|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
15-533 |
0e+00 |
|
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: 669.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 15 MDRVAVCFDEcnNQLPVYYTYKTVVNAASELSNFLLLHCDFqGIREIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPP 94
Cdd:cd17654 1 PDRPALIIDQ--TTSDTTVSYADLAEKISNLSNFLRKKFQT-EERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 95 SLSTHFMKKCNLKYILVEKKQINKFKSFHetllnydtftvehndlvlfrlhwkntevnlmlndgkekyekekiksisseh 174
Cdd:cd17654 78 QRSLTVMKKCHVSYLLQNKELDNAPLSFT--------------------------------------------------- 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 175 vneeKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALS 254
Cdd:cd17654 107 ----PEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLS 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 255 SGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGE 334
Cdd:cd17654 183 SGATLLIVPTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGK 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 335 GNKTQIFNVYGITEVSSWATIYRIPEKtlnstlkcELPVQLGFPLLGTVVEVRDTNGFtiqEGSGQVFLGGRNRVCFLDD 414
Cdd:cd17654 263 GNRTRIFNIYGITEVSCWALAYKVPEE--------DSPVQLGSPLLGTVIEVRDQNGS---EGTGQVFLGGLNRVCILDD 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 415 EVTVPLGTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKdaSVK 494
Cdd:cd17654 332 EVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGE--SSS 409
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034638423 495 EYIFKELQKY-LPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17654 410 SRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
16-533 |
6.72e-97 |
|
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: 314.08 E-value: 6.72e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVCFDecNNQLpvyyTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd05930 2 DAVAVVDG--DQSL----TYAELDARANRLARYLRERGVGPGDL-VAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 96 LSTHFMKKCNLKYILVEkkqinkfksfhetllnydtftveHNDLvlfrlhwkntevnlmlndgkekyekekiksissehv 175
Cdd:cd05930 75 RLAYILEDSGAKLVLTD-----------------------PDDL------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 176 neekaeehmdlrlkhclAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSS 255
Cdd:cd05930 96 -----------------AYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLA 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 256 GASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVlsatTSLRVLALGGEAFPSlTVLRSWRGEG 335
Cdd:cd05930 159 GATLVVLPEEVRKDPEALAD-LLAEEGITVLHLTPSLLRLLLQELELAAL----PSLRLVLVGGEALPP-DLVRRWRELL 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 336 NKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRN--RVCFL 412
Cdd:cd05930 233 PGARLVNLYGPTEATVDATYYRVPPDDEEDG-----RVPIGRPIPNTRVYVLDENLRPVPPGvPGELYIGGAGlaRGYLN 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 413 DDEVT---------VPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYN---- 478
Cdd:cd05930 308 RPELTaerfvpnpfGPGERMYRTGDLVRWLpDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREdgdg 387
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638423 479 QEKLILFMVSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05930 388 EKRLVAYVVPDEGGEldEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
68-474 |
3.51e-60 |
|
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: 211.74 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 68 GIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEkkqinkfkSFHETLLNYDTFTVEHNDLVLfrlhwk 147
Cdd:TIGR01733 35 SAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD--------SALASRLAGLVLPVILLDPLE------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 148 ntevNLMLNDGKekyekekiksiSSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFD 227
Cdd:TIGR01733 101 ----LAALDDAP-----------APPPPDAPSGPDD--------LAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 228 ITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLrrfgsQLIKSTVLS 307
Cdd:TIGR01733 158 LDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL-----ALLAAALPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 308 ATTSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNStlkcELPVQLGFPLLGTVVEVR 387
Cdd:TIGR01733 233 ALASLRLVILGGEALTPALVDR-WRARGPGARLINLYGPTETTVWSTATLVDPDDAPR----ESPVPIGRPLANTRLYVL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 388 DTNGFTIQEG-------SG-QVFLG-----GRNRVCFLDDE-VTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGK 452
Cdd:TIGR01733 308 DDDLRPVPVGvvgelyiGGpGVARGylnrpELTAERFVPDPfAGGDGARLYRTGDLVRYlPDGNLEFLGRIDDQVKIRGY 387
|
410 420
....*....|....*....|....
gi 1034638423 453 RlnIEL--VQQVAEELQQVESCAV 474
Cdd:TIGR01733 388 R--IELgeIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2-475 |
1.39e-54 |
|
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: 207.79 E-value: 1.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 2 TLQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLLhcdfQGIRE---IGLYCQPGIDLPSWILGI 78
Cdd:COG1020 477 TLHELFEAQAARTPDAVAVVFGD--QSL----TYAELNARANRLAHHLRA----LGVGPgdlVGVCLERSLEMVVALLAV 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 79 LQVPAAYVPIEPDSPPS-LstHFM-KKCNLKYILVEKKQINKFKSFHETLLNYDTFTVEHNDlvlfrlhwkntevnlmln 156
Cdd:COG1020 547 LKAGAAYVPLDPAYPAErL--AYMlEDAGARLVLTQSALAARLPELGVPVLALDALALAAEP------------------ 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 157 dgkekyEKEKIKSISSEHvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFL 236
Cdd:COG1020 607 ------ATNPPVPVTPDD-----------------LAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQ 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 237 ASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsQLIkSTVLSATTSLRVLA 316
Cdd:COG1020 664 FASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELL-ARHRVTVLNLTPSLLR----ALL-DAAPEALPSLRLVL 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 317 LGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGftiQ- 395
Cdd:COG1020 738 VGGEALP-PELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGG-----SVPIGRPIANTRVYVLDAHL---Qp 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 396 --EG-SGQVFLGG----------------RnrvcFLDDEVTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRln 455
Cdd:COG1020 809 vpVGvPGELYIGGaglargylnrpeltaeR----FVADPFGFPGARLYRTGDLARWlPDGNLEFLGRADDQVKIRGFR-- 882
|
490 500
....*....|....*....|..
gi 1034638423 456 IEL--VQQVAEELQQVESCAVT 475
Cdd:COG1020 883 IELgeIEAALLQHPGVREAVVV 904
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
16-533 |
1.16e-49 |
|
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: 183.26 E-value: 1.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVcfdECNNQLpvyYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd12116 2 DATAV---RDDDRS---LSYAELDERANRLAARLRARGVGPGDR-VAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 96 LSTHFMKKCNLKYILVEkkqinkfksfhetllnydtftvehnDLVLFRLHWKNTEVNLMLNDGkekyekekiksisseHV 175
Cdd:cd12116 75 RLRYILEDAEPALVLTD-------------------------DALPDRLPAGLPVLLLALAAA---------------AA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 176 NEEKAEEHMDLRLkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSS 255
Cdd:cd12116 115 APAAPRTPVSPDD---LAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLA 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 256 GASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRrfgsqLIKSTVLSATTSLRVLAlGGEAFPS-------LTVL 328
Cdd:cd12116 192 GARVVIAPRETQRDPEALAR-LIEAHSITVMQATPATWR-----MLLDAGWQGRAGLTALC-GGEALPPdlaarllSRVG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 329 RSWrgegnktqifNVYGITEVSSWATIYRI-PEKTlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGG- 405
Cdd:cd12116 265 SLW----------NLYGPTETTIWSTAARVtAAAG---------PIPIGRPLANTQVYVLDAALRPVPPGvPGELYIGGd 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 406 ------RNR-----VCFLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVES 471
Cdd:cd12116 326 gvaqgyLGRpaltaERFVPDPFAGPGSRLYRTGDLVRRRaDGRLEYLGRADGQVKIRGHR--IELgeIEAALAAHPGVAQ 403
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638423 472 CAVTWYNQE---KLILFMVSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd12116 404 AAVVVREDGgdrRLVAYVVLKAGAApdAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
192-533 |
1.24e-49 |
|
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: 182.83 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 271
Cdd:cd05945 99 NAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 272 KLASVLfSHHRVTVLQATPTLLRR-FGSQLIKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVS 350
Cdd:cd05945 179 QLFRFL-AEHGITVWVSTPSFAAMcLLSPTFTPESLP---SLRHFLFCGEVLP-HKTARALQQRFPDARIYNTYGPTEAT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 351 SWATIYRIPEKTLNStlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLG------GRNRVCFLDDEV 416
Cdd:cd05945 254 VAVTYIEVTPEVLDG----YDRLPIGYAKPGAKLVILDEDGRPVPPGekgelvisGPSVSKGylnnpeKTAAAFFPDEGQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 417 TVplgtmRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESC-AVTWYNQEK---LILFMVSKDA 491
Cdd:cd05945 330 RA-----YRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAvVVPKYKGEKvteLIAFVVPKPG 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034638423 492 S----VKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05945 405 AeaglTKA-IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
16-533 |
2.07e-49 |
|
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: 182.79 E-value: 2.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVCFDECNnqlpvyYTYKTVVNAASELSNFLLLHcdfqGIRE---IGLYCQPGIDLPSWILGILQVPAAYVPIEPDS 92
Cdd:cd12117 12 DAVAVVYGDRS------LTYAELNERANRLARRLRAA----GVGPgdvVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 93 PPSLSTHFMKKCNLKyilvekkqinkfksfheTLLNYDTFTVEHNDLVLFRLHwkntevnlmLNDGKEKYEKEKIKSISS 172
Cdd:cd12117 82 PAERLAFMLADAGAK-----------------VLLTDRSLAGRAGGLEVAVVI---------DEALDAGPAGNPAVPVSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 173 EHvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVpniqhfRVLFD-----ITQEDVLFLASPLTFDPSVV 247
Cdd:cd12117 136 DD-----------------LAYVMYTSGSTGRPKGVAVTHRGVV------RLVKNtnyvtLGPDDRVLQTSPLAFDASTF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 248 EIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsqLIKSTVLSATTSLRVLALGGEAFPSLTV 327
Cdd:cd12117 193 EIWGALLNGARLVLAPKGTLLDPDALGALI-AEEGVTVLWLTAALFN-----QLADEDPECFAGLRELLTGGEVVSPPHV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 328 lRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGG- 405
Cdd:cd12117 267 -RRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEV-----AGSIPIGRPIANTRVYVLDEDGRPVPPGvPGELYVGGd 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 406 ------RNRVCfLDDEVTVPL-----GTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVES 471
Cdd:cd12117 341 glalgyLNRPA-LTAERFVADpfgpgERLYRTGDLARWLpDGRLEFLGRIDDQVKIRGFR--IELgeIEAALRAHPGVRE 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 472 CAVTWYNQE----KLILFMVSK----DASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd12117 418 AVVVVREDAggdkRLVAYVVAEgaldAAELRAF----LRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
5-533 |
4.00e-49 |
|
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: 182.14 E-value: 4.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 5 ELVHKAASCYMDRVAVCFDecNNQLpvyyTYKTVVNAASELSNFLLLhcdfQGIRE---IGLYCQPGIDLPSWILGILQV 81
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFE--DQTL----TYRELNERANQLARTLRE----KGVGPdtiVGIMAERSLEMIVGILGILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 82 PAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKfKSFHETLLNYDTFTVEHNDlvlfrlhwkntevnlmlndgkek 161
Cdd:cd17655 71 GGAYLPIDPDYPEERIQYILEDSGADILLTQSHLQPP-IAFIGLIDLLDEDTIYHEE----------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 162 yekekikSISSEHVNeeKAEEhmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT 241
Cdd:cd17655 127 -------SENLEPVS--KSDD---------LAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASIS 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 242 FDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVlFSHHRVTVLQATPTLLrrfgsQLIKSTVLSATTSLRVLALGGEA 321
Cdd:cd17655 189 FDASVTEIFASLLSGNTLYIVRKETVLDGQALTQY-IRQNRITIIDLTPAHL-----KLLDAADDSEGLSLKHLIVGGEA 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 322 FPSLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQ 400
Cdd:cd17655 263 LSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQV-----SVPIGKPLGNTRIYILDQYGRPQPVGVaGE 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 401 VFLGGR-------NR-----VCFLDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQ 467
Cdd:cd17655 338 LYIGGEgvargylNRpeltaEKFVDDPF-VPGERMYRTGDLARwLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHP 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034638423 468 QVESCAVTWY----NQEKLILFMVS-KDASVKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17655 417 DIKEAVVIARkdeqGQNYLCAYIVSeKELPVAQ-LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
61-529 |
4.45e-48 |
|
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: 178.27 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 61 IGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPslsthfmkkcnlkyilvekkqinkfksfhetllnydtftvEHNDLV 140
Cdd:cd17643 40 VALALPRSAELIVALLAILKAGGAYVPIDPAYPV----------------------------------------ERIAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 141 LfrlhwKNTEVNLMLNDGkekyekekiksissehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQ 220
Cdd:cd17643 80 L-----ADSGPSLLLTDP-------------------------------DDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 221 HFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRRFGSQL 300
Cdd:cd17643 124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLL-RDEGVTVLNQTPSAFYQLVEAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 301 IKSTvlSATTSLRVLALGGEAFPsLTVLRSWRG--EGNKTQIFNVYGITEVSSWATIYRIpektLNSTLKCELPVQLGFP 378
Cdd:cd17643 203 DRDG--RDPLALRYVIFGGEALE-AAMLRPWAGrfGLDRPQLVNMYGITETTVHVTFRPL----DAADLPAAAASPIGRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 379 LLGTVVEVRDTNGFTIQEGS-GQVFLGG---------RNRVC---FLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKD 444
Cdd:cd17643 276 LPGLRVYVLDADGRPVPPGVvGELYVSGagvargylgRPELTaerFVANPFGGPGSRMYRTGDLARrLPDGELEYLGRAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 445 SQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWYNQE----KLILFMVSKD------ASVKEYIfKELqkyLPSHAVPD 512
Cdd:cd17643 356 EQVKIRGFR--IELgeIEAALATHPSVRDAAVIVREDEpgdtRLVAYVVADDgaaadiAELRALL-KEL---LPDYMVPA 429
|
490
....*....|....*..
gi 1034638423 513 ELVLIDSLPFTSHGKID 529
Cdd:cd17643 430 RYVPLDALPLTVNGKLD 446
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
6-637 |
5.23e-48 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 188.06 E-value: 5.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 6 LVHKAASCYMDRVAVCFDEcnnqlpVYYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAY 85
Cdd:PRK12467 517 LIEAQARQHPERPALVFGE------QVLSYAELNRQANRLAHVLIAAGVGPDVL-VGIAVERSIEMVVGLLAVLKAGGAY 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 86 VPIEPDSPPSLSTHFMKKCNLKYILvekkqinkfksfhetllnydtftveHNDLVLFRLHWKNTEVNLMLNDGKEKYeke 165
Cdd:PRK12467 590 VPLDPEYPQDRLAYMLDDSGVRLLL-------------------------TQSHLLAQLPVPAGLRSLCLDEPADLL--- 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 166 kiksissehvnEEKAEEHMDLRLK-HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDP 244
Cdd:PRK12467 642 -----------CGYSGHNPEVALDpDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDL 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 245 SVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGGEAFPs 324
Cdd:PRK12467 711 GVTELFGALASGATLHLLPPDCARDAEAFAALM-ADQGVTVLKIVPSHLQ----ALLQASRVALPRPQRALVCGGEALQ- 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 325 LTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFL 403
Cdd:PRK12467 785 VDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFG-----NVPIGQPLANLGLYILDHYLNPVPVGVvGELYI 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 404 GGR--------------NRvcFLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRL---NIELVQQVAEE 465
Cdd:PRK12467 860 GGAglargyhrrpaltaER--FVPDPFGADGGRLYRTGDLARyRADGVIEYLGRMDHQVKIRGFRIelgEIEARLLAQPG 937
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 466 LQQVESCAVTWYNQEKLILFMV-------SKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiyl 538
Cdd:PRK12467 938 VREAVVLAQPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK--- 1014
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 539 NYINLKSENKLSGKEDLWEKLQYLWKSTLnlpeDLLRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVPglLEIILSSS 618
Cdd:PRK12467 1015 PDASAVQATFVAPQTELEKRLAAIWADVL----KVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVP--LRTLFEHQ 1088
|
650
....*....|....*....
gi 1034638423 619 ILEIYnhiLQTVVPDEDVT 637
Cdd:PRK12467 1089 TLAGF---AQAVAAQQQGA 1104
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
59-529 |
1.75e-43 |
|
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: 165.59 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 59 REIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKkqinkfksfhetllnydtftvEHND 138
Cdd:cd17651 46 DLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVLTHP---------------------ALAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 139 LVLFRLHWkntevnlmlndGKEKYEKEKIKSISSEHVNEEKAeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPN 218
Cdd:cd17651 105 ELAVELVA-----------VTLLDQPGAAAGADAEPDPALDA---------DDLAYVIYTSGSTGRPKGVVMPHRSLANL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 219 IQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRRFGS 298
Cdd:cd17651 165 VAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWL-DEQRISRVFLPTVALRALAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 299 QLIKSTVLSAttSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYGITEvSSWATIYRIPektlNSTLKCELPVQLGFP 378
Cdd:cd17651 244 HGRPLGVRLA--ALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTE-THVVTALSLP----GDPAAWPAPPPIGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 379 LLGTVVEVRDTNGFTIQEG-SGQVFLGG-------RNR-----VCFLDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKD 444
Cdd:cd17651 317 IDNTRVYVLDAALRPVPPGvPGELYIGGaglargyLNRpeltaERFVPDPF-VPGARMYRTGDLARwLPDGELEFLGRAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 445 SQIKRHGKRlnIEL--VQQVAEELQQVESCAVT----WYNQEKLILFMVSKDASVK--EYIFKELQKYLPSHAVPDELVL 516
Cdd:cd17651 396 DQVKIRGFR--IELgeIEAALARHPGVREAVVLaredRPGEKRLVAYVVGDPEAPVdaAELRAALATHLPEYMVPSAFVL 473
|
490
....*....|...
gi 1034638423 517 IDSLPFTSHGKID 529
Cdd:cd17651 474 LDALPLTPNGKLD 486
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
187-538 |
1.90e-43 |
|
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: 164.60 E-value: 1.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 187 RLKHCL----------AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFD-PSVVEIFLALSS 255
Cdd:COG0318 87 ELAYILedsgaralvtALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 256 GASLLIVPtsvKLLPSKLASvLFSHHRVTVLQATPTLLRRfgsqLIKSTVLSAT--TSLRVLALGGEAFPSlTVLRSWRG 333
Cdd:COG0318 167 GATLVLLP---RFDPERVLE-LIERERVTVLFGVPTMLAR----LLRHPEFARYdlSSLRLVVSGGAPLPP-ELLERFEE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 334 EGNkTQIFNVYGITEvSSWATIYRIPEKTLnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLG- 404
Cdd:COG0318 238 RFG-VRIVEGYGLTE-TSPVVTVNPEDPGE------RRPGSVGRPLPGVEVRIVDEDGRELPPGevgeivvrGPNVMKGy 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 405 ----GRNRVCFLDdevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNIEL--VQQVAEELQQVESCAVT-- 475
Cdd:COG0318 310 wndpEATAEAFRD-------GWLR-TGDLGRLdEDGYLYIVGRKKDMIISGG--ENVYPaeVEEVLAAHPGVAEAAVVgv 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 476 ----WynQEKLILFMVSKD---ASVKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYL 538
Cdd:COG0318 380 pdekW--GERVVAFVVLRPgaeLDAEE-LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
192-529 |
5.44e-43 |
|
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: 163.87 E-value: 5.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFDPSVVEIFLALSSGASLLIvpTSVKLLP 270
Cdd:cd05918 108 AAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESrVLQFASY-TFDVSILEIFTTLAAGGCLCI--PSEEDRL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASVLfSHHRVTVLQATPTLLRrfgsqLIKstvLSATTSLRVLALGGEAfPSLTVLRSWrgeGNKTQIFNVYGITEvs 350
Cdd:cd05918 185 NDLAGFI-NRLRVTWAFLTPSVAR-----LLD---PEDVPSLRTLVLGGEA-LTQSDVDTW---ADRVRLINAYGPAE-- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 351 swATIYRipekTLNSTLKCELPVQLGFPLLGT--VVEVRDTN-----GFTiqegsGQVFLGG------------RNRVCF 411
Cdd:cd05918 250 --CTIAA----TVSPVVPSTDPRNIGRPLGATcwVVDPDNHDrlvpiGAV-----GELLIEGpilargylndpeKTAAAF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 412 LDDEVTVPLGTMRA------TGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL------VQQVAEELQQVESCAVT--- 475
Cdd:cd05918 319 IEDPAWLKQEGSGRgrrlyrTGDLVRyNPDGSLEYVGRKDTQVKIRGQR--VELgeiehhLRQSLPGAKEVVVEVVKpkd 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 476 WYNQEKLILFMVSKDASVK-------------------EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05918 397 GSSSPQLVAFVVLDGSSSGsgdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKID 469
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
192-529 |
5.34e-42 |
|
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: 157.06 E-value: 5.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPtsvKLLPS 271
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 272 KLASvLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGITEVS 350
Cdd:cd04433 79 AALE-LIEREKVTILLGVPTLLARLLKAPeSAGYDLS---SLRALVSGGAPLPP-ELLERFE-EAPGIKLVNGYGLTETG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 351 SWATIYRIPEKTlnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRVcFLDDEVTVPlGT 422
Cdd:cd04433 153 GTVATGPPDDDA-------RKPGSVGRPVPGVEVRIVDPDGGELPPGeigelvvrGPSVMKGYWNNP-EATAAVDED-GW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 423 MRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNIEL--VQQVAEELQQVESCAV------TWynQEKLILFMVSKDAS- 492
Cdd:cd04433 224 YR-TGDLGRLdEDGYLYIVGRLKDMIKSGGE--NVYPaeVEAVLLGHPGVAEAAVvgvpdpEW--GERVVAVVVLRPGAd 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034638423 493 -----VKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd04433 299 ldaeeLRAH----VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
5-533 |
2.55e-41 |
|
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: 157.86 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 5 ELVHKAASCYMDRVAVcfDECNNQLpvyyTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAA 84
Cdd:cd17653 1 DAFERIAAAHPDAVAV--ESLGGSL----TYGELDAASNALANRLLQLGVVPGDV-VPLLSDRSLEMLVAILAILKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 85 YVPIEPDSPPSLSTHFMKKCNLKYILVEKKQinkfksfhetllnydtftvehndlvlfrlhwkntevnlmlndgkekyek 164
Cdd:cd17653 74 YVPLDAKLPSARIQAILRTSGATLLLTTDSP------------------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 165 ekiksissehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFD 243
Cdd:cd17653 105 -------------------------DDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrVAQVLSI-AFD 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 244 PSVVEIFLALSSGASLLIVPTSvkllpSKLASVLFShhrVTVLQATPTLLrrfgsqliksTVLSATT--SLRVLALGGEA 321
Cdd:cd17653 159 ACIGEIFSTLCNGGTLVLADPS-----DPFAHVART---VDALMSTPSIL----------STLSPQDfpNLKTIFLGGEA 220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 322 fPSLTVLRSWRGEgnkTQIFNVYGITEVSSWATIYRI-PEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SG 399
Cdd:cd17653 221 -VPPSLLDRWSPG---RRLYNAYGPTECTISSTMTELlPGQ----------PVTIGKPIPNSTCYILDADLQPVPEGvVG 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 400 QVFLGG------------RNRVCFLDDEVtVPLGTMRATGD--FVTvKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEE 465
Cdd:cd17653 287 EICISGvqvargylgnpaLTASKFVPDPF-WPGSRMYRTGDygRWT-EDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQ 364
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638423 466 LQQVESCAVTWYNQEKLILFMVSKDASVkEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17653 365 SQPEVTQAAAIVVNGRLVAFVTPETVDV-DGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
16-533 |
3.92e-41 |
|
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: 158.59 E-value: 3.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVCFDECNnqlpvyYTYKTVVNAASELSNFLLLHcdfqGIREIGLYcqpGIDLP-SW-----ILGILQVPAAYVPIE 89
Cdd:cd12114 2 DATAVICGDGT------LTYGELAERARRVAGALKAA----GVRPGDLV---AVTLPkGPeqvvaVLGILAAGAAYVPVD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 90 PDSPPSLSTHFMKKCNLKYILVEKkqinkfksfHETLLNYDTFTVEHNDLVLFRLHWKNTEVNLMLNDgkekyekekiks 169
Cdd:cd12114 69 IDQPAARREAILADAGARLVLTDG---------PDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDD------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 170 issehvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEI 249
Cdd:cd12114 128 ----------------------LAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 250 FLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLrrfgsQLIKSTVLSATT---SLRVLALGGEAFPsLT 326
Cdd:cd12114 186 FGALSAGATLVLPDEARRRDPAHWAELI-ERHGVTLWNSVPALL-----EMLLDVLEAAQAllpSLRLVLLSGDWIP-LD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 327 VLRSWRGEGNKTQIFNVYGITEVSSWATIYRI--PEKTLNStlkcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFL 403
Cdd:cd12114 259 LPARLRALAPDARLISLGGATEASIWSIYHPIdeVPPDWRS-------IPYGRPLANQRYRVLDPRGRDCPDWvPGELWI 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 404 GGRN--RVCFLDDEVT----VPLGTMRA---TGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVES 471
Cdd:cd12114 332 GGRGvaLGYLGDPELTaarfVTHPDGERlyrTGDLGRYRpDGTLEFLGRRDGQVKVRGYR--IELgeIEAALQAHPGVAR 409
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034638423 472 CAVTWY---NQEKLILFMVSKD-------ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd12114 410 AVVVVLgdpGGKRLAAFVVPDNdgtpiapDALRAF----LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
61-533 |
1.20e-40 |
|
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: 156.32 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 61 IGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLsthfmkkcnLKYILvekkqinkfksfhetllnydtftvehndlv 140
Cdd:cd12115 52 VGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPER---------LRFIL------------------------------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 141 lfrlhwKNTEVNLMLNDGkekyekekiksissehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQ 220
Cdd:cd12115 93 ------EDAQARLVLTDP-------------------------------DDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 221 HFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVpTSVKLLPSklasvLFSHHRVTVLQATPTLLRrfgsQL 300
Cdd:cd12115 136 WAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-DNVLALPD-----LPAAAEVTLINTVPSAAA----EL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 301 IKSTVLSatTSLRVLALGGEAFPSlTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRIPEKTLNstlkcelPVQLGFPLL 380
Cdd:cd12115 206 LRHDALP--ASVRVVNLAGEPLPR-DLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASG-------EVSIGRPLA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 381 GTVVEVRDTNGFTIQEG-SGQVFLGGRN-RVCFLDDE-------VTVPLGT---MRATGDFVTVK-DGEIFFLGRKDSQI 447
Cdd:cd12115 276 NTQAYVLDRALQPVPLGvPGELYIGGAGvARGYLGRPgltaerfLPDPFGPgarLYRTGDLVRWRpDGLLEFLGRADNQV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 448 KRHGKRLNIELVQQVAEELQQV-ESCAVTW---YNQEKLILFMVSKD--ASVKEYIFKELQKYLPSHAVPDELVLIDSLP 521
Cdd:cd12115 356 KVRGFRIELGEIEAALRSIPGVrEAVVVAIgdaAGERRLVAYIVAEPgaAGLVEDLRRHLGTRLPAYMVPSRFVRLDALP 435
|
490
....*....|..
gi 1034638423 522 FTSHGKIDVSEL 533
Cdd:cd12115 436 LTPNGKIDRSAL 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
192-533 |
1.78e-40 |
|
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: 156.67 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 271
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 272 KLASvLFSHHRVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGnkTQIFNVYGITE--- 348
Cdd:cd17646 220 YLAA-LIREHGVTTCHFVPSMLRVF----LAEPAAGSCASLRRVFCSGEALPPELAARFLALPG--AELHNLYGPTEaai 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 -VSSWAtiYRIPEKTlnstlkceLPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------NRVC-----FLDD 414
Cdd:cd17646 293 dVTHWP--VRGPAET--------PSVPIGRPVPNTRLYVLDDALRPVPVGvPGELYLGGVqlargylGRPAltaerFVPD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 415 evtvPLGT---MRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFM 486
Cdd:cd17646 363 ----PFGPgsrMYRTGDLARWRpDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApagaARLVGYV 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1034638423 487 VSK-------DASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17646 439 VPAagaagpdTAALRAH----LAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
192-533 |
5.24e-40 |
|
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: 153.95 E-value: 5.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFDPSVVEIFLALSSGASLLIVPTSVKLLP 270
Cdd:cd17652 95 LAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrVLQFASP-SFDASVWELLMALLAGATLVLAPAEELLPG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASVLfSHHRVTVLQATPTLLRrfgsqlikstVLSATT--SLRVLALGGEAfPSLTVLRSWrgeGNKTQIFNVYGITE 348
Cdd:cd17652 174 EPLADLL-REHRITHVTLPPAALA----------ALPPDDlpDLRTLVVAGEA-CPAELVDRW---APGRRMINAYGPTE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 VSSWATIYRIPEKtlnstlkcELPVQLGFPLLGTVVEVRDTN------GFTiqegsGQVFLGGR-------NR-----VC 410
Cdd:cd17652 239 TTVCATMAGPLPG--------GGVPPIGRPVPGTRVYVLDARlrpvppGVP-----GELYIAGAglargylNRpgltaER 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 411 FLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWYNQE----KLI 483
Cdd:cd17652 306 FVADPFGAPGSRMYRTGDLARwRADGQLEFLGRADDQVKIRGFR--IELgeVEAALTEHPGVAEAVVVVRDDRpgdkRLV 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1034638423 484 LFMV--SKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17652 384 AYVVpaPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
7-449 |
7.16e-39 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 150.16 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 7 VHKAASCYMDRVAVCFDEcnnqlPVYYTYKTVVNAASELSNFLLLHcdfqGIRE---IGLYCQPGIDLPSWILGILQVPA 83
Cdd:pfam00501 1 LERQAARTPDKTALEVGE-----GRRLTYRELDERANRLAAGLRAL----GVGKgdrVAILLPNSPEWVVAFLACLKAGA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 84 AYVPIEPDSPPSLSTHFMKKCNLKYILV-EKKQINKFKSFHETLLNYDTFTVEHNDLVLFRLHWKNTEVNlmlndgkeky 162
Cdd:pfam00501 72 VYVPLNPRLPAEELAYILEDSGAKVLITdDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 163 ekekikSISSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVL----FDITQEDVLFLAS 238
Cdd:pfam00501 142 ------ADVPPPPPPPPDPDD--------LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 239 PLTFDPSVV-EIFLALSSGASLLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLA 316
Cdd:pfam00501 208 PLFHDFGLSlGLLGPLLAGATVVLPPGFPALDPAALLELI-ERYKVTVLYGVPTLLNMLlEAGAPKRALLS---SLRLVL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 317 LGGEAFPSlTVLRSWRgEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTLKCelpvqlGFPLLGTVVEVRD--TNGFTI 394
Cdd:pfam00501 284 SGGAPLPP-ELARRFR-ELFGGALVNGYGLTETTGVVTTPLPLDEDLRSLGSV------GRPLPGTEVKIVDdeTGEPVP 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 395 QEGSGQVFLGGRNrV--CFLDD-----EVTVPLGTMRaTGDFVTV-KDGEIFFLGRKDSQIKR 449
Cdd:pfam00501 356 PGEPGELCVRGPG-VmkGYLNDpeltaEAFDEDGWYR-TGDLGRRdEDGYLEIVGRKKDQIKL 416
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
16-529 |
2.05e-38 |
|
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: 150.28 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVCFdeCNNQLpvyyTYKTVVNAASELSNFLllhcDFQGIRE---IGLYCQPGIDLPSWILGILQVPAAYVPIEPDS 92
Cdd:cd17644 15 DAVAVVF--EDQQL----TYEELNTKANQLAHYL----QSLGVKSeslVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 93 PPSlsthfmkkcNLKYILvekkqinkfksfhetllnydtftvehndlvlfrlhwKNTEVNLMLNDGkekyekekiksiss 172
Cdd:cd17644 85 PQE---------RLTYIL------------------------------------EDAQISVLLTQP-------------- 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 173 ehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLA 252
Cdd:cd17644 106 -----------------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVT 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 253 LSSGASLLIVPTsvKLLPSKLASVLFSHH-RVTVLQATPTLLRRFGSQLIKSTvLSATTSLRVLALGGEAF-PSLtvLRS 330
Cdd:cd17644 169 LLSGATLVLRPE--EMRSSLEDFVQYIQQwQLTVLSLPPAYWHLLVLELLLST-IDLPSSLRLVIVGGEAVqPEL--VRQ 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 331 WR-GEGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTLKcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-- 406
Cdd:cd17644 244 WQkNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITS----VPIGRPIANTQVYILDENLQPVPVGvPGELHIGGVgl 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 407 -----NRvcfldDEVTV-----------PLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQV 469
Cdd:cd17644 320 argylNR-----PELTAekfishpfnssESERLYKTGDLARyLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDV 394
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638423 470 ESCAVT----WYNQEKLILFMVSKdaSVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17644 395 KTAVVIvredQPGNKRLVAYIVPH--YEESPSTVELRQFlkakLPDYMIPSAFVVLEELPLTPNGKID 460
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
16-529 |
3.85e-38 |
|
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: 149.06 E-value: 3.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVCFDECnnqlpvYYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd17649 2 DAVALVFGDQ------SLSYAELDARANRLAHRLRALGVGPEVR-VGIALERSLEMVVALLAILKAGGAYVPLDPEYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 96 lsthfmkkcnlkyilvekkqinkfksfhetllnydtftvehndlvlfRLHWkntevnlMLNDGKEKYekekiksISSEHv 175
Cdd:cd17649 75 -----------------------------------------------RLRY-------MLEDSGAGL-------LLTHH- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 176 neekaeehmdlrlKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSS 255
Cdd:cd17649 93 -------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLIC 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 256 GASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRRFgSQLIKSTVLSATTSLRVLALGGEAfpsLTVLRSWRGEG 335
Cdd:cd17649 160 GACVVLRPDELWASADELAE-MVRELGVTVLDLPPAYLQQL-AEEADRTGDGRPPSLRLYIFGGEA---LSPELLRRWLK 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 336 NKTQIFNVYGITEVSSWATIYRIPEKtlNSTLKCELPvqLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------N 407
Cdd:cd17649 235 APVRLFNAYGPTEATVTPLVWKCEAG--AARAGASMP--IGRPLGGRSAYILDADLNPVPVGvTGELYIGGEglargylG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 408 RVC-----FLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---TWYN 478
Cdd:cd17649 311 RPEltaerFVPDPFGAPGSRLYRTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVvalDGAG 390
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034638423 479 QEKLILFMVSKDASV----KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17649 391 GKQLVAYVVLRAAAAqpelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
192-533 |
1.30e-37 |
|
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: 147.55 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED---VLFLASpLTFDPSVVEIFLALSSGASLLIVPTSVKL 268
Cdd:cd17648 96 LAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGdeaVLFFSN-YVFDFFVEQMTLALLNGQKLVVPPDEMRF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 269 LPSKLASvLFSHHRVTVLQATPTLLRRFGsqlikstvLSATTSLRVLALGGEAF--PSLTVLRSwrgeGNKTQIFNVYGI 346
Cdd:cd17648 175 DPDRFYA-YINREKVTYLSGTPSVLQQYD--------LARLPHLKRVDAAGEEFtaPVFEKLRS----RFAGLIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 347 TEVSSWATIYRIP--EKTLNStlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGG-------RNRvcfldDEV 416
Cdd:cd17648 242 TETTVTNHKRFFPgdQRFDKS---------LGRPVRNTKCYVLNDAMKRVPVGAvGELYLGGdgvargyLNR-----PEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 417 T----VP-------------LGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---- 474
Cdd:cd17648 308 TaerfLPnpfqteqerargrNARLYKTGDLVRwLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVvake 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638423 475 -----TWYNQEKLILFMVSKDASVKEY-IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17648 388 dasqaQSRIQKYLVGYYLPEPGHVPESdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
46-597 |
1.54e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 154.34 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 46 SNFLLLHCDFQGI---REIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSlsthfmkkcNLKYILvEKKQINkfksf 122
Cdd:PRK12316 546 ANRLAHALIERGVgpdVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAE---------RLAYML-EDSGVQ----- 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 123 hetLLNYDTFTVEHNDLvlfrlhwkNTEVNLMLNDGKEKYEKEKIKSISSEHVNEEKaeehmdlrlkhcLAYVLHTSGTT 202
Cdd:PRK12316 611 ---LLLSQSHLGRKLPL--------AAGVQVLDLDRPAAWLEGYSEENPGTELNPEN------------LAYVIYTSGST 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 203 GIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASvLFSHHR 282
Cdd:PRK12316 668 GKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVE-LINREG 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 283 VTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSWrGEGNKTQIFNVYGITEVSSWATIYripekT 362
Cdd:PRK12316 747 VDTLHFVPSMLQAF----LQDEDVASCTSLRRIVCSGEALPADAQEQVF-AKLPQAGLYNLYGPTEAAIDVTHW-----T 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 363 LNSTLKCELPVqlGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRN------RVCFLDDE--VTVPLGT---MRATGDFV 430
Cdd:PRK12316 817 CVEEGGDSVPI--GRPIANLACYILDANLEPVPVGvLGELYLAGRGlargyhGRPGLTAErfVPSPFVAgerMYRTGDLA 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 431 TVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKD--ASVKEYIFKELQKYLPS 507
Cdd:PRK12316 895 RYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESegGDWREALKAHLAASLPE 974
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 508 HAVPDELVLIDSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGG 587
Cdd:PRK12316 975 YMVPAQWLALERLPLTPNGKLDRKALPAP---EASVAQQGYVAPRNALERTLAAIWQDVLGVE----RVGLDDNFFELGG 1047
|
570
....*....|
gi 1034638423 588 DSLKSIRLLS 597
Cdd:PRK12316 1048 DSIVSIQVVS 1057
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
192-597 |
1.86e-37 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 153.78 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 271
Cdd:PRK12467 1720 LAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPE 1799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 272 KLASVLfSHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITE--- 348
Cdd:PRK12467 1800 QLIQLI-ERQQVTTLHFVPSMLQQL---LQMDEQVEHPLSLRRVVCGGEALE-VEALRPWLERLPDTGLFNLYGPTEtav 1874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 -VSSWATIYRIPEKTLNStlkcelPVQLGFPLLGTVVEVRDTNGFTIQEgSGQVFLGG-------RNRVC-----FLDDE 415
Cdd:PRK12467 1875 dVTHWTCRRKDLEGRDSV------PIGQPIANLSTYILDASLNPVPIGV-AGELYLGGvglargyLNRPAltaerFVADP 1947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 416 VTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIELVQQVAEELQQ--VESCAVT---WYNQEKLILFMVSK 489
Cdd:PRK12467 1948 FGTVGSRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFR--IELGEIEARLREQggVREAVVIaqdGANGKQLVAYVVPT 2025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 490 DASVKEY---------IFKE-LQKYLPSHAVPDELVLIDSLPFTSHGKI--------DVSELNKIYlnyinlksenkLSG 551
Cdd:PRK12467 2026 DPGLVDDdeaqvalraILKNhLKASLPEYMVPAHLVFLARMPLTPNGKLdrkalpapDASELQQAY-----------VAP 2094
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1034638423 552 KEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 597
Cdd:PRK12467 2095 QSELEQRLAAIWQDVLGLE----QVGLHDNFFELGGDSIISIQVVS 2136
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-608 |
5.50e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 145.87 E-value: 5.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 3 LQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVP 82
Cdd:PRK12316 4553 VHQLVAERARMTPDAVAVVFDE--EKL----TYAELNRRANRLAHALIARGVGPEVL-VGIAMERSAEMMVGLLAVLKAG 4625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 83 AAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKF---KSFHETLLNYD---TFTVEHNDLVlfRLHWKNtevnlmln 156
Cdd:PRK12316 4626 GAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLpipDGLASLALDRDedwEGFPAHDPAV--RLHPDN-------- 4695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 157 dgkekyekekiksissehvneekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFL 236
Cdd:PRK12316 4696 -----------------------------------LAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQ 4740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 237 ASPLTFDPSVVEIFLALSSGASLLIVPTSVKlLPSKLASVLfSHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLA 316
Cdd:PRK12316 4741 FMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEI-HEHRVTVLVFPPVYLQQL---AEHAERDGEPPSLRVYC 4815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 317 LGGEAFPSLTVLRSWRGEGNkTQIFNVYGITEVSSWATIYripeKTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQE 396
Cdd:PRK12316 4816 FGGEAVAQASYDLAWRALKP-VYLFNGYGPTETTVTVLLW----KARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPV 4890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 397 G-SGQVFLGGR--------------NRvcFLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLnielvq 460
Cdd:PRK12316 4891 GvAGELYLGGEgvargylerpaltaER--FVPDPFGAPGGRLYRTGDLARYRaDGVIDYLGRVDHQVKIRGFRI------ 4962
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 461 qvaeELQQVESC-------------AVTWYNQEKLILFMVSKDASVKEYIFKE----------LQKYLPSHAVPDELVLI 517
Cdd:PRK12316 4963 ----ELGEIEARlrehpavreavviAQEGAVGKQLVGYVVPQDPALADADEAQaelrdelkaaLRERLPEYMVPAHLVFL 5038
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 518 DSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 597
Cdd:PRK12316 5039 ARMPLTPNGKLDRKALPQP---DASLLQQAYVAPRSELEQQVAAIWAEVLQLE----RVGLDDNFFELGGHSLLAIQVTS 5111
|
650
....*....|.
gi 1034638423 598 EIEKLVGTSVP 608
Cdd:PRK12316 5112 RIQLELGLELP 5122
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-529 |
4.27e-34 |
|
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: 137.19 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVklLPS 271
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV--LDD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 272 KLASvLFSHHRVTVLQATPT---LLRRFGSQLIKstvlsaTTSLRVLALGGEAFPSLTVlRSWRGEGNKTQIFNVYGITE 348
Cdd:cd05922 197 AFWE-DLREHGATGLAGVPStyaMLTRLGFDPAK------LPSLRYLTQAGGRLPQETI-ARLRELLPGAQVYVMYGQTE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 VSSWATiYRIPEKTLNStlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRVCFLDDEVTVpl 420
Cdd:cd05922 269 ATRRMT-YLPPERILEK------PGSIGLAIPGGEFEILDDDGTPTPPGepgeivhrGPNVMKGYWNDPPYRRKEGRG-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 421 GTMRATGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVT---WYNQEKLILFMVSKDASVKEY 496
Cdd:cd05922 340 GGVLHTGDLaRRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVglpDPLGEKLALFVTAPDKIDPKD 419
|
330 340 350
....*....|....*....|....*....|...
gi 1034638423 497 IFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05922 420 VLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
59-597 |
1.35e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 141.25 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 59 REIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILvekkqinkfksfhetllnydtfTVEHnd 138
Cdd:PRK12316 3108 VLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL----------------------SQSH-- 3163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 139 lvlFRLHWKNTEVNLMLNDGKekyekekiksissehvnEEKAEEHMDLR-LKHCLAYVLHTSGTTGIPKIVRVPHKCIVP 217
Cdd:PRK12316 3164 ---LRLPLAQGVQVLDLDRGD-----------------ENYAEANPAIRtMPENLAYVIYTSGSTGKPKGVGIRHSALSN 3223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 218 NIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFShHRVTVLQATPTLLRRFg 297
Cdd:PRK12316 3224 HLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINS-EGVDVLHAYPSMLQAF- 3301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 298 sqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEgnktQIFNVYGITEVSSWATIYRIPEKTlnstlkcELPVQLGF 377
Cdd:PRK12316 3302 ---LEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGL----PLYNLYGPTEATITVTHWQCVEEG-------KDAVPIGR 3367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 378 PLLGTVVEVRDTNGFTIQEGS-GQVFLGGRN--RVCFLDDEVT---------VPLGTMRATGDFVTVK-DGEIFFLGRKD 444
Cdd:PRK12316 3368 PIANRACYILDGSLEPVPVGAlGELYLGGEGlaRGYHNRPGLTaerfvpdpfVPGERLYRTGDLARYRaDGVIEYIGRVD 3447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 445 SQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPF 522
Cdd:PRK12316 3448 HQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAgdLREALKAHLKASLPEYMVPAHLLFLERMPL 3527
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638423 523 TSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 597
Cdd:PRK12316 3528 TPNGKLDRKALPRP---DAALLQQDYVAPVNELERRLAAIWADVLKLE----QVGLTDNFFELGGDSIISLQVVS 3595
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
190-607 |
7.99e-33 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 138.25 E-value: 7.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 190 HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLL 269
Cdd:PRK10252 598 HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRD 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 270 PSKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSlTVLRSWRGEGNkTQIFNVYGITE- 348
Cdd:PRK10252 678 PLAMQQ-FFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPA-DLCREWQQLTG-APLHNLYGPTEa 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 ---VSSWATiyrIPEKTLNSTlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR--------------NRvc 410
Cdd:PRK10252 755 avdVSWYPA---FGEELAAVR---GSSVPIGYPVWNTGLRILDARMRPVPPGvAGDLYLTGIqlaqgylgrpdltaSR-- 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 411 FLDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL------------VQQVAEELQQVESCAVTWY 477
Cdd:PRK10252 827 FIADPF-APGERMYRTGDVARwLDDGAVEYLGRSDDQLKIRGQR--IELgeidramqalpdVEQAVTHACVINQAAATGG 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 478 NQEKLILFMVSKD------ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiylnyINLKSENKLSG 551
Cdd:PRK10252 904 DARQLVGYLVSQSglpldtSALQAQ----LRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPL-----PELKAQVPGRA 974
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638423 552 KEDLWEK-LQYLWKSTLNLPEdllrVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSV 607
Cdd:PRK10252 975 PKTGTETiIAAAFSSLLGCDV----VDADADFFALGGHSLLAMKLAAQLSRQFARQV 1027
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
16-529 |
1.42e-32 |
|
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: 132.29 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVCFdecNNQlpvYYTYKTVVNAASELSNfLLLHCDFQGIREIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd17645 13 DHVAVVD---RGQ---SLTYKQLNEKANQLAR-HLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 96 lsthfmkkcNLKYILvekkqinkfksfhetllnydtftvehndlvlfrlhwKNTEVNLMLNDgkekyekekiksissehv 175
Cdd:cd17645 86 ---------RIAYML------------------------------------ADSSAKILLTN------------------ 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 176 neekAEEhmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSS 255
Cdd:cd17645 103 ----PDD---------LAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTA 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 256 GASLLIVPTSVKLLPSKLASvLFSHHRVTVlQATPTllrrfgsQLIKSTVLSATTSLRVLALGGEafpsltVLRswRGEG 335
Cdd:cd17645 170 GAALHVVPSERRLDLDALND-YFNQEGITI-SFLPT-------GAAEQFMQLDNQSLRVLLTGGD------KLK--KIER 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 336 NKTQIFNVYGITEVSSWATIYRIPEKTLNstlkcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------N 407
Cdd:cd17645 233 KGYKLVNNYGPTENTVVATSFEIDKPYAN--------IPIGKPIDNTRVYILDEALQLQPIGvAGELCIAGEglargylN 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 408 RvcfldDEVT---------VPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY 477
Cdd:cd17645 305 R-----PELTaekfivhpfVPGERMYRTGDLAKfLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAK 379
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638423 478 NQEK----LILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17645 380 EDADgrkyLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-597 |
1.33e-30 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 131.44 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 2 TLQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLlHCDFQGIREIGLYCQPGIDLPSWILGILQV 81
Cdd:PRK05691 1132 WLPELLNEQARQTPERIALVWDG--GSL----DYAELHAQANRLAHYLR-DKGVGPDVCVAIAAERSPQLLVGLLAILKA 1204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 82 PAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKkqinkfkSFHETLLNYDTFTVehndLVLFRLH---WKNTEVNLMLNDg 158
Cdd:PRK05691 1205 GGAYVPLDPDYPAERLAYMLADSGVELLLTQS-------HLLERLPQAEGVSA----IALDSLHldsWPSQAPGLHLHG- 1272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 159 kekyekekiksissehvneekaeehmdlrlkHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLAS 238
Cdd:PRK05691 1273 -------------------------------DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKA 1321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 239 PLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSKLASVLFSHHrVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALG 318
Cdd:PRK05691 1322 PISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYG-VTTLHFVPPLLQLF----IDEPLAAACTSLRRLFSG 1396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 319 GEAFPS------LTVLrswrgegNKTQIFNVYGITEVSSWATIYRIP-EKTLNStlkcelPVqlGFPLLGTVVEVRDTNG 391
Cdd:PRK05691 1397 GEALPAelrnrvLQRL-------PQVQLHNRYGPTETAINVTHWQCQaEDGERS------PI--GRPLGNVLCRVLDAEL 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 392 FTIQEG-SGQVFLGGR-------NRVCFLDDE-VTVPLGTMRA----TGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIE 457
Cdd:PRK05691 1462 NLLPPGvAGELCIGGAglargylGRPALTAERfVPDPLGEDGArlyrTGDRARWNaDGALEYLGRLDQQVKLRGFRVEPE 1541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 458 LVQQVAEELQQVESCAV---TWYNQEKLILFMVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSE 532
Cdd:PRK05691 1542 EIQARLLAQPGVAQAAVlvrEGAAGAQLVGYYTGEAGQeaEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRA 1621
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638423 533 LNKiylnyINLKSENKLSGKEDLWEKLQYLWKSTLNLPEDLLRvpDEslFLNSGGDSLKSIRLLS 597
Cdd:PRK05691 1622 LPE-----PVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLR--DD--FFALGGHSLLATQIVS 1677
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-608 |
1.67e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 131.44 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 3 LQELVHKAASCYMDRVAVCFDEcnNQLpvyyTYKTVVNAASELSNFLLLH---CDfqgiREIGLYCQPGIDLPSWILGIL 79
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPALVFGD--QQL----SYAELNRRANRLAHRLIAIgvgPD----VLVGVAVERSVEMIVALLAVL 3166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 80 QVPAAYVPIEPDSPPSlsthfmkkcNLKYILVEkkqinkfkSFHETLLnydtfTVEHndlVLFRLHWKNTEVNLMLNDGK 159
Cdd:PRK12467 3167 KAGGAYVPLDPEYPRE---------RLAYMIED--------SGVKLLL-----TQAH---LLEQLPAPAGDTALTLDRLD 3221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 160 EKYEKEKIKSISSEHVNeekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASP 239
Cdd:PRK12467 3222 LNGYSENNPSTRVMGEN---------------LAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMS 3286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 240 LTFDPSVVEIFLALSSGASLLIVPTSVKlLPSKLASVLFSHHrVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGG 319
Cdd:PRK12467 3287 FSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHR-ISIACFPPAYLQ----QFAEDAGGADCASLDIYVFGG 3360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 320 EAFPSLTVLRSWRGEGNKtQIFNVYGITEVSSWATIYRIPektlnSTLKCELP-VQLGFPLLGTVVEVRDTNGFTIQEG- 397
Cdd:PRK12467 3361 EAVPPAAFEQVKRKLKPR-GLTNGYGPTEAVVTVTLWKCG-----GDAVCEAPyAPIGRPVAGRSIYVLDGQLNPVPVGv 3434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 398 SGQVFLGGrnrVC---------------FLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIELVQQ 461
Cdd:PRK12467 3435 AGELYIGG---VGlargyhqrpsltaerFVADPFSGSGGRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFR--IELGEI 3509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 462 VAEELQQ--VESCAVTWYNQE---KLILFMVSKD--ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELN 534
Cdd:PRK12467 3510 EARLLQHpsVREAVVLARDGAggkQLVAYVVPADpqGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALP 3589
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638423 535 KIYLNyinlKSENKLSGKEDLWEKLQYLWkstlnlpEDLLRVPDESL---FLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:PRK12467 3590 DPDAK----GSREYVAPRSEVEQQLAAIW-------ADVLGVEQVGVtdnFFELGGDSLLALQVLSRIRQSLGLKLS 3655
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
16-533 |
2.42e-30 |
|
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: 126.05 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVCFDECNnqlpvyYTYKTVVNAASELSNFLLLhcdfQGI---REIGLYCQPGIDLPSWILGILQVPAAYVPIEPDS 92
Cdd:cd17656 3 DAVAVVFENQK------LTYRELNERSNQLARFLRE----KGVkkdSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 93 PPSLSTHFMKKCNLKYILVEKKQINKFK-SFHETLLNYDTFTVEhndlvlfrlhwkntevnlmlndgkekyekekiksiS 171
Cdd:cd17656 73 PEERRIYIMLDSGVRVVLTQRHLKSKLSfNKSTILLEDPSISQE-----------------------------------D 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 172 SEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVpNIQHFRvlFDITQ----EDVLFLASPlTFDPSVV 247
Cdd:cd17656 118 TSNIDYINNSDD--------LLYIIYTSGTTGKPKGVQLEHKNMV-NLLHFE--REKTNinfsDKVLQFATC-SFDVCYQ 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 248 EIFLALSSGASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRRFGSQliKSTVLSATTSLRVLALGGEAFPSLTV 327
Cdd:cd17656 186 EIFSTLLSGGTLYIIREETKRDVEQLFD-LVKRHNIEVVFLPVAFLKFIFSE--REFINRFPTCVKHIITAGEQLVITNE 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 328 LRSWRGEGNKTqIFNVYGITEvSSWATIYRI-PEKTLNstlkcELPvQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGG 405
Cdd:cd17656 263 FKEMLHEHNVH-LHNHYGPSE-THVVTTYTInPEAEIP-----ELP-PIGKPISNTWIYILDQEQQLQPQGIvGELYISG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 406 RN--RVCFLDDEVTV---------PLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCA 473
Cdd:cd17656 335 ASvaRGYLNRQELTAekffpdpfdPNERMYRTGDLARyLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAV 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034638423 474 V-TWYNQEK---LILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17656 415 VlDKADDKGekyLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
192-533 |
5.48e-30 |
|
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: 124.50 E-value: 5.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKcivpNIQHF------RVLFDITQEDVLFLASpLTFDPSVVEIFLALSSGASLLIVPTS 265
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHR----NVAHAahawrrEYELDSFPVRLLQMAS-FSFDVFAGDFARSLLNGGTLVICPDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 266 VKLLPSKLASVLFShHRVTVLQATPTLLRRFGSQLIKSTVlsATTSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYG 345
Cdd:cd17650 170 VKLDPAALYDLILK-SRITLMESTPALIRPVMAYVYRNGL--DLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 346 ITEVSSWATIYRIPEKTLNSTLKcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRNrVC-------------F 411
Cdd:cd17650 247 VTEATIDSTYYEEGRDPLGDSAN----VPIGRPLPNTAMYVLDERLQPQPVGvAGELYIGGAG-VArgylnrpeltaerF 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 412 LDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY---NQEK-LILFM 486
Cdd:cd17650 322 VENPF-APGERMYRTGDLARwRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRedkGGEArLCAYV 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034638423 487 VSKD----ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd17650 401 VAAAtlntAELRAF----LAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-608 |
5.88e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 129.69 E-value: 5.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 4 QELVHKAASCyMDRVAVCFDEcnnqlpVYYTYKTVVNAASELSNFLLLHCDFQGIReIGLYCQPGIDLPSWILGILQVPA 83
Cdd:PRK12316 2007 QRIAEQAARA-PEAIAVVFGD------QHLSYAELDSRANRLAHRLRARGVGPEVR-VAIAAERSFELVVALLAVLKAGG 2078
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 84 AYVPIEPDSPPSLSTHFMKKCNLKYILVEKKqinkfksfhetllnydtftvehndlVLFRLHWKNTEVNLMLNDGKEKYE 163
Cdd:PRK12316 2079 AYVPLDPNYPAERLAYMLEDSGAALLLTQRH-------------------------LLERLPLPAGVARLPLDRDAEWAD 2133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 164 KekiksiSSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFD 243
Cdd:PRK12316 2134 Y------PDTAPAVQLAGEN--------LAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFD 2199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 244 PSVVEIFLALSSGASLLIVPTSVKLlPSKLASVLfSHHRVTVLQATPTLLRRFGSQLiksTVLSATTSLRVLALGGEAFP 323
Cdd:PRK12316 2200 GAHEQWFHPLLNGARVLIRDDELWD-PEQLYDEM-ERHGVTILDFPPVYLQQLAEHA---ERDGRPPAVRVYCFGGEAVP 2274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 324 SLTVLRSWRGEGnKTQIFNVYGITEVSSWATIYripektlnstlKC--ELPVQLGFPLLGTVVEVRDT----NGFTI--Q 395
Cdd:PRK12316 2275 AASLRLAWEALR-PVYLFNGYGPTEAVVTPLLW-----------KCrpQDPCGAAYVPIGRALGNRRAyildADLNLlaP 2342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 396 EGSGQVFLGGR-------NRVC-----FLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQV 462
Cdd:PRK12316 2343 GMAGELYLGGEglargylNRPGltaerFVPDPFSASGERLYRTGDLARYRaDGVVEYLGRIDHQVKIRGFRIELGEIEAR 2422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 463 AEELQQVESCAVTwyNQE-----KLILFMVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK12316 2423 LQAHPAVREAVVV--AQDgasgkQLVAYVVPDDAAedLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK 2500
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 536 IYLnyiNLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:PRK12316 2501 PDV---SQLRQAYVAPQEGLEQRLAAIWQAVLKVE----QVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVP 2566
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
194-535 |
2.67e-27 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 117.30 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 194 YVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDItQEDVLFLA-SPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSK 272
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL-PEGPQFLNqAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 273 LASVLFSHHrVTVLQATPT------LLRRFGSQLIkstvlsatTSLRVLALGGEAFPSLTVlRSWRGEGNKTQIFNVYGI 346
Cdd:PRK04813 226 LFETLPQLP-INVWVSTPSfadmclLDPSFNEEHL--------PNLTHFLFCGEELPHKTA-KKLLERFPSATIYNTYGP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 347 TEVSSWATIYRIPEKTLNstlKCE-LPVqlGFPLLGTVVEVRDTNG---FTIQEG----SGQ-VFLGgrnrvcFLD---- 413
Cdd:PRK04813 296 TEATVAVTSIEITDEMLD---QYKrLPI--GYAKPDSPLLIIDEEGtklPDGEQGeiviSGPsVSKG------YLNnpek 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 414 -DEVTVPLGTMRA--TGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFM 486
Cdd:PRK04813 365 tAEAFFTFDGQPAyhTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDhkvqYLIAYV 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638423 487 VSKDASV-KEY-----IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDV----SELNK 535
Cdd:PRK04813 445 VPKEEDFeREFeltkaIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRkaliEEVNK 503
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
186-597 |
2.11e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.87 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 186 LRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASllIVPTS 265
Cdd:PRK05691 2329 LSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGAR--VVLRA 2406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 266 VKLLPSKLASVLFSHHRVTVLQATPTllrrFGSQLIKSTVLS-ATTSLRVLALGGEAfpsLTV--LRSWRGEGNKTQIFN 342
Cdd:PRK05691 2407 QGQWGAEEICQLIREQQVSILGFTPS----YGSQLAQWLAGQgEQLPVRMCITGGEA---LTGehLQRIRQAFAPQLFFN 2479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 343 VYGITEVSSWATIYRIPEKtlnstlkceLPVQLGFPLLGTVVEVR-----DTN-GFTIQEGSGQVFLGGR---------- 406
Cdd:PRK05691 2480 AYGPTETVVMPLACLAPEQ---------LEEGAASVPIGRVVGARvayilDADlALVPQGATGELYVGGAglaqgyhdrp 2550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 407 ----NRvcFLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE- 480
Cdd:PRK05691 2551 gltaER--FVADPFAADGGRLYRTGDLVRLRaDGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPs 2628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 481 --KLILFMVSKDAS--------VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNkiyLNYINLKSENKLS 550
Cdd:PRK05691 2629 gkQLAGYLVSAVAGqddeaqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP---APDPELNRQAYQA 2705
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1034638423 551 GKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 597
Cdd:PRK05691 2706 PRSELEQQLAQIWREVLNVE----RVGLGDNFFELGGDSILSIQVVS 2748
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
193-539 |
2.14e-21 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 99.80 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVpnIQH---FRVLFDITQEDVLFLASPL---TFDPSVVeiFLALSSGASLLI---VP 263
Cdd:COG0365 187 LFILYTSGTTGKPKGVVHTHGGYL--VHAattAKYVLDLKPGDVFWCTADIgwaTGHSYIV--YGPLLNGATVVLyegRP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 264 TSVKllPSKLASVLfSHHRVTVLQATPTLLR---RFGSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQI 340
Cdd:COG0365 263 DFPD--PGRLWELI-EKYGVTVFFTAPTAIRalmKAGDEPLKKYDLS---SLRLLGSAGEPLNP-EVWEWWY-EAVGVPI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 341 FNVYGITEVSSW--ATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFL----D 413
Cdd:COG0365 335 VDGWGQTETGGIfiSNLPGLPVK----------PGSMGKPVPGYDVAVVDEDGNPVPPGEeGELVIKGPWPGMFRgywnD 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 414 DEVTV------PLGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRL---NIE--LVQ--QVAEelqqvesCAVTWYNQ 479
Cdd:COG0365 405 PERYRetyfgrFPGWYR-TGDGARRdEDGYFWILGRSDDVINVSGHRIgtaEIEsaLVShpAVAE-------AAVVGVPD 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638423 480 E----KLILFMVSKD-ASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLN 539
Cdd:COG0365 477 EirgqVVKAFVVLKPgVEPSDELAKELQAHvreeLGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
195-528 |
7.30e-21 |
|
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: 95.41 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 195 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRV-LFDITQEDVLFLASPLTFDPSVVEIFLALSSGAsLLIVPTSVKLLPSKL 273
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 274 ASVLFshHRVTVLQATPTLLRRFGSqLIKSTvLSATTSLRVLALGGE-AFPSLTVLRSWRGegnKTQIFNVYGITEVSSW 352
Cdd:cd17635 85 KILTT--NAVTTTCLVPTLLSKLVS-ELKSA-NATVPSLRLIGYGGSrAIAADVRFIEATG---LTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 353 ATI-YRIPEKTLNStlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS-GQ-VFLGGRNRVCFLDDEVTVP---LGTMRAT 426
Cdd:cd17635 158 LCLpTDDDSIEINA---------VGRPYPGVDVYLAATDGIAGPSASfGTiWIKSPANMLGYWNNPERTAevlIDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 427 GDFV-TVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFMVS---KDASVKEYIF 498
Cdd:cd17635 229 GDLGeRREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDeefgELVGLAVVAsaeLDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|
gi 1034638423 499 KELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
192-608 |
9.67e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.47 E-value: 9.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNiQHFRVLF-DITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLP 270
Cdd:PRK05691 3871 LAYVIYTSGSTGLPKGVMVEQRGMLNN-QLSKVPYlALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDP 3949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLAsVLFSHHRVTVLQATPTLLRRFGSQlikstVLSATTSLRVLALGGEAFPSLtVLRSWRGEGNKTQIFNVYGITEVS 350
Cdd:PRK05691 3950 QGLL-AHVQAQGITVLESVPSLIQGMLAE-----DRQALDGLRWMLPTGEAMPPE-LARQWLQRYPQIGLVNAYGPAECS 4022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 351 SWATIYRIpekTLNSTLKCELPVqlGFPL----------------LGTVVE--VRDTngftiqeGSGQVFLGG--RNRVC 410
Cdd:PRK05691 4023 DDVAFFRV---DLASTRGSYLPI--GSPTdnnrlylldealelvpLGAVGElcVAGT-------GVGRGYVGDplRTALA 4090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 411 FLDDEVTVPLGTMRATGDFV-TVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---TWYNQEKLILFM 486
Cdd:PRK05691 4091 FVPHPFGAPGERLYRTGDLArRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVavqEGVNGKHLVGYL 4170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 487 VSKDASVK-----EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNyiNLKSENKLSGKEDLWEKLQY 561
Cdd:PRK05691 4171 VPHQTVLAqgallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIG--QLQSQAYLAPRNELEQTLAT 4248
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1034638423 562 LWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:PRK05691 4249 IWADVLKVE----RVGVHDNFFELGGHSLLATQIASRVQKALQRNVP 4291
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
194-529 |
1.74e-19 |
|
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: 90.54 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 194 YVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIvptSVKLLPSKL 273
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 274 ASVLfSHHRVTVLQATPTLLRrfgsQLIKstVLSATTSLRVLALGGEAFPSLTvLRSWRGEGNKTQIFNVYGITEVSSWA 353
Cdd:cd17633 81 IRKI-NQYNATVIYLVPTMLQ----ALAR--TLEPESKIKSIFSSGQKLFEST-KKKLKNIFPKANLIEFYGTSELSFIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 354 tiYRIPEKTlnstlkcELPVQLGFPLLGTVVEVRDTNGF---TIQEGSGQVFLGgrnrvcFLDDEVTVPLGTMrATGDFV 430
Cdd:cd17633 153 --YNFNQES-------RPPNSVGRPFPNVEIEIRNADGGeigKIFVKSEMVFSG------YVRGGFSNPDGWM-SVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 431 TVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK---LILFMVSKDASVKEYIFKELQKYLP 506
Cdd:cd17633 217 YVDeEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARfgeIAVALYSGDKLTYKQLKRFLKQKLS 296
|
330 340
....*....|....*....|...
gi 1034638423 507 SHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17633 297 RYEIPKKIIFVDSLPYTSSGKIA 319
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
192-535 |
2.39e-19 |
|
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: 92.78 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFlaSPLTFDPS---VVEIFLALSSGASLLIV--PTSV 266
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVF--GALPFFHSfglTGCLWLPLLSGIKVVFHpnPLDY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 267 KLLPSklasvLFSHHRVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGI 346
Cdd:cd05909 227 KKIPE-----LIYDKKATILLGTPTFLRGY----ARAAHPEDFSSLRLVVAGAEKLKD-TLRQEFQ-EKFGIRILEGYGT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 347 TEVSSWATIyripeKTLNSTLKcelPVQLGFPLLGT---VVEVRDTNGFTIQEGsGQVFLGGRNRVC-FLDDE---VTVP 419
Cdd:cd05909 296 TECSPVISV-----NTPQSPNK---EGTVGRPLPGMevkIVSVETHEEVPIGEG-GLLLVRGPNVMLgYLNEPeltSFAF 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 420 LGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEEL--QQVESCAVTWYNQ---EKLILFMVSKDASV 493
Cdd:cd05909 367 GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGrkgEKIVLLTTTTDTDP 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034638423 494 keyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05909 447 -----SSLNDILKNAgisnlAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
192-529 |
2.68e-18 |
|
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: 88.82 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT-FDPSVVEIFLALSSGASLLIVPtsvKLLP 270
Cdd:cd17631 100 LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVILR---KFDP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASvLFSHHRVTVLQATPTLLrrfgsQLIKSTVLSATT---SLRVLALGGEAFPSLtVLRSWRGEGnkTQIFNVYGIT 347
Cdd:cd17631 177 ETVLD-LIERHRVTSFFLVPTMI-----QALLQHPRFATTdlsSLRAVIYGGAPMPER-LLRALQARG--VKFVQGYGMT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 348 EVSSWATIYRiPEKTLnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRvcfldDEVTVP 419
Cdd:cd17631 248 ETSPGVTFLS-PEDHR------RKLGSAGRPVFFVEVRIVDPDGREVPPGevgeivvrGPHVMAGYWNR-----PEATAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 420 L---GTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNI---ElVQQVAEELQQVESCAV------TWynQEKLILFM 486
Cdd:cd17631 316 AfrdGWFH-TGDLGRLdEDGYLYIVDRKKDMIISGGE--NVypaE-VEDVLYEHPAVAEVAVigvpdeKW--GEAVVAVV 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034638423 487 VSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17631 390 VPRPGAEldEDELIAHCRERLARYKIPKSVEFVDALPRNATGKIL 434
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
192-528 |
6.16e-18 |
|
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: 87.82 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT-FDPSVVEIFLALSSGASLLIVPTsvkLLP 270
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKlASVLFSHHRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRVLALGGEAFPSLTVLRSWRGEGNKtqIFNVYGITE 348
Cdd:cd05903 172 DK-ALALMREHGVTFMMGATPFL----TDLLNAVEEAGEplSRLRTFVCGGATVPRSLARRAAELLGAK--VCSAYGSTE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 VSSWATIYRIPEKTLNSTLKcelpvqlGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVC-FLDDevtvPLGTMRA- 425
Cdd:cd05903 245 CPGAVTSITPAPEDRRLYTD-------GRPLPGVEIKVVDDTGATLAPGVeGELLSRGPSVFLgYLDR----PDLTADAa 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 426 ------TGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDASvk 494
Cdd:cd05903 314 pegwfrTGDLaRLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLgeraCAVVVTKSGA-- 391
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034638423 495 EYIFKELQKYLPSHAV-----PDELVLIDSLPFTSHGKI 528
Cdd:cd05903 392 LLTFDELVAYLDRQGVakqywPERLVHVDDLPRTPSGKV 430
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
192-533 |
9.12e-18 |
|
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: 87.13 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHF-RVLFDITQEDVLFLASPLTFDPSV-VEIFLALSSGASLLIVPTSVKll 269
Cdd:cd05919 93 IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWPT-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 270 PSKLASVLfSHHRVTVLQATPTLLRRfgsqLIKSTVLS--ATTSLRVLALGGEAFPsltvlrswRGEGNK------TQIF 341
Cdd:cd05919 171 AERVLATL-ARFRPTVLYGVPTFYAN----LLDSCAGSpdALRSLRLCVSAGEALP--------RGLGERwmehfgGPIL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 342 NVYGITEVSSWATIYRIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGG--------RNRvcfl 412
Cdd:cd05919 238 DGIGATEVGHIFLSNRPGAWRLGST---------GRPVPGYEIRLVDEEGHTIPPGEeGDLLVRGpsaavgywNNP---- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 413 DDEVTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMV 487
Cdd:cd05919 305 EKSRATFNGGWYRTGDKFCRdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPEStglsRLTAFVV 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034638423 488 SK-----DASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05919 385 LKspaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
193-529 |
2.07e-17 |
|
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: 86.65 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHF-RVLFDITQEDVLFlaspltfdpSVVEIFLALSSGASL---LIVPTSVKL 268
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYaRNVLGIREDDVCF---------SAAKLFFAYGLGNSLtfpLSVGATTVL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 269 LPSKLASVLFSH----HRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRVLALGGEAFPSlTVLRSWRgegNKT--QI 340
Cdd:cd05959 237 MPERPTPAAVFKrirrYRPTVFFGVPTLY----AAMLAAPNLPSRdlSSLRLCVSAGEALPA-EVGERWK---ARFglDI 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 341 FNVYGITEVsswATIY---RIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTIQEG-SGQVFL-GGRNRVCFL--- 412
Cdd:cd05959 309 LDGIGSTEM---LHIFlsnRPGRVRYGTT---------GKPVPGYEVELRDEDGGDVADGePGELYVrGPSSATMYWnnr 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 413 DDEVTVPLGTMRATGD-FVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMV 487
Cdd:cd05959 377 DKTRDTFQGEWTRTGDkYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEdgltKPKAFVV 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034638423 488 SKD-ASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05959 457 LRPgYEDSEALEEELKEFvkdrLAPYKYPRWIVFVDELPKTATGKIQ 503
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-535 |
3.84e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 81.37 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL-TFDPSVVEIFLALSSGASLLIVPTSVKLLP 270
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLfHVNGSVVTLLTPLASGAHVVLAGPAGYRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASV--LFSHHRVTVLQATPTLLrrfgSQLIKSTVLSATTSLRVLALGGEAFPslTVLRSWRGEGNKTQIFNVYGITE 348
Cdd:cd05944 84 GLFDNFwkLVERYRITSLSTVPTVY----AALLQVPVNADISSLRFAMSGAAPLP--VELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 VSSWATI-YRIPEKTLNStlkcelpVQLGFPLLGTVVEVRDTNGFTIQE-GSGQVF---------LGG-----RNRVCFL 412
Cdd:cd05944 158 ATCLVAVnPPDGPKRPGS-------VGLRLPYARVRIKVLDGVGRLLRDcAPDEVGeicvagpgvFGGylyteGNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 413 DDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLILFM- 486
Cdd:cd05944 231 AD------GWLN-TGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGqpdaHAGELPVAYVq 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1034638423 487 VSKDASVKEyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05944 304 LKPGAVVEE---EELLAWARDHvperaAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
192-533 |
6.71e-16 |
|
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: 81.84 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQ--HFRVLFDITQEDVLFLASPL--TFDPSVVeIFLALSSGASLLIVPTSVk 267
Cdd:cd05936 127 VAVLQYTSGTTGVPKGAMLTHRNLVANALqiKAWLEDLLEGDDVVLAALPLfhVFGLTVA-LLLPLALGATIVLIPRFR- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 268 llpSKLASVLFSHHRVTVLQATPTLLrrfgSQLI--KSTVLSATTSLRVLALGGEAFPsLTVLRSWRgegnktQIFNV-- 343
Cdd:cd05936 205 ---PIGVLKEIRKHRVTIFPGVPTMY----IALLnaPEFKKRDFSSLRLCISGGAPLP-VEVAERFE------ELTGVpi 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 344 ---YGITEVSSWATIYRIPEKTLNSTlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS--------GQVFLGGRNRvcfl 412
Cdd:cd05936 271 vegYGLTETSPVVAVNPLDGPRKPGS--------IGIPLPGTEVKIVDDDGEELPPGEvgelwvrgPQVMKGYWNR---- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 413 ddevtvPLGTMRA-------TGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNI---ElVQQVAEELQQVESCAVTW----Y 477
Cdd:cd05936 339 ------PEETAEAfvdgwlrTGDIGYMdEDGYFFIVDRKKDMIIVGG--FNVyprE-VEEVLYEHPAVAEAAVVGvpdpY 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638423 478 NQEKLILFMVSKD-ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05936 410 SGEAVKAFVVLKEgASLtEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2-535 |
5.09e-15 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 79.41 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 2 TLQELVHKAASCYMDRVAVCFDECNNqlpvyYTYKTVVNAASELSNFLLLhcdfQGIreiglycQPG----IDLPSW--- 74
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNHGAS-----YTYSALDHAASRLANWLLA----KGI-------EPGdrvaFQLPGWcef 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 75 ---ILGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEK--KQINKFKSFHEtlLNYDTFTVEHndLVLF-RLHWKN 148
Cdd:PRK06087 88 tiiYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAPTlfKQTRPVDLILP--LQNQLPQLQQ--IVGVdKLAPAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 149 TEVNL--MLNDGKekyekekikSISSE---HVNEekaeehmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFR 223
Cdd:PRK06087 164 SSLSLsqIIADYE---------PLTTAittHGDE--------------LAAVLFTSGTEGLPKGVMLTHNNILASERAYC 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 224 VLFDITQEDVLFLASPLT----FDPSVVEIFLAlsSGASLLIvptsvKLLPSKLASVLFSHHRVT-VLQATP------TL 292
Cdd:PRK06087 221 ARLNLTWQDVFMMPAPLGhatgFLHGVTAPFLI--GARSVLL-----DIFTPDACLALLEQQRCTcMLGATPfiydllNL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 293 LRRFGSQLikstvlsatTSLRVLALGGEAFPSLTVLRSWRgegNKTQIFNVYGITEVSSWAtiYRIPEKTLNSTLKCElp 372
Cdd:PRK06087 294 LEKQPADL---------SALRFFLCGGTTIPKKVARECQQ---RGIKLLSVYGSTESSPHA--VVNLDDPLSRFMHTD-- 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 373 vqlGFPLLGTVVEVRDTNGFTI------QEGS--GQVFLGgrnrvcFLDDevtvPLGTMRA--------TGDFVTV-KDG 435
Cdd:PRK06087 358 ---GYAAAGVEIKVVDEARKTLppgcegEEASrgPNVFMG------YLDE----PELTARAldeegwyySGDLCRMdEAG 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 436 EIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDA----SVKEYIFKELQKYLPS 507
Cdd:PRK06087 425 YIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLgersCAYVVLKAPhhslTLEEVVAFFSRKRVAK 504
|
570 580
....*....|....*....|....*...
gi 1034638423 508 HAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK06087 505 YKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
194-528 |
2.43e-14 |
|
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: 77.23 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 194 YVLHTSGTTGIPK-IVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL---TFDPSVveIFLALSSGA-SLLIVPTSVKL 268
Cdd:cd17634 236 FILYTSGTTGKPKgVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVgwvTGHSYL--LYGPLACGAtTLLYEGVPNWP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 269 LPSKLASVLfSHHRVTVLQATPTLLRRF---GSQLIKSTVLSattSLRVLALGGEAFPSLTVLRSWRG-EGNKTQIFNVY 344
Cdd:cd17634 314 TPARMWQVV-DKHGVNILYTAPTAIRALmaaGDDAIEGTDRS---SLRILGSVGEPINPEAYEWYWKKiGKEKCPVVDTW 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 345 GITEVsSWATIYRIPEKTlnsTLKCELPVQlgfPLLGTVVEVRDTNGFTIQEGS-GQVFLG----GRNRVCFLDDE---V 416
Cdd:cd17634 390 WQTET-GGFMITPLPGAI---ELKAGSATR---PVFGVQPAVVDNEGHPQPGGTeGNLVITdpwpGQTRTLFGDHErfeQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 417 TV--PLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMVSK 489
Cdd:cd17634 463 TYfsTFKGMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAikgqAPYAYVVLN 542
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034638423 490 D---------ASVKEYIFKELQKYlpshAVPDELVLIDSLPFTSHGKI 528
Cdd:cd17634 543 HgvepspelyAELRNWVRKEIGPL----ATPDVVHWVDSLPKTRSGKI 586
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
196-528 |
4.63e-14 |
|
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: 75.63 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 196 LHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASpltfDP-------SVVEIFLALSSGASLLIVPTSVKL 268
Cdd:cd05973 94 MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAA----DPgwayglyYAITGPLALGHPTILLEGGFSVES 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 269 LPSKLasvlfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATT---SLRVLALGGEafPSLTVLRSWRGEGNKTQIFNVYG 345
Cdd:cd05973 170 TWRVI-----ERLGVTNLAGSPTAYR----LLMAAGAEVPARpkgRLRRVSSAGE--PLTPEVIRWFDAALGVPIHDHYG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 346 ITEVSswatiyripeKTLNSTLKCELPVQ---LGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVC-----FLDDEV 416
Cdd:cd05973 239 QTELG----------MVLANHHALEHPVHagsAGRAMPGWRVAVLDDDGDELGPGEpGRLAIDIANSPLmwfrgYQLPDT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 417 TVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLILFMV---S 488
Cdd:cd05973 309 PAIDGGYYLTGDTVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGvpdpERTEVVKAFVVlrgG 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034638423 489 KDASvkEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05973 389 HEGT--PALADELQLHvkkrLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
198-529 |
1.14e-13 |
|
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: 74.44 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 198 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASP---LTFDPSVVEIFlALSSGASLLIVPTSVkllPSKLA 274
Cdd:cd05958 105 TSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPplaFTFGLGGVLLF-PFGVGASGVLLEEAT---PDLLL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 275 SVLfSHHRVTVLQATPTLLR------RFGSQLIkstvlsatTSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGITE 348
Cdd:cd05958 181 SAI-ARYKPTVLFTAPTAYRamlahpDAAGPDL--------SSLRKCVSAGEALPA-ALHRAWK-EATGIPIIDGIGSTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 vsswatIYRIpekTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDE--VTVPLGTMRA 425
Cdd:cd05958 250 ------MFHI---FISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTiGRLAVRGPTGCRYLADKrqRTYVQGGWNI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 426 TGD-FVTVKDGEIFFLGRKDSQIKRHGkrLNIELVqQVAEELQQ---VESCAVTWY-NQEKLIL---FMVSK-DASVKEY 496
Cdd:cd05958 321 TGDtYSRDPDGYFRHQGRSDDMIVSGG--YNIAPP-EVEDVLLQhpaVAECAVVGHpDESRGVVvkaFVVLRpGVIPGPV 397
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034638423 497 IFKELQKYLPSHAV----PDELVLIDSLPFTSHGKID 529
Cdd:cd05958 398 LARELQDHAKAHIApykyPRAIEFVTELPRTATGKLQ 434
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
193-528 |
1.17e-13 |
|
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: 74.46 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFlaspLTFDPSVVE-----IFLALSSGASLLIVPTsvK 267
Cdd:cd05969 92 TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW----CTADPGWVTgtvygIWAPWLNGVTNVVYEG--R 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 268 LLPSKLASVLfSHHRVTVLQATPTLLR---RFGSQLIKSTVLSattSLRVLALGGEAFPSLTVlrSWRGEGNKTQIFNVY 344
Cdd:cd05969 166 FDAESWYGII-ERVKVTVWYTAPTAIRmlmKEGDELARKYDLS---SLRFIHSVGEPLNPEAI--RWGMEVFGVPIHDTW 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 345 GITEVSSW--ATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFL--------------GGRN 407
Cdd:cd05969 240 WQTETGSImiANYPCMPIK----------PGSMGKPLPGVKAAVVDENGNELPPGTkGILALkpgwpsmfrgiwndEERY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 408 RVCFLDDEVTvplgtmraTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTwyNQEKLIL-- 484
Cdd:cd05969 310 KNSFIDGWYL--------TGDLAYRdEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVI--GKPDPLRge 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 485 ----FMVSKDA-----SVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05969 380 iikaFISLKEGfepsdELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
170-537 |
1.38e-13 |
|
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: 74.45 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 170 ISSEHVNEEKAEEhmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEI 249
Cdd:cd05908 95 ITEEEVLCELADE---------LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 250 FLA-LSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLqATPTllrrFGSQLIKSTVLSAT------TSLRVLALGGEAF 322
Cdd:cd05908 166 HLApLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIV-SSPN----FGYKYFLKTLKPEKandwdlSSIRMILNGAEPI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 323 PS------LTVLRSWRgeGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTL-------------------KCELPVQLGF 377
Cdd:cd05908 241 DYelchefLDHMSKYG--LKRNAILPVYGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkkdsECLTFVEVGK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 378 PLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNrvcflddeVTV-----PLGTMRA--------TGDFVTVKDGEIFFLGRK 443
Cdd:cd05908 319 PIDETDIRICDEDNKILPDGYiGHIQIRGKN--------VTPgyynnPEATAKVftddgwlkTGDLGFIRNGRLVITGRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 444 DSQIKRHGKRLNIELVQQVAEELQQVES-----CAV--TWYNQEKLILFMVSKDaSVKEYIfkELQKYLPSHAVP----- 511
Cdd:cd05908 391 KDIIFVNGQNVYPHDIERIAEELEGVELgrvvaCGVnnSNTRNEEIFCFIEHRK-SEDDFY--PLGKKIKKHLNKrggwq 467
|
410 420
....*....|....*....|....*..
gi 1034638423 512 -DELVLIDSLPFTSHGKIDVSELNKIY 537
Cdd:cd05908 468 iNEVLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
192-529 |
1.86e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 74.07 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdpsvveiF---------LALSSGASLLIV 262
Cdd:PRK06187 169 AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM---------FhvhawglpyLALMAGAKQVIP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 263 PtsvKLLPSKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVlsATTSLRVLALGGEAFPsLTVLRSWRgEGNKTQIFN 342
Cdd:PRK06187 240 R---RFDPENLLD-LIETERVTFFFAVPTIWQMLLKAPRAYFV--DFSSLRLVIYGGAALP-PALLREFK-EKFGIDLVQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 343 VYGITEVSSWATIYRIPEKTLNSTlkcELPVQLGFPLLGtvVEVR--DTNGFTI--QEGS-GQVFLGGRN--RVCFLDDE 415
Cdd:PRK06187 312 GYGMTETSPVVSVLPPEDQLPGQW---TKRRSAGRPLPG--VEARivDDDGDELppDGGEvGEIIVRGPWlmQGYWNRPE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 416 VTVPL---GTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNI---ELvqqvaEEL----QQVESCAV------TWyn 478
Cdd:PRK06187 387 ATAETidgGWLH-TGDVGYIdEDGYLYITDRIKDVIISGGE--NIyprEL-----EDAlyghPAVAEVAVigvpdeKW-- 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638423 479 QEKLILFMVSKD-ASVKEyifKELQKYLPSH----AVPDELVLIDSLPFTSHGKID 529
Cdd:PRK06187 457 GERPVAVVVLKPgATLDA---KELRAFLRGRlakfKLPKRIAFVDELPRTSVGKIL 509
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
192-535 |
4.45e-13 |
|
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: 72.75 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASpltfDPSvvEIFLALSSGASLLIVPTSV----- 266
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIA----DPG--WAKGAWSSFFGPWLLGATVfvyeg 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 267 -KLLPSKLASVLfSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEafpSLT--VLRSWRGEGNKTqIFNV 343
Cdd:cd05972 157 pRFDAERILELL-ERYGVTSFCGPPTAYRMLIKQDLSSYKFS---HLRLVVSAGE---PLNpeVIEWWRAATGLP-IRDG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 344 YGITEVSSwatiyripekTLNSTLKCEL-PVQLGFPLLGTVVEVRDTNG----------FTIQEGSGQVFLGgrnrvcFL 412
Cdd:cd05972 229 YGQTETGL----------TVGNFPDMPVkPGSMGRPTPGYDVAIIDDDGrelppgeegdIAIKLPPPGLFLG------YV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 413 DDEVtvplgTMRA--------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRL---NIE--LVQQVAeelqqVESCAVTWYN 478
Cdd:cd05972 293 GDPE-----KTEAsirgdyylTGDRAYRdEDGYFWFVGRADDIIKSSGYRIgpfEVEsaLLEHPA-----VAEAAVVGSP 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638423 479 QEkLILFMV------SKDASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05972 363 DP-VRGEVVkafvvlTSGYEPSEELAEELQGHvkkvLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
192-533 |
6.19e-13 |
|
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: 72.08 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIV---PNIQHFRVLFDITqEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKL 268
Cdd:cd05971 90 PALIIYTSGTTGPPKGALHAHRVLLghlPGVQFPFNLFPRD-GDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 269 LPSKLASVLfSHHRVTVLQATPTLLRRFGSQliKSTVLSATTSLRVLALGGEafPSLTVLRSWRGEGNKTQIFNVYGITE 348
Cdd:cd05971 169 DPKAALDLM-SRYGVTTAFLPPTALKMMRQQ--GEQLKHAQVKLRAIATGGE--SLGEELLGWAREQFGVEVNEFYGQTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 ----VSSWATIYRIPektlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFL----DDEVTV- 418
Cdd:cd05971 244 cnlvIGNCSALFPIK------------PGSMGKPIPGHRVAIVDDNGTPLPPGEvGEIAVELPDPVAFLgywnNPSATEk 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 419 -PLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY----NQEKLILFMVSKDAS 492
Cdd:cd05971 312 kMAGDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdpiRGEIVKAFVVLNPGE 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034638423 493 VK-EYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05971 392 TPsDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
192-529 |
6.88e-13 |
|
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: 72.35 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLA-LSSGASLLIVPtsvKLLP 270
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLStLAAGGSVVLPP---RFSA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASvLFSHHRVTVLQATPT----LLRRFgsqliKSTVLSATTSLRVLALGGEAFPsLTVLRSWRgEGNKTQIFNVYGI 346
Cdd:cd05926 228 STFWP-DVRDYNATWYTAVPTihqiLLNRP-----EPNPESPPPKLRFIRSCSASLP-PAVLEALE-ATFGAPVLEAYGM 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 347 TEVSSWATIYRIPEktlnstlKCELPVQLGFPllgTVVEVR--DTNGFTIQEG-SGQVFLGGRNrVC--FLDD-----EV 416
Cdd:cd05926 300 TEAAHQMTSNPLPP-------GPRKPGSVGKP---VGVEVRilDEDGEILPPGvVGEICLRGPN-VTrgYLNNpeanaEA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 417 TVPLGTMRaTGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV-----TWYNQEKLILFMVSKD 490
Cdd:cd05926 369 AFKDGWFR-TGDLgYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfgvpdEKYGEEVAAAVVLREG 447
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034638423 491 ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05926 448 ASVtEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQ 487
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
195-533 |
2.19e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 70.94 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 195 VLHTSGTTGIPKIVRVPHKcivPNIQHFRVLFDIT---QEDVLFLASPLTFDPSVVEIFLALSSGASLLivpTSVKLLPS 271
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGP---GGIGTLKAILDRTpwrAEEPTVIVAPMFHAWGFSQLVLAASLACTIV---TRRRFDPE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 272 klASV-LFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNktQIFNVYGITEVS 350
Cdd:PRK13382 275 --ATLdLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD--VIYNNYNATEAG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 351 sWATIyRIPEktlnstlkcEL---PVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLggRNRVCFldDEVTVplGT---- 422
Cdd:PRK13382 351 -MIAT-ATPA---------DLraaPDTAGRPAEGTEIRILDQDFREVPTGEvGTIFV--RNDTQF--DGYTS--GStkdf 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 423 ---MRATGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVK 494
Cdd:PRK13382 414 hdgFMASGDVGYLDEnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQygqrLAAFVVLKPGASA 493
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034638423 495 --EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:PRK13382 494 tpETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
192-529 |
3.83e-12 |
|
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: 68.51 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASlLIVPTSVKLLPS 271
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAE-LVLLERNQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 272 KLAsvlfsHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLALGGEAFPS-LT---VLRSWRgegnktqIFNVYGIT 347
Cdd:cd17630 81 DLA-----PPGVTHVSLVPTQLQRL---LDSGQGPAALKSLRAVLLGGAPIPPeLLeraADRGIP-------LYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 348 EVSSWATIYRIPEKTLNStlkcelpvqLGFPLLGtvVEVRDTNGFTIQEGSGQVFLGGRNRVC---FLDDevtvplGTMR 424
Cdd:cd17630 146 ETASQVATKRPDGFGRGG---------VGVLLPG--RELRIVEDGEIWVGGASLAMGYLRGQLvpeFNED------GWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 425 aTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW-----YNQeKLILFMVSKDASVKEYIF 498
Cdd:cd17630 209 -TKDLGELhADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGvpdeeLGQ-RPVAVIVGRGPADPAELR 286
|
330 340 350
....*....|....*....|....*....|.
gi 1034638423 499 KELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd17630 287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVD 317
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
192-528 |
4.11e-12 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 70.08 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdpsvveiflALSSG-ASLLIVPTSVK--- 267
Cdd:PRK13295 199 VTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPM-----------AHQTGfMYGLMMPVMLGata 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 268 ----LLPSKLASVLFSHHRVT-VLQATPtllrrFGSQLIKSTVLSATT--SLRVLALGGEAFPSLTVLRSWRGEGnkTQI 340
Cdd:PRK13295 268 vlqdIWDPARAAELIRTEGVTfTMASTP-----FLTDLTRAVKESGRPvsSLRTFLCAGAPIPGALVERARAALG--AKI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 341 FNVYGITEVSSWATIY--RIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTI---QEGSGQV-----FLG--GRNR 408
Cdd:PRK13295 341 VSAWGMTENGAVTLTKldDPDERASTTD---------GCPLPGVEVRVVDADGAPLpagQIGRLQVrgcsnFGGylKRPQ 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 409 VCFLDDEvtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----I 483
Cdd:PRK13295 412 LNGTDAD-----GWFD-TGDLARIdADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLgeraC 485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034638423 484 LFMVSKDASvkEYIFKELQKYLPSHAV-----PDELVLIDSLPFTSHGKI 528
Cdd:PRK13295 486 AFVVPRPGQ--SLDFEEMVEFLKAQKVakqyiPERLVVRDALPRTPSGKI 533
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
192-528 |
1.72e-11 |
|
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: 67.70 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtF--DPSVVEIFLALSSGASLLIVPtsvKLL 269
Cdd:cd05934 83 PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPL-FhiNAQAVSVLAALSVGATLVLLP---RFS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 270 PSKLASVLFSHHrVTVLQATPTLLrrfgSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGnkTQIFNVYGITEV 349
Cdd:cd05934 159 ASRFWSDVRRYG-ATVTNYLGAML----SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG--VRLLEGYGMTET 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 350 SSwATIYRIPEKTlnstlkceLPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDEVTVPLGTMRA--- 425
Cdd:cd05934 232 IV-GVIGPRDEPR--------RPGSIGRPAPGYEVRIVDDDGQELPAGEpGELVIRGLRGWGFFKGYYNMPEATAEAmrn 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 426 ----TGD-FVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV----TWYNQEKLILFMVSKDASV--K 494
Cdd:cd05934 303 gwfhTGDlGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVvavpDEVGEDEVKAVVVLRPGETldP 382
|
330 340 350
....*....|....*....|....*....|....
gi 1034638423 495 EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05934 383 EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
195-533 |
1.81e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 68.03 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 195 VLHTSGTTGIPKIVRVPHkciVPNIQHFRVLFD---ITQEDVLFLASPLTFDPSVVEIFLALSSGASLLivpTSVKLLPS 271
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPE---PSPLAPLAGLLSrvpFRAGETTLLPAPMFHATGWAHLTLAMALGSTVV---LRRRFDPE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 272 K-LASVlfSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKtqIFNVYGITEVS 350
Cdd:PRK07788 286 AtLEDI--AKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV--LYNLYGSTEVA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 351 sWATIYRIPEKTLNSTLkcelpvqLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLG----------GRNRVCflddevtvp 419
Cdd:PRK07788 362 -FATIATPEDLAEAPGT-------VGRPPKGVTVKILDENGNEVPRGvVGRIFVGngfpfegytdGRDKQI--------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 420 LGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV------TWYnqEKLILFMVSKDAS 492
Cdd:PRK07788 425 IDGLLSSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVigvddeEFG--QRLRAFVVKAPGA 502
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034638423 493 ------VKEYIFKELQKylpsHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:PRK07788 503 aldedaIKDYVRDNLAR----YKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
195-536 |
1.87e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 67.96 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 195 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtFDPSVVEIFL--ALSSGAsLLIVPTsvKLLPSK 272
Cdd:PRK06839 154 ICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGG-VIIVPR--KFEPTK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 273 lASVLFSHHRVTVLQATPTLlrrfgSQLIKSTVLSATTSL---RVLALGGEAFPsLTVLRSWR------GEGnktqifnv 343
Cdd:PRK06839 230 -ALSMIEKHKVTVVMGVPTI-----HQALINCSKFETTNLqsvRWFYNGGAPCP-EELMREFIdrgflfGQG-------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 344 YGITEVSswATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDEVTVPLGT 422
Cdd:PRK06839 295 FGMTETS--PTVFMLSEEDARRK-----VGSIGKPVLFCDYELIDENKNKVEVGEvGELLIRGPNVMKEYWNRPDATEET 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 423 MR----ATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDASV 493
Cdd:PRK06839 368 IQdgwlCTGDLARVdEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWgeipIAFIVKKSSSV 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034638423 494 --KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKI 536
Cdd:PRK06839 448 liEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
195-538 |
3.79e-11 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 67.13 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 195 VLHTSGTTGIPK-IVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLI---VPTSVKllP 270
Cdd:cd05968 241 IIYTSGTTGKPKgTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgAPDHPK--A 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLaSVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPsltvLRSW------RGEGNKTqIFNVY 344
Cdd:cd05968 319 DRL-WRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWN----PEPWnwlfetVGKGRNP-IINYS 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 345 GITEVSswATIYRipektlNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFL----GGRNRVCFLDDEVTVPL 420
Cdd:cd05968 393 GGTEIS--GGILG------NVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLlapwPGMTRGFWRDEDRYLET 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 421 GTMR-----ATGDFVTVKDGEIFF-LGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFMVSKD 490
Cdd:cd05968 465 YWSRfdnvwVHGDFAYYDEEGYFYiLGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHpvkgEAIVCFVVLKP 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 491 A-SVKEYIFKELQKYLPSHA----VPDELVLIDSLPFTSHGKIDVSELNKIYL 538
Cdd:cd05968 545 GvTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
198-535 |
4.37e-11 |
|
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: 66.50 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 198 TSGTTGIPKIVRVPHKCIVpnIQHFRVL----FDITQEDVLFLASPLtFD------PsvveiFLALSSGASLliVPTSVK 267
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSLV--LHAMAALltdgLGLSESDVVLPVVPM-FHvnawglP-----YAAAMVGAKL--VLPGPY 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 268 LLPSKLASvLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSlTVLRSWRGEGnkTQIFNVYGI 346
Cdd:cd12119 241 LDPASLAE-LIEREGVTFAAGVPTVWQGLLDHLeANGRDLS---SLRRVVIGGSAVPR-SLIEAFEERG--VRVIHAWGM 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 347 TEVSSWATIYRIPEKTLNSTLKCELPVQL--GFPLLGTVVEVRDTNGFTIQ---EGSGQVFLGGrNRVC---FLDDEVTV 418
Cdd:cd12119 314 TETSPLGTVARPPSEHSNLSEDEQLALRAkqGRPVPGVELRIVDDDGRELPwdgKAVGELQVRG-PWVTksyYKNDEESE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 419 PL---GTMRaTGDFVTV-KDGEIFFLGR-KDSqIKRHGKRL-NIELvQQVAEELQQVESCAV------TWynQEKLILFM 486
Cdd:cd12119 393 ALtedGWLR-TGDVATIdEDGYLTITDRsKDV-IKSGGEWIsSVEL-ENAIMAHPAVAEAAVigvphpKW--GERPLAVV 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034638423 487 VSKD-ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd12119 468 VLKEgATVtAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
193-529 |
4.49e-11 |
|
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: 66.58 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFD-----PSVVEIFLAlssGASLLIVPTsvk 267
Cdd:cd05920 142 ALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNfplacPGVLGTLLA---GGRVVLAPD--- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 268 llPSKLASV-LFSHHRVTVLQATPTLLRRFGSQLIKSTvlSATTSLRVLALGGEAFPSlTVLRSWRGE-GNKTQifNVYG 345
Cdd:cd05920 216 --PSPDAAFpLIEREGVTVTALVPALVSLWLDAAASRR--ADLSSLRLLQVGGARLSP-ALARRVPPVlGCTLQ--QVFG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 346 ITEvsSWATIYRI--PEKTLNSTlkcelpvQlGFPLL-GTVVEVRDTNGFTIQEGS-GQVFLGG------------RNRV 409
Cdd:cd05920 289 MAE--GLLNYTRLddPDEVIIHT-------Q-GRPMSpDDEIRVVDEEGNPVPPGEeGELLTRGpytirgyyrapeHNAR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 410 CFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLIL 484
Cdd:cd05920 359 AFTPD------GFYR-TGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAmpdeLLGERSCA 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034638423 485 FMVSKDASVKeyiFKELQKYL-----PSHAVPDELVLIDSLPFTSHGKID 529
Cdd:cd05920 432 FVVLRDPPPS---AAQLRRFLrerglAAYKLPDRIEFVDSLPLTAVGKID 478
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
750-1047 |
4.56e-11 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 65.72 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 750 TQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILGDRIesSACVSKCGNFIVV 829
Cdd:TIGR03300 35 QPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGK--VYAADADGTVAALDAETGKRLWRVDLDERL--SGGVGADGGLVFV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 830 GCYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTT--GLIYIGSHDQHAYALDIYRKKCVWkskcggtVFSS--PCLN 905
Cdd:TIGR03300 111 GTEKGEVIALDAEDGKELW----RAKLSSEVLSPPLVanGLVVVRTNDGRLTALDAATGERLW-------TYSRvtPPLT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 906 L--------IPHHLYFATLGGLLLAVN-----PVWQFSTSGP-----------IFSSPctSPSEQKIFFGSHDCFIYCCN 961
Cdd:TIGR03300 180 LrgsaspviADGGVLVGFAGGKLVALDlqtgqPLWEQRVALPkgrtelerlvdVDGDP--VVDGGQVYAVSYQGRVAALD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 962 MK-GHLQWKFETTSrvYATPFAFHNYngsnemlLAAASTDGKVWILESQSGQ-LQSVYELPGEVFSSPVVLESMLIIGCR 1039
Cdd:TIGR03300 258 LRsGRVLWKRDASS--YQGPAVDDNR-------LYVTDADGVVVALDRRSGSeLWKNDELKYRQLTAPAVLGGYLVVGDF 328
|
....*...
gi 1034638423 1040 DNYVYCLD 1047
Cdd:TIGR03300 329 EGYLHWLD 336
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
170-536 |
4.90e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 66.34 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 170 ISSEHVNE----EKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdps 245
Cdd:PRK07638 119 IEIDEWKRmiekYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTL----- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 246 VVEIFL-----ALSSGASLLIVPtsvKLLPSKLASVLfSHHRVTVLQATPTLLRRFGSQlikstvlsattslrvlalggE 320
Cdd:PRK07638 194 VHSLFLygaisTLYVGQTVHLMR---KFIPNQVLDKL-ETENISVMYTVPTMLESLYKE--------------------N 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 321 AFP--SLTVLRS---WRGEGNK--------TQIFNVYGITEVSSWAtiYRIPEktlNSTLKcelPVQLGFPLLGTVVEVR 387
Cdd:PRK07638 250 RVIenKMKIISSgakWEAEAKEkiknifpyAKLYEFYGASELSFVT--ALVDE---ESERR---PNSVGRPFHNVQVRIC 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 388 DTNGFTIQEG--------SGQVFLGGRNRVCFLDDEVTVPLGTMRATGdFVTvKDGEIFFLGRKDSQIKRHGkrLNI--E 457
Cdd:PRK07638 322 NEAGEEVQKGeigtvyvkSPQFFMGYIIGGVLARELNADGWMTVRDVG-YED-EEGFIYIVGREKNMILFGG--INIfpE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 458 LVQQVAEELQQVESCAVT------WYNQEKLILfmvsKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVS 531
Cdd:PRK07638 398 EIESVLHEHPAVDEIVVIgvpdsyWGEKPVAII----KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARM 473
|
....*
gi 1034638423 532 ELNKI 536
Cdd:PRK07638 474 EAKSW 478
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
193-546 |
6.89e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 66.53 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFdpsvveiflALSSGASLLIVpTSVK--L 268
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVfhSF---------GLTGGLVLPLL-SGVKvfL 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 269 LPSKLasvlfsHHRVT---VLQATPTLLrrFGSqlikSTVLS--ATT-------SLRVLALGGEAFPSLTvlRSWRGEGN 336
Cdd:PRK06814 866 YPSPL------HYRIIpelIYDTNATIL--FGT----DTFLNgyARYahpydfrSLRYVFAGAEKVKEET--RQTWMEKF 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 337 KTQIFNVYGITEVSswatiyriPEKTLNSTLKCELpvqlgfpllGTV------VEVR--DTNGftIQEGsGQVFLGGRNr 408
Cdd:PRK06814 932 GIRILEGYGVTETA--------PVIALNTPMHNKA---------GTVgrllpgIEYRlePVPG--IDEG-GRLFVRGPN- 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 409 vcflddevtVPLGTMRA---------------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEEL-QQVES 471
Cdd:PRK06814 991 ---------VMLGYLRAenpgvleppadgwydTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALH 1061
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638423 472 CAVTWYNQ---EKLILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNYINLKSE 546
Cdd:PRK06814 1062 AAVSIPDArkgERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
193-533 |
2.48e-10 |
|
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: 63.90 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVrvphkcivpnIQHFRVLF----------DITQEDVLFLASPLtFDPSVVEIFL-ALSSGASLLI 261
Cdd:cd05912 80 ATIMYTSGTTGKPKGV----------QQTFGNHWwsaigsalnlGLTEDDNWLCALPL-FHISGLSILMrSVIYGMTVYL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 262 VPtsvKLLPSKLASVLFSHhRVTVLQATPTLLRRfgsqLIKSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGnkTQIF 341
Cdd:cd05912 149 VD---KFDAEQVLHLINSG-KVTIISVVPTMLQR----LLEILGEGYPNNLRCILLGGGPAP-KPLLEQCKEKG--IPVY 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 342 NVYGITEVSSWATiyripekTLNSTLKCELPVQLGFPLLGTVVEVRDTNGftIQEGSGQVFLGGRNRV-CFL---DDEVT 417
Cdd:cd05912 218 QSYGMTETCSQIV-------TLSPEDALNKIGSAGKPLFPVELKIEDDGQ--PPYEVGEILLKGPNVTkGYLnrpDATEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 418 VPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDAS 492
Cdd:cd05912 289 SFENGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvpVAFVVSERPI 368
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034638423 493 VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05912 369 SEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
192-474 |
2.57e-10 |
|
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: 64.15 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDV--LFLasPLTfdpSVVE----IFLALSSGASLLIVPtS 265
Cdd:cd05907 89 LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRhlSFL--PLA---HVFErragLYVPLLAGARIYFAS-S 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 266 VKLLPSKLASVlfshhRVTVLQATPTLLRRF--GSQLIKST-------VLSATTSLRVLALGGEAFPsLTVLRSWRGEGn 336
Cdd:cd05907 163 AETLLDDLSEV-----RPTVFLAVPRVWEKVyaAIKVKAVPglkrklfDLAVGGRLRFAASGGAPLP-AELLHFFRALG- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 337 kTQIFNVYGITEVSSWATIyripektlnSTLKCELPVQLGFPLLGTVVEVRDTNgfTIQEGSGQVFLGGRNrvcflDDEV 416
Cdd:cd05907 236 -IPVYEGYGLTETSAVVTL---------NPPGDNRIGTVGKPLPGVEVRIADDG--EILVRGPNVMLGYYK-----NPEA 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638423 417 TVPLGTMR---ATGDFVTVK-DGEIFFLGR-KDSQIKRHGKrlNIELvQQVAEELQQ---VESCAV 474
Cdd:cd05907 299 TAEALDADgwlHTGDLGEIDeDGFLHITGRkKDLIITSGGK--NISP-EPIENALKAsplISQAVV 361
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
192-529 |
5.08e-10 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 63.79 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVlfLASPLTFDPS---VVEIFLALSSGASLLIVPTsvkl 268
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDV--ILSSLPFFHSfglTVTLWLPLLEGIKVVYHPD---- 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 269 lPSKLASV--LFSHHRVTVLQATPTLLRRFgsqlIKSTVLSAT--TSLRVLALGGEAFPslTVLRSWRGEGNKTQIFNVY 344
Cdd:PRK08633 858 -PTDALGIakLVAKHRATILLGTPTFLRLY----LRNKKLHPLmfASLRLVVAGAEKLK--PEVADAFEEKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 345 GITEVSSWATIyRIP--EKTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFT---------IQEGSGQVFLGgrnrvcFLD 413
Cdd:PRK08633 931 GATETSPVASV-NLPdvLAADFKRQTGSKEGSVGMPLPGVAVRIVDPETFEelppgedglILIGGPQVMKG------YLG 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 414 D-----EVTVPLGTMR--ATGD--------FVTVKD---------GEIFFLGRkdsqikrhgkrlnielvqqVAEELQQV 469
Cdd:PRK08633 1004 DpektaEVIKDIDGIGwyVTGDkghldedgFLTITDrysrfakigGEMVPLGA-------------------VEEELAKA 1064
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638423 470 -----ESCAVTWYNQEK----LILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 529
Cdd:PRK08633 1065 lggeeVVFAVTAVPDEKkgekLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
16-535 |
6.60e-10 |
|
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: 62.69 E-value: 6.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 16 DRVAVCFDECNnqlpvyYTYKTVVNAASELSNFLLLHCDFQGIREIGLYCQPGIDLPSWILGILQVPAAYVPIEPDSPPS 95
Cdd:cd05941 1 DRIAIVDDGDS------ITYADLVARAARLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 96 lsthfmkkcNLKYILvekkqinkfksfhetllnydtftvehndlvlfrlhwKNTEVNLMLNDgkekyekekiksissehv 175
Cdd:cd05941 75 ---------ELEYVI------------------------------------TDSEPSLVLDP------------------ 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 176 neekaeehmdlrlkhclAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLA-LS 254
Cdd:cd05941 92 -----------------ALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCpLF 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 255 SGAsllivptSVKLLP---SKLASVLFSHHRVTVLQATPTLLRR------FGSQLIKSTVLSATTSLRVLALGGEAFPsL 325
Cdd:cd05941 155 AGA-------SVEFLPkfdPKEVAISRLMPSITVFMGVPTIYTRllqyyeAHFTDPQFARAAAAERLRLMVSGSAALP-V 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 326 TVLRSWRGEGNKTqIFNVYGITEVSswatiyripeKTLNSTLKCE-LPVQLGFPLLGtvVEVR--DTNGFT--------- 393
Cdd:cd05941 227 PTLEEWEAITGHT-LLERYGMTEIG----------MALSNPLDGErRPGTVGMPLPG--VQARivDEETGEplprgevge 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 394 IQEGSGQVFLGGRNRVCFLDDEVTvPLGTMRaTGDFVTVK-DGEIFFLGR-KDSQIKRHGKRLNIELVQQVAEELQQVES 471
Cdd:cd05941 294 IQVRGPSVFKEYWNKPEATKEEFT-DDGWFK-TGDLGVVDeDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSE 371
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 472 CAV------TWynQEKLILFMVSKD--ASVKEYIFKE-LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05941 372 CAVigvpdpDW--GERVVAVVVLRAgaAALSLEELKEwAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
192-535 |
6.87e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 63.05 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtF--DPSVVEIFLALSSGASLLiVPTSVKLL 269
Cdd:PRK07529 215 VAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL-FhvNALLVTGLAPLARGAHVV-LATPQGYR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 270 -PSKLASV--LFSHHRVTVLQATPTLLrrfgSQLIKSTVLSA-TTSLRVlALGGEAFPSLTVLRSWRgEGNKTQIFNVYG 345
Cdd:PRK07529 293 gPGVIANFwkIVERYRINFLSGVPTVY----AALLQVPVDGHdISSLRY-ALCGAAPLPVEVFRRFE-AATGVRIVEGYG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 346 ITEVSSWATI-YRIPEKTLNStlkcelpvqLGFPLLGTVVEV--RDTNGFTIQE------------GSGqVFLG----GR 406
Cdd:PRK07529 367 LTEATCVSSVnPPDGERRIGS---------VGLRLPYQRVRVviLDDAGRYLRDcavdevgvlciaGPN-VFSGyleaAH 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 407 NRVCFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNIElVQQVAEEL---QQVESCAVTW------ 476
Cdd:PRK07529 437 NKGLWLED------GWLN-TGDLGRIdADGYFWLTGRAKDLIIRGGH--NID-PAAIEEALlrhPAVALAAAVGrpdaha 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 477 ------YNQEKlilfmvsKDASVKEyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK07529 507 gelpvaYVQLK-------PGASATE---AELLAFARDHiaeraAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
198-608 |
1.77e-09 |
|
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: 62.00 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 198 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLiVPTSVKL-LPSKLASV 276
Cdd:TIGR03443 423 TSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLL-VPTADDIgTPGRLAEW 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 277 LfSHHRVTVLQATPTLlrrfgSQLikstvLSATTSlrvlalggEAFPSL-------TVL-----RSWRGEGNKTQIFNVY 344
Cdd:TIGR03443 502 M-AKYGATVTHLTPAM-----GQL-----LSAQAT--------TPIPSLhhaffvgDILtkrdcLRLQTLAENVCIVNMY 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 345 GITEVSSWATIYRIPEKTLNST----LKCELP-------VQLgfpL------------LGTVVE--VRD----------- 388
Cdd:TIGR03443 563 GTTETQRAVSYFEIPSRSSDSTflknLKDVMPagkgmknVQL---LvvnrndrtqtcgVGEVGEiyVRAgglaegylglp 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 389 --------TNGFT-----------IQEGSGQVFLGGRNRvcflddevtvplgtMRATGDF-VTVKDGEIFFLGRKDSQIK 448
Cdd:TIGR03443 640 elnaekfvNNWFVdpshwidldkeNNKPEREFWLGPRDR--------------LYRTGDLgRYLPDGNVECCGRADDQVK 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 449 RHGKRL-----------------NIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKDASV-KEYIFKELQKY------ 504
Cdd:TIGR03443 706 IRGFRIelgeidthlsqhplvreNVTLVRRDKDEEPTLVSYIVPQDKSDELEEFKSEVDDEEsSDPVVKGLIKYrklikd 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 505 --------LPSHAVPDELVLIDSLPFTSHGKID--------VSELNKIYLNYINLKSENKLSGKE----DLWEKLqylwk 564
Cdd:TIGR03443 786 ireylkkkLPSYAIPTVIVPLKKLPLNPNGKVDkpalpfpdTAQLAAVAKNRSASAADEEFTETEreirDLWLEL----- 860
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1034638423 565 stlnLPEDLLRV-PDESlFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:TIGR03443 861 ----LPNRPATIsPDDS-FFDLGGHSILATRMIFELRKKLNVELP 900
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
192-474 |
1.86e-09 |
|
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: 61.46 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLF--DITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPtsvkll 269
Cdd:cd05911 148 TAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLygNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 270 psKLASVLF----SHHRVTVLQATPTLLrrfgSQLIKSTVLSATT--SLRVLALGGEAFpSLTVLRSWRGEGNKTQIFNV 343
Cdd:cd05911 222 --KFDSELFldliEKYKITFLYLVPPIA----AALAKSPLLDKYDlsSLRVILSGGAPL-SKELQELLAKRFPNATIKQG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 344 YGITEVSSWATIYRIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTI----QEG-----SGQVFLG--GR---NRV 409
Cdd:cd05911 295 YGMTETGGILTVNPDGDDKPGSV---------GRLLPNVEAKIVDDDGKDSlgpnEPGeicvrGPQVMKGyyNNpeaTKE 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034638423 410 CFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlnielvqQV--AE------ELQQVESCAV 474
Cdd:cd05911 366 TFDED------GWLH-TGDIGYFdEDGYLYIVDRKKELIKYKGF--------QVapAEleavllEHPGVADAAV 424
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
192-554 |
2.51e-09 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 60.84 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLaLSSGASllIVPTSVKLL 269
Cdd:cd17640 90 LATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIwhSYERS-AEYFI-FACGCS--QAYTSIRTL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 270 PSKLASVlfshhRVTVLQATPTLLRRFGSQLIKSTVLSATTS------------LRVLALGGEAFPSlTVLRSWRGEGnk 337
Cdd:cd17640 166 KDDLKRV-----KPHYIVSVPRLWESLYSGIQKQVSKSSPIKqflflfflsggiFKFGISGGGALPP-HVDTFFEAIG-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 338 TQIFNVYGITEVSSWATIYRIPEKTLNStlkcelpvqLGFPLLGTVVEVRD--TNGFTIQEGSGQVFLGGrnrvcfldDE 415
Cdd:cd17640 238 IEVLNGYGLTETSPVVSARRLKCNVRGS---------VGRPLPGTEIKIVDpeGNVVLPPGEKGIVWVRG--------PQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 416 VTV-----PLGTMRA--------TGDFVT-VKDGEIFFLGR-KDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE 480
Cdd:cd17640 301 VMKgyyknPEATSKVldsdgwfnTGDLGWlTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034638423 481 KLILFMVSKdasvkeyiFKELQKYLPSHAVpdelvlidSLPFTSHGKIDVSELNKIYLNYINLKSENKLSGKED 554
Cdd:cd17640 381 RLGALIVPN--------FEELEKWAKESGV--------KLANDRSQLLASKKVLKLYKNEIKDEISNRPGFKSF 438
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
867-1047 |
3.57e-09 |
|
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.
Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 60.04 E-value: 3.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 867 GLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFSSPCLNLIPHHLYFATLGGLLLAVN-----PVWQFSTSGPIFSSPCT 941
Cdd:cd10276 39 DMVYAADANGQVSAFNATTGKIIWETSLSGKGFLGGTPAVGNGKIFVGTESGYLYALDakdgsELWRTEVSDSQLLSPPT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 942 SpSEQKIFFGSHDCFIYCCNMK-GHLQWKFETTS-----RVYATP-----------------------------FAFHNY 986
Cdd:cd10276 119 Y-ADGKIYVGTGDGRLYYCNAEtGKVVWNRTSTApelslRGGAAPvgaydvvfvgdgngtvvalntgtgvdiweFSVSEP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638423 987 NGSNE---------------MLLAAASTDGKVWILESQSGQLQSVYELpGEVFSSPVVLESMLIIGCRDNYVYCLD 1047
Cdd:cd10276 198 RGRTElprmidssvtyvvvgGYLYSTSYQGYLVALDFESGQFLWSRKA-SGGTSTSTDANGRVYVGDGEGSLYCLD 272
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
194-528 |
4.26e-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: 60.36 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 194 YVLHTSGTTGIPKivrvphkCIVPN-----IQH---FRVLFDITQEDVLF------------LASpltfdpsvveiflAL 253
Cdd:cd05943 253 YILYSSGTTGLPK-------CIVHGaggtlLQHlkeHILHCDLRPGDRLFyyttcgwmmwnwLVS-------------GL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 254 SSGASLLIVPTSvKLLPSKLASV-LFSHHRVTVLQATPTL---LRRFGSQLIKSTVLSattSLRVLALGGEAFPSLTVLR 329
Cdd:cd05943 313 AVGATIVLYDGS-PFYPDTNALWdLADEEGITVFGTSAKYldaLEKAGLKPAETHDLS---SLRTILSTGSPLKPESFDY 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 330 SWRGEGNKTQIFNVYGITEVSSwATIYRIPEktlnstlkceLPVQLG---FPLLGTVVEVRDTNGFTIQEGSGQVflggr 406
Cdd:cd05943 389 VYDHIKPDVLLASISGGTDIIS-CFVGGNPL----------LPVYRGeiqCRGLGMAVEAFDEEGKPVWGEKGEL----- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 407 nrVCflddevTVPLGTM-------------RAT-----------GDFVTV-KDGEIFFLGRKDSQIKRHGKRL-NIELVQ 460
Cdd:cd05943 453 --VC------TKPFPSMpvgfwndpdgsryRAAyfakypgvwahGDWIEItPRGGVVILGRSDGTLNPGGVRIgTAEIYR 524
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638423 461 QVaEELQQV-ESCAVTWYNQ---EKLILFMVSK-----DASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05943 525 VV-EKIPEVeDSLVVGQEWKdgdERVILFVKLRegvelDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
735-882 |
4.46e-09 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 59.44 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 735 SCVAKVSEEGKPA---IGTQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILG 811
Cdd:COG1520 9 SGFSSEDDEPPPAplpEFEPSVKVKQLWSASVGDGVGKGYSRLAPAVAGDR--VYAADADGRVAALDAATGKELWRVDLG 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 812 DRIesSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTT--GLIYIGSHDQHAYALD 882
Cdd:COG1520 87 EPL--SGGVGADGGLVVVGTEDGEVIALDADDGEELW----RARLSSEVLAAPAVagGRVVVRTGDGRVYALD 153
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
194-528 |
6.92e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 59.81 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 194 YVLHTSGTTGIPKivrvphkCIVPN-----IQHFRVL---FDITQEDVLF------------LASpltfdpsvveiflAL 253
Cdd:PRK03584 267 WILYSSGTTGLPK-------CIVHGhggilLEHLKELglhCDLGPGDRFFwyttcgwmmwnwLVS-------------GL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 254 SSGASLLIVPTSvkllPSKL-ASVLF---SHHRVTVLQATP---TLLRRFGSQLIKSTVLSAttsLRVLALGG-----EA 321
Cdd:PRK03584 327 LVGATLVLYDGS----PFYPdPNVLWdlaAEEGVTVFGTSAkylDACEKAGLVPGETHDLSA---LRTIGSTGsplppEG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 322 FpsltvlrSW--RGEGNKTQIFNVYGITEVSSwatiyripektlnstlkC------ELPV---QLGFPLLGTVVEVRDTN 390
Cdd:PRK03584 400 F-------DWvyEHVKADVWLASISGGTDICS-----------------CfvggnpLLPVyrgEIQCRGLGMAVEAWDED 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 391 GFTIQEGSGQVflggrnrVCflddevTVPLGTM-------------RAT-----------GDFVTV-KDGEIFFLGRKDS 445
Cdd:PRK03584 456 GRPVVGEVGEL-------VC------TKPFPSMplgfwndpdgsryRDAyfdtfpgvwrhGDWIEItEHGGVVIYGRSDA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 446 QIKRHGKRLNI-ELVQQVaEELQQV-ESCAV--TWYNQ-EKLILFMVSK-----DASVKEYIFKELQKYL-PSHaVPDEL 514
Cdd:PRK03584 523 TLNRGGVRIGTaEIYRQV-EALPEVlDSLVIgqEWPDGdVRMPLFVVLAegvtlDDALRARIRTTIRTNLsPRH-VPDKI 600
|
410
....*....|....
gi 1034638423 515 VLIDSLPFTSHGKI 528
Cdd:PRK03584 601 IAVPDIPRTLSGKK 614
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-443 |
8.18e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 59.53 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 1 MTLQELVHKAASCYMDRVAVCFDEcnnqlpVYYTYKTVVNAASELSNFLLLHcdfqGIReiglycqPG----IDLPS--- 73
Cdd:PRK07656 5 MTLPELLARAARRFGDKEAYVFGD------QRLTYAELNARVRRAAAALAAL----GIG-------KGdrvaIWAPNsph 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 74 WI---LGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVEKKQINKFKSFHETLLNydtftVEHndlvlfrlhwkntE 150
Cdd:PRK07656 68 WViaaLGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSATTRLPA-----LEH-------------V 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 151 VNLMLNDGKEKYEKEKIKS--ISSEHVNEEKAEEHMDLrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDI 228
Cdd:PRK07656 130 VICETEEDDPHTEKMKTFTdfLAAGDPAERAPEVDPDD-----VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 229 TQEDVLFLASPL--TFDPSVVeIFLALSSGASLLIVPtsvKLLPSKLASvLFSHHRVTVLQATPTLLRrfgsQLIKSTVL 306
Cdd:PRK07656 205 TEGDRYLAANPFfhVFGYKAG-VNAPLMRGATILPLP---VFDPDEVFR-LIETERITVLPGPPTMYN----SLLQHPDR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 307 SAT--TSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVSSWATIYRI--PEKTLNSTlkcelpvqLGFPLLGT 382
Cdd:PRK07656 276 SAEdlSSLRLAVTGAASMP-VALLERFESELGVDIVLTGYGLSEASGVTTFNRLddDRKTVAGT--------IGTAIAGV 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 383 VVEVRDTNGFTIQEG-SGQVFLGGRNrVC--FLDDevtvPLGTMRA--------TGDFVTV-KDGEIFFLGRK 443
Cdd:PRK07656 347 ENKIVNELGEEVPVGeVGELLVRGPN-VMkgYYDD----PEATAAAidadgwlhTGDLGRLdEEGYLYIVDRK 414
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
192-528 |
1.04e-08 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 59.30 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFD---ITQEDVLFLASPL--TFDPSVVEIFLALSSGASLLI----- 261
Cdd:PRK08974 208 LAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpllHPGKELVVTALPLyhIFALTVNCLLFIELGGQNLLItnprd 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 262 VPTSVKLLpsklasvlfSHHRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRvLALGGEAFPSLTVLRSWRgEGNKTQ 339
Cdd:PRK08974 288 IPGFVKEL---------KKYPFTAITGVNTLF----NALLNNEEFQELdfSSLK-LSVGGGMAVQQAVAERWV-KLTGQY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 340 IFNVYGITEVSSWATIYRIPEKTLNSTLkcelpvqlGFPLLGTVVEVRDTNGFTIQEGSG--------QVFLGGRNRvcf 411
Cdd:PRK08974 353 LLEGYGLTECSPLVSVNPYDLDYYSGSI--------GLPVPSTEIKLVDDDGNEVPPGEPgelwvkgpQVMLGYWQR--- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 412 ldDEVTVPL---GTMrATGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNI---ELVQQVAEELQQVESCAVTWYNQ---EK 481
Cdd:PRK08974 422 --PEATDEVikdGWL-ATGDIAVMdEEGFLRIVDRKKDMILVSG--FNVypnEIEDVVMLHPKVLEVAAVGVPSEvsgEA 496
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034638423 482 LILFMVSKDASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:PRK08974 497 VKIFVVKKDPSLtEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
198-533 |
6.51e-08 |
|
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: 56.37 E-value: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 198 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLiVPTSVKL-LPSKLASV 276
Cdd:cd17647 117 TSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLL-VPTQDDIgTPGRLAEW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 277 LfSHHRVTVLQATPTLlrrfgSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITEVSSWATIY 356
Cdd:cd17647 196 M-AKYGATVTHLTPAM-----GQLLTAQATTPFPKLHHAFFVGDILTKRDCLR-LQTLAENVRIVNMYGTTETQRAVSYF 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 357 RIPEKTLNST----LKCELPVQLGF---PLLgtVVEVRDTNGFTIQEGSGQVFL--GGR----------NRVCFLDD--- 414
Cdd:cd17647 269 EVPSRSSDPTflknLKDVMPAGRGMlnvQLL--VVNRNDRTQICGIGEVGEIYVraGGLaegyrglpelNKEKFVNNwfv 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 415 ------EVTVPLGT------------MRATGDF-VTVKDGEIFFLGRKDSQIKRHGKRL-----------------NIEL 458
Cdd:cd17647 347 epdhwnYLDKDNNEpwrqfwlgprdrLYRTGDLgRYLPNGDCECCGRADDQVKIRGFRIelgeidthisqhplvreNITL 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 459 VQQVAEElqqvESCAVTWY-----NQEKLILFMVSKDASVK-EYIFKELQKY--------------LPSHAVPDELVLID 518
Cdd:cd17647 427 VRRDKDE----EPTLVSYIvprfdKPDDESFAQEDVPKEVStDPIVKGLIGYrklikdireflkkrLASYAIPSLIVVLD 502
|
410
....*....|....*
gi 1034638423 519 SLPFTSHGKIDVSEL 533
Cdd:cd17647 503 KLPLNPNGKVDKPKL 517
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
195-533 |
1.14e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 55.77 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 195 VLHTSGTTGIPKIV-RVPHkcIVPNIQHFRVLFDITQEDV---LFLASPLTFDPSVVEIFLALSSGASLLivptSVKLLP 270
Cdd:PRK13383 179 VLLTSGTTGKPKGVpRAPQ--LRSAVGVWVTILDRTRLRTgsrISVAMPMFHGLGLGMLMLTIALGGTVL----THRHFD 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAF-PSLTvLRSWRGEGNKtqIFNVYGITEV 349
Cdd:PRK13383 253 AEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLdPTLG-QRFMDTYGDI--LYNGYGSTEV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 350 SswatiyrIPEKTLNSTLKcELPVQLGFPLLGTVVEVRDTNGFTI-QEGSGQVFLGGR-NRVCFLDDEVTVPLGTMRATG 427
Cdd:PRK13383 330 G-------IGALATPADLR-DAPETVGKPVAGCPVRILDRNNRPVgPRVTGRIFVGGElAGTRYTDGGGKAVVDGMTSTG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 428 DFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMVSKD------ASVKEY 496
Cdd:PRK13383 402 DMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErfghRLAAFVVLHPgsgvdaAQLRDY 481
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034638423 497 IFKELQKYlpshAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:PRK13383 482 LKDRVSRF----EQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
192-528 |
1.32e-07 |
|
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: 55.18 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVV-EIFLALSSGASLLIVPTSVKllp 270
Cdd:cd05935 86 LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVgSLNTAVYVGGTYVLMARWDR--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 sKLASVLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSLTVLRSWRgegnKTQIFNV--YGIT 347
Cdd:cd05935 163 -ETALELIEKYKVTFWTNIPTMLVDLLATPeFKTRDLS---SLKVLTGGGAPMPPAVAEKLLK----LTGLRFVegYGLT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 348 EVsswatiyrIPEKTLNSTLKCELPVqLGFPLLGTVVEVRD-TNGFTIQEG-SGQVFLGG------------RNRVCFLD 413
Cdd:cd05935 235 ET--------MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNeVGEIVVRGpqifkgywnrpeETEESFIE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 414 DE-----VTVPLGTMRAtgdfvtvkDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLIL 484
Cdd:cd05935 306 IKgrrffRTGDLGYMDE--------EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISvpdeRVGEEVKA 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034638423 485 FMVSKDA----SVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd05935 378 FIVLRPEyrgkVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
178-535 |
1.42e-07 |
|
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: 55.55 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 178 EKAEEHMDLRLKHCLAYVLH-TSGTTGIPKIVRVPHKCI-VPNIQHFRVLFDITQEDVLFLASPLTFDPSVV-EIFLALS 254
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYfTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 255 SGASLLivptsVKLLPSKLASVL---FSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEAF-PSltVLRS 330
Cdd:cd05928 241 QGACVF-----VHHLPRFDPLVIlktLSSYPITTFCGAPTVYRMLVQQDLSSYKFP---SLQHCVTGGEPLnPE--VLEK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 331 WRgegNKT--QIFNVYGITEVSSWATIYRipektlnsTLKCElPVQLGFPLLGTVVEVRDTNGFTI---QEGSGQVFLGG 405
Cdd:cd05928 311 WK---AQTglDIYEGYGQTETGLICANFK--------GMKIK-PGSMGKASPPYDVQIIDDNGNVLppgTEGDIGIRVKP 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 406 RNRVCFLDDEVTVPLGTMRAT-GDF-------VTVKDGEIFFLGRKDSQIKRHGKRLN-IELVQQVAEELQQVESCAVTW 476
Cdd:cd05928 379 IRPFGLFSGYVDNPEKTAATIrGDFyltgdrgIMDEDGYFWFMGRADDVINSSGYRIGpFEVESALIEHPAVVESAVVSS 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034638423 477 YNQ---EKLILFMV------SKDasvKEYIFKELQKYLPS----HAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:cd05928 459 PDPirgEVVKAFVVlapqflSHD---PEQLTKELQQHVKSvtapYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
192-537 |
1.44e-07 |
|
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: 55.37 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFL-ALSSGASLLIVPTSVKLLP 270
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLrAVYLGCQQVHVPTEEILAD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASVLFSHHRVTVLQAtP----TLLRRFGSQLIKSTV-LSattSLRVLALGGEAFPSLTV---LRSWRGEGNKTQIFN 342
Cdd:cd05906 249 PLRWLDLIDRYRVTITWA-PnfafALLNDLLEEIEDGTWdLS---SLRYLVNAGEAVVAKTIrrlLRLLEPYGLPPDAIR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 343 -VYGITEVSSWATIYRIPEkTLNSTLKCELpVQLGFPLLGTVVEVRDTNGFTIQEG-------SGQVFLGG------RNR 408
Cdd:cd05906 325 pAFGMTETCSGVIYSRSFP-TYDHSQALEF-VSLGRPIPGVSMRIVDDEGQLLPEGevgrlqvRGPVVTKGyynnpeANA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 409 VCFLDDevtvplGTMRaTGDFVTVKDGEIFFLGRKDSQIKRHG-KRLNIELvQQVAEELQQVES-----CAVTWYNQ--E 480
Cdd:cd05906 403 EAFTED------GWFR-TGDLGFLDNGNLTITGRTKDTIIVNGvNYYSHEI-EAAVEEVPGVEPsftaaFAVRDPGAetE 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638423 481 KLILFMVSkdASVKEYIFKELQKYLPSHAV------PDELVLI--DSLPFTSHGKIDVSELNKIY 537
Cdd:cd05906 475 ELAIFFVP--EYDLQDALSETLRAIRSVVSrevgvsPAYLIPLpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
197-540 |
1.53e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 55.14 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 197 HTSGTTGIPKIVRVPHKcivPNIQHFRVlfdITQEDVLFLASPLTFDPsVVEIFLALSSGASLLIVPTSVKL-LP-SKL- 273
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHR---SNVLHALM---ANNGDALGTSAADTMLP-VVPLFHANSWGIAFSAPSMGTKLvMPgAKLd 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 274 -ASV--LFSHHRVTVLQATPT----LLrrfgsQLIKSTVLSATTsLRVLALGGEAFPSlTVLRSWRGEGnkTQIFNVYGI 346
Cdd:PRK06018 257 gASVyeLLDTEKVTFTAGVPTvwlmLL-----QYMEKEGLKLPH-LKMVVCGGSAMPR-SMIKAFEDMG--VEVRHAWGM 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 347 TEVSSWATIYRIPEKTLNSTLKCELPVQL--GFPLLGTVVEVRDTNGFTIQEgSGQVFlgGRNRVC-------------- 410
Cdd:PRK06018 328 TEMSPLGTLAALKPPFSKLPGDARLDVLQkqGYPPFGVEMKITDDAGKELPW-DGKTF--GRLKVRgpavaaayyrvdge 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 411 FLDDEvtvplgTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLN-IELvQQVAEELQQVESCAVT------WYNQEKL 482
Cdd:PRK06018 405 ILDDD------GFFDTGDVATIdAYGYMRITDRSKDVIKSGGEWISsIDL-ENLAVGHPKVAEAAVIgvyhpkWDERPLL 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638423 483 ILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNY 540
Cdd:PRK06018 478 IVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKDY 535
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
198-474 |
1.76e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 55.19 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 198 TSGTTGIPKIVRVPHKCIVpnIQHFRVLFDI--TQEDVLFLASPLtfdpsvVEIFlALSSGASLLIVPTSVKLLP---SK 272
Cdd:PLN02860 180 TSGTTGRPKGVTISHSALI--VQSLAKIAIVgyGEDDVYLHTAPL------CHIG-GLSSALAMLMVGACHVLLPkfdAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 273 LASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLtVLRSWRGEGNKTQIFNVYGITEVSSW 352
Cdd:PLN02860 251 AALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSR-LLPDAKKLFPNAKLFSAYGMTEACSS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 353 ATIYRIPEKTLNS----TLKCELPVQLGFPLLGTV--------VEVRDtnGFTIQEGSGQVFLGGRNRVCFLDDEVTVPL 420
Cdd:PLN02860 330 LTFMTLHDPTLESpkqtLQTVNQTKSSSVHQPQGVcvgkpaphVELKI--GLDESSRVGRILTRGPHVMLGYWGQNSETA 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 421 GTMRA-----TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV 474
Cdd:PLN02860 408 SVLSNdgwldTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
198-366 |
5.63e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 53.05 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 198 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDpSVVEIFLALSSGASLLIVPTSVKLLPSkLAS 275
Cdd:cd05917 10 TSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPSFDPLAV-LEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 276 VlfSHHRVTVLQATPTL-LRRFGSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRGEGNKTQIFNVYGITEVSSWAT 354
Cdd:cd05917 88 I--EKEKCTALHGVPTMfIAELEHPDFDKFDLS---SLRTGIMAGAPCPP-ELMKRVIEVMNMKDVTIAYGMTETSPVST 161
|
170
....*....|....*
gi 1034638423 355 IYRI---PEKTLNST 366
Cdd:cd05917 162 QTRTddsIEKRVNTV 176
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
192-444 |
5.84e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 53.43 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVlFLAspltfdpsVVEIF----------LALSSGASLLI 261
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESV-VLA--------VLPLFhvtgmvhsmnAPIYAGATVVL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 262 VPTSVKllpsKLASVLFSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLALGGEAFPS--------LTVLRSWR 332
Cdd:PRK08314 263 MPRWDR----EAAARLIERYRVTHWTNIPTMVVDFlASPGLAERDLS---SLRYIGGGGAAMPEavaerlkeLTGLDYVE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 333 GegnktqifnvYGITEVSSwATIYRIPEKTlnsTLKCelpvqLGFPLLGTVVEVRDTNgfTIQE-GSG----------QV 401
Cdd:PRK08314 336 G----------YGLTETMA-QTHSNPPDRP---KLQC-----LGIPTFGVDARVIDPE--TLEElPPGevgeivvhgpQV 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034638423 402 FLGGRNRvcflddevtvPLGTMRAtgdFVTVkDGEIFF----LGRKD 444
Cdd:PRK08314 395 FKGYWNR----------PEATAEA---FIEI-DGKRFFrtgdLGRMD 427
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
193-533 |
6.28e-07 |
|
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: 53.28 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPniqhfRVLFDITQEDVLFLAS-------PLTFDPSVVEIFLALSSGASLLIVPTS 265
Cdd:cd05923 153 AFVFYTSGTTGLPKGAVIPQRAAES-----RVLFMSTQAGLRHGRHnvvlglmPLYHVIGFFAVLVAALALDGTYVVVEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 266 VKllpSKLASVLFSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVY 344
Cdd:cd05923 228 FD---PADALKLIEQERVTSLFATPTHLDALaAAAEFAGLKLS---SLRHVTFAGATMPD-AVLERVN-QHLPGEKVNIY 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 345 GITEVSSwATIYRIPekTLNSTLKCELPVQLGF-PLLGTVVE---VRDTNGFTIQEGSGQVFLGGRNRvcFLDDEVTVPL 420
Cdd:cd05923 300 GTTEAMN-SLYMRDA--RTGTEMRPGFFSEVRIvRIGGSPDEalaNGEEGELIVAAAADAAFTGYLNQ--PEATAKKLQD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 421 GTMRaTGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVKE 495
Cdd:cd05923 375 GWYR-TGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwgqsVTACVVPREGTLSA 453
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1034638423 496 yifKELQKY-----LPSHAVPDELVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05923 454 ---DELDQFcraseLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
193-473 |
1.19e-06 |
|
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: 52.46 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvveifLALSSgasllIVPtsvKLLP 270
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLfaLFGPA-----LGLTS-----VIP---DMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASV----LFS---HHRVTVLQATPTLLR---RFGSQLIKStvlsaTTSLRVLALGGEAFPSLTVLRSWRGEGNKTQI 340
Cdd:cd05910 155 TRPARAdpqkLVGairQYGVSIVFGSPALLErvaRYCAQHGIT-----LPSLRRVLSAGAPVPIALAARLRKMLSDEAEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 341 FNVYGITE---VSSwatiyrIPEKTLNSTlKCELPVQ-----LGFPLLGTVVEVRDTNGFTIQE--GSGQVFLGGRNRVC 410
Cdd:cd05910 230 LTPYGATEalpVSS------IGSRELLAT-TTAATSGgagtcVGRPIPGVRVRIIEIDDEPIAEwdDTLELPRGEIGEIT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 411 FLDDEVTV-----PLGTMRA------------TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESC 472
Cdd:cd05910 303 VTGPTVTPtyvnrPVATALAkiddnsegfwhrMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRS 382
|
.
gi 1034638423 473 A 473
Cdd:cd05910 383 A 383
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
191-537 |
1.32e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 52.24 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 191 CLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtFDPSVVEIFL--ALSSGASLLIV--PTSV 266
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPL-YHCAQLDVFLgpYLYVGATNVILdaPDPE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 267 KLLPsklasvLFSHHRVTVLQATPT----LLRrfgSQLIKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFN 342
Cdd:PRK08316 251 LILR------TIEAERITSFFAPPTvwisLLR---HPDFDTRDLS---SLRKGYYGASIMP-VEVLKELRERLPGLRFYN 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 343 VYGITEVSSWATIYRiPEKTLnstlkcELPVQLGFPLLGtvVEVR--DTNGFTIQEG--------SGQVFLGgrnrvcFL 412
Cdd:PRK08316 318 CYGQTEIAPLATVLG-PEEHL------RRPGSAGRPVLN--VETRvvDDDGNDVAPGevgeivhrSPQLMLG------YW 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 413 DD-EVTVP-----------LGTMRATGdFVTVKDgeifflgRKDSQIKRHGkrlniELV--QQVAEELQQ---VESCAVT 475
Cdd:PRK08316 383 DDpEKTAEafrggwfhsgdLGVMDEEG-YITVVD-------RKKDMIKTGG-----ENVasREVEEALYThpaVAEVAVI 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034638423 476 WYNQEKLI----LFMVSKD-ASVKEyifKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKIY 537
Cdd:PRK08316 450 GLPDPKWIeavtAVVVPKAgATVTE---DELIAHcrarLAGFKVPKRVIFVDELPRNPSGKILKRELRERY 517
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
294-535 |
1.52e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 51.58 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 294 RRFGS----QLIKS-TVLSATTSLRVLA---LGGEAFPSlTVLRSWRGEGnkTQIFNVYGITEVSSwatiyripektlns 365
Cdd:PRK07824 127 RRYTSlvpmQLAKAlDDPAATAALAELDavlVGGGPAPA-PVLDAAAAAG--INVVRTYGMSETSG-------------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 366 tlKCelpVQLGFPLLGTVVEVRDtngftiqegsGQVFLGG-------RNRVcflDDEVTVPLGTMRaTGDFVTVKDGEIF 438
Cdd:PRK07824 190 --GC---VYDGVPLDGVRVRVED----------GRIALGGptlakgyRNPV---DPDPFAEPGWFR-TDDLGALDDGVLT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 439 FLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL---ILFMVSKDASVKEYIfKELQKY----LPSHAVP 511
Cdd:PRK07824 251 VLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLgqrVVAAVVGDGGPAPTL-EALRAHvartLDRTAAP 329
|
250 260
....*....|....*....|....
gi 1034638423 512 DELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK07824 330 RELHVVDELPRRGIGKVDRRALVR 353
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
793-1012 |
3.49e-06 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 49.32 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 793 RMKAVDFYSGKVKWEQILGDRIESSACVSkcGNFIVVGCYNGLVYVLKSNSGEKYWMFTTEDAVKSSATMDptTGLIYIG 872
Cdd:pfam13360 4 VVTALDAATGAELWRVDLETGLGGGVAVD--GGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVA--GGRVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 873 SHDQHAYALDIYRKKCVW---KSKCGGTVFSSPCLNLIPHHLYFATLGGLLLAVNP-----VWQFSTSGP---------- 934
Cdd:pfam13360 80 AGDGSLIALDAADGRRLWsyqRSGEPLALRSSGSPAVVGDTVVAGFSSGKLVALDPatgkvRWEAPLAAPrgtnelerlv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 935 -IFSSPctSPSEQKIFFGSHDCFIYCCNMkghlqwkfETTSRVYATPFAfhnynGSNEMLLAA-----ASTDGKVWILES 1008
Cdd:pfam13360 160 dITGTP--VVAGGRVFASAYQGRLVAFDA--------ATGRRLWTREIS-----GPNGPILDGdllyvVSDDGELYALDR 224
|
....
gi 1034638423 1009 QSGQ 1012
Cdd:pfam13360 225 ATGA 228
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
310-536 |
4.78e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 50.59 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 310 TSLRVLALGGEAFPSLTVLRsWRGEGNKTqIFNVYGITEVSSWATIYRIPEKTLNSTLkcelpvqlGFPLLGTVVEVRDT 389
Cdd:PRK12492 333 SALKLTNSGGTALVKATAER-WEQLTGCT-IVEGYGLTETSPVASTNPYGELARLGTV--------GIPVPGTALKVIDD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 390 NGFtiqegsgQVFLGGRNRVCFLDDEV-----TVPLGTMRA--------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLN 455
Cdd:PRK12492 403 DGN-------ELPLGERGELCIKGPQVmkgywQQPEATAEAldaegwfkTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVY 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 456 IELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVKeyiFKELQKY----LPSHAVPDELVLIDSLPFTSHGK 527
Cdd:PRK12492 476 PNEIEDVVMAHPKVANCAAIGVPDERsgeaVKLFVVARDPGLS---VEELKAYckenFTGYKVPKHIVLRDSLPMTPVGK 552
|
....*....
gi 1034638423 528 IDVSELNKI 536
Cdd:PRK12492 553 ILRRELRDI 561
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
191-533 |
8.99e-06 |
|
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: 49.80 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 191 CLAYVlhTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDItQEDVLFLASPLTFDPSVV--EIFLALSSGASLLIVPTSvKL 268
Cdd:cd05970 188 LLVYF--SSGTTGMPKMVEHDFTYPLGHIVTAKYWQNV-REGGLHLTVADTGWGKAVwgKIYGQWIAGAAVFVYDYD-KF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 269 LPSKLASVLfSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEAFpSLTVLRSWRgEGNKTQIFNVYGITE 348
Cdd:cd05970 264 DPKALLEKL-SKYGVTTFCAPPTIYRFLIREDLSRYDLS---SLRYCTTAGEAL-NPEVFNTFK-EKTGIKLMEGFGQTE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 -VSSWATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVflggrnrVCFLDDEVtvPLGTMRA- 425
Cdd:cd05970 338 tTLTIATFPWMEPK----------PGSMGKPAPGYEIDLIDREGRSCEAGeEGEI-------VIRTSKGK--PVGLFGGy 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 426 -----------------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LI 483
Cdd:cd05970 399 ykdaektaevwhdgyyhTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIrgqvVK 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1034638423 484 LFMV-SKDASVKEYIFKELQKYLPSHAVPDE----LVLIDSLPFTSHGKIDVSEL 533
Cdd:cd05970 479 ATIVlAKGYEPSEELKKELQDHVKKVTAPYKypriVEFVDELPKTISGKIRRVEI 533
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
195-528 |
1.01e-05 |
|
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: 49.04 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 195 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLALSSGASllIVPTSVKLLPSK 272
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhTFGYK-AGIVACLLTGAT--VVPVAVFDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 273 LASVlfSHHRVTVLQATPTLlrrFGSQL----IKSTVLSattSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITE 348
Cdd:cd17638 82 LEAI--ERERITVLPGPPTL---FQSLLdhpgRKKFDLS---SLRAAVTGAATVPVELVRR-MRSELGFETVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 349 VSSwATIYRI--PEKTLNSTlkcelpvqLGFPLLGTVVEVRDtngftiqegSGQVFLGGRN-RVCFLDDevtvPLGTMRA 425
Cdd:cd17638 153 AGV-ATMCRPgdDAETVATT--------CGRACPGFEVRIAD---------DGEVLVRGYNvMQGYLDD----PEATAEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 426 --------TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDAS 492
Cdd:cd17638 211 idadgwlhTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgevgKAFVVARPGV 290
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034638423 493 --VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 528
Cdd:cd17638 291 tlTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
757-892 |
1.32e-05 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 47.78 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 757 VRWRSDTGkcvdASPLVVIPTFDKS--STTVYIGSHSHRMKAVDFYSGKVKWEQIL-----GDRIE-----SSACVSKCG 824
Cdd:pfam13360 95 RLWSYQRS----GEPLALRSSGSPAvvGDTVVAGFSSGKLVALDPATGKVRWEAPLaaprgTNELErlvdiTGTPVVAGG 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638423 825 NFIVVGcYNGLVYVLKSNSGEKYWmfttEDAVKSSATMDPTTGLIYIGSHDQHAYALDIYRKKCVWKS 892
Cdd:pfam13360 171 RVFASA-YQGRLVAFDAATGRRLW----TREISGPNGPILDGDLLYVVSDDGELYALDRATGAVVWKT 233
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
72-290 |
1.58e-05 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 48.94 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 72 PSWI---LGILQVPAAYVPIEPDSPPSLSTHFMKKCNLKYILVE-KKQINKFKSFHETLLnydtfTVEHndLVLFrlhwk 147
Cdd:COG1022 76 PEWViadLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDELP-----SLRH--IVVL----- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 148 ntevnlmlnDGKEKYEKEKIKSIS------SEHVNEEKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQH 221
Cdd:COG1022 144 ---------DPRGLRDDPRLLSLDellalgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARA 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034638423 222 FRVLFDITQEDV--LFLasPL--TFDpSVVEIFlALSSGASlLIVPTSVKLLPSKLASVlfshhRVTVLQATP 290
Cdd:COG1022 215 LLERLPLGPGDRtlSFL--PLahVFE-RTVSYY-ALAAGAT-VAFAESPDTLAEDLREV-----KPTFMLAVP 277
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
407-529 |
3.49e-05 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 47.83 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 407 NRVCFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNielvqqvAEELQ-------QVESCAVTWYN 478
Cdd:COG1021 401 NARAFTPD------GFYR-TGDLVRRtPDGYLVVEGRAKDQINRGGEKIA-------AEEVEnlllahpAVHDAAVVAMP 466
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 479 Q----EKLILFMVSKDASVKeyiFKELQKYL-----PSHAVPDELVLIDSLPFTSHGKID 529
Cdd:COG1021 467 DeylgERSCAFVVPRGEPLT---LAELRRFLrerglAAFKLPDRLEFVDALPLTAVGKID 523
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
911-1037 |
3.67e-05 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 47.12 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 911 LYFATLGGLLLAVNP-----VWQFSTSGPIfSSPCTSpSEQKIFFGSHDCFIYCCNMK-GHLQWKFETTSRVYATPFAfh 984
Cdd:COG1520 60 VYAADADGRVAALDAatgkeLWRVDLGEPL-SGGVGA-DGGLVVVGTEDGEVIALDADdGEELWRARLSSEVLAAPAV-- 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638423 985 nyngSNEMLLAAaSTDGKVWILESQSGQLQSVYELPGEVF-----SSPVVLESMLIIG 1037
Cdd:COG1520 136 ----AGGRVVVR-TGDGRVYALDAATGERLWSYQRPVPALtlrgtSSPVIVGGAVLVG 188
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
552-608 |
5.21e-05 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 42.53 E-value: 5.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638423 552 KEDLWEKLQYLWKSTLNLPEDLLRvPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:COG0236 3 REELEERLAEIIAEVLGVDPEEIT-PDDSFFEDLGLDSLDAVELIAALEEEFGIELP 58
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
192-447 |
9.16e-05 |
|
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: 46.28 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFdPSVVEIFLALSSGAS--LLIVPTSVK 267
Cdd:cd05914 91 VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLhhIY-PLTFTLLLPLLNGAHvvFLDKIPSAK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 268 LLPSKLASV----------LFSHHRVTVLQ------------ATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPsL 325
Cdd:cd05914 170 IIALAFAQVtptlgvpvplVIEKIFKMDIIpkltlkkfkfklAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKIN-P 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 326 TVLRSWRGEGNKTQIfnVYGITEVSSWATiYRIPEKT-LNSTlkcelpvqlGFPLLGTVVEVRDTNGFTiqeGSGQVFLG 404
Cdd:cd05914 249 DVEEFLRTIGFPYTI--GYGMTETAPIIS-YSPPNRIrLGSA---------GKVIDGVEVRIDSPDPAT---GEGEIIVR 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034638423 405 GRN--RVCFLDDEVTV----PLGTMRaTGDFVT-VKDGEIFFLGRKDSQI 447
Cdd:cd05914 314 GPNvmKGYYKNPEATAeafdKDGWFH-TGDLGKiDAEGYLYIRGRKKEMI 362
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
193-355 |
1.33e-04 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.96 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVL--FLASPLTFDPSVVEIFLALssgASLLIVPTSVKLLP 270
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMmsFLPPFHAYGFNSCTLFPLL---SGVPVVFAYNPLYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASVLFSHHrVTVLQATPTllrrFGSQLIKSTVLSATT--SLRVLALGGEAFPSltvlrSWRGEGNKT----QIFNVY 344
Cdd:PRK06334 263 KKIVEMIDEAK-VTFLGSTPV----FFDYILKTAKKQESClpSLRFVVIGGDAFKD-----SLYQEALKTfphiQLRQGY 332
|
170
....*....|.
gi 1034638423 345 GITEVSSWATI 355
Cdd:PRK06334 333 GTTECSPVITI 343
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
193-536 |
2.14e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 45.47 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLALSSGAsllivptSVKLLP 270
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLT-VGLFTPLLTGA-------EVFLYP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLasvlfsHHRV----------TVLQATPTLL---RRFGSQLikstvlsATTSLRVLALGGEAFpSLTVLRSWRgEGNK 337
Cdd:PRK08043 440 SPL------HYRIvpelvydrncTVLFGTSTFLgnyARFANPY-------DFARLRYVVAGAEKL-QESTKQLWQ-DKFG 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 338 TQIFNVYGITEVSSWATIyRIPEKTLNSTLKCELPvqlgfpllgtVVEVRDTNGFTIQEGsGQVFLGGRN------RVcF 411
Cdd:PRK08043 505 LRILEGYGVTECAPVVSI-NVPMAAKPGTVGRILP----------GMDARLLSVPGIEQG-GRLQLKGPNimngylRV-E 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 412 LDDEVTVP-----LGTMRA----TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ-- 479
Cdd:PRK08043 572 KPGVLEVPtaenaRGEMERgwydTGDIVRFDEqGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDas 651
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034638423 480 --EKLILFmvSKDASVKEyifKELQKY-----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKI 536
Cdd:PRK08043 652 kgEALVLF--TTDSELTR---EKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
193-535 |
2.21e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.16 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVL--FDITQEDVLFLASPLTFDPSVVEIFLALSSGASLliVPTSVKLLP 270
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPL--VFPGPDLSA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 271 SKLASVL-FSHHRVTvlQATPTLLRRFGSQLIKSTvlSATTSLRVLALGGEAFPSLtVLRSWRgEGNKTQIFNVYGITEV 349
Cdd:PRK05620 262 PTLAKIIaTAMPRVA--HGVPTLWIQLMVHYLKNP--PERMSLQEIYVGGSAVPPI-LIKAWE-ERYGVDVVHVWGMTET 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 350 SSWATIYRIPEKTLNSTL------KCELPVQLGFPLL--GTVVEVRDTNGFTIQ----------------EGSGQVFLGG 405
Cdd:PRK05620 336 SPVGTVARPPSGVSGEARwayrvsQGRFPASLEYRIVndGQVMESTDRNEGEIQvrgnwvtasyyhspteEGGGAASTFR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 406 RNRVCFLDDEVTVPlGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK--- 481
Cdd:PRK05620 416 GEDVEDANDRFTAD-GWLR-TGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwge 493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 482 --LILFMVSKD----ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 535
Cdd:PRK05620 494 rpLAVTVLAPGieptRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PQQ_DH_like |
cd00216 |
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
763-900 |
2.38e-04 |
|
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.
Pssm-ID: 199833 [Multi-domain] Cd Length: 434 Bit Score: 44.91 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 763 TGKCVDASPLVVIpTFDKSSTTVYIGSHShRMKAVDFYSGKVKWEQILGDRIESSAcVSKCGNFIVVGCYNGLVYVLKSN 842
Cdd:cd00216 296 NGELVSARPLVPD-SYDPDRELFYVPANG-RIMALDPVTGVVVWEKSELHPLLGGP-LSTAGNLVFVGTSDGYLKAYNAD 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034638423 843 SGEKYWMFTTEDAVKS---SATMDPTTGL-IYIGSHDqhAYALDIYRKKCVWKSKCGGTVFS 900
Cdd:cd00216 373 TGEKLWQQKVPSGFQAepvTYEVDGEQYVlIQAGGGG--AFPLWGGMADLTRGTQMGGTVVV 432
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
557-608 |
2.53e-04 |
|
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: 40.24 E-value: 2.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1034638423 557 EKLQYLWKSTLNLPEDLLrVPDESLFlNSGGDSLKSIRLLSEIEKLVGTSVP 608
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEI-DPDTDLF-DLGLDSLLAVELIARLEEEFGVEIP 50
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
195-350 |
3.96e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 44.38 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 195 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDpSVVEIFLALSSGASLLIVPTSVKLLPSk 272
Cdd:PRK12583 206 IQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCFG-MVLANLGCMTVGACLVYPNEAFDPLAT- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 273 LASVlfSHHRVTVLQATPTLlrrFGSQL----IKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITE 348
Cdd:PRK12583 284 LQAV--EEERCTALYGVPTM---FIAELdhpqRGNFDLS---SLRTGIMAGAPCP-IEVMRRVMDEMHMAEVQIAYGMTE 354
|
..
gi 1034638423 349 VS 350
Cdd:PRK12583 355 TS 356
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
889-1052 |
4.71e-04 |
|
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274511 [Multi-domain] Cd Length: 377 Bit Score: 43.77 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 889 VWKSKCGGTVFSSPcLNLIPHH----LYFATLGGLLLAVNP-----VWQFSTSGPIFSSPcTSpSEQKIFFGSHDCFIYC 959
Cdd:TIGR03300 43 VWSASVGDGVGHYY-LRLQPAVaggkVYAADADGTVAALDAetgkrLWRVDLDERLSGGV-GA-DGGLVFVGTEKGEVIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 960 CNMK-GHLQWKFETTSRVYATPFAfhnYNGsnemLLAAASTDGKVWILESQSGQLQSVYELPGEVF-----SSPVVLESM 1033
Cdd:TIGR03300 120 LDAEdGKELWRAKLSSEVLSPPLV---ANG----LVVVRTNDGRLTALDAATGERLWTYSRVTPPLtlrgsASPVIADGG 192
|
170
....*....|....*....
gi 1034638423 1034 LIIGCRDNYVYCLDLLGGN 1052
Cdd:TIGR03300 193 VLVGFAGGKLVALDLQTGQ 211
|
|
| PQQ_DH_like |
cd00216 |
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
832-941 |
5.18e-04 |
|
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.
Pssm-ID: 199833 [Multi-domain] Cd Length: 434 Bit Score: 43.75 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 832 YNGLVYVLKSNSGEKYWMFT-TEDAVkssatmDPTTGLIYIGSHDQhAYALDIYRKKCVWKSKCGGTVFSSPCL---NLi 907
Cdd:cd00216 285 KNGNFYVLDRRNGELVSARPlVPDSY------DPDRELFYVPANGR-IMALDPVTGVVVWEKSELHPLLGGPLStagNL- 356
|
90 100 110
....*....|....*....|....*....|....*....
gi 1034638423 908 phhLYFATLGGLLLAVNP-----VWQFSTSGPIFSSPCT 941
Cdd:cd00216 357 ---VFVGTSDGYLKAYNAdtgekLWQQKVPSGFQAEPVT 392
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
192-355 |
6.84e-04 |
|
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: 43.36 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHF----RVLFDITQEDVLFLASPLT--FDPSVVEIFLA------LSSGASL 259
Cdd:cd05927 116 LATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNKINPTDVYISYLPLAhiFERVVEALFLYhgakigFYSGDIR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 260 LIVPTSVKLLPSKLASV--LFS--HHRV-TVLQATPTLLRR---FGSQL----IKSTVLSATTSLRVL-------ALGGE 320
Cdd:cd05927 196 LLLDDIKALKPTVFPGVprVLNriYDKIfNKVQAKGPLKRKlfnFALNYklaeLRSGVVRASPFWDKLvfnkikqALGGN 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1034638423 321 -------AFPS----LTVLRSWRGegnkTQIFNVYGITEVSSWATI 355
Cdd:cd05927 276 vrlmltgSAPLspevLEFLRVALG----CPVLEGYGQTECTAGATL 317
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
192-349 |
8.73e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 43.35 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvveifLALSSgasllIVPtsvKLL 269
Cdd:PRK09274 176 MAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLfaLFGPA-----LGMTS-----VIP---DMD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 270 PSKLASV----LFS---HHRVTVLQATPTLLRRFGsQLIKSTVLSATTSLRVLALGGEAFPSLTV-LRSWRGEGnkTQIF 341
Cdd:PRK09274 243 PTRPATVdpakLFAaieRYGVTNLFGSPALLERLG-RYGEANGIKLPSLRRVISAGAPVPIAVIErFRAMLPPD--AEIL 319
|
....*...
gi 1034638423 342 NVYGITEV 349
Cdd:PRK09274 320 TPYGATEA 327
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
785-883 |
9.04e-04 |
|
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is a non-essential component of the beta-barrel assembly machinery (Bam), a multi-subunit complex that inserts proteins with beta-barrel topology into the outer membrane. BamB has been found to interact with BamA, which in turn binds and stabilizes pre-folded beta-barrel proteins; it has been suggested that BamB participates in the stabilization.
Pssm-ID: 199834 [Multi-domain] Cd Length: 358 Bit Score: 42.70 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 785 VYIGSHSHRMKAVDFYSGKVKWEQ-ILGDRIESSACVSKcGNFIVVGCYN-GLVYVLKSNSGeKYWMFT-TEDAVKSSAT 861
Cdd:cd10276 259 VYVGDGEGSLYCLDASTGDELWSQtVLLGRVLSSPAIYV-GVYIYVTDNAeGYLYCLKDNDG-LTVARVeVDYSQYILQG 336
|
90 100
....*....|....*....|..
gi 1034638423 862 MDPTTGLIYIGSHDQHAYALDI 883
Cdd:cd10276 337 PAVSDGWLYYGTDDGYLYALTR 358
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
193-350 |
1.05e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 42.84 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPN-IQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVkLLPS 271
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGA-FDPG 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638423 272 KLASVLfSHHRVTVLQATPTllrRFGSQLIKSTVLSATTSLRVLALGGeAFPSLTVLRSWRGEGNKTQIFNVYGITEVS 350
Cdd:PRK07786 256 QLLDVL-EAEKVTGIFLVPA---QWQAVCAEQQARPRDLALRVLSWGA-APASDTLLRQMAATFPEAQILAAFGQTEMS 329
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
964-1054 |
1.14e-03 |
|
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441129 [Multi-domain] Cd Length: 370 Bit Score: 42.49 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 964 GHLQWKFETTSRVYATPfafhnynGSNEMLLAAASTDGKVWILESQSGQLQSVYELPGEVFSSPVVLESMLIIGCRDNYV 1043
Cdd:COG1520 77 GKELWRVDLGEPLSGGV-------GADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAPAVAGGRVVVRTGDGRV 149
|
90
....*....|.
gi 1034638423 1044 YCLDLLGGNQK 1054
Cdd:COG1520 150 YALDAATGERL 160
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
833-1053 |
1.54e-03 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 41.23 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 833 NGLVYVLKSNSGEKYWMFTTEDAVKSSATMDptTGLIYIGSHDQHAYALDIYRKKCVWKSKCGGTVFSSPCLNLIphHLY 912
Cdd:pfam13360 2 DGVVTALDAATGAELWRVDLETGLGGGVAVD--GGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVAGG--RVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 913 FATLGGLLLAVN-----PVWQFSTSGP---IFSSPCTSPSEQKIFFGSHDCFIYCCNMK-GHLQWKFETTS--------- 974
Cdd:pfam13360 78 VVAGDGSLIALDaadgrRLWSYQRSGEplaLRSSGSPAVVGDTVVAGFSSGKLVALDPAtGKVRWEAPLAAprgtneler 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 975 --RVYATPFAFHNY----NGSNEMLLAAASTDGKVWILESQSgqlqsvyelpgevFSSPVVLESMLIIGCRDNYVYCLDL 1048
Cdd:pfam13360 158 lvDITGTPVVAGGRvfasAYQGRLVAFDAATGRRLWTREISG-------------PNGPILDGDLLYVVSDDGELYALDR 224
|
....*
gi 1034638423 1049 LGGNQ 1053
Cdd:pfam13360 225 ATGAV 229
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
198-474 |
1.60e-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: 42.17 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 198 TSGTTGIPKIVRVPHKCiVPnIQHFRVLFDITQE--DV-LFLASPLTFDPSVVEIFLALSSGASLLIVpTSVKLLPSKLA 274
Cdd:cd05974 93 TSGTTSKPKLVEHTHRS-YP-VGHLSTMYWIGLKpgDVhWNISSPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 275 SVLfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGGEAF-PSL--TVLRSWrgegNKTqIFNVYGITEVSS 351
Cdd:cd05974 170 AAL-VRYGVTTLCAPPTVWR----MLIQQDLASFDVKLREVVGAGEPLnPEVieQVRRAW----GLT-IRDGYGQTETTA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 352 WATiyripektlNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFLGGRNRVCFL-----DDEVT--VPLGTMR 424
Cdd:cd05974 240 LVG---------NSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVALDLGDTRPVGLMkgyagDPDKTahAMRGGYY 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1034638423 425 ATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV 474
Cdd:cd05974 311 RTGDIAMRdEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
198-294 |
2.07e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 41.89 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 198 TSGTTGIPKIVRVPHKCIVpNIQHFRVLFDITQEDVLFLASPLTFDP-SVVEIFLALSSGASLlivptsvkLLPSKLASV 276
Cdd:cd05938 152 TSGTTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSgFLLGIGGCIELGATC--------VLKPKFSAS 222
|
90 100
....*....|....*....|..
gi 1034638423 277 LF----SHHRVTVLQATPTLLR 294
Cdd:cd05938 223 QFwddcRKHNVTVIQYIGELLR 244
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
196-264 |
4.06e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 41.17 E-value: 4.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638423 196 LHTSGTTGIPKIVRVPhkcivpniqHFRVL---------FDITQEDVLFLASPLTFDPSVVEIF-LALSSGASLLIVPT 264
Cdd:PRK13388 156 IFTSGTTGAPKAVRCS---------HGRLAfagralterFGLTRDDVCYVSMPLFHSNAVMAGWaPAVASGAAVALPAK 225
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
198-252 |
4.20e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 41.13 E-value: 4.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638423 198 TSGTTGIPKIVRVPHKCIVPNI--QHFRVLFDItQEDVL--------------FLASPLTFDPSVVEI----FLA 252
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAeaMFVAAEFDV-ETDVMvswlplfhdmgmvgFLTVPMYFGAELVKVtpmdFLR 233
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
193-261 |
5.29e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 40.63 E-value: 5.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034638423 193 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL------TFDPSVVeiflaLSSGASLLI 261
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLyhntggTVAWSSV-----LAAGATLAL 271
|
|
| PQQ_3 |
pfam13570 |
PQQ-like domain; |
844-881 |
5.96e-03 |
|
PQQ-like domain;
Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 35.26 E-value: 5.96e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1034638423 844 GEKYWMFTTEDAVKSSATMDptTGLIYIGSHDQHAYAL 881
Cdd:pfam13570 1 GEVLWRFETGGPIVSSPAVA--GGLVYVGTGDGTLYAL 36
|
|
| PQQ_3 |
pfam13570 |
PQQ-like domain; |
802-839 |
6.91e-03 |
|
PQQ-like domain;
Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 35.26 E-value: 6.91e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1034638423 802 GKVKWEQILGDRIESSACVSkcGNFIVVGCYNGLVYVL 839
Cdd:pfam13570 1 GEVLWRFETGGPIVSSPAVA--GGLVYVGTGDGTLYAL 36
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
192-295 |
7.84e-03 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 40.24 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638423 192 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL-----TFdpsvVEIFLALSSGASLLIVPtsv 266
Cdd:PRK07514 158 LAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIfhthgLF----VATNVALLAGASMIFLP--- 230
|
90 100
....*....|....*....|....*....
gi 1034638423 267 KLLPSKLASVLfshHRVTVLQATPTLLRR 295
Cdd:PRK07514 231 KFDPDAVLALM---PRATVMMGVPTFYTR 256
|
|
| |
