|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
33-537 |
3.18e-138 |
|
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: 412.69 E-value: 3.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd05930 2 DAVAVVDGDQ----SLTYAELDARANRLARYL--RERGVGPGD----LVAVLLERSLEMVVAILAVLKAGAAYVPLDPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDdsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltSDSIAIVLYTSGGTGIP 192
Cdd:cd05930 72 PAERLAYILEDSGAKLVLTD-------------------------------------------PDDLAYVIYTSGSTGKP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSdSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIER 272
Cdd:cd05930 109 KGVMVEHRGLVNLLLWMQEAYPLT-PGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 273 LVLVPTLLRSILMYLALgpasRPLRRLKLWVCSGETLSKELASEFFKYFgneDGYKLANFYGSTEVMGDVTYYVLEGSDq 352
Cdd:cd05930 188 LHLTPSLLRLLLQELEL----AALPSLRLVLVGGEALPPDLVRRWRELL---PGARLVNLYGPTEATVDATYYRVPPDD- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 353 lDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHatqPDFQRLYRTGDFGT 430
Cdd:cd05930 260 -EEDGRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARgyLNRPELTAERFVPNPF---GPGERMYRTGDLVR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 431 -LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNA 509
Cdd:cd05930 336 wLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAER 415
|
490 500
....*....|....*....|....*....
gi 223890156 510 LTHYMMPQVI-EVESIPLLVNGKVDRQGL 537
Cdd:cd05930 416 LPDYMVPSAFvVLDALPLTPNGKVDRKAL 444
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-605 |
1.29e-111 |
|
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: 366.10 E-value: 1.29e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 7 VAVVTGPRAPVPTAPLTHHLgpLAKS-----DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVI 81
Cdd:COG1020 462 LAEWNATAAPYPADATLHEL--FEAQaartpDAVAVVFGDQ----SLTYAELNARANRLAHHL--RALGVGPGD----LV 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 82 AVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIyDDSADPSMFKESGVPFASFEELAQEAtsHS 161
Cdd:COG1020 530 GVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVL-TQSALAARLPELGVPVLALDALALAA--EP 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 162 ADEPmdaetLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYsDSEEICVWKTALTFVDSVCEIWGPL 241
Cdd:COG1020 607 ATNP-----PVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGL-GPGDRVLQFASLSFDASVWEIFGAL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 242 LHGRALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRsilMYLALGPAsrPLRRLKLWVCSGETLSKELASEFFKYF 321
Cdd:COG1020 681 LSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLR---ALLDAAPE--ALPSLRLVLVGGEALPPELVRRWRARL 755
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 322 GnedGYKLANFYGSTEVMGDVTYYVLEGSDQLDlyPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLaagyvg 401
Cdd:COG1020 756 P---GARLVNLYGPTETTVDSTYYEVTPPDADG--GSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLargyln 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 402 --ggganRFCDNPHAtQPDfQRLYRTGDfgtLVK----GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLC 475
Cdd:COG1020 831 rpeltaeRFVADPFG-FPG-ARLYRTGD---LARwlpdGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVA 905
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 476 YGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIEVESIPLLVNGKVDRQGLLKmyentnnnddaevavD 555
Cdd:COG1020 906 REDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALP---------------A 970
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 223890156 556 IDCSGAGLADLEAARALLETVGAVLGRAARGTLSLRSGFYELGGNSLNSI 605
Cdd:COG1020 971 PAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLL 1020
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
33-537 |
3.31e-102 |
|
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: 321.15 E-value: 3.31e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDeissVQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17646 13 DAPAVVDEG----RTLTYRELDERANRLAHLL--RARGVGPED----RVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSADPSMFKESGVPFASFEELAqeatSHSADEPmdaetLAPLTSDSIAIVLYTSGGTGIP 192
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALA----APPATPP-----LVPPRPDNLAYVIYTSGSTGRP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYsDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIER 272
Cdd:cd17646 154 KGVMVTHAGIVNRLLWMQDEYPL-GPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 273 LVLVPTLLRSILMYLALGpASRPLRRLklwVCSGETLSKELASEFFKYFGNEdgykLANFYGSTEVMGDVTYYVLEGSDQ 352
Cdd:cd17646 233 CHFVPSMLRVFLAEPAAG-SCASLRRV---FCSGEALPPELAARFLALPGAE----LHNLYGPTEAAIDVTHWPVRGPAE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 353 ldlYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQpdfQRLYRTGDFGT 430
Cdd:cd17646 305 ---TPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARgyLGRPALTAERFVPDPFGPG---SRMYRTGDLAR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 431 LVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGART-SAQHIEGELRN 508
Cdd:cd17646 379 WRPdGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGpDTAALRAHLAE 458
|
490 500 510
....*....|....*....|....*....|
gi 223890156 509 ALTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:cd17646 459 RLPEYMVPaAFVVLDALPLTANGKLDRAAL 488
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
49-473 |
3.89e-94 |
|
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: 297.25 E-value: 3.89e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 49 SHAELAARTNVLARAISERaRTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSL 128
Cdd:TIGR01733 1 TYRELDERANRLARHLRAA-GGVGPGD----RVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 129 VIYDDSADPSMfkeSGVPFAsFEELAQEATSHSADEPMDAETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWW 208
Cdd:TIGR01733 76 LLTDSALASRL---AGLVLP-VILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 209 qFRTFPYSDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVN-VLADNQIERLVLVPTLLRsilMYL 287
Cdd:TIGR01733 152 -LARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLA---LLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 288 ALGPASrpLRRLKLWVCSGETLSKELASEFFKYFGNEdgyKLANFYGSTEVMGDVTYYVLEGSDqLDLYPTIPIGRPLDN 367
Cdd:TIGR01733 228 AALPPA--LASLRLVILGGEALTPALVDRWRARGPGA---RLINLYGPTETTVWSTATLVDPDD-APRESPVPIGRPLAN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 368 CAIYLLDEELSPTRDSEPGEVWVAGANLAAGYVGGGGAN--RFCDNPHATqPDFQRLYRTGDfgtLVK----GAVLYAGR 441
Cdd:TIGR01733 302 TRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTaeRFVPDPFAG-GDGARLYRTGD---LVRylpdGNLEFLGR 377
|
410 420 430
....*....|....*....|....*....|..
gi 223890156 442 TDAQVKIRGHRVDLLEVERALAQVPGVDKCVV 473
Cdd:TIGR01733 378 IDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
46-537 |
6.48e-93 |
|
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: 296.95 E-value: 6.48e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 46 VQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAE 125
Cdd:cd17651 19 RRLTYAELDRRANRLAHRL--RARGVGPGD----LVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 126 PSLVIYDDSADPSMfkeSGVPFASFEELAQEATShsadePMDAETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNR 205
Cdd:cd17651 93 PVLVLTHPALAGEL---AVELVAVTLLDQPGAAA-----GADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLANL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 206 LWWQFRTFPYSDSEEICVWKTaLTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRSILm 285
Cdd:cd17651 165 VAWQARASSLGPGARTLQFAG-LGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALA- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 286 yLALGPASRPLRRLKLWVCSGETLSkeLASEFFKYFGNEDGYKLANFYGSTEvMGDVTYYVLEGSDqlDLYP-TIPIGRP 364
Cdd:cd17651 243 -EHGRPLGVRLAALRYLLTGGEQLV--LTEDLREFCAGLPGLRLHNHYGPTE-THVVTALSLPGDP--AAWPaPPPIGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 365 LDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQpdfQRLYRTGDFGT-LVKGAVLYAGR 441
Cdd:cd17651 317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARgyLNRPELTAERFVPDPFVPG---ARMYRTGDLARwLPDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 442 TDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQ-VIE 520
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSaFVL 473
|
490
....*....|....*..
gi 223890156 521 VESIPLLVNGKVDRQGL 537
Cdd:cd17651 474 LDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
33-537 |
3.97e-91 |
|
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: 291.50 E-value: 3.97e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd12116 2 DATAVRDDDR----SLSYAELDERANRLAARL--RARGVGPGD----RVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSADPSMFKESGVPfasfeELAQEATSHSADEPmdaetLAPLTSDSIAIVLYTSGGTGIP 192
Cdd:cd12116 72 PADRLRYILEDAEPALVLTDDALPDRLPAGLPVL-----LLALAAAAAAPAAP-----RTPVSPDDLAYVIYTSGSTGRP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSDSEEIcVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIER 272
Cdd:cd12116 142 KGVVVSHRNLVNFLHSMRERLGLGPGDRL-LAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 273 LVLVPTLLRsilMYLALGPasRPLRRLKLwVCSGETLSKELASEFFkyfgnEDGYKLANFYGSTE-----VMGDVTyyvl 347
Cdd:cd12116 221 MQATPATWR---MLLDAGW--QGRAGLTA-LCGGEALPPDLAARLL-----SRVGSLWNLYGPTEttiwsTAARVT---- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 348 egsdqlDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHAtqPDFQRLYRT 425
Cdd:cd12116 286 ------AAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQgyLGRPALTAERFVPDPFA--GPGSRLYRT 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 426 GDfgtLVK----GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGlDRGNPEILGFVTTKPGARTSAQH 501
Cdd:cd12116 358 GD---LVRrradGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRE-DGGDRRLVAYVVLKAGAAPDAAA 433
|
490 500 510
....*....|....*....|....*....|....*..
gi 223890156 502 IEGELRNALTHYMMPQ-VIEVESIPLLVNGKVDRQGL 537
Cdd:cd12116 434 LRAHLRATLPAYMVPSaFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
33-537 |
8.44e-86 |
|
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: 276.88 E-value: 8.44e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17643 2 EAVAVVDEDR----RLTYGELDARANRLARTL--RAEGVGP----GDRVALALPRSAELIVALLAILKAGGAYVPIDPAY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIyddsadpsmfkesgvpfasfeelaqeatshsaDEPmdaetlapltsDSIAIVLYTSGGTGIP 192
Cdd:cd17643 72 PVERIAFILADSGPSLLL--------------------------------TDP-----------DDLAYVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSDSEeicVWK--TALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQI 270
Cdd:cd17643 109 KGVVVSHANVLALFAATQRWFGFNEDD---VWTlfHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 271 ERLVLVPTLLRSiLMYLALGPASRPLRrLKLWVCSGETLSKELASEFFKYFGNeDGYKLANFYGSTEVMGDVTYYVLEGS 350
Cdd:cd17643 186 TVLNQTPSAFYQ-LVEAADRDGRDPLA-LRYVIFGGEALEAAMLRPWAGRFGL-DRPQLVNMYGITETTVHVTFRPLDAA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 351 DqLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGYVGGGGAN--RFCDNPHATQPDfqRLYRTGDF 428
Cdd:cd17643 263 D-LPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTaeRFVANPFGGPGS--RMYRTGDL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 429 GTLV-KGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELR 507
Cdd:cd17643 340 ARRLpDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLK 419
|
490 500 510
....*....|....*....|....*....|.
gi 223890156 508 NALTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:cd17643 420 ELLPDYMVPaRYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
32-537 |
1.75e-82 |
|
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: 269.58 E-value: 1.75e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 32 SDRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPS 111
Cdd:cd17655 11 PDHTAVVFEDQ----TLTYRELNERANQLARTL--REKGVGP----DTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 112 FPQGRITHILKDAEPSLVIYDDSADPsmfkesGVPFASFEELAQEATSHSADepmdAETLAPLT-SDSIAIVLYTSGGTG 190
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQP------PIAFIGLIDLLDEDTIYHEE----SENLEPVSkSDDLAYVIYTSGSTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 191 IPKGVRLSYSAICNRLWWQFRTFPYSDSEEICVWkTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQI 270
Cdd:cd17655 151 KPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALF-ASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 271 ERLVLVPTLLrSILMYLALGPASrPLRRLklwVCSGETLSKELASEFFKYFGneDGYKLANFYGSTEVMGDVTYYVLEGS 350
Cdd:cd17655 230 TIIDLTPAHL-KLLDAADDSEGL-SLKHL---IVGGEALSTELAKKIIELFG--TNPTITNAYGPTETTVDASIYQYEPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 351 DqlDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGYVggggaNR-------FCDNPHATQpdfQRLY 423
Cdd:cd17655 303 T--DQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYL-----NRpeltaekFVDDPFVPG---ERMY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 424 RTGDFGT-LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAqhI 502
Cdd:cd17655 373 RTGDLARwLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQ--L 450
|
490 500 510
....*....|....*....|....*....|....*.
gi 223890156 503 EGELRNALTHYMMPQ-VIEVESIPLLVNGKVDRQGL 537
Cdd:cd17655 451 REFLARELPDYMIPSyFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
33-537 |
1.89e-82 |
|
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: 269.07 E-value: 1.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd12117 12 DAVAVVYGDR----SLTYAELNERANRLARRL--RAAGVGPGD----VVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIyddsADPSMFKESGVPfASFEELAQEATSHSADEPmdaetLAPLTSDSIAIVLYTSGGTGIP 192
Cdd:cd12117 82 PAERLAFMLADAGAKVLL----TDRSLAGRAGGL-EVAVVIDEALDAGPAGNP-----AVPVSPDDLAYVMYTSGSTGRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAI----CNRLWWQFrtfpysdSEEICVWKTA-LTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLAD 267
Cdd:cd12117 152 KGVAVTHRGVvrlvKNTNYVTL-------GPDDRVLQTSpLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 268 NQIERLVLVPTLLRsilMYLALGPAS-RPLRRLklwVCSGETLSKELASEFFKYFGnedGYKLANFYGSTEVMGDVTYYV 346
Cdd:cd12117 225 EGVTVLWLTAALFN---QLADEDPECfAGLREL---LTGGEVVSPPHVRRVLAACP---GLRLVNGYGPTENTTFTTSHV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 347 LEGSDQLDlyPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHatqPDFQRLYR 424
Cdd:cd12117 296 VTELDEVA--GSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALgyLNRPALTAERFVADPF---GPGERLYR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 425 TGDfgtLVK----GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTtkPGARTSAQ 500
Cdd:cd12117 371 TGD---LARwlpdGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVV--AEGALDAA 445
|
490 500 510
....*....|....*....|....*....|....*...
gi 223890156 501 HIEGELRNALTHYMMPQV-IEVESIPLLVNGKVDRQGL 537
Cdd:cd12117 446 ELRAFLRERLPAYMVPAAfVVLDELPLTANGKVDRRAL 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
18-615 |
1.19e-81 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 283.77 E-value: 1.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 18 PTAPLTHHL---GPLAKSDRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMA 94
Cdd:PRK12316 508 PLQRGVHRLfeeQVERTPEAPALAFGEE----TLDYAELNRRANRLAHAL--IERGVGP----DVLVGVAMERSIEMVVA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 95 LLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPSMFKESGVPFASFEELAQEATSHSADEPMDAetlapL 174
Cdd:PRK12316 578 LLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTE-----L 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 175 TSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEIcVWKTALTFVDSVCEIWGPLLHGRALLILSRET 254
Cdd:PRK12316 653 NPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTV-LQKTPFSFDVSVWEFFWPLMSGARLVVAAPGD 731
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 255 TRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALgPASRPLRRLklwVCSGETLSKELASEFFKYFGNEdgyKLANFYG 334
Cdd:PRK12316 732 HRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDV-ASCTSLRRI---VCSGEALPADAQEQVFAKLPQA---GLYNLYG 804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 335 STEVMGDVTYY--VLEGSDqldlypTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCD 410
Cdd:PRK12316 805 PTEAAIDVTHWtcVEEGGD------SVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARgyHGRPGLTAERFVP 878
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 411 NPHAtqpDFQRLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCygldRGNPEILGFV 489
Cdd:PRK12316 879 SPFV---AGERMYRTGDLARYrADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLA----VDGKQLVGYV 951
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 490 TTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLlkmyentnnnddaeVAVDIDCSGAGLADLEA 568
Cdd:PRK12316 952 VLESEGGDWREALKAHLAASLPEYMVPaQWLALERLPLTPNGKLDRKAL--------------PAPEASVAQQGYVAPRN 1017
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 223890156 569 A--RALLETVGAVLGRAARGtlsLRSGFYELGGNSLNSIYTITKLRDRG 615
Cdd:PRK12316 1018 AleRTLAAIWQDVLGVERVG---LDDNFFELGGDSIVSIQVVSRARQAG 1063
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
24-614 |
4.19e-81 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 282.05 E-value: 4.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 24 HHL---GPLAKSDRTALIYKDEIssvqVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWK 100
Cdd:PRK12467 515 HQLieaQARQHPERPALVFGEQV----LSYAELNRQANRLAHVL--IAAGVGP----DVLVGIAVERSIEMVVGLLAVLK 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 101 AGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPSMFKESGVPFASFEELAQEATSHSADEPMDAetLAPltsDSIA 180
Cdd:PRK12467 585 AGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVA--LDP---DNLA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 181 IVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSdSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQK 260
Cdd:PRK12467 660 YVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLA-ADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEA 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 261 LVNVLADNQIERLVLVPTLLRSILMylalGPASRPLRRLKLWVCSGETLSKELASEFFKYfgnEDGYKLANFYGSTEVMG 340
Cdd:PRK12467 739 FAALMADQGVTVLKIVPSHLQALLQ----ASRVALPRPQRALVCGGEALQVDLLARVRAL---GPGARLINHYGPTETTV 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 341 DVTYYVLEGSDQLdlYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHAtqPD 418
Cdd:PRK12467 812 GVSTYELSDEERD--FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARgyHRRPALTAERFVPDPFG--AD 887
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 419 FQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNpEILGFVTTKPGART 497
Cdd:PRK12467 888 GGRLYRTGDLARYRAdGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGL-QLVAYLVPAAVADG 966
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 498 SAQHIEGE-----LRNALTHYMMPQ-VIEVESIPLLVNGKVDRQGLLKmyENTNNNDDAEVAVDidcsgaglADLEaaRA 571
Cdd:PRK12467 967 AEHQATRDelkaqLRQVLPDYMVPAhLLLLDSLPLTPNGKLDRKALPK--PDASAVQATFVAPQ--------TELE--KR 1034
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 223890156 572 LLETVGAVLGRAARGtlsLRSGFYELGGNSLNSIYTITKLRDR 614
Cdd:PRK12467 1035 LAAIWADVLKVERVG---LTDNFFELGGHSLLATQVISRVRQR 1074
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
47-658 |
1.08e-78 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 273.84 E-value: 1.08e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 47 QVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEP 126
Cdd:PRK10252 483 QFSYREMREQVVALANLL--RERGVKPGD----SVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARP 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 127 SLVIYDDSADPSMFKESGVPFASFEelaqeatshSADEPMDAETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRL 206
Cdd:PRK10252 557 SLLITTADQLPRFADVPDLTSLCYN---------APLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRL 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 207 WWQFRTFPYSdSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRSILMY 286
Cdd:PRK10252 628 LWMQNHYPLT-ADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVAS 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 287 LALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGNEdgykLANFYGSTEVMGDVTYYVLEGSDQLDLYPT-IPIGRPL 365
Cdd:PRK10252 707 LTPEGARQSCASLRQVFCSGEALPADLCREWQQLTGAP----LHNLYGPTEAAVDVSWYPAFGEELAAVRGSsVPIGYPV 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 366 DNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHAtqpDFQRLYRTGDFGT-LVKGAVLYAGRT 442
Cdd:PRK10252 783 WNTGLRILDARMRPVPPGVAGDLYLTGIQLAQgyLGRPDLTASRFIADPFA---PGERMYRTGDVARwLDDGAVEYLGRS 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 443 DAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPE------ILGFVTTKPGARTSAQHIEGELRNALTHYMMP 516
Cdd:PRK10252 860 DDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATggdarqLVGYLVSQSGLPLDTSALQAQLRERLPPHMVP 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 517 QV-IEVESIPLLVNGKVDRQGLLKmyentnnnddAEVAVDIdcsgAGLadleAARALLETVGAVLGRAARG--TLSLRSG 593
Cdd:PRK10252 940 VVlLQLDQLPLSANGKLDRKALPL----------PELKAQV----PGR----APKTGTETIIAAAFSSLLGcdVVDADAD 1001
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223890156 594 FYELGGNSLNSIYTITKL-RDRGYYVEISDFLGASTLGEILSKMSTDPNggADSKEATFIAVPMRD 658
Cdd:PRK10252 1002 FFALGGHSLLAMKLAAQLsRQFARQVTPGQVMVASTVAKLATLLDAEED--ESRRLGFGTILPLRE 1065
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
33-537 |
2.34e-77 |
|
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: 254.48 E-value: 2.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17652 2 DAPAVVFGDE----TLTYAELNARANRLARLL--AARGVGPER----LVALALPRSAELVVAILAVLKAGAAYLPLDPAY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIyddsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapLTSDSIAIVLYTSGGTGIP 192
Cdd:cd17652 72 PAERIAYMLADARPALLL-------------------------------------------TTPDNLAYVIYTSGSTGRP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPY-SDSeeiCVWKTA-LTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQI 270
Cdd:cd17652 109 KGVVVTHRGLANLAAAQIAAFDVgPGS---RVLQFAsPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 271 ERLVLVPTLLRsilmylALGPASRP-LRRLklwVCSGETLSKELASEFfkyfgnEDGYKLANFYGSTEVMGDVTYY-VLE 348
Cdd:cd17652 186 THVTLPPAALA------ALPPDDLPdLRTL---VVAGEACPAELVDRW------APGRRMINAYGPTETTVCATMAgPLP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 349 GSDQLdlyptiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHAtqPDFQRLYRTG 426
Cdd:cd17652 251 GGGVP------PIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARgyLNRPGLTAERFVADPFG--APGSRMYRTG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 427 DFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGE 505
Cdd:cd17652 323 DLARWRAdGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAH 402
|
490 500 510
....*....|....*....|....*....|...
gi 223890156 506 LRNALTHYMMPQVIEV-ESIPLLVNGKVDRQGL 537
Cdd:cd17652 403 LAERLPGYMVPAAFVVlDALPLTPNGKLDRRAL 435
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
33-537 |
3.54e-75 |
|
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: 249.09 E-value: 3.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARtnvlARAISERARTVGPNRDSDyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd05945 6 DRPAVVEGGR----TLTYRELKER----ADALAAALASLGLDAGDP--VVVYGHKSPDAIAAFLAALKAGHAYVPLDASS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltsDSIAIVLYTSGGTGIP 192
Cdd:cd05945 76 PAERIREILDAAKPALLIADG-------------------------------------------DDNAYIIFTSGSTGRP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSDSeeiCVW--KTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQI 270
Cdd:cd05945 113 KGVQISHDNLVSFTNWMLSDFPLGPG---DVFlnQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGI 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 271 ERLVLVPTLLRSILMYLALGPASRPlrRLKLWVCSGETLSKELASEFFKYFgneDGYKLANFYGSTEVMGDVTYYVLEgS 350
Cdd:cd05945 190 TVWVSTPSFAAMCLLSPTFTPESLP--SLRHFLFCGEVLPHKTARALQQRF---PDARIYNTYGPTEATVAVTYIEVT-P 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 351 DQLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAgyvgggganRFCDNPHATQPDF-----QRLYRT 425
Cdd:cd05945 264 EVLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSK---------GYLNNPEKTAAAFfpdegQRAYRT 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 426 GDFGTLVKGAVL-YAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGA-RTSAQHIE 503
Cdd:cd05945 335 GDLVRLEADGLLfYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAeAGLTKAIK 414
|
490 500 510
....*....|....*....|....*....|....*
gi 223890156 504 GELRNALTHYMMPQVIEV-ESIPLLVNGKVDRQGL 537
Cdd:cd05945 415 AELAERLPPYMIPRRFVYlDELPLNANGKIDRKAL 449
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-615 |
6.48e-74 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 260.86 E-value: 6.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 30 AKSDRTALIYKDEissvQVSHAELAARTNVLARAISERArtVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPME 109
Cdd:PRK12467 1586 ATPEAVALVFGEQ----ELTYGELNRRANRLAHRLIALG--VGP----EVLVGIAVERSLEMVVGLLAILKAGGAYVPLD 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 110 PSFPQGRITHILKDAEPSLVIYDDSADPSMFKESGVPFAsfeELAQEATSHSADEPMDAET-LAPltsDSIAIVLYTSGG 188
Cdd:PRK12467 1656 PEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSL---VLDQEDDWLEGYSDSNPAVnLAP---QNLAYVIYTSGS 1729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 189 TGIPKGVRLSYSAICNRLWWQFRTFPYSDSEeicVW--KTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLA 266
Cdd:PRK12467 1730 TGRPKGAGNRHGALVNRLCATQEAYQLSAAD---VVlqFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIE 1806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 267 DNQIERLVLVPTLLRSILMYLALGPASRPLRRLklwVCSGETLSKELASEFFKYFGNEdgyKLANFYGSTEVMGDVTYYV 346
Cdd:PRK12467 1807 RQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRV---VCGGEALEVEALRPWLERLPDT---GLFNLYGPTETAVDVTHWT 1880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 347 LEGSDqLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQPdfQRLYR 424
Cdd:PRK12467 1881 CRRKD-LEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARgyLNRPALTAERFVADPFGTVG--SRLYR 1957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 425 TGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVL-CYGldRGNPEILGFVTTK----PGARTS 498
Cdd:PRK12467 1958 TGDLARYrADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIaQDG--ANGKQLVAYVVPTdpglVDDDEA 2035
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 499 AQHIEGELRNALT----HYMMP-QVIEVESIPLLVNGKVDRQGLLKMyentnnndDAEVAVDidcsgaglaDLEAARALL 573
Cdd:PRK12467 2036 QVALRAILKNHLKaslpEYMVPaHLVFLARMPLTPNGKLDRKALPAP--------DASELQQ---------AYVAPQSEL 2098
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 223890156 574 ETVGA-----VLGRAARGtlsLRSGFYELGGNSLNSIYTITKLRDRG 615
Cdd:PRK12467 2099 EQRLAaiwqdVLGLEQVG---LHDNFFELGGDSIISIQVVSRARQAG 2142
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
33-542 |
1.42e-73 |
|
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: 244.72 E-value: 1.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:COG0318 14 DRPALVFGGR----RLTYAELDARARRLAAAL--RALGVGPGD----RVALLLPNSPEFVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYddsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltsdsiAIVLYTSGGTGIP 192
Cdd:COG0318 84 TAEELAYILEDSGARALVT------------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSDSEEICVWkTALTFVDS-VCEIWGPLLHGRALLILSRettRDPQKLVNVLADNQIE 271
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAALGLTPGDVVLVA-LPLFHVFGlTVGLLAPLLAGATLVLLPR---FDPERVLELIERERVT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 272 RLVLVPTLLRSILMYLALGPasRPLRRLKLWVCSGETLSKELASEFFKYFGNEdgykLANFYGSTEVMGDVTYyvleGSD 351
Cdd:COG0318 192 VLFGVPTMLARLLRHPEFAR--YDLSSLRLVVSGGAPLPPELLERFEERFGVR----IVEGYGLTETSPVVTV----NPE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 352 QLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLaagyvgggganrFC---DNPHATQPDFQ-RLYRTGD 427
Cdd:COG0318 262 DPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNV------------MKgywNDPEATAEAFRdGWLRTGD 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 428 FGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVlcYGL--DRGNPEILGFVTTKPGARTSAQHIEG 504
Cdd:COG0318 330 LGRLDEDGYLYiVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAV--VGVpdEKWGERVVAFVVLRPGAELDAEELRA 407
|
490 500 510
....*....|....*....|....*....|....*....
gi 223890156 505 ELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGLLKMYE 542
Cdd:COG0318 408 FLRERLARYKVPRRVEfVDELPRTASGKIDRRALRERYA 446
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
33-537 |
2.27e-71 |
|
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: 238.76 E-value: 2.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd12115 14 DAIALVCGDE----SLTYAELNRRANRLAARL--RAAGVGP----ESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDdsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltSDSIAIVLYTSGGTGIP 192
Cdd:cd12115 84 PPERLRFILEDAQARLVLTD-------------------------------------------PDDLAYVIYTSGSTGRP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPysdSEEI--CVWKTALTFVDSVCEIWGPLLHGRALLILSrettrDPQKLVNVLADNQI 270
Cdd:cd12115 121 KGVAIEHRNAAAFLQWAAAAFS---AEELagVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 271 ERLVLVPTLLRSILMYLALgPASrpLRRLKLwvcSGETLSKELASEFFkyfGNEDGYKLANFYGSTEVMGDVTYYVLEGS 350
Cdd:cd12115 193 TLINTVPSAAAELLRHDAL-PAS--VRVVNL---AGEPLPRDLVQRLY---ARLQVERVVNLYGPSEDTTYSTVAPVPPG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 351 DQldlyPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHAtqpDFQRLYRTGDF 428
Cdd:cd12115 264 AS----GEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARgyLGRPGLTAERFLPDPFG---PGARLYRTGDL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 429 GT-LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELR 507
Cdd:cd12115 337 VRwRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLG 416
|
490 500 510
....*....|....*....|....*....|.
gi 223890156 508 NALTHYMMPQVIEV-ESIPLLVNGKVDRQGL 537
Cdd:cd12115 417 TRLPAYMVPSRFVRlDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
33-537 |
2.86e-69 |
|
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: 234.29 E-value: 2.86e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17656 3 DAVAVVFENQ----KLTYRELNERSNQLARFL--REKGVKKDS----IVAIMMERSAEMIVGILGILKAGGAFVPIDPEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSAdPSMFKESGvpfaSFEELAQEATSHSADEPMDAETlaplTSDSIAIVLYTSGGTGIP 192
Cdd:cd17656 73 PEERRIYIMLDSGVRVVLTQRHL-KSKLSFNK----STILLEDPSISQEDTSNIDYIN----NSDDLLYIIYTSGTTGKP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQfRTFPYSDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIER 272
Cdd:cd17656 144 KGVQLEHKNMVNLLHFE-REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 273 LVLVPTLLRSIlmYLALGPASRPLRRLKLWVCSGETLskELASEFFKYFgNEDGYKLANFYGSTEVmGDVTYYVLEGSDQ 352
Cdd:cd17656 223 VFLPVAFLKFI--FSEREFINRFPTCVKHIITAGEQL--VITNEFKEML-HEHNVHLHNHYGPSET-HVVTTYTINPEAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 353 LDLYPtiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHatQPDfQRLYRTGDFGT 430
Cdd:cd17656 297 IPELP--PIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARgyLNRQELTAEKFFPDPF--DPN-ERMYRTGDLAR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 431 -LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSaqHIEGELRNA 509
Cdd:cd17656 372 yLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNIS--QLREYLAKQ 449
|
490 500
....*....|....*....|....*....
gi 223890156 510 LTHYMMPQ-VIEVESIPLLVNGKVDRQGL 537
Cdd:cd17656 450 LPEYMIPSfFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
33-537 |
4.73e-68 |
|
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: 229.95 E-value: 4.73e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17649 2 DAVALVFGDQ----SLSYAELDARANRLAHRL--RALGVGP----EVRVGIALERSLEMVVALLAILKAGGAYVPLDPEY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIyddSADPsmfkesgvpfasfeelaqeatshsadepmdaetlapltsDSIAIVLYTSGGTGIP 192
Cdd:cd17649 72 PAERLRYMLEDSGAGLLL---THHP---------------------------------------RQLAYVIYTSGSTGTP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSDSEEICVWKTaLTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIER 272
Cdd:cd17649 110 KGVAVSHGPLAAHCQATAERYGLTPGDRELQFAS-FNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 273 LVLVPTLLRSILMYLALGPASRPLRrLKLWVCSGETLSKELASEFFKyfgneDGYKLANFYGSTEVMGDVTYYVLEgSDQ 352
Cdd:cd17649 189 LDLPPAYLQQLAEEADRTGDGRPPS-LRLYIFGGEALSPELLRRWLK-----APVRLFNAYGPTEATVTPLVWKCE-AGA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 353 LDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQPdfQRLYRTGDFGT 430
Cdd:cd17649 262 ARAGASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARgyLGRPELTAERFVPDPFGAPG--SRLYRTGDLAR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 431 -LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDrGNPEILGFVTTKPGARTSA--QHIEGELR 507
Cdd:cd17649 340 wRDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGA-GGKQLVAYVVLRAAAAQPElrAQLRTALR 418
|
490 500 510
....*....|....*....|....*....|.
gi 223890156 508 NALTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:cd17649 419 ASLPDYMVPaHLVFLARLPLTPNGKLDRKAL 449
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
33-666 |
1.05e-66 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 239.68 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERArtVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK12467 3110 EAPALVFGDQ----QLSYAELNRRANRLAHRLIAIG--VGP----DVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEY 3179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSADPSMFKESGVPFASFEELAQEATS-HSADEPMDAETLApltsdsiaIVLYTSGGTGI 191
Cdd:PRK12467 3180 PRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTALTLDRLDLNGYSeNNPSTRVMGENLA--------YVIYTSGSTGK 3251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 192 PKGVRLSYSAICNRLWWQFRTFPYSDSEEIcVWKTALTFVDSVCEIWGPLLHGrALLILSRETTRDPQKLVNVLADNQIE 271
Cdd:PRK12467 3252 PKGVGVRHGALANHLCWIAEAYELDANDRV-LLFMSFSFDGAQERFLWTLICG-GCLVVRDNDLWDPEELWQAIHAHRIS 3329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 272 RLVLVPTLLRSILMYLalGPASRPlrRLKLWVCSGETLSkelASEFFKYFGNEDGYKLANFYGSTEVMGDVTYYVLeGSD 351
Cdd:PRK12467 3330 IACFPPAYLQQFAEDA--GGADCA--SLDIYVFGGEAVP---PAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKC-GGD 3401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 352 QLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQPdfQRLYRTGDfg 429
Cdd:PRK12467 3402 AVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARgyHQRPSLTAERFVADPFSGSG--GRLYRTGD-- 3477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 430 tLVK----GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNpEILGFVTTKPGARTSAQHIEGE 505
Cdd:PRK12467 3478 -LARyradGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGK-QLVAYVVPADPQGDWRETLRDH 3555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 506 LRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLLKMyentnnndDAEVavdidcSGAGLADLEAARALLETVGA-VLGRA 583
Cdd:PRK12467 3556 LAASLPDYMVPaQLLVLAAMPLGPNGKVDRKALPDP--------DAKG------SREYVAPRSEVEQQLAAIWAdVLGVE 3621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 584 ARGtlsLRSGFYELGGNSLNSIYTITKLRD-RGYYVEISDFLGASTLGEiLSKMSTDPNGGAD------SKEATFIAVPM 656
Cdd:PRK12467 3622 QVG---VTDNFFELGGDSLLALQVLSRIRQsLGLKLSLRDLMSAPTIAE-LAGYSPLGDVPVNllldlnRLETGFPALFC 3697
|
650
....*....|
gi 223890156 657 RDEHKREVID 666
Cdd:PRK12467 3698 RHEGLGTVFD 3707
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
14-537 |
3.85e-66 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 238.14 E-value: 3.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 14 RAPVPTAP------LTHHLgpLAKSDRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQP 87
Cdd:PRK05691 1123 QAPCAPAQawlpelLNEQA--RQTPERIALVWDGG----SLDYAELHAQANRLAHYL--RDKGVGP----DVCVAIAAER 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 88 THNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPSMFKESGVPFASFEELaqeatsHSADEPMD 167
Cdd:PRK05691 1191 SPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIALDSL------HLDSWPSQ 1264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 168 AETLApLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYsDSEEICVWKTALTFVDSVCEIWGPLLHGRAL 247
Cdd:PRK05691 1265 APGLH-LHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYAL-DDSDVLMQKAPISFDVSVWECFWPLITGCRL 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 248 LILSRETTRDPQKLVNVLADNQIERLVLVPTLLRSILMYlalgPASRPLRRLKLWVCSGETLSKELASEFFKYFgneDGY 327
Cdd:PRK05691 1343 VLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDE----PLAAACTSLRRLFSGGEALPAELRNRVLQRL---PQV 1415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 328 KLANFYGSTEVMGDVTYYVLEGSDQLdlypTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGA 405
Cdd:PRK05691 1416 QLHNRYGPTETAINVTHWQCQAEDGE----RSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARgyLGRPALTA 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 406 NRFCDNPHATqpDFQRLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGnPE 484
Cdd:PRK05691 1492 ERFVPDPLGE--DGARLYRTGDRARWnADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQ 1568
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 223890156 485 ILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:PRK05691 1569 LVGYYTGEAGQEAEAERLKAALAAELPEYMVPaQLIRLDQMPLGPSGKLDRRAL 1622
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
33-534 |
1.51e-65 |
|
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: 224.07 E-value: 1.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd12114 2 DATAVICGDG----TLTYGELAERARRVAGAL--KAAGVRPGD----LVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIyddSADPSMFKESGVPFASFEELaqeatshSADEPMDAETLAPLTSDSIAIVLYTSGGTGIP 192
Cdd:cd12114 72 PAARREAILADAGARLVL---TDGPDAQLDVAVFDVLILDL-------DALAAPAPPPPVDVAPDDLAYVIFTSGSTGTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSDSEEI-CVwkTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIE 271
Cdd:cd12114 142 KGVMISHRAALNTILDINRRFAVGPDDRVlAL--SSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 272 RLVLVPTLLRSILMYLALGPASRPLRRLKLWvcSGETLSKELASEFFKYFGNedgyklANFY---GSTEVMGDVTYYVLE 348
Cdd:cd12114 220 LWNSVPALLEMLLDVLEAAQALLPSLRLVLL--SGDWIPLDLPARLRALAPD------ARLIslgGATEASIWSIYHPID 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 349 gsDQLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDF------QRL 422
Cdd:cd12114 292 --EVPPDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALG---------YLGDPELTAARFvthpdgERL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 423 YRTGDFGTLVKGAVL-YAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGlDRGNPEILGFVTTKPGART-SAQ 500
Cdd:cd12114 361 YRTGDLGRYRPDGTLeFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLG-DPGGKRLAAFVVPDNDGTPiAPD 439
|
490 500 510
....*....|....*....|....*....|....*
gi 223890156 501 HIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDR 534
Cdd:cd12114 440 ALRAFLAQTLPAYMIPsRVIALEALPLTANGKVDR 474
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
33-449 |
1.02e-63 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 217.57 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEISsvqVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:pfam00501 10 DKTALEVGEGRR---LTYRELDERANRLAAGL--RALGVGKGD----RVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDD--------SADPSMFKESGVPFASFEELAQEATSHSADEPMDA--ETLAPLTSDSIAIV 182
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVppPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 183 LYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSE---EICVWKTALTFVDSVC-EIWGPLLHGRALLILSRETTRDP 258
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLgpdDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 259 QKLVNVLADNQIERLVLVPTLLRSILMYLALGPASRPlrRLKLWVCSGETLSKELASEFFKYFGNEdgykLANFYGSTEV 338
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFGGA----LVNGYGLTET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 339 MGdVTYYVLEGSDQLDLYPTipIGRPLDNCAIYLLDEE-LSPTRDSEPGEVWVAGANLAAgyvgggganRFCDNPHATQP 417
Cdd:pfam00501 315 TG-VVTTPLPLDEDLRSLGS--VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMK---------GYLNDPELTAE 382
|
410 420 430
....*....|....*....|....*....|....*
gi 223890156 418 DF--QRLYRTGDFGTLVK-GAVLYAGRTDAQVKIR 449
Cdd:pfam00501 383 AFdeDGWYRTGDLGRRDEdGYLEIVGRKKDQIKLG 417
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
33-645 |
7.70e-63 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 228.30 E-value: 7.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERArtVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK12316 4566 DAVAVVFDEE----KLTYAELNRRANRLAHALIARG--VGP----EVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSADPSMFKESGVPFASFEElAQEATSHSADEPmdaetLAPLTSDSIAIVLYTSGGTGIP 192
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLALDR-DEDWEGFPAHDP-----AVRLHPDNLAYVIYTSGSTGRP 4709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWqFRTFPYSDSEEICVWKTALTFVDSVCEIWGPLLHGRALLIlSRETTRDPQKLVNVLADNQIER 272
Cdd:PRK12316 4710 KGVAVSHGSLVNHLHA-TGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVI-RDDSLWDPERLYAEIHEHRVTV 4787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 273 LVLVPTLLRSilmyLALGPASRP-LRRLKLWVCSGETLSKELASEFFKYFGNEdgyKLANFYGSTEVMGDVTYYVLEGSD 351
Cdd:PRK12316 4788 LVFPPVYLQQ----LAEHAERDGePPSLRVYCFGGEAVAQASYDLAWRALKPV---YLFNGYGPTETTVTVLLWKARDGD 4860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 352 QLDLyPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQPdfQRLYRTGDFG 429
Cdd:PRK12316 4861 ACGA-AYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARgyLERPALTAERFVPDPFGAPG--GRLYRTGDLA 4937
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 430 TL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNpEILGFVTTKPGARTSAQHIEGELRN 508
Cdd:PRK12316 4938 RYrADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGK-QLVGYVVPQDPALADADEAQAELRD 5016
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 509 ALT--------HYMMP-QVIEVESIPLLVNGKVDRQGLLKMyeNTNNNDDAEVA--VDIDCSgagLADLEAARALLETVG 577
Cdd:PRK12316 5017 ELKaalrerlpEYMVPaHLVFLARMPLTPNGKLDRKALPQP--DASLLQQAYVAprSELEQQ---VAAIWAEVLQLERVG 5091
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223890156 578 avlgraargtlsLRSGFYELGGNSLNSIYTITKLRDR-GYYVEISDFLGASTLGEILSKMSTDPNGGAD 645
Cdd:PRK12316 5092 ------------LDDNFFELGGHSLLAIQVTSRIQLElGLELPLRELFQTPTLAAFVELAAAAGSGDDE 5148
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-663 |
1.48e-62 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 227.53 E-value: 1.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 13 PRAPVPTAPLTHHL-GPLAKS--DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTH 89
Cdd:PRK12316 1995 TPEAYPRGPGVHQRiAEQAARapEAIAVVFGDQ----HLSYAELDSRANRLAHRL--RARGVGP----EVRVAIAAERSF 2064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 90 NTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPSMFKESGVPFASFE---ELAQEATSHSADEpm 166
Cdd:PRK12316 2065 ELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDrdaEWADYPDTAPAVQ-- 2142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 167 daetLAPltsDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEeiCVW-KTALTFVDSVCEIWGPLLHGr 245
Cdd:PRK12316 2143 ----LAG---ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPAD--CELqFMSFSFDGAHEQWFHPLLNG- 2212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 246 ALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASRPLRRLklwVCSGETLSKELASEFFKYFGNEd 325
Cdd:PRK12316 2213 ARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVY---CFGGEAVPAASLRLAWEALRPV- 2288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 326 gyKLANFYGSTEVMGDVTYYVLEGSDQLDLYpTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLaagyvggggA 405
Cdd:PRK12316 2289 --YLFNGYGPTEAVVTPLLWKCRPQDPCGAA-YVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGL---------A 2356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 406 NRFCDNPHATQPDF---------QRLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLC 475
Cdd:PRK12316 2357 RGYLNRPGLTAERFvpdpfsasgERLYRTGDLARYrADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVA 2436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 476 YGlDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLLKmyENTNNNDDAEVAV 554
Cdd:PRK12316 2437 QD-GASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPaHWVVLERLPLNPNGKLDRKALPK--PDVSQLRQAYVAP 2513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 555 DIDCSgAGLADLEAARALLETVGavlgraargtlsLRSGFYELGGNSLNSIYTITKLR-DRGYYVEISDFLGASTLGEIL 633
Cdd:PRK12316 2514 QEGLE-QRLAAIWQAVLKVEQVG------------LDDHFFELGGHSLLATQVVSRVRqDLGLEVPLRILFERPTLAAFA 2580
|
650 660 670
....*....|....*....|....*....|
gi 223890156 634 SKMSTDPNGGADSKEATFIAVPMRDEHKRE 663
Cdd:PRK12316 2581 ASLESGQTSRAPVLQKVTRVQPLPLSHAQQ 2610
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
33-537 |
1.03e-60 |
|
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: 210.75 E-value: 1.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseraRTVGPNRDSdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17644 15 DAVAVVFEDQ----QLTYEELNTKANQLAHYL----QSLGVKSES--LVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDdsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltSDSIAIVLYTSGGTGIP 192
Cdd:cd17644 85 PQERLTYILEDAQISVLLTQ-------------------------------------------PENLAYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSDSEEICVWkTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIER 272
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVLQF-ASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 273 LVLVPTLLRSILMYLALGPASRPlRRLKLWVCSGETLSKELASEFFKYFGNEdgYKLANFYGSTEVMGDVTYYVLEgSDQ 352
Cdd:cd17644 201 LSLPPAYWHLLVLELLLSTIDLP-SSLRLVIVGGEAVQPELVRQWQKNVGNF--IQLINVYGPTEATIAATVCRLT-QLT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 353 LDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQPdFQRLYRTGDFGT 430
Cdd:cd17644 277 ERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARgyLNRPELTAEKFISHPFNSSE-SERLYKTGDLAR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 431 -LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNA 509
Cdd:cd17644 356 yLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAK 435
|
490 500
....*....|....*....|....*....
gi 223890156 510 LTHYMMPQV-IEVESIPLLVNGKVDRQGL 537
Cdd:cd17644 436 LPDYMIPSAfVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
47-543 |
2.49e-59 |
|
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: 207.39 E-value: 2.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 47 QVSHAELAARTNVLARAISERArtVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEP 126
Cdd:cd05918 24 SLTYAELDRLSSRLAHHLRSLG--VGPGV----FVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 127 SLVIyddsadpsmfkesgvpfasfeelaqeaTShsadepmdaetlaplTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRL 206
Cdd:cd05918 98 KVVL---------------------------TS---------------SPSDAAYVIFTSGSTGKPKGVVIEHRALSTSA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 207 WWQFRTFPYsDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDpqKLVNVLADNQIERLVLVPTLLRSilmy 286
Cdd:cd05918 136 LAHGRALGL-TSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTPSVARL---- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 287 laLGPASRP-LRRLklwVCSGETLSKELASEFfkyfgnEDGYKLANFYGSTEV-MGDVTYYVLEGSDQLDlyptipIGRP 364
Cdd:cd05918 209 --LDPEDVPsLRTL---VLGGEALTQSDVDTW------ADRVRLINAYGPAECtIAATVSPVVPSTDPRN------IGRP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 365 LdNCAIYLLD----EELSPTrdSEPGEVWVAGANLAagyvggggaNRFCDNPHATQPDF---------------QRLYRT 425
Cdd:cd05918 272 L-GATCWVVDpdnhDRLVPI--GAVGELLIEGPILA---------RGYLNDPEKTAAAFiedpawlkqegsgrgRRLYRT 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 426 GDfgtLVK----GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDK--CVVLCYGLDRGNPEIL-GFVTTKPG---- 494
Cdd:cd05918 340 GD---LVRynpdGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKevVVEVVKPKDGSSSPQLvAFVVLDGSssgs 416
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223890156 495 -------------ARTSAQHIEGELRNALTHYMMPQV-IEVESIPLLVNGKVDRQGLLKMYEN 543
Cdd:cd05918 417 gdgdslflepsdeFRALVAELRSKLRQRLPSYMVPSVfLPLSHLPLTASGKIDRRALRELAES 479
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-630 |
3.31e-59 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 217.52 E-value: 3.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 15 APVPTAPLTHHL---GPLAKSDRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNT 91
Cdd:PRK12316 3051 AEYPLERGVHRLfeeQVERTPDAVALAFGEQ----RLSYAELNRRANRLAHRL--IERGVGP----DVLVGVAVERSLEM 3120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 92 IMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIydDSADPSMFKESGVPFASFEELAQEATSHSADEPMDAETL 171
Cdd:PRK12316 3121 VVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL--SQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENL 3198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 172 apltsdsiAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEIcVWKTALTFVDSVCEIWGPLLHGRALLILS 251
Cdd:PRK12316 3199 --------AYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRV-LQFTTFSFDVFVEELFWPLMSGARVVLAG 3269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 252 RETTRDPQKLVNVLADNQIERLVLVPTLLRSILMylalGPASRPLRRLKLWVCSGETLSKELASEFFKyfgnedGYKLAN 331
Cdd:PRK12316 3270 PEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE----EEDAHRCTSLKRIVCGGEALPADLQQQVFA------GLPLYN 3339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 332 FYGSTEVMGDVTyyVLEGSDQLDLYPtiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFC 409
Cdd:PRK12316 3340 LYGPTEATITVT--HWQCVEEGKDAV--PIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARgyHNRPGLTAERFV 3415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 410 DNPHATQpdfQRLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRgnpeILGF 488
Cdd:PRK12316 3416 PDPFVPG---ERLYRTGDLARYrADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ----LVAY 3488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 489 VTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLLKmyentnnnddaevavdIDCSGAGLADLE 567
Cdd:PRK12316 3489 VVPEDEAGDLREALKAHLKASLPEYMVPaHLLFLERMPLTPNGKLDRKALPR----------------PDAALLQQDYVA 3552
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 568 AARALLETVGA----VLGRAARGtlsLRSGFYELGGNSLNSIYTITKLRDRGYYVEISDFLGASTLG 630
Cdd:PRK12316 3553 PVNELERRLAAiwadVLKLEQVG---LTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQ 3616
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
33-537 |
5.64e-59 |
|
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: 205.39 E-value: 5.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERARTVGPnrdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17650 2 DAIAVSDATR----QLTYRELNERANQLARTLRGLGVAPGS------VVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDdsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltSDSIAIVLYTSGGTGIP 192
Cdd:cd17650 72 PAERLQYMLEDSGAKLLLTQ-------------------------------------------PEDLAYVIYTSGTTGKP 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICN-RLWWQFRtfpYS-DSEEICVWKTALTFVD-SVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQ 269
Cdd:cd17650 109 KGVMVEHRNVAHaAHAWRRE---YElDSFPVRLLQMASFSFDvFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSR 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 270 IERLVLVPTLLRSILMYLALGPASrpLRRLKLWVCSGETLSKELASEFFKYFGNedGYKLANFYGSTEVMGDVTYYVlEG 349
Cdd:cd17650 186 ITLMESTPALIRPVMAYVYRNGLD--LSAMRLLIVGSDGCKAQDFKTLAARFGQ--GMRIINSYGVTEATIDSTYYE-EG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 350 SDQLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQpdfQRLYRTGD 427
Cdd:cd17650 261 RDPLGDSANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARgyLNRPELTAERFVENPFAPG---ERMYRTGD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 428 FGT-LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTtkPGARTSAQHIEGEL 506
Cdd:cd17650 338 LARwRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAELRAFL 415
|
490 500 510
....*....|....*....|....*....|..
gi 223890156 507 RNALTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:cd17650 416 AKELPSYMIPsYYVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
33-537 |
1.84e-57 |
|
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: 201.24 E-value: 1.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17645 13 DHVAVVDRGQ----SLTYKQLNEKANQLARHL--RGKGVKP----DDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDdsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltSDSIAIVLYTSGGTGIP 192
Cdd:cd17645 83 PGERIAYMLADSSAKILLTN-------------------------------------------PDDLAYVIYTSGSTGLP 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSDSEEICVWkTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIEr 272
Cdd:cd17645 120 KGVMIEHHNLVNLCEWHRPYFGVTPADKSLVY-ASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 273 LVLVPTLLRSILMYLAlgpaSRPLRRLklwVCSGETLSKelaseffkyfGNEDGYKLANFYGSTEVMGDVTYYVLEGSdq 352
Cdd:cd17645 198 ISFLPTGAAEQFMQLD----NQSLRVL---LTGGDKLKK----------IERKGYKLVNNYGPTENTVVATSFEIDKP-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 353 ldlYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQpdfQRLYRTGDFGT 430
Cdd:cd17645 259 ---YANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARgyLNRPELTAEKFIVHPFVPG---ERMYRTGDLAK 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 431 LV-KGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAqhIEGELRNA 509
Cdd:cd17645 333 FLpDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEE--LREWLKND 410
|
490 500
....*....|....*....|....*....
gi 223890156 510 LTHYMMPQV-IEVESIPLLVNGKVDRQGL 537
Cdd:cd17645 411 LPDYMIPTYfVHLKALPLTANGKVDRKAL 439
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
33-537 |
5.03e-56 |
|
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: 197.62 E-value: 5.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDeissVQVSHAELAARTNVLARAIseraRTVGPNRdSDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17648 2 DRVAVVYGD----KRLTYRELNERANRLAHYL----LSVAEIR-PDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDdsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltSDSIAIVLYTSGGTGIP 192
Cdd:cd17648 73 PDERIQFILEDTGARVVITN-------------------------------------------STDLAYAIYTSGTTGKP 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICN-RLWWQFRTFPYSDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIE 271
Cdd:cd17648 110 KGVLVEHGSVVNlRTSLSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 272 RLVLVPTLLRSILMylalgpASRP-LRRLklwVCSGETLSkelASEFFKYFGNEDGyKLANFYGSTE--VMGDVTYYvlE 348
Cdd:cd17648 190 YLSGTPSVLQQYDL------ARLPhLKRV---DAAGEEFT---APVFEKLRSRFAG-LIINAYGPTEttVTNHKRFF--P 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 349 GSDQLDLyptiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHATQPD-----FQR 421
Cdd:cd17648 255 GDQRFDK----SLGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARgyLNRPELTAERFLPNPFQTEQErargrNAR 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 422 LYRTGD-FGTLVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLC-----YGLDRGNPEILGFVTTKPGA 495
Cdd:cd17648 331 LYKTGDlVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkedasQAQSRIQKYLVGYYLPEPGH 410
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 223890156 496 rTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:cd17648 411 -VPESDLLSFLRAKLPRYMVPaRLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
45-537 |
1.05e-54 |
|
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: 193.29 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 45 SVQVSHAELAARTNVLARAISERARTVGPnrdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDA 124
Cdd:cd17653 20 GGSLTYGELDAASNALANRLLQLGVVPGD------VVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 125 EPSLVIYDDSADpsmfkesgvpfasfeelaqeatshsadepmdaetlapltsdSIAIVLYTSGGTGIPKGVRLSYSAICN 204
Cdd:cd17653 94 GATLLLTTDSPD-----------------------------------------DLAYIIFTSGSTGIPKGVMVPHRGVLN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 205 RLWW---QFRTFPYSDSEEICvwktALTFVDSVCEIWGPLLHGrALLILsrettRDPQKLVNVLADnQIERLVLVPTLLR 281
Cdd:cd17653 133 YVSQppaRLDVGPGSRVAQVL----SIAFDACIGEIFSTLCNG-GTLVL-----ADPSDPFAHVAR-TVDALMSTPSILS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 282 SilmylaLGPASRPlrRLKLWVCSGETLSKELASEFFKyfgnedGYKLANFYGSTEVMGDVTYYVLEGSDQldlyptIPI 361
Cdd:cd17653 202 T------LSPQDFP--NLKTIFLGGEAVPPSLLDRWSP------GRRLYNAYGPTECTISSTMTELLPGQP------VTI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 362 GRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDF--------QRLYRTGDFGTLV- 432
Cdd:cd17653 262 GKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARG---------YLGNPALTASKFvpdpfwpgSRMYRTGDYGRWTe 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 433 KGAVLYAGRTDAQVKIRGHRVDLLEVER-ALAQVPGVDKCVVLcygLDRGNpeILGFVTTKpGARTSAqhIEGELRNALT 511
Cdd:cd17653 333 DGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAI---VVNGR--LVAFVTPE-TVDVDG--LRSELAKHLP 404
|
490 500
....*....|....*....|....*..
gi 223890156 512 HYMMPQVI-EVESIPLLVNGKVDRQGL 537
Cdd:cd17653 405 SYAVPDRIiALDSFPLTANGKVDRKAL 431
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
33-539 |
9.25e-53 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 189.72 E-value: 9.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERArtvgPNRDSDYVIAVCMQPthNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK04813 17 DFPAYDYLGE----KLTYGQLKEDSDALAAFIDSLK----LPDKSPIIVFGHMSP--EMLATFLGAVKAGHAYIPVDVSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIyddSADPSMFKESGVPFASFEELAqeaTSHSADEPMDAEtlAPLTSDSIAIVLYTSGGTGIP 192
Cdd:PRK04813 87 PAERIEMIIEVAKPSLII---ATEELPLEILGIPVITLDELK---DIFATGNPYDFD--HAVKGDDNYYIIFTSGTTGKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTF------------PYSdseeicvwktaltFVDSVCEIWGPLLHGRALLILSRETTRDPQK 260
Cdd:PRK04813 159 KGVQISHDNLVSFTNWMLEDFalpegpqflnqaPYS-------------FDLSVMDLYPTLASGGTLVALPKDMTANFKQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 261 LVNVLADNQIERLVLVPTLLRSILMYLALGPASRPlrRLKLWVCSGETLSKELASEFFKYFGNEdgyKLANFYGSTEVMG 340
Cdd:PRK04813 226 LFETLPQLPINVWVSTPSFADMCLLDPSFNEEHLP--NLTHFLFCGEELPHKTAKKLLERFPSA---TIYNTYGPTEATV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 341 DVTyyVLEGSDQ-LDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDF 419
Cdd:PRK04813 301 AVT--SIEITDEmLDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKG---------YLNNPEKTAEAF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 420 -----QRLYRTGDFGTLVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPG 494
Cdd:PRK04813 370 ftfdgQPAYHTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEE 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 223890156 495 ------ARTSAqhIEGELRNALTHYMMPQ-VIEVESIPLLVNGKVDRQGLLK 539
Cdd:PRK04813 450 dferefELTKA--IKKELKERLMEYMIPRkFIYRDSLPLTPNGKIDRKALIE 499
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
48-615 |
2.78e-50 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 190.38 E-value: 2.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 48 VSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPS 127
Cdd:PRK05691 2214 LSYAELDARANRLARAL--RERGVGP----QVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIG 2287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 128 LVIyddsADPSMFKE-----SGVPFASFEElAQEATSHSADEPMDAETLApltsDSIAIVLYTSGGTGIPKGVRLSYSAI 202
Cdd:PRK05691 2288 LLL----SDRALFEAlgelpAGVARWCLED-DAAALAAYSDAPLPFLSLP----QHQAYLIYTSGSTGKPKGVVVSHGEI 2358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 203 CNRLWWQFRTFPY-SDSEEICVWktALTFvDSVCE-IWGPLLHGrALLILSRETTRDPQKLVNVLADNQIERLVLVPTLL 280
Cdd:PRK05691 2359 AMHCQAVIERFGMrADDCELHFY--SINF-DAASErLLVPLLCG-ARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYG 2434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 281 RSILMYLALGPASRPLRrlkLWVCSGETLSKELASEFFKYFGNEdgyKLANFYGSTEVMgdVTYYVLEGSDQL-DLYPTI 359
Cdd:PRK05691 2435 SQLAQWLAGQGEQLPVR---MCITGGEALTGEHLQRIRQAFAPQ---LFFNAYGPTETV--VMPLACLAPEQLeEGAASV 2506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 360 PIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAA--GYVGGGGANRFCDNPHAtqPDFQRLYRTGDfgtLVK---- 433
Cdd:PRK05691 2507 PIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQgyHDRPGLTAERFVADPFA--ADGGRLYRTGD---LVRlrad 2581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 434 GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNpEILGFVTTKPGARTSAQH------IEGELR 507
Cdd:PRK05691 2582 GLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGK-QLAGYLVSAVAGQDDEAQaalreaLKAHLK 2660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 508 NALTHYMMP-QVIEVESIPLLVNGKVDRQGLlkmyentnnnddaeVAVDIdcsGAGLADLEAARALLETVGAVLGRAAR- 585
Cdd:PRK05691 2661 QQLPDYMVPaHLILLDSLPLTANGKLDRRAL--------------PAPDP---ELNRQAYQAPRSELEQQLAQIWREVLn 2723
|
570 580 590
....*....|....*....|....*....|.
gi 223890156 586 -GTLSLRSGFYELGGNSLNSIYTITKLRDRG 615
Cdd:PRK05691 2724 vERVGLGDNFFELGGDSILSIQVVSRARQLG 2754
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
179-533 |
5.77e-50 |
|
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: 177.48 E-value: 5.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 179 IAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEICVWkTALTFVDSVCEIWGPLLHGRALLILSRettRDP 258
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLST-LPLFHIGGLFGLLGALLAGGTVVLLPK---FDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 259 QKLVNVLADNQIERLVLVPTLLRSILmyLALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGNedgyKLANFYGSTEV 338
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLL--KAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGI----KLVNGYGLTET 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 339 MGDVTYYVLEGsdqlDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAagyvggggaNRFCDNPHATQPD 418
Cdd:cd04433 152 GGTVATGPPDD----DARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVM---------KGYWNNPEATAAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 419 FQR-LYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGAR 496
Cdd:cd04433 219 DEDgWYRTGDLGRLdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAD 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 223890156 497 TSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVD 533
Cdd:cd04433 299 LDAEELRAHVRERLAPYKVPRRVVfVDALPRTASGKID 336
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
33-537 |
3.87e-46 |
|
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: 170.35 E-value: 3.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEISSVQVSHAELAARTNVLARAISERartvgpNRDSDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd17654 2 DRPALIIDQTTSDTTVSYADLAEKISNLSNFLRKK------FQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPAS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDdsadpsmfKESGVPFASFeelaqeatsHSADEPMDAETLAPLtsdsiAIVLYTSGGTGIP 192
Cdd:cd17654 76 PEQRSLTVMKKCHVSYLLQN--------KELDNAPLSF---------TPEHRHFNIRTDECL-----AYVIHTSGTTGTP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRLWWQFRTFPYSdSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLAD-NQIE 271
Cdd:cd17654 134 KIVAVPHKCILPNIQHFRSLFNIT-SEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrHRIT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 272 RLVLVPTLLRsilMYLALGPASRPLRR---LKLWVCSGETLSKELASEFFKYFGNedGYKLANFYGSTEVMGDVTYYVLE 348
Cdd:cd17654 213 VLQATPTLFR---RFGSQSIKSTVLSAtssLRVLALGGEPFPSLVILSSWRGKGN--RTRIFNIYGITEVSCWALAYKVP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 349 GSDQldlypTIPIGRPLDNCAIYLLDEELSptrdSEPGEVWVAGANLAAgyvgggganrFCDNPHaTQPdFQRLYRTGDF 428
Cdd:cd17654 288 EEDS-----PVQLGSPLLGTVIEVRDQNGS----EGTGQVFLGGLNRVC----------ILDDEV-TVP-KGTMRATGDF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 429 GTLVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRgnpeILGFVTTKPgaRTSAQHIEGELRN 508
Cdd:cd17654 347 VTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR----LIAFIVGES--SSSRIHKELQLTL 420
|
490 500
....*....|....*....|....*....
gi 223890156 509 ALTHYMMPQVIEVESIPLLVNGKVDRQGL 537
Cdd:cd17654 421 LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
47-602 |
1.27e-42 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 166.88 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 47 QVSHAELAARTNVLARAIseRARTVGpnrdSDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILK-DAE 125
Cdd:PRK05691 3745 QWSYAELNRAANRLGHAL--RAAGVG----VDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIElSRT 3818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 126 PSLVIYDDSADPSM-----FKESGVPFASFEELAQEATSHSADEPMDAetlaplTSDSIAIVLYTSGGTGIPKGVRLSYS 200
Cdd:PRK05691 3819 PVLVCSAACREQARalldeLGCANRPRLLVWEEVQAGEVASHNPGIYS------GPDNLAYVIYTSGSTGLPKGVMVEQR 3892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 201 AICNRlwwQFRTFPY-SDSEEICVWKTALTFVD-SVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIERLVLVPT 278
Cdd:PRK05691 3893 GMLNN---QLSKVPYlALSEADVIAQTASQSFDiSVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPS 3969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 279 LLRSILmylalGPASRPLRRLKLWVCSGETLSKELASEFFKYFgneDGYKLANFYGSTEVMGDVTYYVLEGSDQLDLYpt 358
Cdd:PRK05691 3970 LIQGML-----AEDRQALDGLRWMLPTGEAMPPELARQWLQRY---PQIGLVNAYGPAECSDDVAFFRVDLASTRGSY-- 4039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 359 IPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDF---------QRLYRTGDFG 429
Cdd:PRK05691 4040 LPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRG---------YVGDPLRTALAFvphpfgapgERLYRTGDLA 4110
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 430 TLVKGAVL-YAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYglDRGNPEIL-GFVTTKPGARTSAQHIE---G 504
Cdd:PRK05691 4111 RRRSDGVLeYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQ--EGVNGKHLvGYLVPHQTVLAQGALLErikQ 4188
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 505 ELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLlkmyentnnnddaeVAVDIdcSGAGLADLEAARALLETVGA----- 578
Cdd:PRK05691 4189 RLRAELPDYMVPlHWLWLDRLPLNANGKLDRKAL--------------PALDI--GQLQSQAYLAPRNELEQTLAtiwad 4252
|
570 580
....*....|....*....|....
gi 223890156 579 VLgRAARgtLSLRSGFYELGGNSL 602
Cdd:PRK05691 4253 VL-KVER--VGVHDNFFELGGHSL 4273
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
33-543 |
8.91e-42 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 160.28 E-value: 8.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEISSVQ-VSHAELAARTNVLARAIseRARTVGP-NRdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEP 110
Cdd:COG0365 24 DKVALIWEGEDGEERtLTYAELRREVNRFANAL--RALGVKKgDR-----VAIYLPNIPEAVIAMLACARIGAVHSPVFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 111 SFPQGRITHILKDAEPSLVIYDD-------------------SADPS-----MFKESGVPFA-----SFEELAQEATSHS 161
Cdd:COG0365 97 GFGAEALADRIEDAEAKVLITADgglrggkvidlkekvdealEELPSlehviVVGRTGADVPmegdlDWDELLAAASAEF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 162 ADEPMDAetlapltsDSIAIVLYTSGGTGIPKGVR------LSYSAICNRLWWQFRT----FPYSDseeiCVWKTALTFV 231
Cdd:COG0365 177 EPEPTDA--------DDPLFILYTSGTTGKPKGVVhthggyLVHAATTAKYVLDLKPgdvfWCTAD----IGWATGHSYI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 232 dsvceIWGPLLHGRALLIL-SRETTRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASRPLRRLKLWVCSGETLS 310
Cdd:COG0365 245 -----VYGPLLNGATVVLYeGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLRLLGSAGEPLN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 311 KELASEFFKYFGNEdgykLANFYGSTEVMGdvtyYVLEGSDQLDLYPTIpIGRPLDNCAIYLLDEELSPTRDSEPGEVWV 390
Cdd:COG0365 320 PEVWEWWYEAVGVP----IVDGWGQTETGG----IFISNLPGLPVKPGS-MGKPVPGYDVAVVDEDGNPVPPGEEGELVI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 391 AGANLAAGYvgggganRFCDNPHATQ----PDFQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQV 465
Cdd:COG0365 391 KGPWPGMFR-------GYWNDPERYRetyfGRFPGWYRTGDGARRDEdGYFWILGRSDDVINVSGHRIGTAEIESALVSH 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 466 PGVDKCVVLcyGL---DRGNpEILGFVTTKPGARTSAQhIEGELRNA----LTHYMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:COG0365 464 PAVAEAAVV--GVpdeIRGQ-VVKAFVVLKPGVEPSDE-LAKELQAHvreeLGPYAYPREIEfVDELPKTRSGKIMRRLL 539
|
....*.
gi 223890156 538 LKMYEN 543
Cdd:COG0365 540 RKIAEG 545
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
33-534 |
4.36e-32 |
|
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: 129.65 E-value: 4.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEIssvqVSHAELAARTNVLARAIseRARTVGP-NRdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPS 111
Cdd:cd17631 10 DRTALVFGGRS----LTYAELDERVNRLAHAL--RALGVAKgDR-----VAVLSKNSPEFLELLFAAARLGAVFVPLNFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 112 FPQGRITHILKDAEPSLVIyddsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltsDSIAIVLYTSGGTGI 191
Cdd:cd17631 79 LTPPEVAYILADSGAKVLF----------------------------------------------DDLALLMYTSGTTGR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 192 PKGVRLSYSaicNRLWW---QFRTFPYSdSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETtrDPQKLVNVLADN 268
Cdd:cd17631 113 PKGAMLTHR---NLLWNavnALAALDLG-PDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKF--DPETVLDLIERH 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 269 QIERLVLVPTLLRSILMYLALgpASRPLRRLKLWVCSGETLSKELASEFFKYfgnedGYKLANFYGSTEVMGDVTyyVLE 348
Cdd:cd17631 187 RVTSFFLVPTMIQALLQHPRF--ATTDLSSLRAVIYGGAPMPERLLRALQAR-----GVKFVQGYGMTETSPGVT--FLS 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 349 GSDQLDLYPTIpiGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAgyvgggganRFCDNPHATQPDFQR-LYRTGD 427
Cdd:cd17631 258 PEDHRRKLGSA--GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMA---------GYWNRPEATAAAFRDgWFHTGD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 428 FGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGNP-----EI-LGFVTTKPGARTSAQ 500
Cdd:cd17631 327 LGRLDEDGYLYiVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVI------GVPdekwgEAvVAVVVPRPGAELDED 400
|
490 500 510
....*....|....*....|....*....|....*
gi 223890156 501 HIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDR 534
Cdd:cd17631 401 ELIAHCRERLARYKIPkSVEFVDALPRNATGKILK 435
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
31-534 |
2.75e-31 |
|
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: 127.68 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 31 KSDRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNrDSdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEP 110
Cdd:cd05936 12 FPDKTALIFMGR----KLTYRELDALAEAFAAGL--QNLGVQPG-DR---VALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 111 SFPQGRITHILKDAEPSLVIYDDSadpsmfkesgvpfasFEELAqeatshSADEPMDAEtlAPLTSDSIAIVLYTSGGTG 190
Cdd:cd05936 82 LYTPRELEHILNDSGAKALIVAVS---------------FTDLL------AAGAPLGER--VALTPEDVAVLQYTSGTTG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 191 IPKGVRLSYSAI-CNRLWWQFRTFPYSDSEEICVwkTAL----TFVDSVCEIWgPLLHGRALLILSREttrDPQKLVNVL 265
Cdd:cd05936 139 VPKGAMLTHRNLvANALQIKAWLEDLLEGDDVVL--AALplfhVFGLTVALLL-PLALGATIVLIPRF---RPIGVLKEI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 266 ADNQIERLVLVPTllrsilMYLAL----GPASRPLRRLKLWVCSGETLSKELASEFFKYFGNedgyKLANFYGSTEVMGD 341
Cdd:cd05936 213 RKHRVTIFPGVPT------MYIALlnapEFKKRDFSSLRLCISGGAPLPVEVAERFEELTGV----PIVEGYGLTETSPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 342 VTYYVLEGSDQldlyptiP--IGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDF 419
Cdd:cd05936 283 VAVNPLDGPRK-------PgsIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKG---------YWNRPEETAEAF 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 420 QR-LYRTGDFGTLvkgavlyagRTDAQVKIRGHRVDLL----------EVERALAQVPGVDKCVVLCYGLDRGNPEILGF 488
Cdd:cd05936 347 VDgWLRTGDIGYM---------DEDGYFFIVDRKKDMIivggfnvyprEVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAF 417
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 223890156 489 VTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDR 534
Cdd:cd05936 418 VVLKEGASLTEEEIIAFCREQLAGYKVPRQVEfRDELPKSAVGKILR 464
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
33-541 |
8.45e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 124.14 E-value: 8.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK06187 21 DKEAVYFDGR----RTTYAELDERVNRLANAL--RALGVKK----GDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDS--------------------ADPSMFKESGVPFASFEELAQEATSHSADEPMDAetla 172
Cdd:PRK06187 91 KPEEIAYILNDAEDRVVLVDSEfvpllaailpqlptvrtvivEGDGPAAPLAPEVGEYEELLAAASDTFDFPDIDE---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 173 pltsDSIAIVLYTSGGTGIPKGVRLSYSAIcnrlwwqfrtfpYSDSEEICVWKTaLTFVDSVCEI--------WG----P 240
Cdd:PRK06187 167 ----NDAAAMLYTSGTTGHPKGVVLSHRNL------------FLHSLAVCAWLK-LSRDDVYLVIvpmfhvhaWGlpylA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 241 LLHGRALLILSRettRDPQKLVNVLADNQIERLVLVPTLLRSILMYLAlgPASRPLRRLKLWVCSGETLSKELASEFFKY 320
Cdd:PRK06187 230 LMAGAKQVIPRR---FDPENLLDLIETERVTFFFAVPTIWQMLLKAPR--AYFVDFSSLRLVIYGGAALPPALLREFKEK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 321 FGnedgYKLANFYGSTEVMGDVTYYVLEgsDQLDLYPTIPI--GRPLDNCAIYLLDEELS--PTRDSEPGEVWVAGANLA 396
Cdd:PRK06187 305 FG----IDLVQGYGMTETSPVVSVLPPE--DQLPGQWTKRRsaGRPLPGVEARIVDDDGDelPPDGGEVGEIIVRGPWLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 397 AgyvgggganRFCDNPHATqpdfQRL-----YRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDK 470
Cdd:PRK06187 379 Q---------GYWNRPEAT----AETidggwLHTGDVGYIDEDGYLYiTDRIKDVIISGGENIYPRELEDALYGHPAVAE 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223890156 471 CVVLcygldrGNP------EILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLLKMY 541
Cdd:PRK06187 446 VAVI------GVPdekwgeRPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPkRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
34-537 |
1.21e-29 |
|
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: 122.19 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 34 RTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFP 113
Cdd:cd05919 1 KTAFYAADR----SVTYGQLHDGANRLGSAL--RNLGVSSGD----RVLLLMLDSPELVQLFLGCLARGAIAVVINPLLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 114 QGRITHILKDAEPSLVIYDDsadpsmfkesgvpfasfeelaqeatshsadepmdaetlapltsDSIAIVLYTSGGTGIPK 193
Cdd:cd05919 71 PDDYAYIARDCEARLVVTSA-------------------------------------------DDIAYLLYSSGTTGPPK 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 194 GVRLSYSAicnrlwwqfrtfPYSDSEEICVWKTALTFVDSVCEI-------------WGPLLHGRALLILSreTTRDPQK 260
Cdd:cd05919 108 GVMHAHRD------------PLLFADAMAREALGLTPGDRVFSSakmffgyglgnslWFPLAVGASAVLNP--GWPTAER 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 261 LVNVLADNQIERLVLVPTLLRSILMYLALGPASrpLRRLKLWVCSGETLSKELASEFFKYFGNE--DGYklanfyGSTEV 338
Cdd:cd05919 174 VLATLARFRPTVLYGVPTFYANLLDSCAGSPDA--LRSLRLCVSAGEALPRGLGERWMEHFGGPilDGI------GATEV 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 339 mgdVTYYVLEGSDQLDLYPTipiGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPD 418
Cdd:cd05919 246 ---GHIFLSNRPGAWRLGST---GRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVG---------YWNNPEKSRAT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 419 FQ-RLYRTGD-FGTLVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGAR 496
Cdd:cd05919 311 FNgGWYRTGDkFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAA 390
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 223890156 497 TS---AQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:cd05919 391 PQeslARDIHRHLLERLSAHKVPRRIAfVDELPRTATGKLQRFKL 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
38-532 |
2.35e-28 |
|
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: 119.24 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 38 IYKDEISSVQVSHAELAARTNVLARAIseraRTVGpNRDSDyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRI 117
Cdd:cd05911 1 AQIDADTGKELTYAQLRTLSRRLAAGL----RKLG-LKKGD-VVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 118 THILKDAEPSLVIyddsADPSMF---KESGVPFASFEEL----AQEATSHSADEPMDAETLAPL---------TSDSIAI 181
Cdd:cd05911 75 AHQLKISKPKVIF----TDPDGLekvKEAAKELGPKDKIivldDKPDGVLSIEDLLSPTLGEEDedlppplkdGKDDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 182 VLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEIcvwkTALTFVdsvceiwgPLLHGRALLIL--------SRE 253
Cdd:cd05911 151 ILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGSND----VILGFL--------PLYHIYGLFTTlasllngaTVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 254 TTR--DPQKLVNVLADNQIERLVLVPtllrSILMYLALGPASRP--LRRLKLWVCSGETLSKELASEFFKYFGNEdgyKL 329
Cdd:cd05911 219 IMPkfDSELFLDLIEKYKITFLYLVP----PIAAALAKSPLLDKydLSSLRVILSGGAPLSKELQELLAKRFPNA---TI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 330 ANFYGSTEVMGDVTY----YVLEGSdqldlyptipIGRPLDNCAIYLLDEElspTRDS----EPGEVWVAGANLaagyvg 401
Cdd:cd05911 292 KQGYGMTETGGILTVnpdgDDKPGS----------VGRLLPNVEAKIVDDD---GKDSlgpnEPGEICVRGPQV------ 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 402 gggANRFCDNPHATQ--PDFQRLYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGV-DKCVVlcyG 477
Cdd:cd05911 353 ---MKGYYNNPEATKetFDEDGWLHTGDIGYFDEDGYLYiVDRKKELIKYKGFQVAPAELEAVLLEHPGVaDAAVI---G 426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 478 L--DRGNPEILGFVTTKPGARTSAQHIEgelrnaltHYMMPQVIE----------VESIPLLVNGKV 532
Cdd:cd05911 427 IpdEVSGELPRAYVVRKPGEKLTEKEVK--------DYVAKKVASykqlrggvvfVDEIPKSASGKI 485
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
32-538 |
2.68e-27 |
|
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: 116.31 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 32 SDRTALIYKdeISSVqvSHAELAARTNVLARAiserARTVGPNRDSDyvIAVCMQPTHNTIMALLATWKAGAAYVPM--- 108
Cdd:cd05959 18 GDKTAFIDD--AGSL--TYAELEAEARRVAGA----LRALGVKREER--VLLIMLDTVDFPTAFLGAIRAGIVPVPVntl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 109 --------------------EPSFPQgRITHILKDAEPSLVIYDdSADPSMfkesgvPFASFEELAQEATSHSADEPMda 168
Cdd:cd05959 88 ltpddyayyledsrarvvvvSGELAP-VLAAALTKSEHTLVVLI-VSGGAG------PEAGALLLAELVAAEAEQLKP-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 169 etlAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAIcnrlWWQFRTFP----YSDSEEICVWKTALTFVdsvceiWG----- 239
Cdd:cd05959 158 ---AATHADDPAFWLYSSGSTGRPKGVVHLHADI----YWTAELYArnvlGIREDDVCFSAAKLFFA------YGlgnsl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 240 --PLLHGRALLILSRETTRDpqklvNVLADNQIERLVL---VPTLLRSILMylALGPASRPLRRLKLWVCSGETLSKELA 314
Cdd:cd05959 225 tfPLSVGATTVLMPERPTPA-----AVFKRIRRYRPTVffgVPTLYAAMLA--APNLPSRDLSSLRLCVSAGEALPAEVG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 315 SEFFKYFGNE--DGYklanfyGSTEVM--------GDVTYyvleGSDqldlyptipiGRPLDNCAIYLLDEELSPTRDSE 384
Cdd:cd05959 298 ERWKARFGLDilDGI------GSTEMLhiflsnrpGRVRY----GTT----------GKPVPGYEVELRDEDGGDVADGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 385 PGEVWVAGANLAAGyvgggganrFCDNPHATQPDFQ-RLYRTGD-FGTLVKGAVLYAGRTDAQVKIRGHRVDLLEVERAL 462
Cdd:cd05959 358 PGELYVRGPSSATM---------YWNNRDKTRDTFQgEWTRTGDkYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESAL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 463 AQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSA---QHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLL 538
Cdd:cd05959 429 VQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYEDSEaleEELKEFVKDRLAPYKYPrWIVFVDELPKTATGKIQRFKLR 508
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
6-540 |
8.61e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 115.41 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 6 RVAVVTGPRAPVPTAPLTHHLGPLAKS---------DRTALIykDEISsvQVSHAELAARTNVLARAIseRARTVGPnrd 76
Cdd:PRK07788 28 GAVDLERPDNGLRLAADIRRYGPFAGLvahaarrapDRAALI--DERG--TLTYAELDEQSNALARGL--LALGVRA--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 77 sDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDD-------SADPSMFKESGVPFAS 149
Cdd:PRK07788 99 -GDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDeftdllsALPPDLGRLRAWGGNP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 150 FEELAQEATSHSADEPMDAETLAPLT--SDSIAIVLYTSGGTGIPKGVR-------LSYSAICNRLWWQfrtfpysdsee 220
Cdd:PRK07788 178 DDDEPSGSTDETLDDLIAGSSTAPLPkpPKPGGIVILTSGTTGTPKGAPrpepsplAPLAGLLSRVPFR----------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 221 icvwktaltfVDSVCEIWGPLLHG------------RALLILSRETtrDPQKLVNVLADNQIERLVLVPTLLRSIlmyLA 288
Cdd:PRK07788 247 ----------AGETTLLPAPMFHAtgwahltlamalGSTVVLRRRF--DPEATLEDIAKHKATALVVVPVMLSRI---LD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 289 LGPASRP---LRRLKLWVCSGETLSKELASEFFKYFgnedGYKLANFYGSTEvmgdVTYYVLEGSDQLDLYPTIpIGRPL 365
Cdd:PRK07788 312 LGPEVLAkydTSSLKIIFVSGSALSPELATRALEAF----GPVLYNLYGSTE----VAFATIATPEDLAEAPGT-VGRPP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 366 DNCAIYLLDEELSPTRDSEPGEVWVAGAnlaagyvggGGANRFCDNPHATQPDfqRLYRTGDFGTLVKGAVLY-AGRTDA 444
Cdd:PRK07788 383 KGVTVKILDENGNEVPRGVVGRIFVGNG---------FPFEGYTDGRDKQIID--GLLSSGDVGYFDEDGLLFvDGRDDD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 445 QVKIRGHRVDLLEVERALAQVPGVDKCVVLcyGLDrgNPE----ILGFVTTKPGARTSAQHIEGELRNALTHYMMPQ-VI 519
Cdd:PRK07788 452 MIVSGGENVFPAEVEDLLAGHPDVVEAAVI--GVD--DEEfgqrLRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRdVV 527
|
570 580
....*....|....*....|.
gi 223890156 520 EVESIPLLVNGKVDRQGLLKM 540
Cdd:PRK07788 528 FLDELPRNPTGKVLKRELREM 548
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
33-539 |
1.21e-26 |
|
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: 113.54 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERARTVGPNRdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd05941 1 DRIAIVDDGD----SITYADLVARAARLANRLLALGKDLRGDR-----VAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIyddsaDPsmfkesgvpfasfeelaqeatshsadepmdaetlapltsdsiAIVLYTSGGTGIP 192
Cdd:cd05941 72 PLAELEYVITDSEPSLVL-----DP------------------------------------------ALILYTSGTTGRP 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRL-----WWQFRTfpySDseeicVWKTAL-------TFVDSVCeiwgPLLHGRALLILSREttrDPQK 260
Cdd:cd05941 105 KGVVLTHANLAANVralvdAWRWTE---DD-----VLLHVLplhhvhgLVNALLC----PLFAGASVEFLPKF---DPKE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 261 LVNVLADNQIERLVLVPTLLRSILMYLAL------GPASRPLRRLKLWVCSGETLSKELASEFFKYFGNedgyKLANFYG 334
Cdd:cd05941 170 VAISRLMPSITVFMGVPTIYTRLLQYYEAhftdpqFARAAAAERLRLMVSGSAALPVPTLEEWEAITGH----TLLERYG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 335 STEVmGDVTYYVLEGsdqldlyPTIP--IGRPLDNCAIYLLDEELSPTRD-SEPGEVWVAGANLAAgyvgggganRFCDN 411
Cdd:cd05941 246 MTEI-GMALSNPLDG-------ERRPgtVGMPLPGVQARIVDEETGEPLPrGEVGEIQVRGPSVFK---------EYWNK 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 412 PHATQPDFQ--RLYRTGDFGTLVK-GAVLYAGRTDAQ-VKIRGHRVDLLEVERALAQVPGVDKCVVLcyGL---DRGNpE 484
Cdd:cd05941 309 PEATKEEFTddGWFKTGDLGVVDEdGYYWILGRSSVDiIKSGGYKVSALEIERVLLAHPGVSECAVI--GVpdpDWGE-R 385
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 485 ILGFVTTKPGART-SAQHIEGELRNALTHYMMPQ-VIEVESIPLLVNGKVDRQGLLK 539
Cdd:cd05941 386 VVAVVVLRAGAAAlSLEELKEWAKQRLAPYKRPRrLILVDELPRNAMGKVNKKELRK 442
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
22-537 |
1.88e-26 |
|
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: 113.72 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 22 LTHHLGPLAKS---DRTALIYKDEissvQVSHAELAARTNVLARAIseraRTVGPNRDSDyvIAVCMQPTHNTIMALLAT 98
Cdd:TIGR03098 1 LLHHLLEDAAArlpDATALVHHDR----TLTYAALSERVLALASGL----RGLGLARGER--VAIYLDKRLETVTAMFGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 99 WKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYD-------DSADPSMFKESGVpfASFEELAQEATSHSADEPM----- 166
Cdd:TIGR03098 71 ALAGGVFVPINPLLKAEQVAHILADCNVRLLVTSserldllHPALPGCHDLRTL--IIVGDPAHASEGHPGEEPAswpkl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 167 ----DAETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYS-----AICNRLWWQFRtfpySDSEEICVwkTALTFVDSVCEI 237
Cdd:TIGR03098 149 lalgDADPPHPVIDSDMAAILYTSGSTGRPKGVVLSHRnlvagAQSVATYLENR----PDDRLLAV--LPLSFDYGFNQL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 238 WGPLLHGRALLILSRETTRDpqkLVNVLADNQIERLVLVPTLLRSiLMYLALGP-ASRPLRRLklwVCSGETLSKELASE 316
Cdd:TIGR03098 223 TTAFYVGATVVLHDYLLPRD---VLKALEKHGITGLAAVPPLWAQ-LAQLDWPEsAAPSLRYL---TNSGGAMPRATLSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 317 FFKYFGNEDGYKLanfYGSTEVMGDvTYYVLEgsdQLDLYPTiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLA 396
Cdd:TIGR03098 296 LRSFLPNARLFLM---YGLTEAFRS-TYLPPE---EVDRRPD-SIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 397 AGYVGGGGANRFCDNPHATQPDFQRLYRTGDF-GTLVK----GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKC 471
Cdd:TIGR03098 368 MGYWNDPEKTAERFRPLPPFPGELHLPELAVWsGDTVRrdeeGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEA 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 472 VVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIEV-ESIPLLVNGKVDRQGL 537
Cdd:TIGR03098 448 VAFGVPDPTLGQAIVLVVTPPGGEELDRAALLAECRARLPNYMVPALIHVrQALPRNANGKIDRKAL 514
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
105-538 |
2.54e-26 |
|
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: 112.92 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 105 YVPMEPSFPQGRITHILKDAEPSLVIYDDSADpSMFKESGVpfasfeELAQEATSHSADEPMDAETLA---PLTSDSIAI 181
Cdd:cd05922 49 FVPLNPTLKESVLRYLVADAGGRIVLADAGAA-DRLRDALP------ASPDPGTVLDADGIRAARASApahEVSHEDLAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 182 VLYTSGGTGIPKGVRLSY-------SAICNRLWWQ-----FRTFPYSdseeicvWKTALTFVDSvceiwgPLLHGRALLI 249
Cdd:cd05922 122 LLYTSGSTGSPKLVRLSHqnllanaRSIAEYLGITaddraLTVLPLS-------YDYGLSVLNT------HLLRGATLVL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 250 lsRETTRDPQKLVNVLADNQIERLVLVPTLLrSILMYLALGPASRP-LRRLklwVCSGETLSKELASEFFKYFgneDGYK 328
Cdd:cd05922 189 --TNDGVLDDAFWEDLREHGATGLAGVPSTY-AMLTRLGFDPAKLPsLRYL---TQAGGRLPQETIARLRELL---PGAQ 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 329 LANFYGSTEVMGDVTYYVLEgsdQLDLYPTiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGYvgggganrF 408
Cdd:cd05922 260 VYVMYGQTEATRRMTYLPPE---RILEKPG-SIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGY--------W 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 409 CDNPHATQPD-FQRLYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDkcVVLCYGLDRGNPEIL 486
Cdd:cd05922 328 NDPPYRRKEGrGGGVLHTGDLARRDEDGFLFiVGRRDRMIKLFGNRISPTEIEAAARSIGLII--EAAAVGLPDPLGEKL 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 223890156 487 GFVTTKPgARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLL 538
Cdd:cd05922 406 ALFVTAP-DKIDPKDVLRSLAERLPPYKVPaTVRVVDELPLTASGKVDYAALR 457
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
94-534 |
4.37e-25 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 108.58 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 94 ALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDdsadpsmfkesgvpfasfeelaqeatshsadepmdaetlap 173
Cdd:cd05972 41 VILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD----------------------------------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 174 ltSDSIAIVLYTSGGTGIPKGVRLSYSA-----ICNRLWWQFRtfpysdSEEIcVWKTALT-FVDSV-CEIWGPLLHGrA 246
Cdd:cd05972 80 --AEDPALIYFTSGTTGLPKGVLHTHSYplghiPTAAYWLGLR------PDDI-HWNIADPgWAKGAwSSFFGPWLLG-A 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 247 LLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRsilMYLALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGnedg 326
Cdd:cd05972 150 TVFVYEGPRFDAERILELLERYGVTSFCGPPTAYR---MLIKQDLSSYKFSHLRLVVSAGEPLNPEVIEWWRAATG---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 327 YKLANFYGSTEVmgdvtyyvlegSDQLDLYPTIPI-----GRPLDNCAIYLLDEELSPTRDSEPGEVWVaganlaaGYVG 401
Cdd:cd05972 223 LPIRDGYGQTET-----------GLTVGNFPDMPVkpgsmGRPTPGYDVAIIDDDGRELPPGEEGDIAI-------KLPP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 402 GGGANRFCDNPHATQPDFQR-LYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygld 479
Cdd:cd05972 285 PGLFLGYVGDPEKTEASIRGdYYLTGDRAYRdEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVV----- 359
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223890156 480 rGNPE------ILGFVTTKPGARTS---AQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDR 534
Cdd:cd05972 360 -GSPDpvrgevVKAFVVLTSGYEPSeelAEELQGHVKKVLAPYKYPREIEfVEELPKTISGKIRR 423
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
48-532 |
5.34e-25 |
|
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: 108.62 E-value: 5.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 48 VSHAELAARTNVLARAIseRARTVGPnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPS 127
Cdd:cd05903 2 LTYSELDTRADRLAAGL--AALGVGP----GDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 128 LVIYddsadPSMFKEsgvpfasfeelaqeaTSHsADEPmdaetlapltsDSIAIVLYTSGGTGIPKGVRLSYSAICNRLW 207
Cdd:cd05903 76 VFVV-----PERFRQ---------------FDP-AAMP-----------DAVALLLFTSGTTGEPKGVMHSHNTLSASIR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 208 WQFRTFPYSDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRettRDPQKLVNVLADNQIERLVLVPTLLRSILMyl 287
Cdd:cd05903 124 QYAERLGLGPGDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTFMMGATPFLTDLLN-- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 288 ALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGNedgyKLANFYGSTEVMGDVTyyVLEGSDQLDLYPTIpiGRPLDN 367
Cdd:cd05903 199 AVEEAGEPLSRLRTFVCGGATVPRSLARRAAELLGA----KVCSAYGSTECPGAVT--SITPAPEDRRLYTD--GRPLPG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 368 CAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDFQRL-YRTGDFGTLVK-GAVLYAGRTdAQ 445
Cdd:cd05903 271 VEIKVVDDTGATLAPGVEGELLSRGPSVFLG---------YLDRPDLTADAAPEGwFRTGDLARLDEdGYLRITGRS-KD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 446 VKIR-GHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTS----AQHIEGElrNALTHYMMPQVIE 520
Cdd:cd05903 341 IIIRgGENIPVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTfdelVAYLDRQ--GVAKQYWPERLVH 418
|
490
....*....|..
gi 223890156 521 VESIPLLVNGKV 532
Cdd:cd05903 419 VDDLPRTPSGKV 430
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-537 |
1.54e-24 |
|
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: 106.99 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 47 QVSHAELAARTNVLARAIseRARTVGPnrdSDYVIAVCmqptHNTIMALLAtW----KAGAAYVPMEPSFPQGRITHILK 122
Cdd:cd05934 3 RWTYAELLRESARIAAAL--AALGIRP---GDRVALML----DNCPEFLFA-WfalaKLGAVLVPINTALRGDELAYIID 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 123 DAEPSLVIyddsADPSMfkesgvpfasfeelaqeatshsadepmdaetlapltsdsiaiVLYTSGGTGIPKGVRLSYSAI 202
Cdd:cd05934 73 HSGAQLVV----VDPAS------------------------------------------ILYTSGTTGPPKGVVITHANL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 203 CNRLWWQFRTFPYSDsEEICVWKTALTFVDSVCEIWGP-LLHGRALLILSRETTRdpqklvNVLAdnQIERL-VLVPTLL 280
Cdd:cd05934 107 TFAGYYSARRFGLGE-DDVYLTVLPLFHINAQAVSVLAaLSVGATLVLLPRFSAS------RFWS--DVRRYgATVTNYL 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 281 RSILMYLALGPASRPLRRLKLWVCSGETLSKELASEFFKYFgnedGYKLANFYGSTE----VMGDVTYYVLEGSdqldly 356
Cdd:cd05934 178 GAMLSYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERF----GVRLLEGYGMTEtivgVIGPRDEPRRPGS------ 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 357 ptipIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGAnlaagyVGGGGANRFCDNPHATQPDFQRL-YRTGDFGTL-VKG 434
Cdd:cd05934 248 ----IGRPAPGYEVRIVDDDGQELPAGEPGELVIRGL------RGWGFFKGYYNMPEATAEAMRNGwFHTGDLGYRdADG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 435 AVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVlcYGL--DRGNPEILGFVTTKPGARTSAQHIEGELRNALTH 512
Cdd:cd05934 318 FFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAV--VAVpdEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAY 395
|
490 500
....*....|....*....|....*.
gi 223890156 513 YMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:cd05934 396 FKVPRYIRfVDDLPKTPTEKVAKAQL 421
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
47-537 |
2.18e-24 |
|
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: 106.75 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 47 QVSHAELAARTNVLARAISERartvGPNRDSdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEP 126
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEI----GLEKGD--RVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 127 SLVIYDDSADPsmfkesgvpfasfeelaqeatshsadepmdaetlapltsdsiAIVLYTSGGTGIPKGVRLSYSAICNRL 206
Cdd:cd05971 80 SALVTDGSDDP------------------------------------------ALIIYTSGTTGPPKGALHAHRVLLGHL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 207 ---WWQFRTFPYSDSeeiCVWKTA-LTFVDSVCEIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRs 282
Cdd:cd05971 118 pgvQFPFNLFPRDGD---LYWTPAdWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALK- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 283 iLMYLALGPASRPLRRLKLWVCSGETLSKEL---ASEFFKYFGNEdgyklanFYGSTEvmgdvTYYVLegSDQLDLYPTI 359
Cdd:cd05971 194 -MMRQQGEQLKHAQVKLRAIATGGESLGEELlgwAREQFGVEVNE-------FYGQTE-----CNLVI--GNCSALFPIK 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 360 P--IGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGYVgggganrFCDNPHATQPDFQRLY-RTGDFGTL-VKGA 435
Cdd:cd05971 259 PgsMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAFLG-------YWNNPSATEKKMAGDWlLTGDLGRKdSDGY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 436 VLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGNPE------ILGFVTTKPGARTSaQHIEGELRN- 508
Cdd:cd05971 332 FWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVV------GIPDpirgeiVKAFVVLNPGETPS-DALAREIQEl 404
|
490 500 510
....*....|....*....|....*....|...
gi 223890156 509 ---ALTHYMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:cd05971 405 vktRLAAHEYPREIEfVNELPRTATGKIRRREL 437
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
31-537 |
3.14e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 103.83 E-value: 3.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 31 KSDRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdSDYViAVCMQPTHNTIMALLATWKAGAAYVPMEP 110
Cdd:PRK07656 18 FGDKEAYVFGDQ----RLTYAELNARVRRAAAAL--AALGIGK---GDRV-AIWAPNSPHWVIAALGALKAGAVVVPLNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 111 SFPQGRITHILKDAEPSLVIYDDSADPsMFKESGVPFASFEELAQEATSHSADEP-------------MDAETLAPLTSD 177
Cdd:PRK07656 88 RYTADEAAYILARGDAKALFVLGLFLG-VDYSATTRLPALEHVVICETEEDDPHTekmktftdflaagDPAERAPEVDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 178 SIAIVLYTSGGTGIPKGVRLS-------YSAICNRLwwQFRtfpySDSEEICVWKTALTFVDSVCeIWGPLLHGRALLIL 250
Cdd:PRK07656 167 DVADILFTSGTTGRPKGAMLThrqllsnAADWAEYL--GLT----EGDRYLAANPFFHVFGYKAG-VNAPLMRGATILPL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 251 SretTRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASrpLRRLKLWVCSGETLSKELASEFFKYFGNEdgyKLA 330
Cdd:PRK07656 240 P---VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAED--LSSLRLAVTGAASMPVALLERFESELGVD---IVL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 331 NFYGSTEVMGDVTYYVLEGSDQldlypTIP--IGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrF 408
Cdd:PRK07656 312 TGYGLSEASGVTTFNRLDDDRK-----TVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKG---------Y 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 409 CDNPHATQ----PDfQRLYrTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGNP 483
Cdd:PRK07656 378 YDDPEATAaaidAD-GWLH-TGDLGRLDEEGYLYiVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI------GVP 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223890156 484 -EILG-----FVTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:PRK07656 450 dERLGevgkaYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEfLDELPKNATGKVLKRAL 510
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
49-534 |
1.06e-22 |
|
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: 101.44 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 49 SHAELAARTNVLARAISERArtVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSL 128
Cdd:cd05973 2 TFGELRALSARFANALQELG--VGPGD----VVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 129 VIyddsadpsmfkesgvpfasfeelaqeatshsadepMDAETLAPLTSDSIaIVLYTSGGTGIPKGVRLSYSAICNrlWW 208
Cdd:cd05973 76 VV-----------------------------------TDAANRHKLDSDPF-VMMFTSGTTGLPKGVPVPLRALAA--FG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 209 QFRTFPYSDSEEICVWKTA-------LTFVdsvceIWGPLLHGRALLIL----SRETTRDpqklvnVLADNQIERLVLVP 277
Cdd:cd05973 118 AYLRDAVDLRPEDSFWNAAdpgwaygLYYA-----ITGPLALGHPTILLeggfSVESTWR------VIERLGVTNLAGSP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 278 TLLRSiLMYLALGPASRPLRRLKLWVCSGETLSKELASeffkYFGNEDGYKLANFYGSTEV---------MGDVtyyVLE 348
Cdd:cd05973 187 TAYRL-LMAAGAEVPARPKGRLRRVSSAGEPLTPEVIR----WFDAALGVPIHDHYGQTELgmvlanhhaLEHP---VHA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 349 GSdqldlyptipIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGYvgggganrFCDNPHATQPDFQ-RLYRTGD 427
Cdd:cd05973 259 GS----------AGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPLMW--------FRGYQLPDTPAIDgGYYLTGD 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 428 FGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGNP-----EIL-GFVTTKPGARTS-- 498
Cdd:cd05973 321 TVEFdPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVI------GVPdpertEVVkAFVVLRGGHEGTpa 394
|
490 500 510
....*....|....*....|....*....|....*...
gi 223890156 499 -AQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDR 534
Cdd:cd05973 395 lADELQLHVKKRLSAHAYPRTIHfVDELPKTPSGKIQR 432
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
33-532 |
1.98e-22 |
|
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: 101.88 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEISSV--QVSHAELAARTNVLARAISERARTVGPnrdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEP 110
Cdd:cd17634 68 DRTAIIYEGDDTSQsrTISYRELHREVCRFAGTLLDLGVKKGD------RVAIYMPMIPEAAVAMLACARIGAVHSVIFG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 111 SFPQGRITHILKDAEPSLVI-----------------YDDSADPS--------MFKESGVPFA-------SFEELAQEAT 158
Cdd:cd17634 142 GFAPEAVAGRIIDSSSRLLItadggvragrsvplkknVDDALNPNvtsvehviVLKRTGSDIDwqegrdlWWRDLIAKAS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 159 SHSADEPMDAETlaPLtsdsiaIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEICVWKTALTFV-DSVCEI 237
Cdd:cd17634 222 PEHQPEAMNAED--PL------FILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVGWVtGHSYLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 238 WGPLLHG-RALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRSILmylALGP---ASRPLRRLKLWVCSGETLSKEL 313
Cdd:cd17634 294 YGPLACGaTTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALM---AAGDdaiEGTDRSSLRILGSVGEPINPEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 314 ASEFFKYFGNEdGYKLANFYGSTEVMGDVTYyVLEGSDQLDL-YPTipigRPLDNCAIYLLDEELSPTRDSEPGEVWVAG 392
Cdd:cd17634 371 YEWYWKKIGKE-KCPVVDTWWQTETGGFMIT-PLPGAIELKAgSAT----RPVFGVQPAVVDNEGHPQPGGTEGNLVITD 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 393 ANLAAGYVGGGGANRFCDNPHATqpdFQRLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKC 471
Cdd:cd17634 445 PWPGQTRTLFGDHERFEQTYFST---FKGMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 223890156 472 VVLCYGLDRGNPEILGFVTTKPGArTSAQHIEGELRNALTHYMMP-----QVIEVESIPLLVNGKV 532
Cdd:cd17634 522 AVVGIPHAIKGQAPYAYVVLNHGV-EPSPELYAELRNWVRKEIGPlatpdVVHWVDSLPKTRSGKI 586
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
34-537 |
4.28e-22 |
|
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: 99.86 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 34 RTALIYKDEissvQVSHAELAARTNVLARAISERARTVGPNRdsdyviaVCMQPTHNTIMAllATW----KAGAAYVPME 109
Cdd:cd05958 1 RTCLRSPER----EWTYRDLLALANRIANVLVGELGIVPGNR-------VLLRGSNSPELV--ACWfgiqKAGAIAVATM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 110 PSFPQGRITHILKDAEPSLVIYDDsadpsmfkesgvpfasfeelaqeatshsadepmdAETlaplTSDSIAIVLYTSGGT 189
Cdd:cd05958 68 PLLRPKELAYILDKARITVALCAH----------------------------------ALT----ASDDICILAFTSGTT 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 190 GIPKGV---RLSYSAICnRLWWQFRTFPYSDSEEICVWKTALTFVDSVCEIWgPLLHGRALLILSRETtrdPQKLVNVLA 266
Cdd:cd05958 110 GAPKATmhfHRDPLASA-DRYAVNVLRLREDDRFVGSPPLAFTFGLGGVLLF-PFGVGASGVLLEEAT---PDLLLSAIA 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 267 DNQIERLVLVPTLLRSILmylALGPASRP-LRRLKLWVCSGETLSKELASEFFKYFGNE--DGYklanfyGSTEVmgdvt 343
Cdd:cd05958 185 RYKPTVLFTAPTAYRAML---AHPDAAGPdLSSLRKCVSAGEALPAALHRAWKEATGIPiiDGI------GSTEM----- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 344 YYVLEGSDQLDLYPTiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGYVGGGGANRFCDNPHATQPDFqrlY 423
Cdd:cd05958 251 FHIFISARPGDARPG-ATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRTYVQGGWNITGDTY---S 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 424 RTGDfgtlvkGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIE 503
Cdd:cd05958 327 RDPD------GYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVLAR 400
|
490 500 510
....*....|....*....|....*....|....*....
gi 223890156 504 gELRN----ALTHYMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:cd05958 401 -ELQDhakaHIAPYKYPRAIEfVTELPRTATGKLQRFAL 438
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
33-537 |
4.34e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 100.46 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERArtVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK13383 50 GRTAIIDDDG----ALSYRELQRATESLARRLTRDG--VAPGR----AVGVMCRNGRGFVTAVFAVGLLGADVVPISTEF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSadpsmFKESgVPFASFEELAQEATSHSADEPMDAETLAPltsdSIAIVLYTSGGTGIP 192
Cdd:PRK13383 120 RSDALAAALRAHHISTVVADNE-----FAER-IAGADDAVAVIDPATAGAEESGGRPAVAA----PGRIVLLTSGTTGKP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAicnrlwwqfrtfpysdSEEICVWKTALTF----VDSVCEIWGPLLHGRAL--LILSRET-----TRDPQKL 261
Cdd:PRK13383 190 KGVPRAPQL----------------RSAVGVWVTILDRtrlrTGSRISVAMPMFHGLGLgmLMLTIALggtvlTHRHFDA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 262 VNVLADNQIER---LVLVPTLLRSILMYLALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGNedgyKLANFYGSTEV 338
Cdd:PRK13383 254 EAALAQASLHRadaFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGD----ILYNGYGSTEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 339 -MGdvtyyVLEGSDQLDLYPTIpIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGanlaagyvgGGGANRFCDNPHATQP 417
Cdd:PRK13383 330 gIG-----ALATPADLRDAPET-VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG---------ELAGTRYTDGGGKAVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 418 DfqRLYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGAR 496
Cdd:PRK13383 395 D--GMTSTGDMGYLDNAGRLFiVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSG 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 223890156 497 TSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:PRK13383 473 VDAAQLRDYLKDRVSRFEQPRDINiVSSIPRNPTGKVLRKEL 514
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
33-543 |
2.12e-21 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 98.11 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISErartVGPNRDSdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK03640 17 DRTAIEFEEK----KVTFMELHEAVVSVAGKLAA----LGVKKGD--RVALLMKNGMEMILVIHALQQLGAVAVLLNTRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSADPsmfKESGVPFASFEELAQEATShsadepmDAETLAPLTSDSIAIVLYTSGGTGIP 192
Cdd:PRK03640 87 SREELLWQLDDAEVKCLITDDDFEA---KLIPGISVKFAELMNGPKE-------EAEIQEEFDLDEVATIMYTSGTTGKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSY-----SAICNRLWWQFRtfpysdsEEICvWKTALtfvdsvceiwgPLLHGRALLILSR----------ETTRD 257
Cdd:PRK03640 157 KGVIQTYgnhwwSAVGSALNLGLT-------EDDC-WLAAV-----------PIFHISGLSILMRsviygmrvvlVEKFD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 258 PQKLVNVLADNQIERLVLVPTLLRSIL--------------MYLALGPASRPLrrlkLWVCSgetlskelaseffkyfgn 323
Cdd:PRK03640 218 AEKINKLLQTGGVTIISVVSTMLQRLLerlgegtypssfrcMLLGGGPAPKPL----LEQCK------------------ 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 324 EDGYKLANFYGSTEVMGDVTY----YVLE--GSdqldlyptipIGRPLDNCAIYLLDeELSPTRDSEPGEVWVAGANLAA 397
Cdd:PRK03640 276 EKGIPVYQSYGMTETASQIVTlspeDALTklGS----------AGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 398 GyvgggganrFCDNPHATQPDFQR-LYRTGDFGTLVKGAVLYagrtdaqvkIRGHRVDLL----------EVERALAQVP 466
Cdd:PRK03640 345 G---------YLNREDATRETFQDgWFKTGDIGYLDEEGFLY---------VLDRRSDLIisggeniypaEIEEVLLSHP 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 467 GVDKCVVLcygldrGNP-EILGFVttkPGA--RTSAQHIEGEL----RNALTHYMMP-QVIEVESIPLLVNGKVDRQGLL 538
Cdd:PRK03640 407 GVAEAGVV------GVPdDKWGQV---PVAfvVKSGEVTEEELrhfcEEKLAKYKVPkRFYFVEELPRNASGKLLRHELK 477
|
....*
gi 223890156 539 KMYEN 543
Cdd:PRK03640 478 QLVEE 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
33-537 |
6.57e-21 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 96.75 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIykDEISSVqvSHAELAARTNVLARAISeraRTVGPNRDsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK13382 58 DRPGLI--DELGTL--TWRELDERSDALAAALQ---ALPIGEPR---VVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSADPSMFKE-SGVPFA--------SFEELAQEA--TSHSADEPMDAetlaPLTSDSIai 181
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSATVDRAlADCPQAtrivawtdEDHDLTVEVliAAHAGQRPEPT----GRKGRVI-- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 182 vLYTSGGTGIPKGVRLS-------YSAICNRLWWQfrtfpysdSEEICVwktaltfvdsvceIWGPLLHG-------RAL 247
Cdd:PRK13382 202 -LLTSGTTGTPKGARRSgpggigtLKAILDRTPWR--------AEEPTV-------------IVAPMFHAwgfsqlvLAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 248 LILSRETTR---DPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGNe 324
Cdd:PRK13382 260 SLACTIVTRrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD- 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 325 dgyKLANFYGSTEVmgdvTYYVLEGSDQLDLYPTIPiGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLaagyvgggg 404
Cdd:PRK13382 339 ---VIYNNYNATEA----GMIATATPADLRAAPDTA-GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQ--------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 405 anrFCDNPHATQPDFQRLY-RTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGN 482
Cdd:PRK13382 402 ---FDGYTSGSTKDFHDGFmASGDVGYLDENGRLFvVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYG 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 223890156 483 PEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIEV-ESIPLLVNGKVDRQGL 537
Cdd:PRK13382 479 QRLAAFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVlDELPRGATGKILRREL 534
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
92-537 |
5.71e-20 |
|
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: 93.74 E-value: 5.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 92 IMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIyddsadpsMFKESGVpfasfeelaqeatshsadepmdaeTL 171
Cdd:cd17647 59 MVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLI--------VIRAAGV------------------------VV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 172 APltsDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEIcvwkTALTFV--DSVC-EIWGPLLHGRALL 248
Cdd:cd17647 107 GP---DSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKF----TMLSGIahDPIQrDMFTPLFLGAQLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 249 ILSRETTRDPQKLVNVLADNQIERLVLVPTLLRsilmyLALGPASRPLRRLKLWVCSGETLSKElasEFFKYFGNEDGYK 328
Cdd:cd17647 180 VPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQ-----LLTAQATTPFPKLHHAFFVGDILTKR---DCLRLQTLAENVR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 329 LANFYGSTEVMGDVTYYVLEGSDQ----LD-LYPTIPIGRPLDNCAIYLLDEElSPTRD---SEPGEVWVAGANLAAGYV 400
Cdd:cd17647 252 IVNMYGTTETQRAVSYFEVPSRSSdptfLKnLKDVMPAGRGMLNVQLLVVNRN-DRTQIcgiGEVGEIYVRAGGLAEGYR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 401 GGGGAN--RFCDN------------PHATQPDFQ-------RLYRTGDFGT-LVKGAVLYAGRTDAQVKIRGHRVDLLEV 458
Cdd:cd17647 331 GLPELNkeKFVNNwfvepdhwnyldKDNNEPWRQfwlgprdRLYRTGDLGRyLPNGDCECCGRADDQVKIRGFRIELGEI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 459 ERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKP---------------------------GARTSAQHIEGELRNALT 511
Cdd:cd17647 411 DTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFdkpddesfaqedvpkevstdpivkgliGYRKLIKDIREFLKKRLA 490
|
490 500
....*....|....*....|....*..
gi 223890156 512 HYMMPQVIEV-ESIPLLVNGKVDRQGL 537
Cdd:cd17647 491 SYAIPSLIVVlDKLPLNPNGKVDKPKL 517
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
33-542 |
1.97e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 91.87 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARtnVLARAISERARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK06145 17 DRAALVYRDQ----EISYAEFHQR--ILQAAGMLHARGIGQGD----VVALLMKNSAAFLELAFAASYLGAVFLPINYRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDD--SADPSMfkesGVPFASFEELAQEATSHSADEPMDAETLAPLTSDSIAIVLYTSGGTG 190
Cdd:PRK06145 87 AADEVAYILGDAGAKLLLVDEefDAIVAL----ETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 191 IPKGVRLSYsaicNRLWWQfrtfpySDSEEICVWKTALTFVDSVceiwGPLLH-------GRALL----ILSRETTRDPQ 259
Cdd:PRK06145 163 RPKGVMHSY----GNLHWK------SIDHVIALGLTASERLLVV----GPLYHvgafdlpGIAVLwvggTLRIHREFDPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 260 KLVNVLADNQIERLVLVPTLLRSIlmyLALGPASR-PLRRLKLWVCSGETLSKELASEFFKYFGNEdgyKLANFYGSTEV 338
Cdd:PRK06145 229 AVLAAIERHRLTCAWMAPVMLSRV---LTVPDRDRfDLDSLAWCIGGGEKTPESRIRDFTRVFTRA---RYIDAYGLTET 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 339 MGDVTYyvLEGSDQLDLYPTipIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPD 418
Cdd:PRK06145 303 CSGDTL--MEAGREIEKIGS--TGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKG---------YWKDPEKTAEA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 419 F-QRLYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGAR 496
Cdd:PRK06145 370 FyGDWFRSGDVGYLDEEGFLYlTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGAT 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 223890156 497 TSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLLKMYE 542
Cdd:PRK06145 450 LTLEALDRHCRQRLASFKVPrQLKVRDELPRNPSGKVLKRVLRDELN 496
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
44-539 |
2.51e-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: 91.60 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 44 SSVQVSHAELAARTNVLARAISERARTVGPnrdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKD 123
Cdd:cd05926 11 STPALTYADLAELVDDLARQLAALGIKKGD------RVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 124 AEPSLVIYDDSADPSMFKESGVPFASFEELAQEATShsADEPMDAETLAPLTS-------------DSIAIVLYTSGGTG 190
Cdd:cd05926 85 LGSKLVLTPKGELGPASRAASKLGLAILELALDVGV--LIRAPSAESLSNLLAdkknaksegvplpDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 191 IPKGVRLSYSAICnrlwwqfrtfpySDSEEICvwKT-ALTFVDS-------------VCEIWGPLLHGRALLILSRettR 256
Cdd:cd05926 163 RPKGVPLTHRNLA------------ASATNIT--NTyKLTPDDRtlvvmplfhvhglVASLLSTLAAGGSVVLPPR---F 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 257 DPQKLVNVLADNQIERLVLVPTLLrSILMYLALGPASRPLRRLKLWVCSGETLSKELASEFFKYFgnedGYKLANFYGST 336
Cdd:cd05926 226 SASTFWPDVRDYNATWYTAVPTIH-QILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF----GAPVLEAYGMT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 337 EVMGDVTyyvlegSDQLDLYPTIP--IGRPlDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHA 414
Cdd:cd05926 301 EAAHQMT------SNPLPPGPRKPgsVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRG---------YLNNPEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 415 TQPDFQR--LYRTGDFGTLvkgavlyagRTDAQVKIRGHRVDL----------LEVERALAQVPGVDKCVVLC-----YG 477
Cdd:cd05926 365 NAEAAFKdgWFRTGDLGYL---------DADGYLFLTGRIKELinrggekispLEVDGVLLSHPAVLEAVAFGvpdekYG 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223890156 478 ldrgnPEILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGLLK 539
Cdd:cd05926 436 -----EEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPkKVYFVDELPKTATGKIQRRKVAE 493
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
75-679 |
9.01e-19 |
|
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: 91.28 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 75 RDSDYVIAVcmqpthntiMALLatwKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSA---DPSMFK--------ES 143
Cdd:TIGR03443 304 RGVDLVVAV---------MGVL---KAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAgtlDQLVRDyidkelelRT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 144 GVP-FASFEELAQEATSHSADEpmdAETLAPLTS------------DSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQF 210
Cdd:TIGR03443 372 EIPaLALQDDGSLVGGSLEGGE---TDVLAPYQAlkdtptgvvvgpDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMA 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 211 RTFPYSDSEEIcvwkTALTFV--DSVC-EIWGPLLHGRALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRsilmyL 287
Cdd:TIGR03443 449 KRFGLSENDKF----TMLSGIahDPIQrDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQ-----L 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 288 ALGPASRPLRRLKLWVCSGETLSKE-------LASEFFkyfgnedgykLANFYGSTEVMGDVTYYVL----EGSDQLD-L 355
Cdd:TIGR03443 520 LSAQATTPIPSLHHAFFVGDILTKRdclrlqtLAENVC----------IVNMYGTTETQRAVSYFEIpsrsSDSTFLKnL 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 356 YPTIPIGRPLDN--------------CAIylldeelsptrdSEPGEVWVAGANLAAGYVGGGGANR-------FCDNPHA 414
Cdd:TIGR03443 590 KDVMPAGKGMKNvqllvvnrndrtqtCGV------------GEVGEIYVRAGGLAEGYLGLPELNAekfvnnwFVDPSHW 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 415 TQPDFQ--------------RLYRTGDFGT-LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVL----- 474
Cdd:TIGR03443 658 IDLDKEnnkperefwlgprdRLYRTGDLGRyLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLvrrdk 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 475 -------CYGLDRGN-PEILGFVTTKPGARTSAQHIEG-------------ELRNALTHYMMPQVIEV-ESIPLLVNGKV 532
Cdd:TIGR03443 738 deeptlvSYIVPQDKsDELEEFKSEVDDEESSDPVVKGlikyrklikdireYLKKKLPSYAIPTVIVPlKKLPLNPNGKV 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 533 DRQGL----LKMYENTNNNDDAEvAVDIDCSG--AGLADLEAarALLETVGAvlgraargTLSLRSGFYELGGNSLNSIY 606
Cdd:TIGR03443 818 DKPALpfpdTAQLAAVAKNRSAS-AADEEFTEteREIRDLWL--ELLPNRPA--------TISPDDSFFDLGGHSILATR 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 607 TITKLRdRGYYVEISdfLGA----STL----GEILSKMSTDPNGGADSKEATFIAVPMRDEHKREV---IDMVVSSFYEK 675
Cdd:TIGR03443 887 MIFELR-KKLNVELP--LGLifksPTIkgfaKEVDRLKKGEELADEGDSEIEEEETVLELDYAKDAktlVDSLPKSYPSR 963
|
....
gi 223890156 676 AELE 679
Cdd:TIGR03443 964 KELD 967
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
16-540 |
1.90e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 89.03 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 16 PVPTAPLTHHLGPL------AKSDRTALIYKDeissVQVSHAELAARTNVLARAISE----RARTVG---PNRdSDY--- 79
Cdd:PRK06164 2 PHDAAPRADTLASLldaharARPDAVALIDED----RPLSRAELRALVDRLAAWLAAqgvrRGDRVAvwlPNC-IEWvvl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 80 ----------VIAVCMQPTHNTIMALLAtwKAGAAYVPMEPSFPQGRITHILKDAEPSLV-------IYDDSADPSMFKE 142
Cdd:PRK06164 77 flacarlgatVIAVNTRYRSHEVAHILG--RGRARWLVVWPGFKGIDFAAILAAVPPDALpplraiaVVDDAADATPAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 143 SGVPFASFEELAQEATSHSADEPMDAetlapltsDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEIC 222
Cdd:PRK06164 155 PGARVQLFALPDPAPPAAAGERAADP--------DAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 223 VwktaltfVDSVCEIWG-----PLLHGRALLILsrETTRDPQKLVNVLADNQIERLVLVPTLLRSILmylALGPASRPLR 297
Cdd:PRK06164 227 A-------ALPFCGVFGfstllGALAGGAPLVC--EPVFDAARTARALRRHRVTHTFGNDEMLRRIL---DTAGERADFP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 298 RLKLW-VCSGETLSKELASEffkyfGNEDGYKLANFYGSTEVMG---------DVTYYVLEGSdqLDLYPTIPIgRPLDN 367
Cdd:PRK06164 295 SARLFgFASFAPALGELAAL-----ARARGVPLTGLYGSSEVQAlvalqpatdPVSVRIEGGG--RPASPEARV-RARDP 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 368 caiylLDEELSPtrDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDFQR--LYRTGDFGTLV-KGAVLYAGRTDA 444
Cdd:PRK06164 367 -----QDGALLP--DGESGEIEIRAPSLMRG---------YLDNPDATARALTDdgYFRTGDLGYTRgDGQFVYQTRMGD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 445 QVKIRGHRVDLLEVERALAQVPGVDKCVVLcyGLDR-GNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQ-VIEVE 522
Cdd:PRK06164 431 SLRLGGFLVNPAEIEHALEALPGVAAAQVV--GATRdGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPArVQVVE 508
|
570 580
....*....|....*....|.
gi 223890156 523 SIPLLVNG---KVDRQGLLKM 540
Cdd:PRK06164 509 AFPVTESAngaKIQKHRLREM 529
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
94-542 |
1.96e-18 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 88.33 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 94 ALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIyddsadpsmfkesgvpfaSFEELAqeatshsadEPMDAETLAp 173
Cdd:cd05969 41 SMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI------------------TTEELY---------ERTDPEDPT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 174 ltsdsiaIVLYTSGGTGIPKGVRLSYSAICNrlWWQFRTFPYSDSEEICVWKTA----LTfvDSVCEIWGPLLHGraLLI 249
Cdd:cd05969 93 -------LLHYTSGTTGTPKGVLHVHDAMIF--YYFTGKYVLDLHPDDIYWCTAdpgwVT--GTVYGIWAPWLNG--VTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 250 LSRETTRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGnedgYKL 329
Cdd:cd05969 160 VVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSLRFIHSVGEPLNPEAIRWGMEVFG----VPI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 330 ANFYGSTEVmgdvtyyvleGSDQLDLYPTIPI-----GRPLDNCAIYLLDEELSPTRDSEPGevwvagaNLAAGYVGGGG 404
Cdd:cd05969 236 HDTWWQTET----------GSIMIANYPCMPIkpgsmGKPLPGVKAAVVDENGNELPPGTKG-------ILALKPGWPSM 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 405 ANRFCDNPHATQPDFQR-LYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGN 482
Cdd:cd05969 299 FRGIWNDEERYKNSFIDgWYLTGDLAYRdEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVI------GK 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 483 PE------ILGFVTTKPGARTSAQ---HIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQgLLKMYE 542
Cdd:cd05969 373 PDplrgeiIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEfVDNLPKTRSGKIMRR-VLKAKE 441
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
47-537 |
3.60e-18 |
|
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: 87.53 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 47 QVSHAELAARTNVLARAISERARtvgpnRDSDYViAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEP 126
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGV-----RKGDRV-GICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 127 SLVIyddsadpsmfkesgvpfasfeelaqeatshsadepmdaeTLAPLtsDSIAIVLYTSGGTGIPKGVRLSY-----SA 201
Cdd:cd05935 75 KVAV---------------------------------------VGSEL--DDLALIPYTSGTTGLPKGCMHTHfsaaaNA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 202 ICNRLWWQFR-------TFPYSDSEEicvwktaltFVDSVCeiwGPLLHGRALLILSRettRDPQKLVNVLADNQIERLV 274
Cdd:cd05935 114 LQSAVWTGLTpsdvilaCLPLFHVTG---------FVGSLN---TAVYVGGTYVLMAR---WDRETALELIEKYKVTFWT 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 275 LVPTLLRSILMylALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGnedgYKLANFYGSTEVMGDVTyyvlegsdqld 354
Cdd:cd05935 179 NIPTMLVDLLA--TPEFKTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG----LRFVEGYGLTETMSQTH----------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 355 lypTIPIGRPLDNC---------AIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDF-----Q 420
Cdd:cd05935 242 ---TNPPLRPKLQClgip*fgvdARVIDIETGRELPPNEVGEIVVRGPQIFKG---------YWNRPEETEESFieikgR 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 421 RLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGAR--T 497
Cdd:cd05935 310 RFFRTGDLGYMdEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRgkV 389
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 223890156 498 SAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:cd05935 390 TEEDIIEWAREQMAAYKYPREVEfVDELPRSASGKILWRLL 430
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
33-533 |
4.68e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 88.02 E-value: 4.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNrdsDYViAVCMqptHNTIM---ALLATWKAGAA----- 104
Cdd:PRK07798 18 DRVALVCGDR----RLTYAELEERANRLAHYL--IAQGLGPG---DHV-GIYA---RNRIEyveAMLGAFKARAVpvnvn 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 105 --YVPMEpsfpqgrITHILKDAEPSLVIYDDSADP----------------SMFKESGVPFASFEELAQEATSHSADEPM 166
Cdd:PRK07798 85 yrYVEDE-------LRYLLDDSDAVALVYEREFAPrvaevlprlpklrtlvVVEDGSGNDLLPGAVDYEDALAAGSPERD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 167 DAETlaplTSDSIaIVLYTSGGTGIPKGVrlsysaicnrLWWQ------------FRTFPYSDSEEICVWKTALTFVDSV 234
Cdd:PRK07798 158 FGER----SPDDL-YLLYTGGTTGMPKGV----------MWRQedifrvllggrdFATGEPIEDEEELAKRAAAGPGMRR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 235 CEIwGPLLHGRAL------------LILSRETTRDPQKLVNVLADNQIERLVLV------PtLLRsilmylALGPASRP- 295
Cdd:PRK07798 223 FPA-PPLMHGAGQwaafaalfsgqtVVLLPDVRFDADEVWRTIEREKVNVITIVgdamarP-LLD------ALEARGPYd 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 296 LRRLKLWVCSGETLSKELASEFFKYFGNedgYKLANFYGSTE--VMGDVTyyVLEGSDQLDlYPTIPIGRpldNCAiyLL 373
Cdd:PRK07798 295 LSSLFAIASGGALFSPSVKEALLELLPN---VVLTDSIGSSEtgFGGSGT--VAKGAVHTG-GPRFTIGP---RTV--VL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 374 DEELSPTRDSEPGEVWVA-GANLaagyvggggANRFCDNPHATQPDF-----QRLYRTGDFGTL-VKGAVLYAGRTDAQV 446
Cdd:PRK07798 364 DEDGNPVEPGSGEIGWIArRGHI---------PLGYYKDPEKTAETFptidgVRYAIPGDRARVeADGTITLLGRGSVCI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 447 KIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIP 525
Cdd:PRK07798 435 NTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPrAIWFVDEVQ 514
|
....*...
gi 223890156 526 LLVNGKVD 533
Cdd:PRK07798 515 RSPAGKAD 522
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
30-224 |
5.34e-18 |
|
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: 87.68 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 30 AKSDRTALIY--KDEISSVQVSHAELAARTNVLARAISERARTvgpnrdSDYVIAVCMQPTHNTImALLATWKAGAAYVP 107
Cdd:cd05931 5 ARPDRPAYTFldDEGGREETLTYAELDRRARAIAARLQAVGKP------GDRVLLLAPPGLDFVA-AFLGCLYAGAIAVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 108 M---EPSFPQGRITHILKDAEPSLVIYDDSADPSmFKESGVPFASFEELAQEATSHSADEPMDAETLAPLTSDSIAIVLY 184
Cdd:cd05931 78 LpppTPGRHAERLAAILADAGPRVVLTTAAALAA-VRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 223890156 185 TSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEICVW 224
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSW 196
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
178-535 |
2.11e-17 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 83.92 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 178 SIAIVLYTSGGTGIPKGVRLSYS-------AICNRLwwQFrtfpysDSEEICVWKTALTFVDSVCEIWGPLLHGRALLIL 250
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAnllasaaGLHSRL--GF------GGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 251 SREttrdpQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASRPLRRLKLwvcSGETLSKELASEFFKYfgnedGYKLA 330
Cdd:cd17630 73 ERN-----QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLL---GGAPIPPELLERAADR-----GIPLY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 331 NFYGSTEVMGDVTYYVLEGSDQLDLYPTIPiGRPLdncaiylldeelsptRDSEPGEVWVAGANLAAGYVGGGGANRFCD 410
Cdd:cd17630 140 TTYGMTETASQVATKRPDGFGRGGVGVLLP-GREL---------------RIVEDGEIWVGGASLAMGYLRGQLVPEFNE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 411 NPhatqpdfqrLYRTGDFGTLVKGAVLYA-GRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFV 489
Cdd:cd17630 204 DG---------WFTTKDLGELHADGRLTVlGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 223890156 490 TTKPGARTSAqhIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQ 535
Cdd:cd17630 275 VGRGPADPAE--LRAWLKDKLARFKLPkRIYPVPELPRTGGGKVDRR 319
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
184-534 |
5.97e-17 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 82.45 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 184 YTSGGTGIPKGVRLSYsaicnRLWWQF----RTFPYSDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSretTRDPQ 259
Cdd:cd17633 7 FTSGTTGLPKAYYRSE-----RSWIESfvcnEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFNPK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 260 KLVNVLADNQIERLVLVPTLLRSILMYLalgpasRPLRRLKLWVCSGETLSKELASEFFKYFGNEdgyKLANFYGSTEvM 339
Cdd:cd17633 79 SWIRKINQYNATVIYLVPTMLQALARTL------EPESKIKSIFSSGQKLFESTKKKLKNIFPKA---NLIEFYGTSE-L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 340 GDVTYYVLEgsdqlDLYPTIPIGRPLDNCAIYLLDEElsptrDSEPGEVWVAGANLAAGYVGGGganrfCDNPHAtqpdf 419
Cdd:cd17633 149 SFITYNFNQ-----ESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGG-----FSNPDG----- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 420 qrLYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNpEILGFVTTkpGARTS 498
Cdd:cd17633 209 --WMSVGDIGYVDEEGYLYlVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFG-EIAVALYS--GDKLT 283
|
330 340 350
....*....|....*....|....*....|....*..
gi 223890156 499 AQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDR 534
Cdd:cd17633 284 YKQLKRFLKQKLSRYEIPkKIIFVDSLPYTSSGKIAR 320
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
179-534 |
2.23e-16 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 81.15 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 179 IAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETTRdp 258
Cdd:cd17635 3 PLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 259 QKLVNVLADNQIERLVLVPTLLRSI-LMYLALGPASRPLRrlklWVCSGETLSKELASEFFKYFGNEdgyKLANFYGSTE 337
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLvSELKSANATVPSLR----LIGYGGSRAIAADVRFIEATGLT---NTAQVYGLSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 338 VmGDVTyYVLEGSDQLDLYptiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWV-AGANLAAgyvgggganrFCDNPHATQ 416
Cdd:cd17635 154 T-GTAL-CLPTDDDSIEIN---AVGRPYPGVDVYLAATDGIAGPSASFGTIWIkSPANMLG----------YWNNPERTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 417 PDFQRLY-RTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVvlCYGL---DRGNPEILGFVTT 491
Cdd:cd17635 219 EVLIDGWvNTGDLGERREDGFLFiTGRSSESINCGGVKIAPDEVERIAEGVSGVQECA--CYEIsdeEFGELVGLAVVAS 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 223890156 492 KPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDR 534
Cdd:cd17635 297 AELDENAIRALKHTIRRELEPYARPSTIViVTDIPRTQSGKVKR 340
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
44-543 |
4.28e-16 |
|
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: 81.94 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 44 SSVQVSHAELAARtnvlARAISERARTVGpNRDSDYVIAVCmQPTHNTIMALLATWKAGAAYVPM-------EPSFPQGR 116
Cdd:cd05906 36 SEEFQSYQDLLED----ARRLAAGLRQLG-LRPGDSVILQF-DDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 117 ITHILKDAEPSLVIyddsADPSMFKEsgvpFASFEELAQEA--TSHSADEPMDAETLAPL---TSDSIAIVLYTSGGTGI 191
Cdd:cd05906 110 LRHIWQLLGSPVVL----TDAELVAE----FAGLETLSGLPgiRVLSIEELLDTAADHDLpqsRPDDLALLMLTSGSTGF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 192 PKGVRLSYSAICNRLWWQFRTFPYSDSEEICVWK-----TALTFvdsvCEIWGPLLHGRALLILSRETTRDPQKLVNVLA 266
Cdd:cd05906 182 PKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVpldhvGGLVE----LHLRAVYLGCQQVHVPTEEILADPLRWLDLID 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 267 DNQIER-------LVLVPTLLRSIlmylalGPASRPLRRLKLWVCSGETLSKELASEFF----KYFGNEDGYKLAnfYGS 335
Cdd:cd05906 258 RYRVTItwapnfaFALLNDLLEEI------EDGTWDLSSLRYLVNAGEAVVAKTIRRLLrllePYGLPPDAIRPA--FGM 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 336 TEVMGDVTYYVLEGSDQLDLYPT-IPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAagyvggggaNRFCDNPHA 414
Cdd:cd05906 330 TETCSGVIYSRSFPTYDHSQALEfVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVT---------KGYYNNPEA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 415 TQPDFQR--LYRTGDFGTLVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGL-DRGNPE---ILGF 488
Cdd:cd05906 401 NAEAFTEdgWFRTGDLGFLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVrDPGAETeelAIFF 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223890156 489 VTT-KPGARTSAQH--IEGELRNALT---HYMMPqvIEVESIPLLVNGKVDRQGLLKMYEN 543
Cdd:cd05906 481 VPEyDLQDALSETLraIRSVVSREVGvspAYLIP--LPKEEIPKTSLGKIQRSKLKAAFEA 539
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
33-537 |
9.06e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 80.80 E-value: 9.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDeissVQVSHAELAARTNVLARAIseraRTVGPNRDSDYVIAVCMQPthNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK06188 27 DRPALVLGD----TRLTYGQLADRISRYIQAF----EALGLGTGDAVALLSLNRP--EVLMAIGAAQLAGLRRTALHPLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIyddsADPSMFKESGV----------------PFASFEELAQEATShSADEPMDAETLAPlts 176
Cdd:PRK06188 97 SLDDHAYVLEDAGISTLI----VDPAPFVERALallarvpslkhvltlgPVPDGVDLLAAAAK-FGPAPLVAAALPP--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 177 dSIAIVLYTSGGTGIPKGVRLSYSAIcnrlwWQFRTFPYSDSEeicvWKTALTFVdsVCEiwgPLLHGRALLIL------ 250
Cdd:PRK06188 169 -DIAGLAYTGGTTGKPKGVMGTHRSI-----ATMAQIQLAEWE----WPADPRFL--MCT---PLSHAGGAFFLptllrg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 251 -SRETTR--DPQKLVNVLADNQIERLVLVPTLLRSILMYLALgpASRPLRRLKLWVCSGETLSKELASEFFKYFGNedgy 327
Cdd:PRK06188 234 gTVIVLAkfDPAEVLRAIEEQRITATFLVPTMIYALLDHPDL--RTRDLSSLETVYYGASPMSPVRLAEAIERFGP---- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 328 KLANFYGSTEVMGDVTYYvlegsDQLDLYPTIP-----IGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAagyvgg 402
Cdd:PRK06188 308 IFAQYYGQTEAPMVITYL-----RKRDHDPDDPkrltsCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVM------ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 403 ggaNRFCDNPHATQPDFQRLY-RTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDR 480
Cdd:PRK06188 377 ---DGYWNRPEETAEAFRDGWlHTGDVAREDEDGFYYiVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEK 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223890156 481 GNPEILGFVTTKPGARTSAQhiegELRNALTHYMMP-----QVIEVESIPLLVNGKVDRQGL 537
Cdd:PRK06188 454 WGEAVTAVVVLRPGAAVDAA----ELQAHVKERKGSvhapkQVDFVDSLPLTALGKPDKKAL 511
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
37-468 |
9.75e-16 |
|
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: 80.18 E-value: 9.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 37 LIYKDEissvQVSHAELAARTNVLARAISERARTVGPNrdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGR 116
Cdd:cd05914 1 LYYGGE----PLTYKDLADNIAKFALLLKINGVGTGDR------VALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 117 ITHILKDAEPSLViyddsadpsmfkesgvpFASFEelaqeatshsadepmdaetlapltsDSIAIVLYTSGGTGIPKGVR 196
Cdd:cd05914 71 VHHILNHSEAKAI-----------------FVSDE-------------------------DDVALINYTSGTTGNSKGVM 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 197 LSYsaicNRLWWQ----FRTFPYSDSEEIC-------VWKTALTFVDsvceiwgPLLHGRALLILsretTRDPQKLVNVL 265
Cdd:cd05914 109 LTY----RNIVSNvdgvKEVVLLGKGDKILsilplhhIYPLTFTLLL-------PLLNGAHVVFL----DKIPSAKIIAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 266 ADNQIERLVLVPTLL---------------RSILMY-LALGPASRPLR-------------RLKLWVCSGETLSKELAsE 316
Cdd:cd05914 174 AFAQVTPTLGVPVPLviekifkmdiipkltLKKFKFkLAKKINNRKIRklafkkvheafggNIKEFVIGGAKINPDVE-E 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 317 FFKyfgnEDGYKLANFYGSTEVMGDVTYYVlEGSDQLDlyptiPIGRPLDN--CAIYlldeelSPTRDSEPGEVWVAGAN 394
Cdd:cd05914 253 FLR----TIGFPYTIGYGMTETAPIISYSP-PNRIRLG-----SAGKVIDGveVRID------SPDPATGEGEIIVRGPN 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223890156 395 LAAGyvgggganrFCDNPHATQPDFQR--LYRTGDFGTLVKGAVLY-AGRT-DAQVKIRGHRVDLLEVERALAQVPGV 468
Cdd:cd05914 317 VMKG---------YYKNPEATAEAFDKdgWFHTGDLGKIDAEGYLYiRGRKkEMIVLSSGKNIYPEEIEAKINNMPFV 385
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
33-534 |
1.10e-15 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 80.62 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEIS-SVQVSHAELAARTNVLARAIseRARTVGpnrDSDYVIAVcMQPTHNTIMALLATWKAGAAYVPMEPS 111
Cdd:cd05970 32 DKLALVWCDDAGeERIFTFAELADYSDKTANFF--KAMGIG---KGDTVMLT-LKRRYEFWYSLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 112 FPQGRITHILKDAEPSLVIYDDSAD-PSMFKES---------------GVP--FASFEELAQEAtshSAD-EPMDAETLA 172
Cdd:cd05970 106 LTAKDIVYRIESADIKMIVAIAEDNiPEEIEKAapecpskpklvwvgdPVPegWIDFRKLIKNA---SPDfERPTANSYP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 173 plTSDSIAIVLYTSGGTGIPKGVRLSYS----AICNRLWWQ-----FRTFPYSDSE-EICVWKtaltfvdsvcEIWGPLL 242
Cdd:cd05970 183 --CGEDILLVYFSSGTTGMPKMVEHDFTyplgHIVTAKYWQnvregGLHLTVADTGwGKAVWG----------KIYGQWI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 243 HGRALLILSRETTrDPQKLVNVLADNQIERLVLVPTLLRsilmYLALGPASR-PLRRLKLWVCSGETLSKELasefFKYF 321
Cdd:cd05970 251 AGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTIYR----FLIREDLSRyDLSSLRYCTTAGEALNPEV----FNTF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 322 GNEDGYKLANFYGSTE-VMGDVTYYVLE---GSdqldlyptipIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANlaa 397
Cdd:cd05970 322 KEKTGIKLMEGFGQTEtTLTIATFPWMEpkpGS----------MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSK--- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 398 gYVGGGGANRFCDNPHATQPDFQR-LYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLC 475
Cdd:cd05970 389 -GKPVGLFGGYYKDAEKTAEVWHDgYYHTGDAAWMDEdGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTG 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223890156 476 YGLDRGNPEILGFVTTKPGARTSaQHIEGELRNALTH----YMMPQVIE-VESIPLLVNGKVDR 534
Cdd:cd05970 468 VPDPIRGQVVKATIVLAKGYEPS-EELKKELQDHVKKvtapYKYPRIVEfVDELPKTISGKIRR 530
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
33-203 |
6.97e-15 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 78.22 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEISSVQVSHAELAARTNVLARAIseRARTVGPNrdsDyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:COG1022 26 DRVALREKEDGIWQSLTWAEFAERVRALAAGL--LALGVKPG---D-RVAILSDNRPEWVIADLAILAAGAVTVPIYPTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAE----------------------PSL--VIYDDSADPsmfkESGVPFASFEELAQEATSHSADEPMDa 168
Cdd:COG1022 100 SAEEVAYILNDSGakvlfvedqeqldkllevrdelPSLrhIVVLDPRGL----RDDPRLLSLDELLALGREVADPAELE- 174
|
170 180 190
....*....|....*....|....*....|....*
gi 223890156 169 ETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAIC 203
Cdd:COG1022 175 ARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLL 209
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
20-538 |
1.16e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 76.95 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 20 APLTHHLGPLAKSDRTALiykdEISSVQVSHAELAArtnvLARAISERARTVGPnrdsdyvIAVCMQPTHNTIMALLATW 99
Cdd:PRK07787 2 ASLNPAAVAAAADIADAV----RIGGRVLSRSDLAG----AATAVAERVAGARR-------VAVLATPTLATVLAVVGAL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 100 KAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPSmfkesGVPFASFEELAQEAtsHSADEPmdaetlaplTSDSI 179
Cdd:PRK07787 67 IAGVPVVPVPPDSGVAERRHILADSGAQAWLGPAPDDPA-----GLPHVPVRLHARSW--HRYPEP---------DPDAP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 180 AIVLYTSGGTGIPKGVRLSYSAICNRL-----WWQFrtfpysDSEEICVWKTALTFVDS-VCEIWGPLLHGRALLILSRE 253
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLdalaeAWQW------TADDVLVHGLPLFHVHGlVLGVLGPLRIGNRFVHTGRP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 254 TtrdPQKLVNVLADNQiERLVLVPTllrsilMY--LALGPAS-RPLRRLKLWVcSGetlSKELASEFFKYFGNEDGYKLA 330
Cdd:PRK07787 205 T---PEAYAQALSEGG-TLYFGVPT------VWsrIAADPEAaRALRGARLLV-SG---SAALPVPVFDRLAALTGHRPV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 331 NFYGSTEVMGDVTYYVlEGSDQLDLyptipIGRPLDNCAIYLLDEELSP-TRDSEP-GEVWVAGANLAAGyvgggganrF 408
Cdd:PRK07787 271 ERYGMTETLITLSTRA-DGERRPGW-----VGLPLAGVETRLVDEDGGPvPHDGETvGELQVRGPTLFDG---------Y 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 409 CDNPHATQPDFQR--LYRTGDFGTL-VKGAVLYAGR--TDAqVKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGNP 483
Cdd:PRK07787 336 LNRPDATAAAFTAdgWFRTGDVAVVdPDGMHRIVGResTDL-IKSGGYRIGAGEIETALLGHPGVREAAVV------GVP 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223890156 484 E------ILGFV--TTKPGARTSAQHIEGElrnaLTHYMMPQVIE-VESIPLLVNGKVDRQGLL 538
Cdd:PRK07787 409 DddlgqrIVAYVvgADDVAADELIDFVAQQ----LSVHKRPREVRfVDALPRNAMGKVLKKQLL 468
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
177-537 |
1.64e-14 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 76.23 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 177 DSIAIVLYTSGGTGIPKGVRLSY-----SAICNRLWWQFRtfpysdsEEICvWKTALtfvdsvceiwgPLLHGRALLILS 251
Cdd:cd05912 77 DDIATIMYTSGTTGKPKGVQQTFgnhwwSAIGSALNLGLT-------EDDN-WLCAL-----------PLFHISGLSILM 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 252 RE-----TTR-----DPQKLVNVLADNQIERLVLVPTLLRSIL-------------MYLALGPASRPLrrlkLWVCSget 308
Cdd:cd05912 138 RSviygmTVYlvdkfDAEQVLHLINSGKVTIISVVPTMLQRLLeilgegypnnlrcILLGGGPAPKPL----LEQCK--- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 309 lskelaseffkyfgnEDGYKLANFYGSTEVMGD-VTYYVLEGSDQLDlyptiPIGRPLDNCAIYLLDEELSPtrdSEPGE 387
Cdd:cd05912 211 ---------------EKGIPVYQSYGMTETCSQiVTLSPEDALNKIG-----SAGKPLFPVELKIEDDGQPP---YEVGE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 388 VWVAGANLaagyvggggANRFCDNPHATQPDFQRLY-RTGDFGTLVKGAVLYagrtdaqvkIRGHRVDLL---------- 456
Cdd:cd05912 268 ILLKGPNV---------TKGYLNRPDATEESFENGWfKTGDIGYLDEEGFLY---------VLDRRSDLIisggeniypa 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 457 EVERALAQVPGVDKCVVLcyGLDR---GNPEILGFVTTKPgarTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKV 532
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVV--GIPDdkwGQVPVAFVVSERP---ISEEELIAYCSEKLAKYKVPKKIYfVDELPRTASGKL 404
|
....*
gi 223890156 533 DRQGL 537
Cdd:cd05912 405 LRHEL 409
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
17-537 |
3.77e-14 |
|
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: 75.35 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 17 VPTAPLTH---HLGPLAKSDRTALIykDEISSVQVSHAELAARTNVLARAISERARTVG-------PNrDSDYVIAVcmq 86
Cdd:cd05904 1 LPTDLPLDsvsFLFASAHPSRPALI--DAATGRALTYAELERRVRRLAAGLAKRGGRKGdvvlllsPN-SIEFPVAF--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 87 pthntiMALLAtwkAGAAYVPMEPSFPQGRITHILKDAEPSLVIyddsADPSMF---KESGVPFASFEELAQEATSHSAD 163
Cdd:cd05904 75 ------LAVLS---LGAVVTTANPLSTPAEIAKQVKDSGAKLAF----TTAELAeklASLALPVVLLDSAEFDSLSFSDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 164 EPMDAETLAP---LTSDSIAIVLYTSGGTGIPKGVRLS---YSAICNRLWWQFRTFPYSDSEEICVwktaLTFvdsvCEI 237
Cdd:cd05904 142 LFEADEAEPPvvvIKQDDVAALLYSSGTTGRSKGVMLThrnLIAMVAQFVAGEGSNSDSEDVFLCV----LPM----FHI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 238 WG-------PLLHGRALLILSRettRDPQKLVNVLADNQIERLVLVPtllrSILMYLALGPA--SRPLRRLKLWVCSGET 308
Cdd:cd05904 214 YGlssfalgLLRLGATVVVMPR---FDLEELLAAIERYKVTHLPVVP----PIVLALVKSPIvdKYDLSSLRQIMSGAAP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 309 LSKELASEFFKYFGNEDgykLANFYGSTEVMGDVTYYVLEGSDQLdlyPTIPIGRPLDNCAIYLLD----EELSPTRdse 384
Cdd:cd05904 287 LGKELIEAFRAKFPNVD---LGQGYGMTESTGVVAMCFAPEKDRA---KYGSVGRLVPNVEAKIVDpetgESLPPNQ--- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 385 PGEVWVAGANLAAGyvgggganrFCDNPHATQP--DFQRLYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERA 461
Cdd:cd05904 358 TGELWIRGPSIMKG---------YLNNPEATAAtiDKEGWLHTGDLCYIDEDGYLFiVDRLKELIKYKGFQVAPAELEAL 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223890156 462 LAQVPGV-DKCVVLCYGLDRGnpEI-LGFVTTKPGARTSAQHIEGELRNALTHY-MMPQVIEVESIPLLVNGKVDRQGL 537
Cdd:cd05904 429 LLSHPEIlDAAVIPYPDEEAG--EVpMAFVVRKPGSSLTEDEIMDFVAKQVAPYkKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
33-540 |
4.00e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 75.28 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERARTVGPNRdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK06839 17 DRIAIITEEE----EMTYKQLHEYVSKVAAYLIYELNVKKGER-----IAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYD---DSADPSMFKESGV-PFASFEELAqEATSHSADEPMDAETLAPLtsdsiaIVLYTSGG 188
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEktfQNMALSMQKVSYVqRVISITSLK-EIEDRKIDNFVEKNESASF------IICYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 189 TGIPKGVRLS-----YSAICNRLWWQFRtfpysdSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRETtrDPQKLVN 263
Cdd:PRK06839 161 TGKPKGAVLTqenmfWNALNNTFAIDLT------MHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRKF--EPTKALS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 264 VLADNQIERLVLVPTLLRSILMylALGPASRPLRRLKLWVCSGETLSKELASEFfkyfgNEDGYKLANFYGSTEVMGDVt 343
Cdd:PRK06839 233 MIEKHKVTVVMGVPTIHQALIN--CSKFETTNLQSVRWFYNGGAPCPEELMREF-----IDRGFLFGQGFGMTETSPTV- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 344 YYVLE-------GSdqldlyptipIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLaagyvggggANRFCDNPHATQ 416
Cdd:PRK06839 305 FMLSEedarrkvGS----------IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNV---------MKEYWNRPDATE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 417 PDFQR-LYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPG 494
Cdd:PRK06839 366 ETIQDgWLCTGDLARVdEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSS 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 223890156 495 ARTSAQHIEGELRNALTHYMMPQ-VIEVESIPLLVNGKVDRQGLLKM 540
Cdd:PRK06839 446 SVLIEKDVIEHCRLFLAKYKIPKeIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
81-540 |
5.45e-14 |
|
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: 75.06 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 81 IAVCMQPTHNTIMALLATwkAGAAYVPMEPSFPQG--RITHILKDAEPSLVIYDD------SADPSMFKESGVPFASFEE 152
Cdd:cd05909 34 VGVMLPPSAGGALANFAL--ALSGKVPVMLNYTAGlrELRACIKLAGIKTVLTSKqfieklKLHHLFDVEYDARIVYLED 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 153 LAQEAT-----------SHSADEPMDAETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEI 221
Cdd:cd05909 112 LRAKISkadkckaflagKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 222 CvwkTALTFVDS----VCeIWGPLLHGRALLILSRETtrDPQKLVNVLADNQIERLVLVPTLLRSILMYLalgpASRPLR 297
Cdd:cd05909 192 F---GALPFFHSfgltGC-LWLPLLSGIKVVFHPNPL--DYKKIPELIYDKKATILLGTPTFLRGYARAA----HPEDFS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 298 RLKLWVCSGETLSKELASEFFKYFgnedGYKLANFYGSTEV-----MGDVTYYVLEGSdqldlyptipIGRPLDNCAIYL 372
Cdd:cd05909 262 SLRLVVAGAEKLKDTLRQEFQEKF----GIRILEGYGTTECspvisVNTPQSPNKEGT----------VGRPLPGMEVKI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 373 LDEE-LSPTRDSEPGEVWVAGANLaagyvggggANRFCDNPHATQPDFQR-LYRTGDFGTLVKGAVLY-AGRTDAQVKIR 449
Cdd:cd05909 328 VSVEtHEEVPIGEGGLLLVRGPNV---------MLGYLNEPELTSFAFGDgWYDTGDIGKIDGEGFLTiTGRLSRFAKIA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 450 GHRVDLLEVERALAQVPGVDK--CVVLCYGLDRGNPEILgFVTTKPGARTsaqhiegELRNALTHYMMPQ------VIEV 521
Cdd:cd05909 399 GEMVSLEAIEDILSEILPEDNevAVVSVPDGRKGEKIVL-LTTTTDTDPS-------SLNDILKNAGISNlakpsyIHQV 470
|
490
....*....|....*....
gi 223890156 522 ESIPLLVNGKVDRQGLLKM 540
Cdd:cd05909 471 EEIPLLGTGKPDYVTLKAL 489
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
29-553 |
7.56e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 74.81 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 29 LAKSDRTALIYKdeisSVQVSHAELAARTNVLARAISERARTVGpnrdsDYVIAVCMQPTHnTIMALLATWKAGAAYVPM 108
Cdd:PRK07786 28 LMQPDAPALRFL----GNTTTWRELDDRVAALAGALSRRGVGFG-----DRVLILMLNRTE-FVESVLAANMLGAIAVPV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 109 EPSFPQGRITHILKDAEPSLVIYDDSADP----------------SMFKESGVPFASFEELAQEATShsADEPMDaetla 172
Cdd:PRK07786 98 NFRLTPPEIAFLVSDCGAHVVVTEAALAPvatavrdivpllstvvVAGGSSDDSVLGYEDLLAEAGP--AHAPVD----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 173 pLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEIcvwktalTFVDSvceiwgPLLHGRAL----- 247
Cdd:PRK07786 171 -IPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDV-------GFVGV------PLFHIAGIgsmlp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 248 -LILSRETTR------DPQKLVNVLADNQIERLVLVPTLLRSILMylalGPASRPlRRLKLWVCS------GETLSKELA 314
Cdd:PRK07786 237 gLLLGAPTVIyplgafDPGQLLDVLEAEKVTGIFLVPAQWQAVCA----EQQARP-RDLALRVLSwgaapaSDTLLRQMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 315 SEFfkyfgnEDGYKLAnFYGSTEvMGDVTyYVLEGSDQLDLYPTipIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGAN 394
Cdd:PRK07786 312 ATF------PEAQILA-AFGQTE-MSPVT-CMLLGEDAIRKLGS--VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPT 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 395 LAAGyvgggganrFCDNPHATQPDFQ-RLYRTGDfgtLVK----GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVD 469
Cdd:PRK07786 381 LMSG---------YWNNPEATAEAFAgGWFHSGD---LVRqdeeGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 470 KCVVLCYGLDR-GNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGLLKMYENTNNN 547
Cdd:PRK07786 449 EVAVIGRADEKwGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEiVDALPRNPAGKVLKTELRERYGACVNV 528
|
....*.
gi 223890156 548 DDAEVA 553
Cdd:PRK07786 529 ERRSAS 534
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
33-537 |
2.58e-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: 72.93 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIykDEISSVQVSHAELAARTNVLARAISERartvGPNRDSdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:cd05923 16 DACAIA--DPARGLRLTYSELRARIEAVAARLHAR----GLRPGQ--RVAVVLPNSVEAVIALLALHRLGAVPALINPRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSADPSmfKESGVPFASFEELAQEATSHSADEPMDAETLAPLTSDSIAIVLYTSGGTGIP 192
Cdd:cd05923 88 KAAELAELIERGEMTAAVIAVDAQVM--DAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 193 KGVRLSYSAICNRlwwqfrtfpysdseeicvwktALTFVDSVCEIWG---------PLLHG---RALLILSRE------- 253
Cdd:cd05923 166 KGAVIPQRAAESR---------------------VLFMSTQAGLRHGrhnvvlglmPLYHVigfFAVLVAALAldgtyvv 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 254 -TTRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALgpASRPLRRLKLWVCSGETLSKELASEFFKYFGNEdgykLANF 332
Cdd:cd05923 225 vEEFDPADALKLIEQERVTSLFATPTHLDALAAAAEF--AGLKLSSLRHVTFAGATMPDAVLERVNQHLPGE----KVNI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 333 YGSTEVMGDVtyYVLEGSDQLDLYP-------TIPIGRPLDNCAIYLLDEELSPTRDSEpgEVWVaganlaagyvgggga 405
Cdd:cd05923 299 YGTTEAMNSL--YMRDARTGTEMRPgffsevrIVRIGGSPDEALANGEEGELIVAAAAD--AAFT--------------- 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 406 nRFCDNPHATQPDFQ-RLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNP 483
Cdd:cd05923 360 -GYLNQPEATAKKLQdGWYRTGDVGYVdPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQ 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 223890156 484 EILGFVTTKPGaRTSAQHIEGELR-NALTHYMMPQ-VIEVESIPLLVNGKVDRQGL 537
Cdd:cd05923 439 SVTACVVPREG-TLSADELDQFCRaSELADFKRPRrYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
4-542 |
5.45e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 72.00 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 4 LPRVavvtgPRAPVPTAPLTHHLGPLAKS--DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGP-NRdsdyv 80
Cdd:PRK06178 22 IPRE-----PEYPHGERPLTEYLRAWARErpQRPAIIFYGH----VITYAELDELSDRFAALL--RQRGVGAgDR----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 81 IAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPSMfkESGVPFASFEELAqeATSH 160
Cdd:PRK06178 86 VAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVV--EQVRAETSLRHVI--VTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 161 SA---DEP------------------------MDAET----LAPLTSDSIAIVLYTSGGTGIPKGV-----RLSYSAICN 204
Cdd:PRK06178 162 ADvlpAEPtlplpdslraprlaaagaidllpaLRACTapvpLPPPALDALAALNYTGGTTGMPKGCehtqrDMVYTAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 205 RLWWQFRTfpySDSeeicvwkTALTFVDsvcEIW--G-------PLLHGRALLILSRettRDPQKLVNVLADNQIERLVL 275
Cdd:PRK06178 242 YAVAVVGG---EDS-------VFLSFLP---EFWiaGenfgllfPLFSGATLVLLAR---WDAVAFMAAVERYRVTRTVM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 276 VPTLLRSILMYLALgpASRPLRRLKLWVCSgeTLSKELASEFFKYFGNEDGYKLANF-YGSTEVMGDVTYYVLEGSDQLD 354
Cdd:PRK06178 306 LVDNAVELMDHPRF--AEYDLSSLRQVRVV--SFVKKLNPDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAGFQDDDFD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 355 LY--PTIpIGRPLDNCAIYLLDEELSPTRD-SEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDFQR-LYRTGDFGT 430
Cdd:PRK06178 382 LLsqPVF-VGLPVPGTEFKICDFETGELLPlGAEGEIVVRTPSLLKG---------YWNKPEATAEALRDgWLHTGDIGK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 431 L-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNA 509
Cdd:PRK06178 452 IdEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCREN 531
|
570 580 590
....*....|....*....|....*....|...
gi 223890156 510 LTHYMMPQVIEVESIPLLVNGKVDRQGLLKMYE 542
Cdd:PRK06178 532 MAVYKVPEIRIVDALPMTATGKVRKQDLQALAE 564
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
49-537 |
6.14e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 71.76 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 49 SHAELAARTNVLARAIseRARTVGPNRDsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSL 128
Cdd:PRK09088 24 TYAELDALVGRLAAVL--RRRGCVDGER----LAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 129 VIYDDSadPSMFKESGVPFASFeelAQEATSHsadEPMDAETLAPltsDSIAIVLYTSGGTGIPKGVRLS-----YSAIc 203
Cdd:PRK09088 98 LLGDDA--VAAGRTDVEDLAAF---IASADAL---EPADTPSIPP---ERVSLILFTSGTSGQPKGVMLSernlqQTAH- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 204 nrlwwQFRTFPYSDSEEICVWKTAL-TFVDSVCEIWGPLLHGRALLIlsrETTRDPQKLVNVLADNQ--IERLVLVPTLL 280
Cdd:PRK09088 166 -----NFGVLGRVDAHSSFLCDAPMfHIIGLITSVRPVLAVGGSILV---SNGFEPKRTLGRLGDPAlgITHYFCVPQMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 281 RSILMYLALGPASrpLRRLKLWVCSGetlSKELASEFFKYFgnEDGYKLANFYGSTE---VMG-DVTYYVLEGSDQLDLY 356
Cdd:PRK09088 238 QAFRAQPGFDAAA--LRHLTALFTGG---APHAAEDILGWL--DDGIPMVDGFGMSEagtVFGmSVDCDVIRAKAGAAGI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 357 PTIPIGrpldncaIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDF--QRLYRTGD------- 427
Cdd:PRK09088 311 PTPTVQ-------TRVVDDQGNDCPAGVPGELLLRGPNLSPG---------YWRRPQATARAFtgDGWFRTGDiarrdad 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 428 -FGTLV--KGAVLYAGrtdaqvkirGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEG 504
Cdd:PRK09088 375 gFFWVVdrKKDMFISG---------GENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRS 445
|
490 500 510
....*....|....*....|....*....|....
gi 223890156 505 ELRNALTHYMMPQ-VIEVESIPLLVNGKVDRQGL 537
Cdd:PRK09088 446 HLSTRLAKYKVPKhLRLVDALPRTASGKLQKARL 479
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
21-537 |
7.03e-13 |
|
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: 71.20 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 21 PLTHHLGPLAKS--DRTALIYKDeissVQVSHAELAARTNVLARAISERARTVG-------PNrDSDYVIavcmqpthnT 91
Cdd:cd05920 16 PLGDLLARSAARhpDRIAVVDGD----RRLTYRELDRRADRLAAGLRGLGIRPGdrvvvqlPN-VAEFVV---------L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 92 IMALLatwKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPsmfkesgvpfASFEELAQEATSHSADepmdaetl 171
Cdd:cd05920 82 FFALL---RLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHAG----------FDHRALARELAESIPE-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 172 apltsdsIAIVLYTSGGTGIPKGV-----RLSYSAICNRLWWQFRtfpySDSEEICVWKTALTFVDSVCEIWGPLLHGrA 246
Cdd:cd05920 141 -------VALFLLSGGTTGTPKLIprthnDYAYNVRASAEVCGLD----QDTVYLAVLPAAHNFPLACPGVLGTLLAG-G 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 247 LLILSreTTRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPasRPLRRLKLWVCSGETLSKELASEFFKYFGNedg 326
Cdd:cd05920 209 RVVLA--PDPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRR--ADLSSLRLLQVGGARLSPALARRVPPVLGC--- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 327 yKLANFYGSTEvmGDVTYYVLEGSDQLDLYPTipiGRPL--DNcAIYLLDEELSPTRDSEPGEVWVAGAnlaagyvggGG 404
Cdd:cd05920 282 -TLQQVFGMAE--GLLNYTRLDDPDEVIIHTQ---GRPMspDD-EIRVVDEEGNPVPPGEEGELLTRGP---------YT 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 405 ANRFCDNPHATQPDF--QRLYRTGDfgtLVK----GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygl 478
Cdd:cd05920 346 IRGYYRAPEHNARAFtpDGFYRTGD---LVRrtpdGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV---- 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 479 drGNP-EILG-----FVTTKPgARTSAQHIEGELRNA-LTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:cd05920 419 --AMPdELLGerscaFVVLRD-PPPSAAQLRRFLRERgLAAYKLPdRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
24-537 |
8.27e-13 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 71.47 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 24 HHLGPLAKS--DRTALIY------KDEISSVQVSHAELAARTNVLARAIseRARTVGPNrdsdyVIAVCM-QPTHNTIMA 94
Cdd:PRK09274 10 RHLPRAAQErpDQLAVAVpggrgaDGKLAYDELSFAELDARSDAIAHGL--NAAGIGRG-----MRAVLMvTPSLEFFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 95 LLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIyddsadpsmfkesGVPFA---------SFEELAQ---------- 155
Cdd:PRK09274 83 TFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFI-------------GIPKAhlarrlfgwGKPSVRRlvtvggrllw 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 156 ------EATSHSADEPMDaetLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNrlwwQFR----TFPYSDSEeicvwk 225
Cdd:PRK09274 150 ggttlaTLLRDGAAAPFP---MADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEA----QIEalreDYGIEPGE------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 226 taltfVDSVCEiwgPL--LHGRAL--------LILSRETTRDPQKLVNVLADNQIERLVLVPTLLRSILMY-LALGpasR 294
Cdd:PRK09274 217 -----IDLPTF---PLfaLFGPALgmtsvipdMDPTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYgEANG---I 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 295 PLRRLKLWVCSGETLSKELASEFFKYFgnEDGYKLANFYGSTEVMgDVTyyVLEGSDQLDLYPTIP-------IGRPLD- 366
Cdd:PRK09274 286 KLPSLRRVISAGAPVPIAVIERFRAML--PPDAEILTPYGATEAL-PIS--SIESREILFATRAATdngagicVGRPVDg 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 367 -NCAIYLLDEELSPTRDS-------EPGEVWVAGAnlaagyvggGGANRFCDNPHATQ----PDFQRL--YRTGDFGTL- 431
Cdd:PRK09274 361 vEVRIIAISDAPIPEWDDalrlatgEIGEIVVAGP---------MVTRSYYNRPEATRlakiPDGQGDvwHRMGDLGYLd 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 432 VKGAVLYAGRtdaqvkiRGHRVDL-------LEVERALAQVPGVDKCVVLCYGLDRGNPEILgFVTTKPGARTSAQHIEG 504
Cdd:PRK09274 432 AQGRLWFCGR-------KAHRVETaggtlytIPCERIFNTHPGVKRSALVGVGVPGAQRPVL-CVELEPGVACSKSALYQ 503
|
570 580 590
....*....|....*....|....*....|....*....
gi 223890156 505 ELRNALTHYMMPQVIEV----ESIPLLV--NGKVDRQGL 537
Cdd:PRK09274 504 ELRALAAAHPHTAGIERflihPSFPVDIrhNAKIFREKL 542
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
46-474 |
9.88e-13 |
|
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: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 46 VQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAE 125
Cdd:cd05907 4 QPITWAEFAEEVRALAKGL--IALGVEPGD----RVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 126 PSLVIYDDSADPsmfkesgvpfasfeelaqeatshsadepmdaetlapltsdsiAIVLYTSGGTGIPKGVRLSYSAICnr 205
Cdd:cd05907 78 AKALFVEDPDDL------------------------------------------ATIIYTSGTTGRPKGVMLSHRNIL-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 206 lwWQFRTFpysdSEEICVWKTA--LTF------VDSVCEIWGPLLHGRALLILSR-ETTRD------PQKLVNVLAdnQI 270
Cdd:cd05907 114 --SNALAL----AERLPATEGDrhLSFlplahvFERRAGLYVPLLAGARIYFASSaETLLDdlsevrPTVFLAVPR--VW 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 271 ERL------VLVPTLLRSILMYLALGpasrplrRLKLWVCSGETLSKELAsEFFKYFGNE--DGyklanfYGSTEVMGDV 342
Cdd:cd05907 186 EKVyaaikvKAVPGLKRKLFDLAVGG-------RLRFAASGGAPLPAELL-HFFRALGIPvyEG------YGLTETSAVV 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 343 TYYVLE----GSdqldlyptipIGRPLDNCAIylldeelsptRDSEPGEVWVAGANLAAgyvgggganRFCDNPHATQPD 418
Cdd:cd05907 252 TLNPPGdnriGT----------VGKPLPGVEV----------RIADDGEILVRGPNVML---------GYYKNPEATAEA 302
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 419 F--QRLYRTGDFGTLVKGAVLY-AGRT-DAQVKIRGHRVDLLEVERALAQVPGVDKCVVL 474
Cdd:cd05907 303 LdaDGWLHTGDLGEIDEDGFLHiTGRKkDLIITSGGKNISPEPIENALKASPLISQAVVI 362
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
11-537 |
1.27e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 71.03 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 11 TGPRAPVPTAP----LTHHLGPLAKSDRTALIykDEISSVQVSHAELAARTNVLARAISERartvGPNRDSDYVIAVCMQ 86
Cdd:PLN02574 28 KHPPVPLPSDPnldaVSFIFSHHNHNGDTALI--DSSTGFSISYSELQPLVKSMAAGLYHV----MGVRQGDVVLLLLPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 87 PTHNTiMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLViYDDSADPSMFKESGVPF------ASFEELAQEATSH 160
Cdd:PLN02574 102 SVYFP-VIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLA-FTSPENVEKLSPLGVPVigvpenYDFDSKRIEFPKF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 161 SADEPMDAETLA--PLTSDSIAIVLYTSGGTGIPKGVRLSYSAICN--RLWWQFRTFPYSDSEEICVWKTALtfvdSVCE 236
Cdd:PLN02574 180 YELIKEDFDFVPkpVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAmvELFVRFEASQYEYPGSDNVYLAAL----PMFH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 237 IWGPLLHGRALLILSRETTR----DPQKLVNVLADNQIERLVLVPTLLRSiLMYLALGPASRPLRRLKLWVCSGETLSKE 312
Cdd:PLN02574 256 IYGLSLFVVGLLSLGSTIVVmrrfDASDMVKVIDRFKVTHFPVVPPILMA-LTKKAKGVCGEVLKSLKQVSCGAAPLSGK 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 313 LASEFFKYFGNEDgykLANFYGSTEVMGDVTYYVleGSDQLDLYPTIPIGRPldNCAIYLLDEE---LSPTRDSepGEVW 389
Cdd:PLN02574 335 FIQDFVQTLPHVD---FIQGYGMTESTAVGTRGF--NTEKLSKYSSVGLLAP--NMQAKVVDWStgcLLPPGNC--GELW 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 390 VAGANLAAGyvgggganrFCDNPHATQP--DFQRLYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVP 466
Cdd:PLN02574 406 IQGPGVMKG---------YLNNPKATQStiDKDGWLRTGDIAYFDEDGYLYiVDRLKEIIKYKGFQIAPADLEAVLISHP 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223890156 467 GVDKCVVLCYGlDRGNPEI-LGFVTTKPGARTSAQHIEGELRNALTHY-MMPQVIEVESIPLLVNGKVDRQGL 537
Cdd:PLN02574 477 EIIDAAVTAVP-DKECGEIpVAFVVRRQGSTLSQEAVINYVAKQVAPYkKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
33-556 |
2.42e-12 |
|
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: 70.04 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEISSVQ--VSHAELAARTNVLARAIseraRTVGPNRDSDYVIAVCMQPthNTIMALLATWKAGA------- 103
Cdd:cd05967 66 DQIALIYDSPVTGTErtYTYAELLDEVSRLAGVL----RKLGVVKGDRVIIYMPMIP--EAAIAMLACARIGAihsvvfg 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 104 AYVPMEPSfpqGRIthilKDAEPSLVI-------------YDDSAD------------------PSMFKESGVPFASFE- 151
Cdd:cd05967 140 GFAAKELA---SRI----DDAKPKLIVtascgiepgkvvpYKPLLDkalelsghkphhvlvlnrPQVPADLTKPGRDLDw 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 152 -ELAQEATSHSAdepmdaetlAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRT----------FPYSDSEe 220
Cdd:cd05967 213 sELLAKAEPVDC---------VPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNiygikpgdvwWAASDVG- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 221 icvWKTALTFVdsvceIWGPLLHGRALLILSRETTR--DPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASR--PL 296
Cdd:cd05967 283 ---WVVGHSYI-----VYGPLLHGATTVLYEGKPVGtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKYIKkyDL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 297 RRLKLWVCSGETL---SKELASEFFK------YFGNEDGYKLAnfygstevmgdvTYYVleGSDQLDLYPTIPiGRPLDN 367
Cdd:cd05967 355 SSLRTLFLAGERLdppTLEWAENTLGvpvidhWWQTETGWPIT------------ANPV--GLEPLPIKAGSP-GKPVPG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 368 CAIYLLDEELSPTRDSEPGEVWVAGAnLAAGYVGGGGAN--RFcdnPHATQPDFQRLYRTGDFGTLVKGAVLYA-GRTDA 444
Cdd:cd05967 420 YQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTLWKNdeRF---KKLYLSKFPGYYDTGDAGYKDEDGYLFImGRTDD 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 445 QVKIRGHRVDLLEVERALAQVPGVDKCVVLcyGL-DRGNPEI-LGFVTTKPGARTSAQHIEGELRNALTHYMMP-----Q 517
Cdd:cd05967 496 VINVAGHRLSTGEMEESVLSHPAVAECAVV--GVrDELKGQVpLGLVVLKEGVKITAEELEKELVALVREQIGPvaafrL 573
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 223890156 518 VIEVESIPLLVNGKVDRQGLLKMYENTNNN-----DDAEVAVDI 556
Cdd:cd05967 574 VIFVKRLPKTRSGKILRRTLRKIADGEDYTipstiEDPSVLDEI 617
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
33-540 |
8.18e-12 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 68.16 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALI--YKDEISSVQVSHAELAARTNVLARAISERArtVGPNRdsdyVIAvCMQPTHNTIMAL-LATWKAGAAYVPME 109
Cdd:PRK13295 39 DKTAVTavRLGTGAPRRFTYRELAALVDRVAVGLARLG--VGRGD----VVS-CQLPNWWEFTVLyLACSRIGAVLNPLM 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 110 PSFPQGRITHILKDAEPSLVIYddsadPSMFKesGVPFA-------------------------SFEELAqeATSHSADE 164
Cdd:PRK13295 112 PIFRERELSFMLKHAESKVLVV-----PKTFR--GFDHAamarrlrpelpalrhvvvvggdgadSFEALL--ITPAWEQE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 165 PMDAETLAPLT--SDSIAIVLYTSGGTGIPKGVRLSYsaicNRLWWQFRtfPYSDseeicvwKTALTfVDSVCEIWGPLL 242
Cdd:PRK13295 183 PDAPAILARLRpgPDDVTQLIYTSGTTGEPKGVMHTA----NTLMANIV--PYAE-------RLGLG-ADDVILMASPMA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 243 H------GRALLILSRETTR-----DPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPasRPLRRLKLWVCSGETLSK 311
Cdd:PRK13295 249 HqtgfmyGLMMPVMLGATAVlqdiwDPARAAELIRTEGVTFTMASTPFLTDLTRAVKESG--RPVSSLRTFLCAGAPIPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 312 ELASEFFKYFGNedgyKLANFYGSTEvMGDVTYYVLEGSDQL----DlyptipiGRPLDNCAIYLLDEELSPTRDSEPGE 387
Cdd:PRK13295 327 ALVERARAALGA----KIVSAWGMTE-NGAVTLTKLDDPDERasttD-------GCPLPGVEVRVVDADGAPLPAGQIGR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 388 VWVAGANLAAGyvgggganrFCDNPHATQPDFQRLYRTGDFGTL-VKGAVLYAGRTDaQVKIRG-HRVDLLEVERALAQV 465
Cdd:PRK13295 395 LQVRGCSNFGG---------YLKRPQLNGTDADGWFDTGDLARIdADGYIRISGRSK-DVIIRGgENIPVVEIEALLYRH 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 466 PGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNA-LTHYMMPQVIEV-ESIPLLVNGKVDRQGLLKM 540
Cdd:PRK13295 465 PAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKAQkVAKQYIPERLVVrDALPRTPSGKIQKFRLREM 541
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
171-537 |
1.32e-11 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 68.03 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 171 LAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWwQFRT-FPYSDSEEICvwkTALTFVDS---VCEIWGPLLHGRA 246
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDvFNLRNDDVIL---SSLPFFHSfglTVTLWLPLLEGIK 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 247 LLILSRETtrDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASrpLRRLKLWVCSGETLSKELASEFFKYFGNE-- 324
Cdd:PRK08633 852 VVYHPDPT--DALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLM--FASLRLVVAGAEKLKPEVADAFEEKFGIRil 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 325 DGYklanfyGSTEV------------MGDVTYYV--LEGSdqldlyptipIGRPLDNCAIYLLD----EELSPtrdSEPG 386
Cdd:PRK08633 928 EGY------GATETspvasvnlpdvlAADFKRQTgsKEGS----------VGMPLPGVAVRIVDpetfEELPP---GEDG 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 387 EVWVAGANLAagyvggggaNRFCDNPHAT-----QPDFQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVER 460
Cdd:PRK08633 989 LILIGGPQVM---------KGYLGDPEKTaevikDIDGIGWYVTGDKGHLDEdGFLTITDRYSRFAKIGGEMVPLGAVEE 1059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 461 ALAQVPGVDKCVVLCYGLD---RGnpEILGFVTTKPGarTSAQHIEGELRNA-LTHYMMP-QVIEVESIPLLVNGKVDRQ 535
Cdd:PRK08633 1060 ELAKALGGEEVVFAVTAVPdekKG--EKLVVLHTCGA--EDVEELKRAIKESgLPNLWKPsRYFKVEALPLLGSGKLDLK 1135
|
..
gi 223890156 536 GL 537
Cdd:PRK08633 1136 GL 1137
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
20-532 |
1.51e-11 |
|
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: 67.32 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 20 APLThhlgPLAKSDRTALIYKDEIS----SVQVSHAELAARTNVLARAISERArtVGPNrdsDYVIAVCmqP-THNTIMA 94
Cdd:cd12118 2 VPLT----PLSFLERAAAVYPDRTSivygDRRYTWRQTYDRCRRLASALAALG--ISRG---DTVAVLA--PnTPAMYEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 95 LLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADpsmfkesgvpfasFEELAQEATSHSADEPMDAEtlapl 174
Cdd:cd12118 71 HFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFE-------------YEDLLAEGDPDFEWIPPADE----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 175 tSDSIAIVlYTSGGTGIPKGVRLSY-----SAICNRLWWQFRTFPysdseeICVWKTALTFVDSVCEIWGPLLHGRALLI 249
Cdd:cd12118 133 -WDPIALN-YTSGTTGRPKGVVYHHrgaylNALANILEWEMKQHP------VYLWTLPMFHCNGWCFPWTVAAVGGTNVC 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 250 LsRETtrDPQKLVNVLADNQIERLVLVPTLLRSILmylalgpASRPLRRLKL-WVCSGETL-SKELASEFFKYfgNEDGY 327
Cdd:cd12118 205 L-RKV--DAKAIYDLIEKHKVTHFCGAPTVLNMLA-------NAPPSDARPLpHRVHVMTAgAPPPAAVLAKM--EELGF 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 328 KLANFYGSTEVMGDVTyyVLEGSDQLDLYPT-------------IPIGRPLDncaiyLLDEELSPT--RDSEP-GEVWVA 391
Cdd:cd12118 273 DVTHVYGLTETYGPAT--VCAWKPEWDELPTeerarlkarqgvrYVGLEEVD-----VLDPETMKPvpRDGKTiGEIVFR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 392 GANLAagyvggggaNRFCDNPHATQPDFQR-LYRTGDFgtlvkgAVLYAgrtDAQVKIR----------GHRVDLLEVER 460
Cdd:cd12118 346 GNIVM---------KGYLKNPEATAEAFRGgWFHSGDL------AVIHP---DGYIEIKdrskdiiisgGENISSVEVEG 407
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223890156 461 ALAQVPGVDKCVVLcygldrGNP-EILG-----FVTTKPGARTSAQHIEGELRNALTHYMMPQVIEVESIPLLVNGKV 532
Cdd:cd12118 408 VLYKHPAVLEAAVV------ARPdEKWGevpcaFVELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGELPKTSTGKI 479
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
181-533 |
1.92e-11 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 65.79 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 181 IVLYTSGGTGIPKGVRLSYSAIcnrLWWQFRTFPYSDSEEICVwktaltFVDSvceiwGPLLH-------------GRAL 247
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQAL---LAQALVLAVLQAIDEGTV------FLNS-----GPLFHigtlmftlatfhaGGTN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 248 LILSREttrDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPAS----RPLRRLKLWvcsgETLSKELASEFFKYFGN 323
Cdd:cd17636 70 VFVRRV---DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDlsslRSSPAAPEW----NDMATVDTSPWGRKPGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 324 edgyklanfYGSTEVMGDVTYYVLEGSDqldlypTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLaagyvggg 403
Cdd:cd17636 143 ---------YGQTEVMGLATFAALGGGA------IGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTV-------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 404 gANRFCDNPHATQpdfQRL----YRTGDFGT-LVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGL 478
Cdd:cd17636 200 -MAGYWNRPEVNA---RRTrggwHHTNDLGRrEPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPD 275
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 223890156 479 DRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVD 533
Cdd:cd17636 276 PRWAQSVKAIVVLKPGASVTEAELIEHCRARIASYKKPKSVEfADALPRTAGGADD 331
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
49-541 |
4.58e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 65.88 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 49 SHAELAARTNVLARAISERArtVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPS- 127
Cdd:PRK12406 13 SFDELAQRAARAAGGLAALG--VRPGD----CVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 128 LVIYDD------SADPSmfkesGVPFASFEELAQEATSHSAD--------------------EPMDAETLAPLTSdsiai 181
Cdd:PRK12406 87 LIAHADllhglaSALPA-----GVTVLSVPTPPEIAAAYRISpalltppagaidwegwlaqqEPYDGPPVPQPQS----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 182 VLYTSGGTGIPKGVRlsysaicnrlwwqfRTFPysDSEEICVWKTALTFV-----DSVCEIWGPLLH------------- 243
Cdd:PRK12406 157 MIYTSGTTGHPKGVR--------------RAAP--TPEQAAAAEQMRALIyglkpGIRALLTGPLYHsapnayglragrl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 244 GRALLILSRettRDPQKLVNVLADNQIERLVLVPTLLRSILmylALGPASRP---LRRLKLWVCSGETLSKELASEFFKY 320
Cdd:PRK12406 221 GGVLVLQPR---FDPEELLQLIERHRITHMHMVPTMFIRLL---KLPEEVRAkydVSSLRHVIHAAAPCPADVKRAMIEW 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 321 FG---NEdgyklanFYGSTEVmGDVTYYVLEgsDQLDLYPTIpiGRPLDNCAIYLLDEELSPTRDSEPGEVWVaganlaa 397
Cdd:PRK12406 295 WGpviYE-------YYGSTES-GAVTFATSE--DALSHPGTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYS------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 398 gyvgggganRFCDNPHAT---QPDFQRLYRTGDFGTLvkGAVLYAGRtDAQVKIRGHRVDLL----------EVERALAQ 464
Cdd:PRK12406 356 ---------RIAGNPDFTyhnKPEKRAEIDRGGFITS--GDVGYLDA-DGYLFLCDRKRDMVisggvniypaEIEAVLHA 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 465 VPGVDKCVVlcYGL-DRGNPEIL-GFVTTKPGARTSAQHIEGELRNALTHYMMPQVIEVE-SIPLLVNGKVDRQGLLKMY 541
Cdd:PRK12406 424 VPGVHDCAV--FGIpDAEFGEALmAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMaELPREDSGKIFKRRLRDPY 501
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
48-670 |
4.88e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 66.21 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 48 VSHAELAARTNVLARAISERARTVGpnrdsDYVIaVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPS 127
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSG-----DRVL-LCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 128 LVIYDDSADpSMFKESGVPFASfeELAQEATSHsadEPMDAEtlaPLTSDSIAIVLYTSGGTGIPKgvrlsySAI---CN 204
Cdd:PRK06060 105 LVVTSDALR-DRFQPSRVAEAA--ELMSEAARV---APGGYE---PMGGDALAYATYTSGTTGPPK------AAIhrhAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 205 rlwwqfrtfPYSDSEEICVWKTALTFVD-SVCE------------IWGPLLHGRALLILSRETTRDpqklVNVLADNQIE 271
Cdd:PRK06060 170 ---------PLTFVDAMCRKALRLTPEDtGLCSarmyfayglgnsVWFPLATGGSAVINSAPVTPE----AAAILSARFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 272 RLVL--VPTLLRSILMylALGPASrpLRRLKLWVCSGETLSKELASEFFKYFGnedGYKLANFYGSTEVmgDVTYYvleg 349
Cdd:PRK06060 237 PSVLygVPNFFARVID--SCSPDS--FRSLRCVVSAGEALELGLAERLMEFFG---GIPILDGIGSTEV--GQTFV---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 350 SDQLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLaagyvGGGGANRfcDNPHATQPDF----QRLYRT 425
Cdd:PRK06060 304 SNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAI-----AKGYWNR--PDSPVANEGWldtrDRVCID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 426 GDfgtlvkGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGA---RTSAQHI 502
Cdd:PRK06060 377 SD------GWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAtidGSVMRDL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 503 EGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGL-----------LKMYENTNN-----NDDAEVAVDIDCSGAGLAD 565
Cdd:PRK06060 451 HRGLLNRLSAFKVPHRFAvVDRLPRTPNGKLVRGALrkqsptkpiweLSLTEPGSGvraqrDDLSASNMTIAGGNDGGAT 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 566 L---------EAARALLETVGA----VLGRAARGTLSLRSGFYELGGNS------LNSIYTITKLR-------DRGYYVE 619
Cdd:PRK06060 531 LrerlvalrqERQRLVVDAVCAeaakMLGEPDPWSVDQDLAFSELGFDSqmtvtlCKRLAAVTGLRlpetvgwDYGSISG 610
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 223890156 620 ISDFLGASTLGeILSKMSTDPNGGADSKeatfiAVPMRDEHKREVIDMVVS 670
Cdd:PRK06060 611 LAQYLEAELAG-GHGRLKSAGPVNSGAT-----GLWAIEEQLNKVEELVAV 655
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
33-532 |
1.08e-10 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 64.78 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERARTVGpnrdsDYVIAVCmqptHNTImALLATWKA----GAAYVPM 108
Cdd:PRK06155 36 DRPLLVFGGT----RWTYAEAARAAAAAAHALAAAGVKRG-----DRVALMC----GNRI-EFLDVFLGcawlGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 109 EPSFPQGRITHILKDAEPSLVIYD-------DSADPSMFKESGVpfasfeELAQEATSHSADEPMDAETLAPLTS----- 176
Cdd:PRK06155 102 NTALRGPQLEHILRNSGARLLVVEaallaalEAADPGDLPLPAV------WLLDAPASVSVPAGWSTAPLPPLDApapaa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 177 -----DSIAIvLYTSGGTGIPKGVRLSYSAIcnrLWWQFRTFPYSDSEEICVWKTALtfvdsvceiwgPLLHGRALLILS 251
Cdd:PRK06155 176 avqpgDTAAI-LYTSGTTGPSKGVCCPHAQF---YWWGRNSAEDLEIGADDVLYTTL-----------PLFHTNALNAFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 252 rettrdpQKLVN----VLA---------DNQIERLVLVPTLLRSILMYLALGPASRPLRRLKLWVCSGETLSKELASEFF 318
Cdd:PRK06155 241 -------QALLAgatyVLEprfsasgfwPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRVALGPGVPAALHAAFR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 319 KYFGnedgYKLANFYGSTE---VMGDVTYYVLEGSdqldlyptipIGRPLDNCAIYLLDEELSPTRDSEPGEVwvaganL 395
Cdd:PRK06155 314 ERFG----VDLLDGYGSTEtnfVIAVTHGSQRPGS----------MGRLAPGFEARVVDEHDQELPDGEPGEL------L 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 396 AAGYVGGGGANRFCDNPHATQPDFQRL-YRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVV 473
Cdd:PRK06155 374 LRADEPFAFATGYFGMPEKTVEAWRNLwFHTGDRVVRdADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAV 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 474 LCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKV 532
Cdd:PRK06155 454 FPVPSELGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEfVAALPKTENGKV 513
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
184-534 |
1.49e-10 |
|
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: 63.45 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 184 YTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEICVWKTALTFVDSVCEIWGPLLHGRALLILSRetTRDPQKLVN 263
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFGSVLGVLACLTHGATMVFPSP--SFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 264 VLADNQIERLVLVPTllrsilMYLAL----GPASRPLRRLKLWVCSGETLSKELASEFFKYFGNEDgykLANFYGSTEVM 339
Cdd:cd05917 87 AIEKEKCTALHGVPT------MFIAElehpDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKD---VTIAYGMTETS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 340 GDVTYYVLEGSDQLDLyptIPIGRPLDNCAIYLLDEE--LSPTRdSEPGEVWVAGANLAAGyvgggganrFCDNPHATQP 417
Cdd:cd05917 158 PVSTQTRTDDSIEKRV---NTVGRIMPHTEAKIVDPEggIVPPV-GVPGELCIRGYSVMKG---------YWNDPEKTAE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 418 --DFQRLYRTGDFGTLVK-GAVLYAGRTDAQVkIRG-HRVDLLEVERALAQVPGV-DKCVVlcyGL--DRGNPEILGFVT 490
Cdd:cd05917 225 aiDGDGWLHTGDLAVMDEdGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVsDVQVV---GVpdERYGEEVCAWIR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 223890156 491 TKPGARTSAQHIEGELRNALTHYMMPQ-VIEVESIPLLVNGKVDR 534
Cdd:cd05917 301 LKEGAELTEEDIKAYCKGKIAHYKVPRyVFFVDEFPLTVSGKIQK 345
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-660 |
2.14e-10 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 64.42 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIY--KDEISSVQVSHAELAARTNVLARAISERA----RTV-----GPnrdsDYVIAV--CmqpthntimaLLATW 99
Cdd:PRK05691 24 DRLALRFlaDDPGEGVVLSYRDLDLRARTIAAALQARAsfgdRAVllfpsGP----DYVAAFfgC----------LYAGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 100 KAGAAYVPmEPSFP--QGRITHILKDAEPSLVIYD-DSADPSMFKESGVPFASFEELAQEATSHSADEPMDAETLAPlts 176
Cdd:PRK05691 90 IAVPAYPP-ESARRhhQERLLSIIADAEPRLLLTVaDLRDSLLQMEELAAANAPELLCVDTLDPALAEAWQEPALQP--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 177 DSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEeicvwktaltfvDSVCEIWGPLLHGRALL------IL 250
Cdd:PRK05691 166 DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNP------------DDVIVSWLPLYHDMGLIggllqpIF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 251 SRettrdpqklvnvladnqierlvlVPTLLRSILMYLAlgpasRPLRRLKLWVCSGETLSK------ELASEFFK----- 319
Cdd:PRK05691 234 SG-----------------------VPCVLMSPAYFLE-----RPLRWLEAISEYGGTISGgpdfayRLCSERVSesale 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 320 ----------YFGNED----------------GYKLANFYGSTEvMGDVTYYV-----------LEGSDQL--------- 353
Cdd:PRK05691 286 rldlsrwrvaYSGSEPirqdslerfaekfaacGFDPDSFFASYG-LAEATLFVsggrrgqgipaLELDAEAlarnraepg 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 354 DLYPTIPIGRPLDNCAIYLLD----EELSptrDSEPGEVWVAGANLAagyvggggaNRFCDNPHAT-----QPDFQRLYR 424
Cdd:PRK05691 365 TGSVLMSCGRSQPGHAVLIVDpqslEVLG---DNRVGEIWASGPSIA---------HGYWRNPEASaktfvEHDGRTWLR 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 425 TGDFGTLVKGAVLYAGRTDAQVKIRGHRVDLLEVERAL-AQVPGVDKCVVLCYGLDRGNPEILGF---VTTKPGARTSAQ 500
Cdd:PRK05691 433 TGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVRKGRVAAFAVNHQGEEGIGIaaeISRSVQKILPPQ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 501 HIEGELRNAL--THYMMPQVI---EVESIPLLVNGKVDRQ--------GLLKMYENTNNNDDAEVAVDiDCSGAGLADLE 567
Cdd:PRK05691 513 ALIKSIRQAVaeACQEAPSVVlllNPGALPKTSSGKLQRSacrlrladGSLDSYALFPALQAVEAAQT-AASGDELQARI 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 568 AA--RALLETvgavlgraarGTLSLRSGFYELGGNSLNSIYTITKLRDR-GYYVEISDFLGASTLGEILSKMSTDPNGGA 644
Cdd:PRK05691 592 AAiwCEQLKV----------EQVAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAVARQLAGGG 661
|
730
....*....|....*.
gi 223890156 645 DSKEAtfIAVPMRDEH 660
Cdd:PRK05691 662 AAQAA--IARLPRGQA 675
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
47-537 |
2.20e-10 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 63.49 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 47 QVSHAELAARTNVLARAISERARTVGPNrdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEP 126
Cdd:PRK05857 41 ALRYRELVAEVGGLAADLRAQSVSRGSR------VLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 127 SLVI------YDDSADPSMFKESGVPFASFEELAQEaTSHSADEPMDAETLAPLTSDSIAIVlYTSGGTGIPKGVRLSys 200
Cdd:PRK05857 115 AAALvapgskMASSAVPEALHSIPVIAVDIAAVTRE-SEHSLDAASLAGNADQGSEDPLAMI-FTSGTTGEPKAVLLA-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 201 aicNRlwwQFRTFPYSDSEEICVWKT-----------ALTFVDSVCEIWGPLLHGrALLILSRETTrdpQKLVNVLADNQ 269
Cdd:PRK05857 191 ---NR---TFFAVPDILQKEGLNWVTwvvgettysplPATHIGGLWWILTCLMHG-GLCVTGGENT---TSLLEILTTNA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 270 IERLVLVPTLLRSILMYLALGPASRPlrRLKLWVCSGetlSKELASEFfkYFGNEDGYKLANFYGSTEVmGDVTYYVLEG 349
Cdd:PRK05857 261 VATTCLVPTLLSKLVSELKSANATVP--SLRLVGYGG---SRAIAADV--RFIEATGVRTAQVYGLSET-GCTALCLPTD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 350 SDQLDLYPTIPIGRPLDNCAIYLLDEE-LSPT-RDSEP----GEVWV-AGANLAAgyvgggganrFCDNPHatqpdfqrl 422
Cdd:PRK05857 333 DGSIVKIEAGAVGRPYPGVDVYLAATDgIGPTaPGAGPsasfGTLWIkSPANMLG----------YWNNPE--------- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 423 yRTGDfgTLVKGAV----LYAGRTDAQVKIRGHRVDLL----------EVERALAQVPGVDKCVvlCYGLDrgNPEI--- 485
Cdd:PRK05857 394 -RTAE--VLIDGWVntgdLLERREDGFFYIKGRSSEMIicggvniapdEVDRIAEGVSGVREAA--CYEIP--DEEFgal 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 223890156 486 --LGFVTT----KPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:PRK05857 467 vgLAVVASaeldESAARALKHTIAARFRRESEPMARPsTIVIVTDIPRTQSGKVMRASL 525
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
30-575 |
3.18e-10 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 63.42 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 30 AKSDRTALIYK-DEISSVQV-SHAELAARTNVLARAISERartvGPNRDSDYVIAVCMQPthNTIMALLATWKAGAAYVP 107
Cdd:TIGR02188 69 ARPDKVAIIWEgDEPGEVRKiTYRELHREVCRFANVLKSL----GVKKGDRVAIYMPMIP--EAAIAMLACARIGAIHSV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 108 MEPSFP----QGRIThilkDAEPSLVIyddSADPSM----------------------------FKESGVPFAS------ 149
Cdd:TIGR02188 143 VFGGFSaealADRIN----DAGAKLVI---TADEGLrggkviplkaivdealekcpvsvehvlvVRRTGNPVVPwvegrd 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 150 --FEELAQEATSHSADEPMDAETlaPLtsdsiaIVLYTSGGTGIPKGVR------LSYSAICnrLWWqfrTFPYSDsEEI 221
Cdd:TIGR02188 216 vwWHDLMAKASAYCEPEPMDSED--PL------FILYTSGSTGKPKGVLhttggyLLYAAMT--MKY---VFDIKD-GDI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 222 --CV----WKTALTFVdsvceIWGPLLHGRALLIL-SRETTRDPQKLVNVLADNQIERLVLVPTLLRsilMYLALG---P 291
Cdd:TIGR02188 282 fwCTadvgWITGHSYI-----VYGPLANGATTVMFeGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIR---ALMRLGdewV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 292 ASRPLRRLKLWVCSGETLSKELASEFFKYFGNEDgYKLANFYGSTEVMGDVTYYvLEGsdqldLYPTIP--IGRPLDNCA 369
Cdd:TIGR02188 354 KKHDLSSLRLLGSVGEPINPEAWMWYYKVVGKER-CPIVDTWWQTETGGIMITP-LPG-----ATPTKPgsATLPFFGIE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 370 IYLLDEELSPTRDSEPGEV------W------VAGANlaagyvggggaNRFCDNPHATQPDFqrlYRTGDFGTLVK-GAV 436
Cdd:TIGR02188 427 PAVVDEEGNPVEGPGEGGYlvikqpWpgmlrtIYGDH-----------ERFVDTYFSPFPGY---YFTGDGARRDKdGYI 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 437 LYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQhIEGELRNALTH---- 512
Cdd:TIGR02188 493 WITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDE-LRKELRKHVRKeigp 571
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223890156 513 YMMPQVIE-VESIPLLVNGKVDRQGLLKMYENtnnndDAEVAVDIdcsgAGLADLEAARALLET 575
Cdd:TIGR02188 572 IAKPDKIRfVPGLPKTRSGKIMRRLLRKIAAG-----EAEILGDT----STLEDPSVVEELIEA 626
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
23-198 |
4.65e-10 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 62.59 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 23 THHL-----GPLAKSDRTALIYKDEISsvqVSHAELAARTNVLARAIseRARTVGP-NRdsdyvIAVCMQPTHNTIMALL 96
Cdd:PRK07514 2 NNNLfdalrAAFADRDAPFIETPDGLR---YTYGDLDAASARLANLL--VALGVKPgDR-----VAVQVEKSPEALALYL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 97 ATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPSMFK---ESGVPF---------ASFEELAQEATSHSADE 164
Cdd:PRK07514 72 ATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCDPANFAWLSKiaaAAGAPHvetldadgtGSLLEAAAAAPDDFETV 151
|
170 180 190
....*....|....*....|....*....|....
gi 223890156 165 PMDAETLApltsdsiAIvLYTSGGTGIPKGVRLS 198
Cdd:PRK07514 152 PRGADDLA-------AI-LYTSGTTGRSKGAMLS 177
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
33-198 |
5.39e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 62.58 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAyVPMEPSF 112
Cdd:PRK08279 52 DRPALLFEDQ----SISYAELNARANRYAHWA--AARGVGKGD----VVALLMENRPEYLAAWLGLAKLGAV-VALLNTQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQG-RITHILKDAEPSLVIYDD-------------SADPSMFKESGVPFAS---FEELAQEATSHSADEPmdAETlAPLT 175
Cdd:PRK08279 121 QRGaVLAHSLNLVDAKHLIVGEelveafeearadlARPPRLWVAGGDTLDDpegYEDLAAAAAGAPTTNP--ASR-SGVT 197
|
170 180
....*....|....*....|...
gi 223890156 176 SDSIAIVLYTSGGTGIPKGVRLS 198
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMS 220
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
101-537 |
7.98e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 61.96 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 101 AGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPsMFKESGVPFASFEELAQ---------EATSHSADEPMDAETL 171
Cdd:PLN03102 87 AGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEP-LAREVLHLLSSEDSNLNlpvifiheiDFPKRPSSEELDYECL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 172 ------APLTSDSIAIVL---------YTSGGTGIPKGVRLSY-----SAICNRLWWQFRTFPysdseeICVWKTALTFV 231
Cdd:PLN03102 166 iqrgepTPSLVARMFRIQdehdpislnYTSGTTADPKGVVISHrgaylSTLSAIIGWEMGTCP------VYLWTLPMFHC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 232 DSVCEIWGPLLHGRALLILSRETTrdPQKLVNVLADNqIERLVLVPTLLRSILM--YLALGPASRPLRRLKLWVCSGETL 309
Cdd:PLN03102 240 NGWTFTWGTAARGGTSVCMRHVTA--PEIYKNIEMHN-VTHMCCVPTVFNILLKgnSLDLSPRSGPVHVLTGGSPPPAAL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 310 SKELaseffkyfgNEDGYKLANFYGSTEVMGDVTYyvLEGSDQLDLYP-----TIPIGRPLDNCAIYLLDEELSPTRDSE 384
Cdd:PLN03102 317 VKKV---------QRLGFQVMHAYGLTEATGPVLF--CEWQDEWNRLPenqqmELKARQGVSILGLADVDVKNKETQESV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 385 P------GEVWVAGANLAAGyvgggganrFCDNPHATQPDFQRLY-RTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLL 456
Cdd:PLN03102 386 PrdgktmGEIVIKGSSIMKG---------YLKNPKATSEAFKHGWlNTGDVGVIhPDGHVEIKDRSKDIIISGGENISSV 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 457 EVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHI------EGEL----RNALTHYMMP-QVIEVESIP 525
Cdd:PLN03102 457 EVENVLYKYPKVLETAVVAMPHPTWGETPCAFVVLEKGETTKEDRVdklvtrERDLieycRENLPHFMCPrKVVFLQELP 536
|
490
....*....|..
gi 223890156 526 LLVNGKVDRQGL 537
Cdd:PLN03102 537 KNGNGKILKPKL 548
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
33-543 |
1.00e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 61.33 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERARTvgPNRdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK07638 16 NKIAIKENDR----VLTYKDWFESVCKVANWLNEKESK--NKT-----IAILLENRIEFLQLFAGAAMAGWTCVPLDIKW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILKDAEPSLVIYDDSADPSMFKESGvPFASFEELaQEATSHSADEPMDAETL--APLTSDsiaivlYTSGGTG 190
Cdd:PRK07638 85 KQDELKERLAISNADMIVTERYKLNDLPDEEG-RVIEIDEW-KRMIEKYLPTYAPIENVqnAPFYMG------FTSGSTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 191 IPKG-VRLSYSAI----CNRlwwqfRTFPYSDSEEICVwktALTFVDSVCeIWGPL--LHGRALLILSRETTrdPQKLVN 263
Cdd:PRK07638 157 KPKAfLRAQQSWLhsfdCNV-----HDFHMKREDSVLI---AGTLVHSLF-LYGAIstLYVGQTVHLMRKFI--PNQVLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 264 VLADNQIERLVLVPTLLRSILmylalgPASRPLRRLKLWVCSG---ETLSKELASEFFKYFgnedgyKLANFYGSTEvMG 340
Cdd:PRK07638 226 KLETENISVMYTVPTMLESLY------KENRVIENKMKIISSGakwEAEAKEKIKNIFPYA------KLYEFYGASE-LS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 341 DVTYYVLEGSDQldlyPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGYVGggganrfcDNPHATQPDFQ 420
Cdd:PRK07638 293 FVTALVDEESER----RPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII--------GGVLARELNAD 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 421 RLYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGNPEilGFVTTKPGA---- 495
Cdd:PRK07638 361 GWMTVRDVGYEDEEGFIYiVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVI------GVPD--SYWGEKPVAiikg 432
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 223890156 496 RTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGLLKMYEN 543
Cdd:PRK07638 433 SATKQQLKSFCLQRLSSFKIPKEWHfVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
33-202 |
1.90e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 60.72 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDeissVQVSHAELAARTNVLARAISERARTVGpnrdsDYVIAVcmqpTHNTiMALLATW----KAGAAYVPM 108
Cdd:PRK08316 26 DKTALVFGD----RSWTYAELDAAVNRVAAALLDLGLKKG-----DRVAAL----GHNS-DAYALLWlacaRAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 109 EPSFPQGRITHILKDAEPSLVIYDDS----ADPSMFKESGVPF------------ASFEELAQEATSHSADEPmdaetLA 172
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLVDPAlaptAEAALALLPVDTLilslvlggreapGGWLDFADWAEAGSVAEP-----DV 166
|
170 180 190
....*....|....*....|....*....|
gi 223890156 173 PLTSDSIAIVLYTSGGTGIPKGVRLSYSAI 202
Cdd:PRK08316 167 ELADDDLAQILYTSGTESLPKGAMLTHRAL 196
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
47-537 |
1.98e-09 |
|
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: 60.55 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 47 QVSHAELAARTNVLARAIseRARTVGPNrdsdyVIAVCM-QPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAE 125
Cdd:cd05910 2 RLSFRELDERSDRIAQGL--TAYGIRRG-----MRAVLMvPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 126 PSLVIyddsadpsmfkesGVPfasfeelaqeatshSADEPmdaetlapltsdsiAIVLYTSGGTGIPKGVRLSYSAICNR 205
Cdd:cd05910 75 PDAFI-------------GIP--------------KADEP--------------AAILFTSGSTGTPKGVVYRHGTFAAQ 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 206 LWwQFRTFPYSDSEEICVwKTALTFVdsvceIWGPLLhGRALLILSRETTR----DPQKLVNVLADNQIERLVLVPTLLR 281
Cdd:cd05910 114 ID-ALRQLYGIRPGEVDL-ATFPLFA-----LFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 282 SILMYLAlgPASRPLRRLKLWVCSGETLSKELASEFFKYFgnEDGYKLANFYGSTEVMgDVTyyVLEGSDQLDLYPTIP- 360
Cdd:cd05910 186 RVARYCA--QHGITLPSLRRVLSAGAPVPIALAARLRKML--SDEAEILTPYGATEAL-PVS--SIGSRELLATTTAATs 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 361 ------IGRPLD--NCAIYLLDEELSPTRDS-------EPGEVWVAGANLAAGYVGGGGANRFCDNPhatQPDFQRLYRT 425
Cdd:cd05910 259 ggagtcVGRPIPgvRVRIIEIDDEPIAEWDDtlelprgEIGEITVTGPTVTPTYVNRPVATALAKID---DNSEGFWHRM 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 426 GDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILgFVTTKPGARTSAQHIEG 504
Cdd:cd05910 336 GDLGYLdDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVL-CVEPLPGTITPRARLEQ 414
|
490 500 510
....*....|....*....|....*....|....*....
gi 223890156 505 ELRNALTHYMMPQVIEV----ESIPLLV--NGKVDRQGL 537
Cdd:cd05910 415 ELRALAKDYPHTQRIGRflihPSFPVDIrhNAKIFREKL 453
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
5-531 |
2.02e-09 |
|
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: 60.75 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 5 PRVAVVTGPRAPVPT----APLT---HHLGPLAKSDRTALIYKDEISSVQVSHAELAARTNVLARAIseRARTVGPnrdS 77
Cdd:cd05943 49 YDVVVVSGRIMPGARwfpgARLNyaeNLLRHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAAL--RALGVKP---G 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 78 DYVIAVcMQPTHNTIMALLATWKAGAAYVPMEPSF-PQG------------------------------RITHILK---D 123
Cdd:cd05943 124 DRVAGY-LPNIPEAVVAMLATASIGAIWSSCSPDFgVPGvldrfgqiepkvlfavdaytyngkrhdvreKVAELVKglpS 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 124 AEPSLVIYDDSADPSMFKESGVPFASFEE-LAQEATSHSADEPMDAEtlAPLtsdsiaIVLYTSGGTGIPKGV------- 195
Cdd:cd05943 203 LLAVVVVPYTVAAGQPDLSKIAKALTLEDfLATGAAGELEFEPLPFD--HPL------YILYSSGTTGLPKCIvhgaggt 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 196 ---RLSYSAICNRLWWQFRTFPYSDseeiCVWK------TALTFVDSVCEIWGPLLHgrallilsrettRDPQKLVNVLA 266
Cdd:cd05943 275 llqHLKEHILHCDLRPGDRLFYYTT----CGWMmwnwlvSGLAVGATIVLYDGSPFY------------PDTNALWDLAD 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 267 DNQIERLVLVPTLLrSILMYLALGPA-SRPLRRLKlwvCSGETLSKeLASEFFKYFGNE--DGYKLANFYGSTEVMGdvt 343
Cdd:cd05943 339 EEGITVFGTSAKYL-DALEKAGLKPAeTHDLSSLR---TILSTGSP-LKPESFDYVYDHikPDVLLASISGGTDIIS--- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 344 YYVLEGsdqldlyPTIPIGR-----PLDNCAIYLLDEELSPTRDsEPGEVwvaganlaagyvgggganrFCDNPHATQP- 417
Cdd:cd05943 411 CFVGGN-------PLLPVYRgeiqcRGLGMAVEAFDEEGKPVWG-EKGEL-------------------VCTKPFPSMPv 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 418 -----------------DFQRLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCvvLCYGLD 479
Cdd:cd05943 464 gfwndpdgsryraayfaKYPGVWAHGDWIEItPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDS--LVVGQE 541
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 223890156 480 R--GNPEILGFVTTKPGARTS---AQHIEGELRNALTHYMMP-QVIEVESIPLLVNGK 531
Cdd:cd05943 542 WkdGDERVILFVKLREGVELDdelRKRIRSTIRSALSPRHVPaKIIAVPDIPRTLSGK 599
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
96-539 |
2.10e-09 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 60.53 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 96 LATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYddsadPSMFKESgvpfaSFEELA-----------------QEAT 158
Cdd:PRK06087 92 LACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFA-----PTLFKQT-----RPVDLIlplqnqlpqlqqivgvdKLAP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 159 SHSAD---------EPMDAETlaPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNrlwwqfrtfpysdSEEICVWKTALT 229
Cdd:PRK06087 162 ATSSLslsqiiadyEPLTTAI--TTHGDELAAVLFTSGTEGLPKGVMLTHNNILA-------------SERAYCARLNLT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 230 FVDSvceIWGP--------LLHGRALLILSRETTRDPQKLVNVLADNQIER----LVLVPT-LLRSILMYLALGPASrpL 296
Cdd:PRK06087 227 WQDV---FMMPaplghatgFLHGVTAPFLIGARSVLLDIFTPDACLALLEQqrctCMLGATpFIYDLLNLLEKQPAD--L 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 297 RRLKLWVCSGETLSKELASEFFKYfgnedGYKLANFYGSTEvmgDVTYYVLEGSDQLDLYPTIPiGRPLDNCAIYLLDEE 376
Cdd:PRK06087 302 SALRFFLCGGTTIPKKVARECQQR-----GIKLLSVYGSTE---SSPHAVVNLDDPLSRFMHTD-GYAAAGVEIKVVDEA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 377 LSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQP--DFQRLYRTGDFGTL-VKGAVLYAGRTDaQVKIR-GHR 452
Cdd:PRK06087 373 RKTLPPGCEGEEASRGPNVFMG---------YLDEPELTARalDEEGWYYSGDLCRMdEAGYIKITGRKK-DIIVRgGEN 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 453 VDLLEVERALAQVPGV-DKCVVLCYGlDRGNPEILGFVTTKPGARTS--AQHIEGELRNALTHYMMPQVIEV-ESIPLLV 528
Cdd:PRK06087 443 ISSREVEDILLQHPKIhDACVVAMPD-ERLGERSCAYVVLKAPHHSLtlEEVVAFFSRKRVAKYKYPEHIVViDKLPRTA 521
|
490
....*....|.
gi 223890156 529 NGKVDRQGLLK 539
Cdd:PRK06087 522 SGKIQKFLLRK 532
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
49-537 |
2.20e-09 |
|
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: 60.34 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 49 SHAELAARTNVLARAISERARTVGPNrdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSL 128
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDR------VATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 129 VIYDDS----------------------ADPSMFKESGVPFASFEEL-AQEATShsADEPMDAETLApltsdsiAIVLYT 185
Cdd:cd12119 101 VFVDRDflplleaiaprlptvehvvvmtDDAAMPEPAGVGVLAYEELlAAESPE--YDWPDFDENTA-------AAICYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 186 SGGTGIPKGVRLSYS-------AICNRLwwqfrTFPYSDSEeicvwkTALTFVdsvceiwgPLLH--------------- 243
Cdd:cd12119 172 SGTTGNPKGVVYSHRslvlhamAALLTD-----GLGLSESD------VVLPVV--------PMFHvnawglpyaaamvga 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 244 -----GRALlilsrettrDPQKLVNVLADNQIERLVLVPTLLRSILMYL-ALGPASRPLRRLklwVCSGETLSKELASEF 317
Cdd:cd12119 233 klvlpGPYL---------DPASLAELIEREGVTFAAGVPTVWQGLLDHLeANGRDLSSLRRV---VIGGSAVPRSLIEAF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 318 fkyfgNEDGYKLANFYGSTE-----VMGDVTYYVLEGSDQLDLYPTIPIGRPLDNCAIYLLDEELS--PTRDSEPGEV-- 388
Cdd:cd12119 301 -----EERGVRVIHAWGMTEtsplgTVARPPSEHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRelPWDGKAVGELqv 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 389 ---WVAGanlaagyvgggganRFCDNPHATQPDFQRLY-RTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALA 463
Cdd:cd12119 376 rgpWVTK--------------SYYKNDEESEALTEDGWlRTGDVATIdEDGYLTITDRSKDVIKSGGEWISSVELENAIM 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223890156 464 QVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVDRQGL 537
Cdd:cd12119 442 AHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVAKWWLPdDVVFVDEIPKTSTGKIDKKAL 516
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
149-539 |
2.39e-09 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 60.17 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 149 SFEELAQEA-TSHSAdepMDAETLAPLTsdsiaiVLYTSGGTGIPKGVRLSYS------AICNRLWWQFRTfpySDseei 221
Cdd:cd05928 154 NFKELLNEAsTEHHC---VETGSQEPMA------IYFTSGTTGSPKMAEHSHSslglglKVNGRYWLDLTA---SD---- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 222 CVWKTALT--FVDSVCEIWGPLLHGrALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRsilMYLALGPASRPLRRL 299
Cdd:cd05928 218 IMWNTSDTgwIKSAWSSLFEPWIQG-ACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYR---MLVQQDLSSYKFPSL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 300 KLWVCSGETLSKELASEffkyFGNEDGYKLANFYGSTE-VMGDVTYYVLE---GSdqldlyptipIGRPLDNCAIYLLDE 375
Cdd:cd05928 294 QHCVTGGEPLNPEVLEK----WKAQTGLDIYEGYGQTEtGLICANFKGMKikpGS----------MGKASPPYDVQIIDD 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 376 ELSPTRDSEPGEVWVAganlAAGYVGGGGANRFCDNPHATQPDFQR-LYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRV 453
Cdd:cd05928 360 NGNVLPPGTEGDIGIR----VKPIRPFGLFSGYVDNPEKTAATIRGdFYLTGDRGIMDEdGYFWFMGRADDVINSSGYRI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 454 DLLEVERALAQVPGVDKCVVLcygldrGNPE-ILG-----FVTTKPGARTSAQ-----HIEGELRNALTHYMMPQVIE-V 521
Cdd:cd05928 436 GPFEVESALIEHPAVVESAVV------SSPDpIRGevvkaFVVLAPQFLSHDPeqltkELQQHVKSVTAPYKYPRKVEfV 509
|
410
....*....|....*...
gi 223890156 522 ESIPLLVNGKVDRQGLLK 539
Cdd:cd05928 510 QELPKTVTGKIQRNELRD 527
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
179-532 |
4.47e-09 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 58.67 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 179 IAIVLYTSGGTGIPKGV----RLSYSAICNrlwWQFRTFPYSDSEEICVWKTALTFVDSVCEIWGpLLHGRALLilsRET 254
Cdd:cd17638 2 VSDIMFTSGTTGRSKGVmcahRQTLRAAAA---WADCADLTEDDRYLIINPFFHTFGYKAGIVAC-LLTGATVV---PVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 255 TRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASrpLRRLKLWVCSGETLSKELASEFFKYFGNEDgykLANFYG 334
Cdd:cd17638 75 VFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFD--LSSLRAAVTGAATVPVELVRRMRSELGFET---VLTAYG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 335 STEVmgdVTYYVLEGSDQLDLYPTIpIGRPLDNCAIYLLDeelsptrdsePGEVWVAGANLAAGyvgggganrFCDNPHA 414
Cdd:cd17638 150 LTEA---GVATMCRPGDDAETVATT-CGRACPGFEVRIAD----------DGEVLVRGYNVMQG---------YLDDPEA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 415 TQP--DFQRLYRTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTT 491
Cdd:cd17638 207 TAEaiDADGWLHTGDVGELdERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVA 286
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 223890156 492 KPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKV 532
Cdd:cd17638 287 RPGVTLTEEDVIAWCRERLANYKVPRFVRfLDELPRNASGKV 328
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
175-473 |
5.25e-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: 58.91 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 175 TSDSIAIVLYTSGGTGIPKGVRLSYSAicnrLWWQFRTF-----PYSDSEEICV---WKTALTFVDSVCEIWGPLLHGRA 246
Cdd:cd17640 86 DSDDLATIIYTSGTTGNPKGVMLTHAN----LLHQIRSLsdivpPQPGDRFLSIlpiWHSYERSAEYFIFACGCSQAYTS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 247 LLILSRETTR-DPQKLVNV------LADNQIERLVLVPTLLRSILMYLALGpasrplRRLKLWVCSGETLSKELaseffK 319
Cdd:cd17640 162 IRTLKDDLKRvKPHYIVSVprlwesLYSGIQKQVSKSSPIKQFLFLFFLSG------GIFKFGISGGGALPPHV-----D 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 320 YFGNEDGYKLANFYGSTEVMGDVT----YYVLEGSdqldlyptipIGRPLDNCAIYLLDEEL-SPTRDSEPGEVWVAGAN 394
Cdd:cd17640 231 TFFEAIGIEVLNGYGLTETSPVVSarrlKCNVRGS----------VGRPLPGTEIKIVDPEGnVVLPPGEKGIVWVRGPQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 395 LaagyvggggANRFCDNPHATQP--DFQRLYRTGDFGTLVKGAVL-YAGRT-DAQVKIRGHRVDLLEVERALAQVPGVDK 470
Cdd:cd17640 301 V---------MKGYYKNPEATSKvlDSDGWFNTGDLGWLTCGGELvLTGRAkDTIVLSNGENVEPQPIEEALMRSPFIEQ 371
|
...
gi 223890156 471 CVV 473
Cdd:cd17640 372 IMV 374
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
153-472 |
1.35e-08 |
|
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: 58.00 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 153 LAQEATSHSADEpmdAETLAPLTS---DSIAIVLYTSGGTGIPKGVRLSYS-------AICNRLwwqfrtfpysdSEEIC 222
Cdd:cd17639 64 LGEDALIHSLNE---TECSAIFTDgkpDDLACIMYTSGSTGNPKGVMLTHGnlvagiaGLGDRV-----------PELLG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 223 VWKTALTF----------VDSVCEIWGPLL-HGRALlILSRETTRDPQK---------LVNVLA------DNQIERLVLV 276
Cdd:cd17639 130 PDDRYLAYlplahifelaAENVCLYRGGTIgYGSPR-TLTDKSKRGCKGdltefkptlMVGVPAiwdtirKGVLAKLNPM 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 277 PTLLRSI--------LMYLALGPAS--------RPLR-----RLKLWVCSGETLSKElASEFFKYFGNEdgykLANFYGS 335
Cdd:cd17639 209 GGLKRTLfwtayqskLKALKEGPGTplldelvfKKVRaalggRLRYMLSGGAPLSAD-TQEFLNIVLCP----VIQGYGL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 336 TEVMGDVTYyvlegSDQLDLYPTIpIGRPLDNCAIYLLD-EELSPTRDSEP--GEVWVAGANLaagyvggggANRFCDNP 412
Cdd:cd17639 284 TETCAGGTV-----QDPGDLETGR-VGPPLPCCEIKLVDwEEGGYSTDKPPprGEILIRGPNV---------FKGYYKNP 348
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223890156 413 HATQPDF--QRLYRTGDFGTLVK-GAVLYAGRTDAQVKIR-GHRVDLLEVERALAQVPGVDK-CV 472
Cdd:cd17639 349 EKTKEAFdgDGWFHTGDIGEFHPdGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNiCV 413
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
24-195 |
1.66e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 57.60 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 24 HHLGPLAksDRTALIYKDEISSVQVSHAELAARTNVLARAIseRARTVGPNrdsDYVIaVCMQPTHNTIMALLATWKAGA 103
Cdd:PRK04319 52 HADGGRK--DKVALRYLDASRKEKYTYKELKELSNKFANVL--KELGVEKG---DRVF-IFMPRIPELYFALLGALKNGA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 104 AYVPMEPSFPQGRITHILKDAE-------------------PSL---VIYDDSAdpsmfkESGVPFASFEELAQEATSHS 161
Cdd:PRK04319 124 IVGPLFEAFMEEAVRDRLEDSEakvlittpallerkpaddlPSLkhvLLVGEDV------EEGPGTLDFNALMEQASDEF 197
|
170 180 190
....*....|....*....|....*....|....
gi 223890156 162 ADEPMDAETLApltsdsiaIVLYTSGGTGIPKGV 195
Cdd:PRK04319 198 DIEWTDREDGA--------ILHYTSGSTGKPKGV 223
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
145-541 |
2.03e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 56.59 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 145 VPFASFEELAQEATSHSADEPMDaetlapltsDSIAIVLYTSGGTGIPKGVRL-------SYSAICNRLWWQFRtfpysd 217
Cdd:PRK07824 12 VPAQDERRAALLRDALRVGEPID---------DDVALVVATSGTTGTPKGAMLtaaaltaSADATHDRLGGPGQ------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 218 seeicvWKTAL---------TFVDSVceiwgplLHGRALLILSRETTRDPQKLVNVLADNQIER--LVLVPTLLRSILMY 286
Cdd:PRK07824 77 ------WLLALpahhiaglqVLVRSV-------IAGSEPVELDVSAGFDPTALPRAVAELGGGRryTSLVPMQLAKALDD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 287 LAlgpASRPLRRLKLWVCSGETLSKELASEffkyfGNEDGYKLANFYGSTEVMGDVTYyvlegsdqlDlyptipiGRPLD 366
Cdd:PRK07824 144 PA---ATAALAELDAVLVGGGPAPAPVLDA-----AAAAGINVVRTYGMSETSGGCVY---------D-------GVPLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 367 NCAIYLLDeelsptrdsepGEVWVAGANLAAGYvgggganRFCDNPHA-TQPDFqrlYRTGDFGTLVKGAVLYAGRTDAQ 445
Cdd:PRK07824 200 GVRVRVED-----------GRIALGGPTLAKGY-------RNPVDPDPfAEPGW---FRTDDLGALDDGVLTVLGRADDA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 446 VKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESI 524
Cdd:PRK07824 259 ISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPrELHVVDEL 338
|
410
....*....|....*..
gi 223890156 525 PLLVNGKVDRQGLLKMY 541
Cdd:PRK07824 339 PRRGIGKVDRRALVRRF 355
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
32-540 |
4.25e-08 |
|
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: 56.38 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 32 SDRTALIykDEISSVQVSHAELAARTNVLARAISERARTVgpnrdsDYVIAVCMQPTHNTIMALLATWKAGAAYVPMEPS 111
Cdd:cd17642 31 PGTIAFT--DAHTGVNYSYAEYLEMSVRLAEALKKYGLKQ------NDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 112 FPQGRITHILKDAEPSLVIYDDSADPSMFK--------------ESGVPFASFEELAQEATSHSaDEPMDAETLAPLTSD 177
Cdd:cd17642 103 YNERELDHSLNISKPTIVFCSKKGLQKVLNvqkklkiiktiiilDSKEDYKGYQCLYTFITQNL-PPGFNEYDFKPPSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 178 ---SIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFR-TFPYSDSEEICVwktaLTFVdsvceiwgPLLHGRALLI---- 249
Cdd:cd17642 182 rdeQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDpIFGNQIIPDTAI----LTVI--------PFHHGFGMFTtlgy 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 250 ------LSRETTRDPQKLVNVLADNQIERLVLVPTLlrsiLMYLALGPA--SRPLRRLKLWVCSGETLSKELASEFFKYF 321
Cdd:cd17642 250 licgfrVVLMYKFEEELFLRSLQDYKVQSALLVPTL----FAFFAKSTLvdKYDLSNLHEIASGGAPLSKEVGEAVAKRF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 322 GnedgyklANF----YGSTEvmgdVTYYVLEGSDQLDLYPTIPIGRPLDNCAIYLLD--EELSPtrdSEPGEVWVAGANL 395
Cdd:cd17642 326 K-------LPGirqgYGLTE----TTSAILITPEGDDKPGAVGKVVPFFYAKVVDLDtgKTLGP---NERGELCVKGPMI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 396 AAGyvgggganrFCDNPHATQP--DFQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKC- 471
Cdd:cd17642 392 MKG---------YVNNPEATKAliDKDGWLHSGDIAYYDEdGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAg 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 472 ----------------VVLCYGLDRGNPEILGFVTTKPgarTSAQHIEGelrnalthymmpQVIEVESIPLLVNGKVDRQ 535
Cdd:cd17642 463 vagipdedagelpaavVVLEAGKTMTEKEVMDYVASQV---STAKRLRG------------GVKFVDEVPKGLTGKIDRR 527
|
....*
gi 223890156 536 GLLKM 540
Cdd:cd17642 528 KIREI 532
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
175-534 |
4.65e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 56.16 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 175 TSDSIAIVLYTSGGTGIPKGVRLSYSAIC-----NRLWWQfrtfPYSDSEEicVWKTALTFVD----SVCEIWGPLLHGR 245
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNLFanaaqGKAWVP----GLGDGPE--RVLAALPMFHayglTLCLTLAVSIGGE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 246 ALLIlsreTTRDPQKLVNVLADNQIERLVLVPTLlrsilmYLALGPASR----PLRRLKLWVCSGETLSKELASEFFKYF 321
Cdd:PRK05605 291 LVLL----PAPDIDLILDAMKKHPPTWLPGVPPL------YEKIAEAAEergvDLSGVRNAFSGAMALPVSTVELWEKLT 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 322 GnedGYkLANFYGSTE----VMGDVTyyvleGSDQLDLYptipIGRPLDNCAIYLLD-EELSPTR-DSEPGEVWVAGANL 395
Cdd:PRK05605 361 G---GL-LVEGYGLTEtspiIVGNPM-----SDDRRPGY----VGVPFPDTEVRIVDpEDPDETMpDGEEGELLVRGPQV 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 396 AAGyvgggganrFCDNPHATQPDFQ-RLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVV 473
Cdd:PRK05605 428 FKG---------YWNRPEETAKSFLdGWFRTGDVVVMEEdGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAV 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 223890156 474 LCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQ-VIEVESIPLLVNGKVDR 534
Cdd:PRK05605 499 VGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRrFYHVDELPRDQLGKVRR 560
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
176-537 |
4.67e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 56.31 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 176 SDSIAIVLYTSGGTGIPKGVRLSY-SAICNRLwwQFRTFPYSDSEEIC-VWKTALtfvdSVCEIWGPLLHGRALLILSRE 253
Cdd:PRK05677 206 ADDVAVLQYTGGTTGVAKGAMLTHrNLVANML--QCRALMGSNLNEGCeILIAPL----PLYHIYAFTFHCMAMMLIGNH 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 254 TT-----RDPQKLVNVLADNQIERLVLVPTLlrsilmYLAL--GPASRPL--RRLKLWVCSGETLSKELASEFFKYFGNE 324
Cdd:PRK05677 280 NIlisnpRDLPAMVKELGKWKFSGFVGLNTL------FVALcnNEAFRKLdfSALKLTLSGGMALQLATAERWKEVTGCA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 325 dgykLANFYGSTEVMGDVTYYVLEGSdQLDlyptiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggg 404
Cdd:PRK05677 354 ----ICEGYGMTETSPVVSVNPSQAI-QVG-----TIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKG------ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 405 anrFCDNPHATQP--DFQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRG 481
Cdd:PRK05677 418 ---YWQRPEATDEilDSDGWLKTGDIALIQEdGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKS 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 482 NPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIEV-ESIPLLVNGKVDRQGL 537
Cdd:PRK05677 495 GEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFrDELPTTNVGKILRREL 551
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
333-534 |
7.17e-08 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 54.97 E-value: 7.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 333 YGSTEVMGDVT---YYVLEGSdqldlyptipIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLaagyvggggANRFC 409
Cdd:cd17637 143 YGQTETSGLVTlspYRERPGS----------AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLV---------FQGYW 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 410 DNPHATQPDFQR-LYRTGDFGTLVKGAVL-YAGRTDAQ--VKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGNPE- 484
Cdd:cd17637 204 NLPELTAYTFRNgWHHTGDLGRFDEDGYLwYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVI------GVPDp 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 223890156 485 -----ILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDR 534
Cdd:cd17637 278 kwgegIKAVCVLKPGATLTADELIEFVGSRIARYKKPRYVVfVEALPKTADGSIDR 333
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
182-533 |
7.68e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 55.08 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 182 VLYTSGGTGIPKGVrlsysaicnrLWWQ---FRT----FPYSDSEEICVWKTALTFVDSVCEIW---GPLLHGRAL---- 247
Cdd:cd05924 8 ILYTGGTTGMPKGV----------MWRQediFRMlmggADFGTGEFTPSEDAHKAAAAAAGTVMfpaPPLMHGTGSwtaf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 248 --------LILSRETTrDPQKLVNVLADNQIERLVLV-PTLLRSILMYLAlGPASRPLRRLKLWVCSGETLSKELASEFF 318
Cdd:cd05924 78 ggllggqtVVLPDDRF-DPEEVWRTIEKHKVTSMTIVgDAMARPLIDALR-DAGPYDLSSLFAISSGGALLSPEVKQGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 319 KYFGNedgYKLANFYGSTEVMGDVTYYVLEGSDQldlyptipiGRPLDNCA--IYLLDEELSPTRDSEPGEVWVAGANLA 396
Cdd:cd05924 156 ELVPN---ITLVDAFGSSETGFTGSGHSAGSGPE---------TGPFTRANpdTVVLDDDGRVVPPGSGGVGWIARRGHI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 397 AgyvggggaNRFCDNPHATQPDF-----QRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDK 470
Cdd:cd05924 224 P--------LGYYGDEAKTAETFpevdgVRYAVPGDRATVEAdGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYD 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223890156 471 CVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGKVD 533
Cdd:cd05924 296 VLVVGRPDERWGQEVVAVVQLREGAGVDLEELREHCRTRIARYKLPkQVVFVDEIERSPAGKAD 359
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
176-537 |
7.82e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 54.79 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 176 SDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYsDSEEICVWKTALTFVD-SVCEIWGPLLHGRALLILSRET 254
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLF-DPDDVLLCGLPLFHVNgSVVTLLTPLASGAHVVLAGPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 255 TRDP---QKLVNVLADNQIERLVLVPTllrsILMYLALGPASRPLRRLKLWVCSGETLSKELasefFKYFGNEDGYKLAN 331
Cdd:cd05944 80 YRNPglfDNFWKLVERYRITSLSTVPT----VYAALLQVPVNADISSLRFAMSGAAPLPVEL----RARFEDATGLPVVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 332 FYGSTEVMGDVTYYVLEGSDQLDlyptiPIGRPLDNCA--IYLLDEELSPTRDSEPGEV---WVAGANLAAGyvggggan 406
Cdd:cd05944 152 GYGLTEATCLVAVNPPDGPKRPG-----SVGLRLPYARvrIKVLDGVGRLLRDCAPDEVgeiCVAGPGVFGG-------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 407 rFCDNPHATQPDFQRLY-RTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLcygldrGNPE 484
Cdd:cd05944 219 -YLYTEGNKNAFVADGWlNTGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAV------GQPD 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223890156 485 I------LGFVTTKPGARTSAQHIEGELRNALTHY-MMPQVIEV-ESIPLLVNGKVDRQGL 537
Cdd:cd05944 292 AhagelpVAYVQLKPGAVVEEEELLAWARDHVPERaAVPKHIEVlEELPVTAVGKVFKPAL 352
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
32-537 |
8.48e-08 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 55.46 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 32 SDRTALIYKDEISSVQ-VSHAELAARTNVLARAIseraRTVGPNRDsDYViAVCMQPTHNTIMALLATWKAGAAYVPMEP 110
Cdd:PRK08008 21 GHKTALIFESSGGVVRrYSYLELNEEINRTANLF----YSLGIRKG-DKV-ALHLDNCPEFIFCWFGLAKIGAIMVPINA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 111 SFPQGRITHILKDAEPSLVIYDDSADP---SMFKESGVP----FASFEELAQEATSHS-----ADEPMDAETLAPLTSDS 178
Cdd:PRK08008 95 RLLREESAWILQNSQASLLVTSAQFYPmyrQIQQEDATPlrhiCLTRVALPADDGVSSftqlkAQQPATLCYAPPLSTDD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 179 IAIVLYTSGGTGIPKGVRLSYsaiCNRLWWQFrtfpYSDseeicvWKTALT------------FVDSVCEIWGPLLHGRA 246
Cdd:PRK08008 175 TAEILFTSGTTSRPKGVVITH---YNLRFAGY----YSA------WQCALRdddvyltvmpafHIDCQCTAAMAAFSAGA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 247 LLILSRETT--------RDPQKLVNVLADNQIERLVLVPTL-------LRSILMYLAlgpasrplrrlklwvcsgetLSK 311
Cdd:PRK08008 242 TFVLLEKYSarafwgqvCKYRATITECIPMMIRTLMVQPPSandrqhcLREVMFYLN--------------------LSD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 312 ELASEFFKYFgnedGYKLANFYGSTE----VMGDVtyyvlegSDQLDLYPTipIGRPLDNCAIYLLDEELSPTRDSEPGE 387
Cdd:PRK08008 302 QEKDAFEERF----GVRLLTSYGMTEtivgIIGDR-------PGDKRRWPS--IGRPGFCYEAEIRDDHNRPLPAGEIGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 388 VWVAGanlaagYVGGGGANRFCDNPHATQPDFQR---LYrTGDFGTL-VKGAVLYAGRTDAQVKIRGHRVDLLEVERALA 463
Cdd:PRK08008 369 ICIKG------VPGKTIFKEYYLDPKATAKVLEAdgwLH-TGDTGYVdEEGFFYFVDRRCNMIKRGGENVSCVELENIIA 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223890156 464 QVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGL 537
Cdd:PRK08008 442 THPKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEiRKDLPRNCSGKIIKKNL 516
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
117-204 |
1.41e-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: 54.53 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 117 ITHILKDAEPSLVIYDDsadpsmfkesGVPFASFEELAQEATSHSADEPmdaetlaPLTSDSIAIVLYTSGGTGIPKGVR 196
Cdd:cd05927 71 IEYILNHAEISIVFCDA----------GVKVYSLEEFEKLGKKNKVPPP-------PPKPEDLATICYTSGTTGNPKGVM 133
|
....*...
gi 223890156 197 LSYSAICN 204
Cdd:cd05927 134 LTHGNIVS 141
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1-535 |
1.44e-07 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 54.51 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 1 MGSLPRVAVVTGPRAPvptaplthhlGPLAKSDRTALIYKDEISSVQvshaELAARTNVLARAISERartvgpnrdsdyv 80
Cdd:PRK05852 18 IADLVEVAATRLPEAP----------ALVVTADRIAISYRDLARLVD----DLAGQLTRSGLLPGDR------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 81 IAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYD-----DSADPSM----FKESGVPFASFE 151
Cdd:PRK05852 71 VALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDadgphDRAEPTTrwwpLTVNVGGDSGPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 152 ELAQEATSHSADEPMDAETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICnrlwwqfrtfpySDSEEICVwKTALTFV 231
Cdd:PRK05852 151 GGTLSVHLDAATEPTPATSTPEGLRPDDAMIMFTGGTTGLPKMVPWTHANIA------------SSVRAIIT-GYRLSPR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 232 DSVCEIWgPLLHGRALLILSRETTRDPQKLV-------------NVLADNQIERLVLVPTLLRSILMYLALGPASR---P 295
Cdd:PRK05852 218 DATVAVM-PLYHGHGLIAALLATLASGGAVLlpargrfsahtfwDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpaA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 296 LRRLKlwVCSGeTLSKELASEFFKYFGNedgyKLANFYGSTEVMGDVTYYVLEGSDQlDLYPTIPIGRPLDNCA--IYLL 373
Cdd:PRK05852 297 LRFIR--SCSA-PLTAETAQALQTEFAA----PVVCAFGMTEATHQVTTTQIEGIGQ-TENPVVSTGLVGRSTGaqIRIV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 374 DEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDFQR-LYRTGDFGTL-VKGAVLYAGRTDAQVKIRGH 451
Cdd:PRK05852 369 GSDGLPLPAGAVGEVWLRGTTVVRG---------YLGDPTITAANFTDgWLRTGDLGSLsAAGDLSIRGRIKELINRGGE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 452 RVDLLEVERALAQVPGVDKCVVLcygldrGNPEIL------GFVTTKPGARTSAQHIEGELRNALTHYMMPQVI-EVESI 524
Cdd:PRK05852 440 KISPERVEGVLASHPNVMEAAVF------GVPDQLygeavaAVIVPRESAPPTAEELVQFCRERLAAFEIPASFqEASGL 513
|
570
....*....|.
gi 223890156 525 PLLVNGKVDRQ 535
Cdd:PRK05852 514 PHTAKGSLDRR 524
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
150-546 |
2.28e-07 |
|
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: 54.10 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 150 FEELAQEATSHSADEPMDAETlaPLtsdsiaIVLYTSGGTGIPKGVR------LSYSAICNRLwwqfrTFPYSDsEEI-- 221
Cdd:cd05966 212 WHDLMAKQSPECEPEWMDSED--PL------FILYTSGSTGKPKGVVhttggyLLYAATTFKY-----VFDYHP-DDIyw 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 222 CV----WKTALTFVdsvceIWGPLLHGRALLIL-SRETTRDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGPASRPL 296
Cdd:cd05966 278 CTadigWITGHSYI-----VYGPLANGATTVMFeGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 297 RRLKLWVCSGETLSKELASEFFKYFGNED-------------GYKLANFYGSTevmgdvtyyvlegsdqldlyPTIP--I 361
Cdd:cd05966 353 SSLRVLGSVGEPINPEAWMWYYEVIGKERcpivdtwwqtetgGIMITPLPGAT--------------------PLKPgsA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 362 GRPLDNCAIYLLDEELSPtrdsEPGEVwvaGANLAagyvgggganrfcdnphATQP----------DFQR---------- 421
Cdd:cd05966 413 TRPFFGIEPAILDEEGNE----VEGEV---EGYLV-----------------IKRPwpgmartiygDHERyedtyfskfp 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 422 -LYRTGDfgtlvkGAVL----Y---AGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLD-RGNpEILGFVTTK 492
Cdd:cd05966 469 gYYFTGD------GARRdedgYywiTGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGE-AIYAFVTLK 541
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 223890156 493 PGARTSaQHIEGELRNALTHYMMP-----QVIEVESIPLLVNGKVDRQGLLKMYENTNN 546
Cdd:cd05966 542 DGEEPS-DELRKELRKHVRKEIGPiatpdKIQFVPGLPKTRSGKIMRRILRKIAAGEEE 599
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
75-534 |
8.92e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 52.08 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 75 RDSDYviavcmqptHNTIMALLATWKAGAAYVPMEPSFPQGRithilkdaepsLVIYDDSADPSmfkesgvPFASFEELA 154
Cdd:PRK12583 128 KTSDY---------HAMLQELLPGLAEGQPGALACERLPELR-----------GVVSLAPAPPP-------GFLAWHELQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 155 QEATSHSaDEPMDAETLAPLTSDSIAIvLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSEEICVWKTALTFVDSV 234
Cdd:PRK12583 181 ARGETVS-REALAERQASLDRDDPINI-QYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLYHCFGMV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 235 CEIWGPLLHGRALLILSRETtrDPQKLVNVLADNQIERLVLVPTLLRSILMYLALGpaSRPLRRLKLWVCSGETLSKELA 314
Cdd:PRK12583 259 LANLGCMTVGACLVYPNEAF--DPLATLQAVEEERCTALYGVPTMFIAELDHPQRG--NFDLSSLRTGIMAGAPCPIEVM 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 315 SEFFKYFGNEDgYKLAnfYGSTEVmGDVTYYVlEGSDQLDLYPTiPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGAN 394
Cdd:PRK12583 335 RRVMDEMHMAE-VQIA--YGMTET-SPVSLQT-TAADDLERRVE-TVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYS 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 395 LAAGyvgggganrFCDNPHATQP--DFQRLYRTGDFGTLvkgavlyagrtDAQ--VKIRGHRVDLL----------EVER 460
Cdd:PRK12583 409 VMKG---------YWNNPEATAEsiDEDGWMHTGDLATM-----------DEQgyVRIVGRSKDMIirggeniyprEIEE 468
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 223890156 461 ALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDR 534
Cdd:PRK12583 469 FLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRfVDEFPMTVTGKVQK 543
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
457-531 |
8.96e-07 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 46.77 E-value: 8.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 223890156 457 EVERALAQVPGVDKCVVlcYGLD---RGNpEILGFVTTKPGARTSAQHIEGELRNALTHYMMP-QVIEVESIPLLVNGK 531
Cdd:pfam13193 1 EVESALVSHPAVAEAAV--VGVPdelKGE-APVAFVVLKPGVELLEEELVAHVREELGPYAVPkEVVFVDELPKTRSGK 76
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
176-537 |
1.12e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 51.74 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 176 SDSIAIVLYTSGGTGIPKGVRLSYSaicNRLWWQFRTFPYSDSEEICVWKTAL----TFVDSVCEIWgPLLHGRALLILS 251
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHA---NLLANQRACLKFFSPKEDDVMMSFLppfhAYGFNSCTLF-PLLSGVPVVFAY 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 252 RETtrDPQKLVNVLADNQIERLVLVPTLLRSILMylALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGNedgYKLAN 331
Cdd:PRK06334 258 NPL--YPKKIVEMIDEAKVTFLGSTPVFFDYILK--TAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPH---IQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 332 FYGSTEVMGDVTYYVLEGsdqldlyPTIP--IGRPLDNCAIYLLDEELS-PTRDSEPGEVWVAGANLAAGYVGGGGANRF 408
Cdd:PRK06334 331 GYGTTECSPVITINTVNS-------PKHEscVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDFGQGF 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 409 cdnphaTQPDFQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGV-----DKCVVLCyGLDrGN 482
Cdd:PRK06334 404 ------VELGGETWYVTGDLGYVDRhGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQnaadhAGPLVVC-GLP-GE 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 483 PEILGFVTTKPgarTSAQHIEGELRNALTHYMM--PQVIEVESIPLLVNGKVDRQGL 537
Cdd:PRK06334 476 KVRLCLFTTFP---TSISEVNDILKNSKTSSILkiSYHHQVESIPMLGTGKPDYCSL 529
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
48-196 |
1.14e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 51.83 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 48 VSHAELAARTNVLARAIseraRTVGPNRDSdyVIAVCMqptHNTIMALLATW---KAGAAYVPMEPSFPQGRITHILKDA 124
Cdd:PRK08276 12 VTYGELEARSNRLAHGL----RALGLREGD--VVAILL---ENNPEFFEVYWaarRSGLYYTPINWHLTAAEIAYIVDDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 125 EPSLVI----YDDSADP------------SMFKESGVPFASFEE-LAQEATSHSADEPMDAEtlapltsdsiaiVLYTSG 187
Cdd:PRK08276 83 GAKVLIvsaaLADTAAElaaelpagvpllLVVAGPVPGFRSYEEaLAAQPDTPIADETAGAD------------MLYSSG 150
|
....*....
gi 223890156 188 GTGIPKGVR 196
Cdd:PRK08276 151 TTGRPKGIK 159
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
33-585 |
2.61e-06 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 50.72 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIY------KDEisSVQVSHAELAARTNVLARAIseRARTVGPNRdsdyVIAVCMQPTHNTIMALLATWKAGAAyV 106
Cdd:PRK07529 40 DAPALSFlldadpLDR--PETWTYAELLADVTRTANLL--HSLGVGPGD----VVAFLLPNLPETHFALWGGEAAGIA-N 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 107 PMEPSFPQGRITHILKDAEPSLVI--------------------------------------YDDSADPSMFKESGVPFA 148
Cdd:PRK07529 111 PINPLLEPEQIAELLRAAGAKVLVtlgpfpgtdiwqkvaevlaalpelrtvvevdlarylpgPKRLAVPLIRRKAHARIL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 149 SF-EELAQEatshSADEPMDAEtlaPLTSDSIAIVLYTSGGTGIPKGVRLSYSA-ICNRlwWQFRTFPYSDSEEICVWKT 226
Cdd:PRK07529 191 DFdAELARQ----PGDRLFSGR---PIGPDDVAAYFHTGGTTGMPKLAQHTHGNeVANA--WLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 227 ALTFVD-SVCEIWGPLLHGRALLILSRETTRDPQKLVN---VLADNQIERLVLVPTLLRSILmylALGPASRPLRRLKLW 302
Cdd:PRK07529 262 PLFHVNaLLVTGLAPLARGAHVVLATPQGYRGPGVIANfwkIVERYRINFLSGVPTVYAALL---QVPVDGHDISSLRYA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 303 VCSGETLSKELASEFfkyfgnED--GYKLANFYGSTEVMGDVTYYVLEGSDQLDlyptiPIGRPLDNCA--IYLLDEELS 378
Cdd:PRK07529 339 LCGAAPLPVEVFRRF------EAatGVRIVEGYGLTEATCVSSVNPPDGERRIG-----SVGLRLPYQRvrVVILDDAGR 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 379 PTRDSEPGEV---WVAGANLAAGYVGGGGANRFCdnphatqpDFQRLYRTGDFGTL-VKGAVLYAGRTDAQVkIR-GHRV 453
Cdd:PRK07529 408 YLRDCAVDEVgvlCIAGPNVFSGYLEAAHNKGLW--------LEDGWLNTGDLGRIdADGYFWLTGRAKDLI-IRgGHNI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 454 DLLEVERALAQVPGVDKCVVLcygldrGNP-----EI-LGFVTTKPGARTSaqhiEGELRnaltHYMMPQVIE------- 520
Cdd:PRK07529 479 DPAAIEEALLRHPAVALAAAV------GRPdahagELpVAYVQLKPGASAT----EAELL----AFARDHIAEraavpkh 544
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 223890156 521 ---VESIPLLVNGKVDRQGL-----LKMYE---NTNNNDDAEVAVDIDCSGAGLADLEAARALLET-VGAVLGRAAR 585
Cdd:PRK07529 545 vriLDALPKTAVGKIFKPALrrdaiRRVLRaalRDAGVEAEVVDVVEDGRRGLVAQVALRGAEDREaVAAVLGRYAF 621
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
93-203 |
3.48e-06 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 50.26 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 93 MALLATWkAGAAYVPMEPSFPQ-----GRITHILKDAEPSLVIYDDsADP-----SMFKESGVPFA------------SF 150
Cdd:PRK08180 110 LALAAMY-AGVPYAPVSPAYSLvsqdfGKLRHVLELLTPGLVFADD-GAAfaralAAVVPADVEVVavrgavpgraatPF 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 223890156 151 EELAQEATSHSADEPMDAetlapLTSDSIAIVLYTSGGTGIPKGVRLSYSAIC 203
Cdd:PRK08180 188 AALLATPPTAAVDAAHAA-----VGPDTIAKFLFTSGSTGLPKAVINTHRMLC 235
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
92-201 |
1.22e-05 |
|
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: 48.23 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 92 IMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVI---YDDSADpsmfKESGVP----------------FASFEE 152
Cdd:cd05932 45 FITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvgkLDDWKA----MAPGVPeglisislpppsaancQYQWDD 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 223890156 153 LAQEATSHSADEPMDAETLAPLtsdsiaivLYTSGGTGIPKGVRLSYSA 201
Cdd:cd05932 121 LIAQHPPLEERPTRFPEQLATL--------IYTSGTTGQPKGVMLTFGS 161
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
356-542 |
1.54e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 47.87 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 356 YPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDFQR--LYRTGDFGTLVK 433
Cdd:cd05908 311 LTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPG---------YYNNPEATAKVFTDdgWLKTGDLGFIRN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 434 GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKC-VVLC--YGLDRGNPEILGFVTTKPGAR---TSAQHIEGELr 507
Cdd:cd05908 382 GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGrVVACgvNNSNTRNEEIFCFIEHRKSEDdfyPLGKKIKKHL- 460
|
170 180 190
....*....|....*....|....*....|....*
gi 223890156 508 NALTHYMMPQVIEVESIPLLVNGKVDRQGLLKMYE 542
Cdd:cd05908 461 NKRGGWQINEVLPIRRIPKTTSGKVKRYELAQRYQ 495
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
129-202 |
4.11e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 47.03 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 129 VIY----DDSADPSMFKESGVPFASF---EELAQEAtshsadePMDAETlaPLTSDsIAIVLYTSGGTGIPKGVRLSYSA 201
Cdd:PLN02387 205 VIYmddeGVDSDSSLSGSSNWTVSSFsevEKLGKEN-------PVDPDL--PSPND-IAVIMYTSGSTGLPKGVMMTHGN 274
|
.
gi 223890156 202 I 202
Cdd:PLN02387 275 I 275
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
410-540 |
6.62e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.50 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 410 DNPHATQPDFQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQV-PGVDKCVVLCYGLDRGNPEILg 487
Cdd:PRK06814 999 ENPGVLEPPADGWYDTGDIVTIDEeGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAVSIPDARKGERIIL- 1077
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 223890156 488 fVTTKPGArTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQGLLKM 540
Cdd:PRK06814 1078 -LTTASDA-TRAAFLAHAKAAGASELMVPAEIItIDEIPLLGTGKIDYVAVTKL 1129
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
570-631 |
9.20e-05 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 40.62 E-value: 9.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223890156 570 RALLETVGAVLGRAArGTLSLRSGFYELGGNSLNSIYTITKLRDRgYYVEIS--DFLGASTLGE 631
Cdd:pfam00550 1 ERLRELLAEVLGVPA-EEIDPDTDLFDLGLDSLLAVELIARLEEE-FGVEIPpsDLFEHPTLAE 62
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
96-219 |
9.34e-05 |
|
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: 45.50 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 96 LATWKAGAAYVPMEPSFP-----QGRITHILKDAEPSLVIYDDSAdpsMFKES-------GVPFA------------SFE 151
Cdd:cd05921 68 LAAMYAGVPAAPVSPAYSlmsqdLAKLKHLFELLKPGLVFAQDAA---PFARAlaaifplGTPLVvsrnavagrgaiSFA 144
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223890156 152 ELAqeATSHSADEPmdaETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNRLWWQFRTFPYSDSE 219
Cdd:cd05921 145 ELA--ATPPTAAVD---AAFAAVGPDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEE 207
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
92-202 |
9.43e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 45.60 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 92 IMALLATWKAGAAYVPMEPSFPQGRITHILKDAEPSLVIYDDSADPSMF---------------------------KESG 144
Cdd:PLN02861 116 IIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQESKISSILsclpkcssnlktivsfgdvsseqkeeaEELG 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 223890156 145 VPFASFEELAQEATshsadepMDAEtLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAI 202
Cdd:PLN02861 196 VSCFSWEEFSLMGS-------LDCE-LPPKQKTDICTIMYTSGTTGEPKGVILTNRAI 245
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
59-481 |
1.15e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.14 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 59 VLARAISERARTVgpNRDSDYVIAVCMQPTHNTIMALLATWKAGAAyVPMEPSFPQGrithilkdAEPslviyDDSADPS 138
Cdd:PRK05851 37 VHGRAENVAARLL--DRDRPGAVGLVGEPTVELVAAIQGAWLAGAA-VSILPGPVRG--------ADD-----GRWADAT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 139 M--FKESGVP--FASFEELAQEATSHSADEPMD---------AETLAPLTSDSIAIVLYTSGGTGIPKGVRLSYSAICNR 205
Cdd:PRK05851 101 LtrFAGIGVRtvLSHGSHLERLRAVDSSVTVHDlataahtnrSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 206 L--WWQfRTFPYSDSEEICVW-----KTALTFVDSV----CEIWgpllhgralLILSRETTRDPQKLVNVLADNQiERLV 274
Cdd:PRK05851 181 LrgLNA-RVGLDAATDVGCSWlplyhDMGLAFLLTAalagAPLW---------LAPTTAFSASPFRWLSWLSDSR-ATLT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 275 LVPTLLRSILMYLALGPASRPLRRLKLWVCSGETLSKELASEFFKY---FGNEDGyKLANFYGSTEVMGDVTYYVLEGSD 351
Cdd:PRK05851 250 AAPNFAYNLIGKYARRVSDVDLGALRVALNGGEPVDCDGFERFATAmapFGFDAG-AAAPSYGLAESTCAVTVPVPGIGL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 352 QLDLYPTIP---------IGRPLDNCAIYLL-DEELSPTRDSEPGEVWVAGANLAAGYVgggganrfcdnphATQP-DFQ 420
Cdd:PRK05851 329 RVDEVTTDDgsgarrhavLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSGYL-------------GQAPiDPD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223890156 421 RLYRTGDFGTLVKGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRG 481
Cdd:PRK05851 396 DWFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEG 456
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
33-201 |
1.16e-04 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 45.25 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAISERartvGPNRDSdyVIAVCMQPTHNTIMALLATWKAGAAYVPMEPSF 112
Cdd:PRK09029 18 QAIALRLNDE----VLTWQQLCARIDQLAAGFAQQ----GVVEGS--GVALRGKNSPETLLAYLALLQCGARVLPLNPQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 113 PQGRITHILkdaePSL---VIYDDSADPSmfkesgvpFASFEELAQEATSHSADEPMDAETLAPLTsdsiaivlYTSGGT 189
Cdd:PRK09029 88 PQPLLEELL----PSLtldFALVLEGENT--------FSALTSLHLQLVEGAHAVAWQPQRLATMT--------LTSGST 147
|
170
....*....|..
gi 223890156 190 GIPKGVRLSYSA 201
Cdd:PRK09029 148 GLPKAAVHTAQA 159
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
150-195 |
1.19e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 45.52 E-value: 1.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 223890156 150 FEELAQEATSHSADEPMDAEtlAPLtsdsiaIVLYTSGGTGIPKGV 195
Cdd:PRK00174 226 WHELVAGASDECEPEPMDAE--DPL------FILYTSGSTGKPKGV 263
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
144-482 |
1.22e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 45.37 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 144 GVPFASFEELAQEA--TSHSADEPMDAETLAPL--TSDSIAIVLYTSGGTGIPKGVRLSYSAIcnrlwwqfrtfpYSDSE 219
Cdd:PRK07768 115 GEPFLAAAPVLEEKgiRVLTVADLLAADPIDPVetGEDDLALMQLTSGSTGSPKAVQITHGNL------------YANAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 220 EICVwKTALTFVDSVCEIWGPLLHGRAL---LILsrettrdPQKLVNvladnqiERLVLVPT-LLRSILMYLAL------ 289
Cdd:PRK07768 183 AMFV-AAEFDVETDVMVSWLPLFHDMGMvgfLTV-------PMYFGA-------ELVKVTPMdFLRDPLLWAELiskyrg 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 290 ----GP------ASRPLRR-----------LKLWVCSGETLSKELASEFF---KYFGNEDGyKLANFYGSTEVM------ 339
Cdd:PRK07768 248 tmtaAPnfayalLARRLRRqakpgafdlssLRFALNGAEPIDPADVEDLLdagARFGLRPE-AILPAYGMAEATlavsfs 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 340 ----GDVTYYV----LEG------SDQLDLYPTIPIGRPLDNCAIYLLDEELSPTRDSEPGEVWVAGANLAAGYvgggga 405
Cdd:PRK07768 327 pcgaGLVVDEVdadlLAAlrravpATKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY------ 400
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223890156 406 nRFCDNPHATQpDFQRLYRTGDFGTLV-KGAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLDRGN 482
Cdd:PRK07768 401 -LTMDGFIPAQ-DADGWLDTGDLGYLTeEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGH 476
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
41-218 |
1.31e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.16 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 41 DEISSVQVSHAELAARTNVLARAISERARTVGPNRdsdyvIAVCMQPTHNTIMALLATWKAGAAYVPMEPSFPQGRITHI 120
Cdd:PRK05620 32 GGAEQEQTTFAAIGARAAALAHALHDELGITGDQR-----VGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 121 LKDAEPSLVIYD--------------------------DSADPSMFKESGVPFASFEELAQEATSHsADEPMDAETLApl 174
Cdd:PRK05620 107 INHAEDEVIVADprlaeqlgeilkecpcvravvfigpsDADSAAAHMPEGIKVYSYEALLDGRSTV-YDWPELDETTA-- 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 223890156 175 tsdsiAIVLYTSGGTGIPKGVRLSYSAicnrLWWQFRTFPYSDS 218
Cdd:PRK05620 184 -----AAICYSTGTTGAPKGVVYSHRS----LYLQSLSLRTTDS 218
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
92-195 |
1.44e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 45.04 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 92 IMALlATWKAGAAYVPMEPSF---PQG--RITHILKDAEPSLVIYDDSAdpsMF-------KESGVPFASFEELAQ-EAT 158
Cdd:PRK12582 120 LMTL-AAMQAGVPAAPVSPAYslmSHDhaKLKHLFDLVKPRVVFAQSGA---PFaralaalDLLDVTVVHVTGPGEgIAS 195
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 223890156 159 SHSAD----EPMD--AETLAPLTSDSIAIVLYTSGGTGIPKGV 195
Cdd:PRK12582 196 IAFADlaatPPTAavAAAIAAITPDTVAKYLFTSGSTGMPKAV 238
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
46-206 |
1.59e-04 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 44.73 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 46 VQVSHAELAARTnvlaRAISERARTVgpNRDSDYVIAVCMQPThNTIMALLATWKAGAAYVPM-EPSFP--QGRITHILK 122
Cdd:PRK12476 67 VELTWTQLGVRL----RAVGARLQQV--AGPGDRVAILAPQGI-DYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 123 DAEPSLVIYDDSADPSMFK-ESGVPFASFEE-LAQEATSHSADEPMDAetlAPLTSDSIAIVLYTSGGTGIPKGVRLSYS 200
Cdd:PRK12476 140 DAEPTVVLTTTAAAEAVEGfLRNLPRLRRPRvIAIDAIPDSAGESFVP---VELDTDDVSHLQYTSGSTRPPVGVEITHR 216
|
....*.
gi 223890156 201 AICNRL 206
Cdd:PRK12476 217 AVGTNL 222
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
36-539 |
1.75e-04 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 44.58 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 36 ALIYKDEISSVQ------VSHAELAARTNVLARAIseraRTVGPnRDSDYVIAVCMQPTHNTIMALlATWKAGAAYVPME 109
Cdd:PLN02330 38 AELYADKVAFVEavtgkaVTYGEVVRDTRRFAKAL----RSLGL-RKGQVVVVVLPNVAEYGIVAL-GIMAAGGVFSGAN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 110 PSfpqGRITHILKDAEPS---LVIYDDsADPSMFKESGVPFASFEELAQEATSH------SADEPMDAETLAPLTSDSIA 180
Cdd:PLN02330 112 PT---ALESEIKKQAEAAgakLIVTND-TNYGKVKGLGLPVIVLGEEKIEGAVNwkelleAADRAGDTSDNEEILQTDLC 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 181 IVLYTSGGTGIPKGVRLSY----SAICNRLwwqfrtfpYSDSEEICVWKTALTFVdsvceiwgPLLHGRALLILSRETTR 256
Cdd:PLN02330 188 ALPFSSGTTGISKGVMLTHrnlvANLCSSL--------FSVGPEMIGQVVTLGLI--------PFFHIYGITGICCATLR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 257 DPQKLV-----------NVLADNQIERLVLVPtllrSILMYLALGPASRPLRRLKLWVCSGETLSKELASEFFKYFGNE- 324
Cdd:PLN02330 252 NKGKVVvmsrfelrtflNALITQEVSFAPIVP----PIILNLVKNPIVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKf 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 325 DGYKLANFYGSTEvMGDVTYYVLEGSDQLDLYPTIPIGRPLDNCAIYLLDEE--LSPTRDSePGEVWVAGANLAAGyvgg 402
Cdd:PLN02330 328 PGVQVQEAYGLTE-HSCITLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDPDtgRSLPKNT-PGELCVRSQCVMQG---- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 403 gganrFCDNPHATQP--DFQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVLCYGLD 479
Cdd:PLN02330 402 -----YYNNKEETDRtiDEDGWLHTGDIGYIDDdGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDE 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223890156 480 RGNPEILGFVTTKPGARTSAQHIEGELRNALTHYMMPQVIE-VESIPLLVNGKVDRQgLLK 539
Cdd:PLN02330 477 EAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQfVDSIPKSLSGKIMRR-LLK 536
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
26-473 |
6.81e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 42.71 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 26 LGPLAKSDRTALIYKDEissvQVSHAELAARTNVLARAISERARTVGPnrdsdYVIAVCMQPTHNTIMALLATWKAGAAY 105
Cdd:PRK13388 9 LRDRAGDDTIAVRYGDR----TWTWREVLAEAAARAAALIALADPDRP-----LHVGVLLGNTPEMLFWLAAAALGGYVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 106 VPMEPSFPQGRITHILKDAEPSLVIYDDSADPSM--FKESGVPF-----ASFEELAQEATshsadepmDAETLAPLTSDS 178
Cdd:PRK13388 80 VGLNTTRRGAALAADIRRADCQLLVTDAEHRPLLdgLDLPGVRVldvdtPAYAELVAAAG--------ALTPHREVDAMD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 179 IAIVLYTSGGTGIPKGVRLSysaicnrlwwQFRT--FPYSDSEeicvwKTALTFVDsVCEIWGPLLHGRALLIL------ 250
Cdd:PRK13388 152 PFMLIFTSGTTGAPKAVRCS----------HGRLafAGRALTE-----RFGLTRDD-VCYVSMPLFHSNAVMAGwapava 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 251 SRETTRDPQKL--VNVLADnqIERL-VLVPTLLRSILMYLALGP-----ASRPLRrlklwVCSGETLSKELASEFFKYFG 322
Cdd:PRK13388 216 SGAAVALPAKFsaSGFLDD--VRRYgATYFNYVGKPLAYILATPerpddADNPLR-----VAFGNEASPRDIAEFSRRFG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 323 NE--DGYklanfyGSTEVMGDVTyyvlegsdQLDLYPTIPIGRPLDNCAIYLLD--EELSPTR----------DSEPGE- 387
Cdd:PRK13388 289 CQveDGY------GSSEGAVIVV--------REPGTPPGSIGRGAPGVAIYNPEtlTECAVARfdahgallnaDEAIGEl 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 388 VWVAGANLAAGyvgggganrFCDNPHATQPDFQR-LYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVDLLEVERALAQV 465
Cdd:PRK13388 355 VNTAGAGFFEG---------YYNNPEATAERMRHgMYWSGDLAYRDADGWIYfAGRTADWMRVDGENLSAAPIERILLRH 425
|
....*...
gi 223890156 466 PGVDKCVV 473
Cdd:PRK13388 426 PAINRVAV 433
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
114-429 |
6.83e-04 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 42.80 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 114 QGRITHILKdaepslVIYDDSADPSMFKESGVpfASFEELAQEATSHSADEP--MDAEtLAPLTSDSIAIVLYTSGGTGI 191
Cdd:cd17641 102 ADRIPSVRY------VIYCDPRGMRKYDDPRL--ISFEDVVALGRALDRRDPglYERE-VAAGKGEDVAVLCTTSGTTGK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 192 PKGVRLSYSAICNR-----------------------------------LWWQFRT-FPYS------DSEEIcvwktALT 229
Cdd:cd17641 173 PKLAMLSHGNFLGHcaaylaadplgpgdeyvsvlplpwigeqmysvgqaLVCGFIVnFPEEpetmmeDLREI-----GPT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 230 FVDSVCEIWgpllHGRALLILSR--ETTRDPQKLVNVL------ADNQIERLVLVPTLLRsILMYLALGPASRPLR-RLK 300
Cdd:cd17641 248 FVLLPPRVW----EGIAADVRARmmDATPFKRFMFELGmklglrALDRGKRGRPVSLWLR-LASWLADALLFRPLRdRLG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 301 LWVC-SGETLSKELASEFFKYFgNEDGYKLANFYGSTEVMGdvtYYVLEGSDQLDlYPTIpiGRPLDNCAIylldeelsp 379
Cdd:cd17641 323 FSRLrSAATGGAALGPDTFRFF-HAIGVPLKQLYGQTELAG---AYTVHRDGDVD-PDTV--GVPFPGTEV--------- 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 223890156 380 tRDSEPGEVWVAGANLAAGyvgggganrFCDNPHATQPDFQR--LYRTGDFG 429
Cdd:cd17641 387 -RIDEVGEILVRSPGVFVG---------YYKNPEATAEDFDEdgWLHTGDAG 428
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
33-204 |
1.17e-03 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 42.11 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDeiSSVQVSHAELAARTNVLARAIS----ERARTVG---PNRdSDYVIavcMQpthntimalLATWKAGAAY 105
Cdd:PRK08315 31 DREALVYRD--QGLRWTYREFNEEVDALAKGLLalgiEKGDRVGiwaPNV-PEWVL---TQ---------FATAKIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 106 VPMEPSFPQGRITHILKDAE---------------------------------------PSL--VIY-DDSADPSMFkes 143
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGckaliaadgfkdsdyvamlyelapelatcepgqlqsarlPELrrVIFlGDEKHPGML--- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 223890156 144 gvpfaSFEELAQEATsHSADEPMDA--ETLAPltSDSIAIvLYTSGGTGIPKGVRLSYSAICN 204
Cdd:PRK08315 173 -----NFDELLALGR-AVDDAELAArqATLDP--DDPINI-QYTSGTTGFPKGATLTHRNILN 226
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
128-199 |
1.18e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 42.01 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223890156 128 LVIY--DDSADPSMFKESGVPFASFEELAQEATSHSadepmdaETLAPLTSDSIAIVLYTSGGTGIPKGVRLSY 199
Cdd:PLN02736 177 IVVVggADEPLPSLPSGTGVEIVTYSKLLAQGRSSP-------QPFRPPKPEDVATICYTSGTTGTPKGVVLTH 243
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
164-540 |
1.75e-03 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 41.42 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 164 EPMDAETlaPLtsdsiaIVLYTSGGTGIPKGV------RLSYSAICNRlwwqfRTFPYSDSE-----EICVWKTALTFVd 232
Cdd:PLN02654 270 EWVDAED--PL------FLLYTSGSTGKPKGVlhttggYMVYTATTFK-----YAFDYKPTDvywctADCGWITGHSYV- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 233 svceIWGPLLHGRALLILSRETTR-DPQKLVNVLADNQIERLVLVPTLLRSiLMYLALGPASRPLRR-LKLWVCSGETLS 310
Cdd:PLN02654 336 ----TYGPMLNGATVLVFEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRS-LMRDGDEYVTRHSRKsLRVLGSVGEPIN 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 311 KELASEFFKYFGNEDgYKLANFYGSTEVMGDV------TYYVLEGSDQLDLYPTIPI-----GRPLD-NCAIYLLdeels 378
Cdd:PLN02654 411 PSAWRWFFNVVGDSR-CPISDTWWQTETGGFMitplpgAWPQKPGSATFPFFGVQPVivdekGKEIEgECSGYLC----- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 379 pTRDSEPGEVwvaganlaagyvgggganRFCDNPHAT------QPdFQRLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGH 451
Cdd:PLN02654 485 -VKKSWPGAF------------------RTLYGDHERyettyfKP-FAGYYFSGDGCSRDKdGYYWLTGRVDDVINVSGH 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 452 RVDLLEVERALAQVPGVDKCVVLCYGLDRGNPEILGFVTTKPGARTSAQ---HIEGELRNALTHYMMPQVIE-VESIPLL 527
Cdd:PLN02654 545 RIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEElrkSLILTVRNQIGAFAAPDKIHwAPGLPKT 624
|
410
....*....|...
gi 223890156 528 VNGKVDRQGLLKM 540
Cdd:PLN02654 625 RSGKIMRRILRKI 637
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
33-532 |
2.03e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 41.18 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 33 DRTALIYKDEissvQVSHAELAARTNVLARAIseRARTVGPnrdSDYVIavCMQPTHNTIM-ALLATWKAGAAYVPmePS 111
Cdd:PRK07470 22 DRIALVWGDR----SWTWREIDARVDALAAAL--AARGVRK---GDRIL--VHSRNCNQMFeSMFAAFRLGAVWVP--TN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 112 FPQ--GRITHILKDAEPSLVIYDdsADpsmfkesgvpFASFEELAQEATSH--------SADEPMDAETL---------- 171
Cdd:PRK07470 89 FRQtpDEVAYLAEASGARAMICH--AD----------FPEHAAAVRAASPDlthvvaigGARAGLDYEALvarhlgarva 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 172 -APLTSDSIAIVLYTSGGTGIPKGVRLSYS----AICNRLwwqfrtfpysdseeiCVWKTALTFVDsVCEIWGPLLHG-- 244
Cdd:PRK07470 157 nAAVDHDDPCWFFFTSGTTGRPKAAVLTHGqmafVITNHL---------------ADLMPGTTEQD-ASLVVAPLSHGag 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 245 -RALLILSRETTR--------DPQKLVNVLADNQIERLVLVPTLLR-------------SILMYL--ALGPASRPLRRLK 300
Cdd:PRK07470 221 iHQLCQVARGAATvllpserfDPAEVWALVERHRVTNLFTVPTILKmlvehpavdrydhSSLRYViyAGAPMYRADQKRA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 301 LwvcsgETLskelaseffkyfgnedGYKLANFYGSTEVMGDVTyyVLEGSDQ-LDLYPTIPIG---RPLDNCAIYLLDEE 376
Cdd:PRK07470 301 L-----AKL----------------GKVLVQYFGLGEVTGNIT--VLPPALHdAEDGPDARIGtcgFERTGMEVQIQDDE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 377 LSPTRDSEPGEVWVAGANLAAGYVGGgganrfcdnPHATQPDFQR-LYRTGDFGTLVKGAVLY-AGRTDAQVKIRGHRVD 454
Cdd:PRK07470 358 GRELPPGETGEICVIGPAVFAGYYNN---------PEANAKAFRDgWFRTGDLGHLDARGFLYiTGRASDMYISGGSNVY 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 455 LLEVERALAQVPGVDKCVVLcygldrGNP-----EI-LGFVTTKPGARTSAQHIEGELRNALTHYMMPQ-VIEVESIPLL 527
Cdd:PRK07470 429 PREIEEKLLTHPAVSEVAVL------GVPdpvwgEVgVAVCVARDGAPVDEAELLAWLDGKVARYKLPKrFFFWDALPKS 502
|
....*
gi 223890156 528 VNGKV 532
Cdd:PRK07470 503 GYGKI 507
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
150-299 |
4.52e-03 |
|
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: 40.03 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 150 FEELAQEATSHSADEPMDaeTLAPltsDSIAIVLYTSGGTGIPKGVRLSYSAICnrlwW-------QFRTFPYSDSEEIC 222
Cdd:cd05933 128 FMELGRSIPDEQLDAIIS--SQKP---NQCCTLIYTSGTTGMPKGVMLSHDNIT----WtakaasqHMDLRPATVGQESV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 223 VWKTALTFVDS-VCEIWGPLLHGrallilsrETTRDPQK------LVNVLADNQIERLVLVPTLLRSIL-MYLALGPASR 294
Cdd:cd05933 199 VSYLPLSHIAAqILDIWLPIKVG--------GQVYFAQPdalkgtLVKTLREVRPTAFMGVPRVWEKIQeKMKAVGAKSG 270
|
....*
gi 223890156 295 PLRRL 299
Cdd:cd05933 271 TLKRK 275
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
246-534 |
6.44e-03 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 39.47 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 246 ALLILSRETTRDPQKLVNVLADNQIERLVLVPTLLRsILMYLALGPASRPLRRLklwVCSGETLSKELASEFFKYFGN-- 323
Cdd:cd05974 153 ATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWR-MLIQQDLASFDVKLREV---VGAGEPLNPEVIEQVRRAWGLti 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 324 EDGYklanfyGSTEVMgdvtyyVLEGSDQLDLYPTIPIGRPLDNCAIYLLDEELSPTRDsepGEV-WVAGANlaagyVGG 402
Cdd:cd05974 229 RDGY------GQTETT------ALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATE---GEVaLDLGDT-----RPV 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223890156 403 GGANRFCDNPHATQPDFQ-RLYRTGDFGTLVK-GAVLYAGRTDAQVKIRGHRVDLLEVERALAQVPGVDKCVVlcygLDR 480
Cdd:cd05974 289 GLMKGYAGDPDKTAHAMRgGYYRTGDIAMRDEdGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV----VPS 364
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223890156 481 GNPEILG----FVTTKPGA---RTSAQHIEGELRNALTHYMMPQVIEVESIPLLVNGKVDR 534
Cdd:cd05974 365 PDPVRLSvpkaFIVLRAGYepsPETALEIFRFSRERLAPYKRIRRLEFAELPKTISGKIRR 425
|
|
| |
