAGPVFgpRInIVAYDN----RWEFGGSLATLHALANGLVNdFAVTV-------TG 382
Cdd:cd19538 318 LEAYEHQDipFErlVEALNPTRSRSRHPLF--QI-MLALQNtpqpSLDLPGLEAKLELRTVGSAK-FDLTFelreqynDG 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1939408627 383 NPRdpGCTLHVDGNAELYDGADVQAHRKRLLHFIEAALADP 423
Cdd:cd19538 394 TPN--GIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
480-639 |
5.83e-11 |
|
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: 65.16 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLV 559
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 560 dpvgrkaladalgdahrathalvdvtagSPPWDalppdnlsshsreltshhLAYVIYTSGSTGVPKGVMVEHRQLVNLVT 639
Cdd:cd05914 86 ----------------------------SDEDD------------------VALINYTSGTTGNSKGVMLTYRNIVSNVD 119
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
465-628 |
7.10e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 64.98 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 465 QARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSAR 544
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 545 LAHVLDDAKPPVVLVDPVgrkaLADALGDAHRATHA-LVDVTAGSPPWDAlppdnlSSHSRELTShhlayVIYTSGSTGV 623
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDD----FEAKLIPGISVKFAeLMNGPKEEAEIQE------EFDLDEVAT-----IMYTSGTTGK 155
|
....*
gi 1939408627 624 PKGVM 628
Cdd:PRK03640 156 PKGVI 160
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
459-676 |
8.03e-11 |
|
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: 65.29 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQARQMPEAVALVAEHEQ------LSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGA 532
Cdd:cd17634 56 ANALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 533 YLPVDPAYSSARLAHVLDDAKPPVVLVDPVG---------RKALADALG-DAHRATHALVDVTAGSPP---------WDA 593
Cdd:cd17634 136 HSVIFGGFAPEAVAGRIIDSSSRLLITADGGvragrsvplKKNVDDALNpNVTSVEHVIVLKRTGSDIdwqegrdlwWRD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 594 LPPDNLSSHSRE-LTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGR-FELHAGSRVPATASLAF-DASVWEIWS 670
Cdd:cd17634 216 LIAKASPEHQPEaMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvFDYGPGDIYWCTADVGWvTGHSYLLYG 295
|
....*.
gi 1939408627 671 ALCAGA 676
Cdd:cd17634 296 PLACGA 301
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
481-634 |
8.32e-11 |
|
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: 64.42 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 481 QLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVd 560
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939408627 561 pvgrkaladalgdahratHALVDvtagsppwdalppdnlsshsreltshHLAYVIYTSGSTGVPKGVMVEHRQL 634
Cdd:cd05935 80 ------------------GSELD--------------------------DLALIPYTSGTTGLPKGCMHTHFSA 109
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
468-635 |
1.05e-10 |
|
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: 64.47 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 468 QMPEAVALVAEH--EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARL 545
Cdd:cd17642 29 SVPGTIAFTDAHtgVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNEREL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 546 AHVLDDAKPPVVLVDpvgRKALADALGDAHRATH--------ALVD----------VTAGSPP----WDALPPdnlsSHS 603
Cdd:cd17642 109 DHSLNISKPTIVFCS---KKGLQKVLNVQKKLKIiktiiildSKEDykgyqclytfITQNLPPgfneYDFKPP----SFD 181
|
170 180 190
....*....|....*....|....*....|..
gi 1939408627 604 RELTshhLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:cd17642 182 RDEQ---VALIMNSSGSTGLPKGVQLTHKNIV 210
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
474-640 |
2.91e-10 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 63.24 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 474 ALVAEHEQLSYGELNARANRLARYLVTLG-VGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDA 552
Cdd:cd17632 60 RLLPRFETITYAELWERVGAVAAAHDPEQpVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAET 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 553 KPPVVLVD----PVGRKALADALG-------------DAHRA-----------------THALVDVTAGS-PPWDALPPD 597
Cdd:cd17632 140 EPRLLAVSaehlDLAVEAVLEGGTpprlvvfdhrpevDAHRAalesarerlaavgipvtTLTLIAVRGRDlPPAPLFRPE 219
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1939408627 598 NlsshsrelTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTW 640
Cdd:cd17632 220 P--------DDDPLALLIYTSGSTGTPKGAMYTERLVATFWLK 254
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
480-638 |
3.47e-10 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.10 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGG--AYLPVDPAYSS-----ARLAHVLDDA 552
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPLPMGFGGresyiAQLRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 553 KPPVVLVdPVGRKALADALGDAHRATHALVDVTAGSPPWD--ALPPdnlsshsreLTSHHLAYVIYTSGSTGVPKGVMVE 630
Cdd:PRK09192 128 QPAAIIT-PDELLPWVNEATHGNPLLHVLSHAWFKALPEAdvALPR---------PTPDDIAYLQYSSGSTRFPRGVIIT 197
|
....*....
gi 1939408627 631 HRQLV-NLV 638
Cdd:PRK09192 198 HRALMaNLR 206
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
458-676 |
3.79e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 62.72 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEH--EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLP 535
Cdd:PRK05857 16 VLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 536 VD---PAYSSARLAHVLDdakPPVVLVDPVGRKALADALGDAHRATHALVDVTAGSPPWDALPP-DNLSSHSRELTSHHL 611
Cdd:PRK05857 96 ADgnlPIAAIERFCQITD---PAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDaASLAGNADQGSEDPL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939408627 612 AyVIYTSGSTGVPKGVMVEHRQL-----------VNLVTWHIGRFELhagSRVPATASlafdASVWEIWSALCAGA 676
Cdd:PRK05857 173 A-MIFTSGTTGEPKAVLLANRTFfavpdilqkegLNWVTWVVGETTY---SPLPATHI----GGLWWILTCLMHGG 240
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
459-635 |
4.98e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 63.26 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQAR---QMPEAVALV------AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAErSISMVVSLLAVLKA 529
Cdd:PRK05691 9 LTLVQALQRraaQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLLFPS-GPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 530 GGAYLPVDPAYSS-----ARLAHVLDDAKPPVVLVDPVGRKALADAlgDAHRAthalvdvtAGSPPW---DALPPdNLSS 601
Cdd:PRK05691 88 GVIAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRDSLLQM--EELAA--------ANAPELlcvDTLDP-ALAE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1939408627 602 HSRE--LTSHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK05691 157 AWQEpaLQPDDIAFLQYTSGSTALPKGVQVSHGNLV 192
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
470-627 |
5.16e-10 |
|
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: 62.72 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAE------HEQLSYGELNARANRLARYLVTLGVG---------PDVPVAVCAersismvvsLLAVLKAGGAYL 534
Cdd:cd05967 65 GDQIALIYDspvtgtERTYTYAELLDEVSRLAGVLRKLGVVkgdrviiymPMIPEAAIA---------MLACARIGAIHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 535 PVDPAYSSARLAHVLDDAKPPVVLVDPVG---------RKALADALGDA-HRATHALV----DVTAGS--PPWDALPPDN 598
Cdd:cd05967 136 VVFGGFAAKELASRIDDAKPKLIVTASCGiepgkvvpyKPLLDKALELSgHKPHHVLVlnrpQVPADLtkPGRDLDWSEL 215
|
170 180 190
....*....|....*....|....*....|...
gi 1939408627 599 LSSHSRE----LTSHHLAYVIYTSGSTGVPKGV 627
Cdd:cd05967 216 LAKAEPVdcvpVAATDPLYILYTSGTTGKPKGV 248
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
482-634 |
8.56e-10 |
|
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: 61.38 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 482 LSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDP 561
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939408627 562 VGRKALADALgdahrathaLVdvtagsppwdalppdnlsshsreltshhlayVIYTSGSTGVPKGVMVEHRQL 634
Cdd:cd05973 81 ANRHKLDSDP---------FV-------------------------------MMFTSGTTGLPKGVPVPLRAL 113
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
458-628 |
1.04e-09 |
|
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: 61.42 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 458 VHELVEAQARQMPEAVALVAEHE------QLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGG 531
Cdd:cd05966 55 SYNCLDRHLKERGDKVAIIWEGDepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 532 AYLPVDPAYSSARLAHVLDDAKPPVVL-VD-------PVGRKALAD-ALGDAHRATHALV-DVTAGSPPW----DALPPD 597
Cdd:cd05966 135 VHSVVFAGFSAESLADRINDAQCKLVItADggyrggkVIPLKEIVDeALEKCPSVEKVLVvKRTGGEVPMtegrDLWWHD 214
|
170 180 190
....*....|....*....|....*....|....*.
gi 1939408627 598 NLSSHSRE-----LTSHHLAYVIYTSGSTGVPKGVM 628
Cdd:cd05966 215 LMAKQSPEcepewMDSEDPLFILYTSGSTGKPKGVV 250
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
480-653 |
1.51e-09 |
|
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: 60.84 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLV 559
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 560 dpvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsrELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVT 639
Cdd:cd17640 84 ---------------------------------------------ENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIR 118
|
170
....*....|....*
gi 1939408627 640 wHIGRFE-LHAGSRV 653
Cdd:cd17640 119 -SLSDIVpPQPGDRF 132
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
480-628 |
1.61e-09 |
|
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: 60.95 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLv 559
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939408627 560 dpVGRkaLADALGDAHRATHALVDVTAGSPP-------WDALPPDNLSSHSRELT-SHHLAYVIYTSGSTGVPKGVM 628
Cdd:cd05932 84 --VGK--LDDWKAMAPGVPEGLISISLPPPSaancqyqWDDLIAQHPPLEERPTRfPEQLATLIYTSGTTGQPKGVM 156
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
472-661 |
2.67e-09 |
|
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: 59.80 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 472 AVALVAEHEQLSYGELNARANRLARYLV-TLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLD 550
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 551 DAKPPVVLVDpvgrkaladalgdaHRATHalvdvtagsppwdalppdnlsshsreltSHHLAYVIYTSGSTGVPKGVMVE 630
Cdd:cd05958 81 KARITVALCA--------------HALTA----------------------------SDDICILAFTSGTTGAPKATMHF 118
|
170 180 190
....*....|....*....|....*....|..
gi 1939408627 631 HRQLVNLV-TWHIGRFELHAGSRVPATASLAF 661
Cdd:cd05958 119 HRDPLASAdRYAVNVLRLREDDRFVGSPPLAF 150
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
448-625 |
3.16e-09 |
|
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: 59.65 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 448 TEAAYPEHQRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVL 527
Cdd:cd05920 7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 528 KAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDpvGRKALADALGDAHRATHALVDVtagsppwdalppdnlsshsrelt 607
Cdd:cd05920 87 RLGAVPVLALPSHRRSELSAFCAHAEAVAYIVP--DRHAGFDHRALARELAESIPEV----------------------- 141
|
170
....*....|....*...
gi 1939408627 608 shhlAYVIYTSGSTGVPK 625
Cdd:cd05920 142 ----ALFLLSGGTTGTPK 155
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
478-635 |
3.22e-09 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 59.92 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 478 EHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGgayLPVDPAYssarlahvlddakppvv 557
Cdd:cd17639 2 EYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVY----------------- 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939408627 558 lvDPVGRKALADALgdahRATHALVDVTAGSPpwdalppdnlsshsreltsHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:cd17639 62 --ATLGEDALIHSL----NETECSAIFTDGKP-------------------DDLACIMYTSGSTGNPKGVMLTHGNLV 114
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
453-638 |
1.20e-08 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 58.07 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 453 PEHQRVHELVEAQARQMPEAVALV--AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAG 530
Cdd:PLN02246 20 PNHLPLHDYCFERLSEFSDRPCLIdgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 531 GAYLPVDPAYSSARLAHVLDDAKPPVVlvdpVGRKALADALgDAHRATHALVDVTAGSPP------WDALPPDNLSSHSR 604
Cdd:PLN02246 100 AVTTTANPFYTPAEIAKQAKASGAKLI----ITQSCYVDKL-KGLAEDDGVTVVTIDDPPegclhfSELTQADENELPEV 174
|
170 180 190
....*....|....*....|....*....|....
gi 1939408627 605 ELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLV 638
Cdd:PLN02246 175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSV 208
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
480-635 |
1.23e-08 |
|
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: 57.83 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLV 559
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939408627 560 DpvgrkaladalgdahrathalvdvtagsppwdalppdnlsshsrelTSHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:cd05971 85 D----------------------------------------------GSDDPALIIYTSGTTGPPKGALHAHRVLL 114
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
482-627 |
2.03e-08 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 57.40 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 482 LSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDP 561
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 562 VGRKALADAL---------------------GDAHRATHA-LVDVT---AGSPPWDALPPDNLSShsreltshhlayVIY 616
Cdd:PRK12406 92 DLLHGLASALpagvtvlsvptppeiaaayriSPALLTPPAgAIDWEgwlAQQEPYDGPPVPQPQS------------MIY 159
|
170
....*....|.
gi 1939408627 617 TSGSTGVPKGV 627
Cdd:PRK12406 160 TSGTTGHPKGV 170
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
478-652 |
2.07e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 57.43 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 478 EHEQLSYGELNARANRLARYL--VTlgvGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPV-DPAYS--SARLAHVLDDA 552
Cdd:PRK07769 52 VARDLTWSQFGARNRAVGARLqqVT---KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 553 KPPVVLVdpvgrkaladALGDAHRATHALVDVTAGSPPW----DALPPDNLSSHSR-ELTSHHLAYVIYTSGSTGVPKGV 627
Cdd:PRK07769 129 TPSAILT----------TTDSAEGVRKFFRARPAKERPRviavDAVPDEVGATWVPpEANEDTIAYLQYTSGSTRIPAGV 198
|
170 180
....*....|....*....|....*
gi 1939408627 628 MVEHRQLVNLVTWHIGRFELHAGSR 652
Cdd:PRK07769 199 QITHLNLPTNVLQVIDALEGQEGDR 223
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
459-653 |
2.24e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 57.31 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDP 538
Cdd:PRK13383 38 YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 539 AYSSARLAHVLDDAKPPVVLVDpvgrKALADALGDAHRATHALVDVTAGSPPWDALPpdNLSSHSReltshhlaYVIYTS 618
Cdd:PRK13383 118 EFRSDALAAALRAHHISTVVAD----NEFAERIAGADDAVAVIDPATAGAEESGGRP--AVAAPGR--------IVLLTS 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 1939408627 619 GSTGVPKGV--MVEHRQLVNLVTWHIGRFELHAGSRV 653
Cdd:PRK13383 184 GTTGKPKGVprAPQLRSAVGVWVTILDRTRLRTGSRI 220
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
470-644 |
4.16e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 56.49 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVL 549
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 550 DDAKPPVVLVDPVGRKALADALGDAHRATHALVDV--------------------TAGSPPWDALPPDNlsshsrELTSH 609
Cdd:PRK08162 112 RHGEAKVLIVDTEFAEVAREALALLPGPKPLVIDVddpeypggrfigaldyeaflASGDPDFAWTLPAD------EWDAI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1939408627 610 HLAYviyTSGSTGVPKGVMVEHR-----QLVNLVTWHIGR 644
Cdd:PRK08162 186 ALNY---TSGTTGNPKGVVYHHRgaylnALSNILAWGMPK 222
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
470-678 |
1.02e-07 |
|
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: 55.35 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVA----EHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSarl 545
Cdd:cd05943 83 DDPAAIYAaedgERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGV--- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 546 AHVLDDAKP--PVVL--VDPVGRK-----------ALADALGDAhrATHALVDVTAGSPPWDALPPDNLSSHSRELTSH- 609
Cdd:cd05943 160 PGVLDRFGQiePKVLfaVDAYTYNgkrhdvrekvaELVKGLPSL--LAVVVVPYTVAAGQPDLSKIAKALTLEDFLATGa 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 610 ------------HLAYVIYTSGSTGVPKGVMveHRQLVNLVTwHIGRFELHAGSRvPATASLAFDASVWEIW----SALC 673
Cdd:cd05943 238 agelefeplpfdHPLYILYSSGTTGLPKCIV--HGAGGTLLQ-HLKEHILHCDLR-PGDRLFYYTTCGWMMWnwlvSGLA 313
|
....*
gi 1939408627 674 AGAAL 678
Cdd:cd05943 314 VGATI 318
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
481-656 |
1.98e-07 |
|
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: 54.00 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 481 QLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVD 560
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 561 PvgrKALADALgdahrathalvdvtagsppwdalppdnlsshsreltshhlayVIYTSGSTGVPKGVMVEHRQLVNLVTW 640
Cdd:cd05910 82 P---KADEPAA------------------------------------------ILFTSGSTGTPKGVVYRHGTFAAQIDA 116
|
170
....*....|....*.
gi 1939408627 641 HIGRFELHAGSRVPAT 656
Cdd:cd05910 117 LRQLYGIRPGEVDLAT 132
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
478-633 |
2.58e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 53.75 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 478 EHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVV 557
Cdd:PRK04319 70 RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 558 LVDP-VGRKALADALGDAHratHALV---DVTAGSPPWDAlpPDNLSSHSRELTSHHL-----AYVIYTSGSTGVPKGV- 627
Cdd:PRK04319 150 ITTPaLLERKPADDLPSLK---HVLLvgeDVEEGPGTLDF--NALMEQASDEFDIEWTdredgAILHYTSGSTGKPKGVl 224
|
170
....*....|.
gi 1939408627 628 -----MVEHRQ 633
Cdd:PRK04319 225 hvhnaMLQHYQ 235
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
462-635 |
3.26e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 53.63 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 462 VEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYS 541
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 542 SARLAHVLDDAKPPVVLVDPVgRKALADALGDAhRATHALVDVTAGSPPWDALPPDNLSSHSRE------LTSHHLAYVI 615
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAA-LAPVATAVRDI-VPLLSTVVVAGGSSDDSVLGYEDLLAEAGPahapvdIPNDSPALIM 180
|
170 180
....*....|....*....|
gi 1939408627 616 YTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK07786 181 YTSGTTGRPKGAVLTHANLT 200
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
459-627 |
3.29e-07 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 53.41 E-value: 3.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQARQMPEAVALVA------EHEQLSYGELNARANRLARYLVTLGVG---------PDVPVAVCAersismvvsL 523
Cdd:PRK10524 56 HNAVDRHLAKRPEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLGVQrgdrvliymPMIAEAAFA---------M 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 524 LAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVL-VD-------PVGRKALAD-ALGDA-HRATHALVdVTAGSPPWDA 593
Cdd:PRK10524 127 LACARIGAIHSVVFGGFASHSLAARIDDAKPVLIVsADagsrggkVVPYKPLLDeAIALAqHKPRHVLL-VDRGLAPMAR 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1939408627 594 LPP-DNLSSHSRE-----------LTSHHLAYVIYTSGSTGVPKGV 627
Cdd:PRK10524 206 VAGrDVDYATLRAqhlgarvpvewLESNEPSYILYTSGTTGKPKGV 251
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
478-635 |
3.87e-07 |
|
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: 53.06 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 478 EHEQLSYGELNARANRLARYLVT-LGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPV 556
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 557 VLVDPVGRKALADAL---------------GDAHRATHALVDVTAGSPpwDALPPDNLSSHSRELTshhLAYVIYTSGST 621
Cdd:cd05938 82 LVVAPELQEAVEEVLpalradgvsvwylshTSNTEGVISLLDKVDAAS--DEPVPASLRAHVTIKS---PALYIYTSGTT 156
|
170
....*....|....
gi 1939408627 622 GVPKGVMVEHRQLV 635
Cdd:cd05938 157 GLPKAARISHLRVL 170
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
478-638 |
4.22e-07 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 52.99 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 478 EHEQLSYGELNARANRLARYLVTLGV--GPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPP 555
Cdd:cd05927 2 PYEWISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 556 VVLVDPvGRK--ALAD--ALGDAHRATHalvdvtagSPPwdalppdnlsshsrelTSHHLAYVIYTSGSTGVPKGVMVEH 631
Cdd:cd05927 82 IVFCDA-GVKvySLEEfeKLGKKNKVPP--------PPP----------------KPEDLATICYTSGTTGNPKGVMLTH 136
|
....*..
gi 1939408627 632 RQLVNLV 638
Cdd:cd05927 137 GNIVSNV 143
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
477-634 |
4.44e-07 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 53.25 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 477 AEHEQLSYGELNARANRLARYLV-TLGVGPDVPVAV----CAERsismVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDD 551
Cdd:PRK05620 34 AEQEQTTFAAIGARAAALAHALHdELGITGDQRVGSmmynCAEH----LEVLFAVACMGAVFNPLNKQLMNDQIVHIINH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 552 AKPPVVLVDPVGRKALADALGDAHRATHALVdvtAGSPPWD---ALPPDNLSSHSRE--------------LTSHHLAYV 614
Cdd:PRK05620 110 AEDEVIVADPRLAEQLGEILKECPCVRAVVF---IGPSDADsaaAHMPEGIKVYSYEalldgrstvydwpeLDETTAAAI 186
|
170 180
....*....|....*....|
gi 1939408627 615 IYTSGSTGVPKGVMVEHRQL 634
Cdd:PRK05620 187 CYSTGTTGAPKGVVYSHRSL 206
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
478-635 |
6.58e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 52.81 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 478 EHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGgayLPVDPAYSS---ARLAHVLDDAKP 554
Cdd:PLN02387 103 EYEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQN---ITVVTIYASlgeEALCHSLNETEV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 555 PVVLVDPVGRKALADALG-------------DAHRATHALVDVTAgsppWDALPPDNLSSHSRELTSH-------HLAYV 614
Cdd:PLN02387 180 TTVICDSKQLKKLIDISSqletvkrviymddEGVDSDSSLSGSSN----WTVSSFSEVEKLGKENPVDpdlpspnDIAVI 255
|
170 180
....*....|....*....|.
gi 1939408627 615 IYTSGSTGVPKGVMVEHRQLV 635
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIV 276
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
481-638 |
7.32e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 52.44 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 481 QLSYGELNARANRLARYLVTLgVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPV---DPAYSSARLAHVLDDAKPPVV 557
Cdd:PRK12476 68 ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapELPGHAERLDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 558 LVDPVGRKALADALGDAHRATHALVDVTagsppwDALPPDNLSSHSR-ELTSHHLAYVIYTSGSTGVPKGVMVEHRQL-V 635
Cdd:PRK12476 147 LTTTAAAEAVEGFLRNLPRLRRPRVIAI------DAIPDSAGESFVPvELDTDDVSHLQYTSGSTRPPVGVEITHRAVgT 220
|
...
gi 1939408627 636 NLV 638
Cdd:PRK12476 221 NLV 223
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
12-423 |
8.66e-07 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 51.93 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 12 LTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFIDA 91
Cdd:cd20484 4 LSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 92 SG----DADPFaacwnaMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLR-Q 166
Cdd:cd20484 84 SSlkesEIIAY------LREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQgK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 167 QPVPDS------DFGPIEpmtngdRAYRSSSRYVTDRRYW-QDYVAALPATETLAGTAARASGAFRRA--SAPLPVPFVE 237
Cdd:cd20484 158 QPTLASspasyyDFVAWE------QDMLAGAEGEEHRAYWkQQLSGTLPILELPADRPRSSAPSFEGQtyTRRLPSELSN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 238 QLDTI--EARIAKwPLVLTAIVAAYLYRMSNGRITVFDFPVSARTKET-RTLPGMFANILPMRLPITPRTTLAELTRQVG 314
Cdd:cd20484 232 QIKSFarSQSINL-STVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERfDSLIGYFINMLPIRSRILGEETFSDFIRKLQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 315 AEVFAHMKHQQF----RVKEIKQMRGAFAGPVFGpriNIVAYDNRWEFGGslatLHALANGLVNDFAVTVTGNPRDPG-- 388
Cdd:cd20484 311 LTVLDGLDHAAYpfpaMVRDLNIPRSQANSPVFQ---VAFFYQNFLQSTS----LQQFLAEYQDVLSIEFVEGIHQEGey 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1939408627 389 ------------CTLHVDGNAELYDGADVQAHRKRLLHFIEAALADP 423
Cdd:cd20484 384 elvlevyeqedrFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
459-635 |
1.32e-06 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 51.49 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 459 HELVEAQARQMPEAVALV--------AEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAG 530
Cdd:PRK07529 28 YELLSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 531 GAYlPVDPAYSSARLAHVLDDAKP-----------------------------PVVLVD------PVGRKALADALGDAH 575
Cdd:PRK07529 108 IAN-PINPLLEPEQIAELLRAAGAkvlvtlgpfpgtdiwqkvaevlaalpelrTVVEVDlarylpGPKRLAVPLIRRKAH 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 576 RATHALVDVTAGSppwdalpPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PRK07529 187 ARILDFDAELARQ-------PGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEV 239
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
481-628 |
1.32e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 51.82 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 481 QLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVL-- 558
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVItc 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 559 ------VDPVGRKALADALGDAHRATHALVDVtagsppwdALPPDNLSSHSRELT------------------------- 607
Cdd:PLN02654 200 navkrgPKTINLKDIVDAALDESAKNGVSVGI--------CLTYENQLAMKREDTkwqegrdvwwqdvvpnyptkcevew 271
|
170 180
....*....|....*....|...
gi 1939408627 608 --SHHLAYVIYTSGSTGVPKGVM 628
Cdd:PLN02654 272 vdAEDPLFLLYTSGSTGKPKGVL 294
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
483-635 |
1.83e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 51.15 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 483 SYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAK--------P 554
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTLrvigmigaK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 555 PVVLVDPVGrkALADALgDAHRATHALVDVTAGSPPWDalPPdnlsshsrELTSHHLAYVIYTSGSTGVPKGVMVEHRQL 634
Cdd:PRK07768 111 AVVVGEPFL--AAAPVL-EEKGIRVLTVADLLAADPID--PV--------ETGEDDLALMQLTSGSTGSPKAVQITHGNL 177
|
.
gi 1939408627 635 V 635
Cdd:PRK07768 178 Y 178
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
470-678 |
2.51e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 50.56 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 470 PEAVALVAEHE-----QLSYGELNARANRLARYLVTLGVGP-DVPVAV---CAERSISM--VVSLLA------------- 525
Cdd:PRK03584 98 DDRPAIIFRGEdgprrELSWAELRRQVAALAAALRALGVGPgDRVAAYlpnIPETVVAMlaTASLGAiwsscspdfgvqg 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 526 -----------VLKAGGAYL----PVDpaySSARLAHVLDDAKP--PVVLVDPVGRKALADALGDAHRATHALVDVTAGS 588
Cdd:PRK03584 178 vldrfgqiepkVLIAVDGYRyggkAFD---RRAKVAELRAALPSleHVVVVPYLGPAAAAAALPGALLWEDFLAPAEAAE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 589 PPWDALPPDnlsshsreltshHLAYVIYTSGSTGVPK-------GVMVEHRQLVNLvtwHigrFELHAGSRVpatasLAF 661
Cdd:PRK03584 255 LEFEPVPFD------------HPLWILYSSGTTGLPKcivhghgGILLEHLKELGL---H---CDLGPGDRF-----FWY 311
|
250 260
....*....|....*....|.
gi 1939408627 662 DASVWEIW----SALCAGAAL 678
Cdd:PRK03584 312 TTCGWMMWnwlvSGLLVGATL 332
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
447-657 |
2.66e-06 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 50.65 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 447 ATEAAYPEHQRVHELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLV-TLGVGPDVPVAVCAERSISMVVSLLA 525
Cdd:PRK08751 16 AAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 526 VLKAGGAYLPVDPAYSSARLAHVLDDAKPPV-VLVDPVGRK----------------ALADALGDAHRA--THALVDVTA 586
Cdd:PRK08751 96 VLRAGLTVVNVNPLYTPRELKHQLIDSGASVlVVIDNFGTTvqqviadtpvkqvittGLGDMLGFPKAAlvNFVVKYVKK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 587 GSPPW---------DALPPDnlSSHS---RELTSHHLAYVIYTSGSTGVPKGVMVEHRQLV-NLVT---WHIGRFELHAG 650
Cdd:PRK08751 176 LVPEYringairfrEALALG--RKHSmptLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVaNMQQahqWLAGTGKLEEG 253
|
....*..
gi 1939408627 651 SRVPATA 657
Cdd:PRK08751 254 CEVVITA 260
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-169 |
4.10e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.34 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 7 QEILELTAAQMEMWF-SQQLEPdsplfdsrgyvdiRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFE 85
Cdd:PRK12316 3646 QQFFEEPVPERHHWNqSLLLKP-------------REALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGG 3712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 86 LAFIDASGDAdpfAACWNAMQAESDRPYDLLSSKLFSQTLFKLSDDRYIWYQRYHHIVMDGASIPLATRRVARIYTSLLR 165
Cdd:PRK12316 3713 ALLWRAELDD---AEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQ 3789
|
....
gi 1939408627 166 QQPV 169
Cdd:PRK12316 3790 GEAP 3793
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
464-626 |
4.38e-06 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 49.76 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 464 AQARQMPEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSA 543
Cdd:PRK13382 51 IAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 544 RLAHVLDDAKPPVVLVD----PVGRKALADALG---------DAHRATH-ALVDVTAGSPPwdalppdnlsshsrELTSH 609
Cdd:PRK13382 131 ALAEVVTREGVDTVIYDeefsATVDRALADCPQatrivawtdEDHDLTVeVLIAAHAGQRP--------------EPTGR 196
|
170
....*....|....*..
gi 1939408627 610 HLAYVIYTSGSTGVPKG 626
Cdd:PRK13382 197 KGRVILLTSGTTGTPKG 213
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
456-634 |
5.28e-06 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 49.68 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 456 QRVHELVEAQARQMPEAVALVAEH-----EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAG 530
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 531 GAYLPVDPAYSSARLAHVLDDAKPPVVLVD----PVGRKALADalgDAHRATHALVdVTAGSPPWD---------ALPPD 597
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSaqfyPMYRQIQQE---DATPLRHICL-TRVALPADDgvssftqlkAQQPA 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1939408627 598 NLSsHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQL 634
Cdd:PRK08008 163 TLC-YAPPLSTDDTAEILFTSGTTSRPKGVVITHYNL 198
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
453-678 |
1.16e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 48.52 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 453 PEHQRVHELVEAQARQMpeAVALVAEHEQLSYGELNARANRLARYLVTLgVGPDVP--VAVCAERSISMVVSLLAVLKAG 530
Cdd:PRK07867 2 SSAPTVAELLLPLAEDD--DRGLYFEDSFTSWREHIRGSAARAAALRAR-LDPTRPphVGVLLDNTPEFSLLLGAAALSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 531 GAYLPVDPAYSSARLAHVLDDAKPPVVLVDPVGRKALADALGDAhrathALVDVTagSPPWDAL---PPDNLSSHSReLT 607
Cdd:PRK07867 79 IVPVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLDPGV-----RVINVD--SPAWADElaaHRDAEPPFRV-AD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939408627 608 SHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAFDASVWEIWS-ALCAGAAL 678
Cdd:PRK07867 151 PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAvALAAGASI 222
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
460-657 |
5.27e-05 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 46.20 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 460 ELVEAQARQMPEAVALVAEHEQLSYGELNARANRLARYLVT-LGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDP 538
Cdd:PRK08974 27 DMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 539 AYSSARLAHVLDD--AKPPVV----------LVD--PVgRKALADALGDA-HRATHALVD-----VTAGSPPWDaLPP-- 596
Cdd:PRK08974 107 LYTPRELEHQLNDsgAKAIVIvsnfahtlekVVFktPV-KHVILTRMGDQlSTAKGTLVNfvvkyIKRLVPKYH-LPDai 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939408627 597 ---DNLSSHSR------ELTSHHLAYVIYTSGSTGVPKGVMVEHRQLV-NL--VTWHIGRFeLHAGSRVPATA 657
Cdd:PRK08974 185 sfrSALHKGRRmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLeqAKAAYGPL-LHPGKELVVTA 256
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
480-656 |
8.95e-05 |
|
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: 45.81 E-value: 8.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 480 EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLV 559
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 560 DpvGRKALADALGDAHRATHALVDVTAGSPPWDALPP----DNLSSHSRELTSHHL------------AYVIYTSGSTGV 623
Cdd:cd05933 87 E--NQKQLQKILQIQDKLPHLKAIIQYKEPLKEKEPNlyswDEFMELGRSIPDEQLdaiissqkpnqcCTLIYTSGTTGM 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1939408627 624 PKGVMVEHRQLvnlvTW---HIGRfelhAGSRVPAT 656
Cdd:cd05933 165 PKGVMLSHDNI----TWtakAASQ----HMDLRPAT 192
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
465-627 |
1.26e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 45.00 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 465 QARQMPE-AVALVAEH-EQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSS 542
Cdd:PRK13390 6 HAQIAPDrPAVIVAETgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 543 ARLAHVLDDAKPPvVLVDPVGRKALADALGDAHRATHALVDVTAGSPPWDAlppdNLSSHSRELTSHHL-AYVIYTSGST 621
Cdd:PRK13390 86 PEADYIVGDSGAR-VLVASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEA----ALAGAGPRLTEQPCgAVMLYSSGTT 160
|
....*.
gi 1939408627 622 GVPKGV 627
Cdd:PRK13390 161 GFPKGI 166
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
609-635 |
3.56e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.93 E-value: 3.56e-04
10 20
....*....|....*....|....*..
gi 1939408627 609 HHLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLI 247
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
482-635 |
1.11e-03 |
|
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: 41.93 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 482 LSYGELNARANRLARYLVTlGVGPDVPVAVCAERSISMVVSLLAVLKAGgaYLPVDPAYSSA--RLAHVLDDAKPPVVLV 559
Cdd:cd05909 8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAGlrELRACIKLAGIKTVLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 560 DpvgrKALADALGDAHRATHA-------LVDVTAGSPPWD---------ALPPD---NLSSHSREltSHHLAYVIYTSGS 620
Cdd:cd05909 85 S----KQFIEKLKLHHLFDVEydarivyLEDLRAKISKADkckaflagkFPPKWllrIFGVAPVQ--PDDPAVILFTSGS 158
|
170
....*....|....*
gi 1939408627 621 TGVPKGVMVEHRQLV 635
Cdd:cd05909 159 EGLPKGVVLSHKNLL 173
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-308 |
1.53e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 42.25 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 11 ELTAAQMEMWFSQQLEPDSPLFDSRGYVDIRGAIDRDAFEMALRRFIEEARSLHFRFVETSTGPMQFGCDLDAFELAFID 90
Cdd:PRK12316 1100 EVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQR 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 91 ASGDADPFAACWNAMQaesdRPYDLLSSKLFSQTLFKLSDDRyiwyQRY----HHIVMDGASIPLATRRVARIYTSLLRQ 166
Cdd:PRK12316 1180 QAASEEELLALCEEAQ----RSLDLEQGPLLRALLVDMADGS----QRLllviHHLVVDGVSWRILLEDLQRAYADLDAD 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 167 QPVPDSDFgpiepMTNGDRAYRSSSRYVTDRRYWQ----DYVAALPATETLAGTAARASgafRRASAPLPVPFVEQL--D 240
Cdd:PRK12316 1252 LPARTSSY-----QAWARRLHEHAGARAEELDYWQaqleDAPHELPCENPDGALENRHE---RKLELRLDAERTRQLlqE 1323
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939408627 241 TIEA-RIAKWPLVLTAIV---------AAYLYRMS-NGRITVFDfpvsaRTKETRTLpGMFANILPMRLpiTPRTTLAE 308
Cdd:PRK12316 1324 APAAyRTQVNDLLLTALArvtcrwsgqASVLVQLEgHGREDLFE-----DIDLSRTV-GWFTSLFPVRL--TPAADLGE 1394
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
505-678 |
1.54e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 41.55 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 505 PDVP--VAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPPVVLVDPVGRkALADALgDAHRATHALV 582
Cdd:PRK13388 49 PDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDAEHR-PLLDGL-DLPGVRVLDV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 583 DvtagSPPW-DALPPDNLSSHSRELTSHHLAYVIYTSGSTGVPKGVMVEHRQLVNLVTWHIGRFELHAGSRVPATASLAF 661
Cdd:PRK13388 127 D----TPAYaELVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFH 202
|
170
....*....|....*...
gi 1939408627 662 DASVWEIWS-ALCAGAAL 678
Cdd:PRK13388 203 SNAVMAGWApAVASGAAV 220
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
461-545 |
1.88e-03 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 41.51 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 461 LVEAQARQM-PEAVALVAEHEQLSYGELNARANRLARYLVTLGVGPD----VPVAVCAERSIsmvvSLLAVLKAGGAylP 535
Cdd:PRK10946 27 LTDILTRHAaSDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGdtalVQLGNVAEFYI----TFFALLKLGVA--P 100
|
90
....*....|
gi 1939408627 536 VDPAYSSARL 545
Cdd:PRK10946 101 VNALFSHQRS 110
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
477-637 |
2.00e-03 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 41.18 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 477 AEHEQLSYGELNARANRLARYLVT-LGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAYSSARLAHVLDDAKPP 555
Cdd:cd05905 10 KEATTLTWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 556 VVLVDPVGRKALaDALGDAHRATHALVDVTAGSPPWDALP-PDNLSSHSRELTSHH------LAYVIYTSGSTGVPKGVM 628
Cdd:cd05905 90 VALTVEACLKGL-PKKLLKSKTAAEIAKKKGWPKILDFVKiPKSKRSKLKKWGPHPptrdgdTAYIEYSFSSDGSLSGVA 168
|
....*....
gi 1939408627 629 VEHRQLVNL 637
Cdd:cd05905 169 VSHSSLLAH 177
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
616-636 |
2.46e-03 |
|
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: 40.72 E-value: 2.46e-03
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
464-631 |
3.85e-03 |
|
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: 40.44 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 464 AQARQMPEAVALVaeHEQLSYGELNARANRLARYLVTLGVGPDVPVAVCAERSISMVVSLLAVLKAGGAYLPVDPAySSA 543
Cdd:cd05929 2 EARDLDRAQVFHQ--RRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSR-APR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939408627 544 RLAHVLDDAKPPVVLVdpvgrkaLADALGDAHRATHALVDVTAGSPpwdALPPDNLSSHSreltshhlaYVIYTSGSTGV 623
Cdd:cd05929 79 AEACAIIEIKAAALVC-------GLFTGGGALDGLEDYEAAEGGSP---ETPIEDEAAGW---------KMLYSGGTTGR 139
|
....*...
gi 1939408627 624 PKGVMVEH 631
Cdd:cd05929 140 PKGIKRGL 147
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
611-634 |
5.91e-03 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 39.91 E-value: 5.91e-03
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
611-635 |
6.57e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 39.57 E-value: 6.57e-03
10 20
....*....|....*....|....*
gi 1939408627 611 LAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:PTZ00216 266 LALIMYTSGTTGDPKGVMHTHGSLT 290
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
610-635 |
6.96e-03 |
|
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: 39.39 E-value: 6.96e-03
10 20
....*....|....*....|....*.
gi 1939408627 610 HLAYVIYTSGSTGVPKGVMVEHRQLV 635
Cdd:cd05908 107 ELAFIQFSSGSTGDPKGVMLTHENLV 132
|
|
| |
