|
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 ... |
34-347 |
5.51e-177 |
|
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: 519.72 E-value: 5.51e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 34 ESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILFSRHRVTVLQATPTLLRRFGSE 113
Cdd:cd17654 148 QHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 114 LIKSTVLSAHTSLRVLALGGEAFPSLTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEilnsavkhESPVQLGSPL 193
Cdd:cd17654 228 SIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEE--------DSPVQLGSPL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 194 LGTVIEVRDQNGSpvlEGTGQVFLGGKNRVCFLDDEMTVPLGTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIALV 273
Cdd:cd17654 300 LGTVIEVRDQNGS---EGTGQVFLGGLNRVCILDDEVTVPKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLI 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720413180 274 QQVAEELRQVESCAVTWYNQERLILFIVSKvdLVKDCIFKELQKH-LPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd17654 377 QQVIESCLGVESCAVTLSDQQRLIAFIVGE--SSSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
32-347 |
1.06e-84 |
|
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: 279.03 E-value: 1.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 32 HYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVLQATPTLLRRFG 111
Cdd:cd05930 121 LLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALAD-LLAEEGITVLHLTPSLLRLLL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 112 SELIkstvLSAHTSLRVLALGGEAFPSlTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEILnsavkHESPVQLGS 191
Cdd:cd05930 200 QELE----LAALPSLRLVLVGGEALPP-DLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDE-----EDGRVPIGR 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 192 PLLGTVIEVRDQNGSPVLEG-TGQVFLGGKN--RVCFLDDEMT---------VPLGTMRATGDFVTVK-DGEIFFLGRKD 258
Cdd:cd05930 270 PIPNTRVYVLDENLRPVPPGvPGELYIGGAGlaRGYLNRPELTaerfvpnpfGPGERMYRTGDLVRWLpDGNLEFLGRID 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 259 SQIKRHGKRLNIALVQQVAEELRQVESCAVTWYN----QERLILFIVSKV--DLVKDCIFKELQKHLPAHALPDDMVLID 332
Cdd:cd05930 350 DQVKIRGYRIELGEIEAALLAHPGVREAAVVAREdgdgEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLD 429
|
330
....*....|....*
gi 1720413180 333 TLPFTCHGKVDVSEL 347
Cdd:cd05930 430 ALPLTPNGKVDRKAL 444
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
34-288 |
2.67e-46 |
|
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: 171.29 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 34 ESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILFSRHRVTVLQATPTLLRRFGSE 113
Cdd:TIGR01733 150 AWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 114 LIkstvlSAHTSLRVLALGGEAFPSlTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEILNSavkhESPVQLGSPL 193
Cdd:TIGR01733 230 LP-----PALASLRLVILGGEALTP-ALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDAPR----ESPVPIGRPL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 194 LGTVIEVRDQNGSPVLEG-TGQVFLGG------------KNRVCFLDDE-MTVPLGTMRATGDFVTV-KDGEIFFLGRKD 258
Cdd:TIGR01733 300 ANTRLYVLDDDLRPVPVGvVGELYIGGpgvargylnrpeLTAERFVPDPfAGGDGARLYRTGDLVRYlPDGNLEFLGRID 379
|
250 260 270
....*....|....*....|....*....|
gi 1720413180 259 SQIKRHGKRLNIALVQQVAEELRQVESCAV 288
Cdd:TIGR01733 380 DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
32-343 |
7.26e-41 |
|
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: 163.49 E-value: 7.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 32 HYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATPTLLRRFG 111
Cdd:COG1020 645 LLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELL-ARHRVTVLNLTPSLLRALL 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 112 SELikstvLSAHTSLRVLALGGEAFPsLTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEILNSAvkhesPVQLGS 191
Cdd:COG1020 724 DAA-----PEALPSLRLVLVGGEALP-PELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGG-----SVPIGR 792
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 192 PLLGTVIEVRDQNGSPVLEG-TGQVFLGGKN--------------RvcFLDDEMTVPLGTMRATGDFVTV-KDGEIFFLG 255
Cdd:COG1020 793 PIANTRVYVLDAHLQPVPVGvPGELYIGGAGlargylnrpeltaeR--FVADPFGFPGARLYRTGDLARWlPDGNLEFLG 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 256 RKDSQIKRHGKRlnIAL--VQQVAEELRQVESCAVTWY----NQERLILFIVSKVDLVKD--CIFKELQKHLPAHALPDD 327
Cdd:COG1020 871 RADDQVKIRGFR--IELgeIEAALLQHPGVREAVVVARedapGDKRLVAYVVPEAGAAAAaaLLRLALALLLPPYMVPAA 948
|
330
....*....|....*.
gi 1720413180 328 MVLIDTLPFTCHGKVD 343
Cdd:COG1020 949 VVLLLPLPLTGNGKLD 964
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
37-347 |
2.14e-40 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 155.10 E-value: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 37 RSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATPTLLRRfgseLIK 116
Cdd:cd05945 130 LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFL-AEHGITVWVSTPSFAAM----CLL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 117 STVLSAHT--SLRVLALGGEAFPsLTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEILNSAvkheSPVQLGSPLL 194
Cdd:cd05945 205 SPTFTPESlpSLRHFLFCGEVLP-HKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEVLDGY----DRLPIGYAKP 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 195 GTVIEVRDQNGSPVLEG-TGQVFLGGK-------------NRVCFLDDEMTVplgtmRATGDFVTVK-DGEIFFLGRKDS 259
Cdd:cd05945 280 GAKLVILDEDGRPVPPGeKGELVISGPsvskgylnnpektAAAFFPDEGQRA-----YRTGDLVRLEaDGLLFYRGRLDF 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 260 QIKRHGKRLNIALVQQVAEELRQVESC-AVTWYNQE---RLILFIVSKVD----LVKDcIFKELQKHLPAHALPDDMVLI 331
Cdd:cd05945 355 QVKLNGYRIELEEIEAALRQVPGVKEAvVVPKYKGEkvtELIAFVVPKPGaeagLTKA-IKAELAERLPPYMIPRRFVYL 433
|
330
....*....|....*.
gi 1720413180 332 DTLPFTCHGKVDVSEL 347
Cdd:cd05945 434 DELPLNANGKIDRKAL 449
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
36-347 |
4.08e-39 |
|
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: 152.36 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 36 HRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATPTLLRrfgseLI 115
Cdd:cd12117 167 NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALI-AEEGVTVLWLTAALFN-----QL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 116 KSTVLSAHTSLRVLALGGEAFPSLTIlKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEilnsaVKHESPVQLGSPLLG 195
Cdd:cd12117 241 ADEDPECFAGLRELLTGGEVVSPPHV-RRVLAACPGLRLVNGYGPTENTTFTTSHVVTEL-----DEVAGSIPIGRPIAN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 196 TVIEVRDQNGSPVLEG-TGQVFLGGK-------NRVC-----FLDDEMTvPLGTMRATGDFVTVK-DGEIFFLGRKDSQI 261
Cdd:cd12117 315 TRVYVLDEDGRPVPPGvPGELYVGGDglalgylNRPAltaerFVADPFG-PGERLYRTGDLARWLpDGRLEFLGRIDDQV 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 262 KRHGKRLNIALVQQVAEELRQVESCAVTWYNQE----RLILFIVSKVDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFT 337
Cdd:cd12117 394 KIRGFRIELGEIEAALRAHPGVREAVVVVREDAggdkRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLT 473
|
330
....*....|
gi 1720413180 338 CHGKVDVSEL 347
Cdd:cd12117 474 ANGKVDRRAL 483
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
37-343 |
9.25e-39 |
|
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: 150.54 E-value: 9.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 37 RSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILFSRhRVTVLQATPTLLRRFGSELIK 116
Cdd:cd17643 126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDE-GVTVLNQTPSAFYQLVEAADR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 117 STvlSAHTSLRVLALGGEAFPsLTILKSWRGK--GNRTQIFNIYGITEVSSWATFYRIPEEILNSAVkhESPVqlGSPLL 194
Cdd:cd17643 205 DG--RDPLALRYVIFGGEALE-AAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAADLPAAA--ASPI--GRPLP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 195 GTVIEVRDQNGSPVLEG-TGQVFLGGK-------NR-----VCFLDDEMTVPLGTMRATGDFVT-VKDGEIFFLGRKDSQ 260
Cdd:cd17643 278 GLRVYVLDADGRPVPPGvVGELYVSGAgvargylGRpeltaERFVANPFGGPGSRMYRTGDLARrLPDGELEYLGRADEQ 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 261 IKRHGKRLNIALVQQVAEELRQVESCAVTWYNQE----RLILFIVSK--VDLVKDCIFKELQKHLPAHALPDDMVLIDTL 334
Cdd:cd17643 358 VKIRGFRIELGEIEAALATHPSVRDAAVIVREDEpgdtRLVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDAL 437
|
....*....
gi 1720413180 335 PFTCHGKVD 343
Cdd:cd17643 438 PLTVNGKLD 446
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
35-347 |
1.64e-37 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 147.05 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSL----------FDITQED-ILFLASPlTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQAT 103
Cdd:cd12116 147 SHRNLvnflhsmrerLGLGPGDrLLAVTTY-AFDISLLELLLPLLAGARVVIAPRETQRDPEALARLI-EAHSITVMQAT 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 104 PTLLRrfgseLIKSTVLSAHTSLRVLAlGGEAFPslTILKswRGKGNRT-QIFNIYGITEVSSWATFYRIPEEilnsavk 182
Cdd:cd12116 225 PATWR-----MLLDAGWQGRAGLTALC-GGEALP--PDLA--ARLLSRVgSLWNLYGPTETTIWSTAARVTAA------- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 183 hESPVQLGSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGKNrVC-------------FLDDEMTVPLGTMRATGDFVTVK- 247
Cdd:cd12116 288 -AGPIPIGRPLANTQVYVLDAALRPVPPGVpGELYIGGDG-VAqgylgrpaltaerFVPDPFAGPGSRLYRTGDLVRRRa 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 248 DGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQE---RLILFIVSKVDLVKDC--IFKELQKHLPAH 322
Cdd:cd12116 366 DGRLEYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGgdrRLVAYVVLKAGAAPDAaaLRAHLRATLPAY 445
|
330 340
....*....|....*....|....*
gi 1720413180 323 ALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd12116 446 MVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
50-347 |
4.15e-37 |
|
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: 145.54 E-value: 4.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 50 LAS-PLTFDPSVVEIFVSLSSGACLLIVpTSVKVLPSkladiLFSRHRVTVLQATPTLLRrfgsELIKSTVLSahTSLRV 128
Cdd:cd12115 150 LAStSICFDLSVFELFGPLATGGKVVLA-DNVLALPD-----LPAAAEVTLINTVPSAAA----ELLRHDALP--ASVRV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 129 LALGGEAFPSlTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEilnsavkHESPVQLGSPLLGTVIEVRDQNGSPV 208
Cdd:cd12115 218 VNLAGEPLPR-DLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPG-------ASGEVSIGRPLANTQAYVLDRALQPV 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 209 LEGT-GQVFLGGKN-RVCFLDD-EMTV---------PLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIALVQQ 275
Cdd:cd12115 290 PLGVpGELYIGGAGvARGYLGRpGLTAerflpdpfgPGARLYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEA 369
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720413180 276 VAEELRQV-ESCAVTW---YNQERLILFIVSKVD--LVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd12115 370 ALRSIPGVrEAVVVAIgdaAGERRLVAYIVAEPGaaGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
35-447 |
8.74e-36 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 148.00 E-value: 8.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSL----------FDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATP 104
Cdd:PRK12467 677 SHGALanyvcviaerLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALM-ADQGVTVLKIVP 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 105 TLLRRFgselIKSTVLSAHTSLRVLALGGEAFPsLTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEILNSavkhe 184
Cdd:PRK12467 756 SHLQAL----LQASRVALPRPQRALVCGGEALQ-VDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDF----- 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 185 SPVQLGSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGK--------------NRvcFLDDEMTVPLGTMRATGDFVT-VKD 248
Cdd:PRK12467 826 GNVPIGQPLANLGLYILDHYLNPVPVGVvGELYIGGAglargyhrrpaltaER--FVPDPFGADGGRLYRTGDLARyRAD 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 249 GEIFFLGRKDSQIKRHGKRLNIALVQ---QVAEELRQVESCAVTWYNQERLILFIVSKVDL-------VKDCIFKELQKH 318
Cdd:PRK12467 904 GVIEYLGRMDHQVKIRGFRIELGEIEarlLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVAdgaehqaTRDELKAQLRQV 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 319 LPAHALPDDMVLIDTLPFTCHGKVDVSELNKiyldYISSQPRNELHGKE-ELWGKLQYLWKSILclpedpeDTLKVPANS 397
Cdd:PRK12467 984 LPDYMVPAHLLLLDSLPLTPNGKLDRKALPK----PDASAVQATFVAPQtELEKRLAAIWADVL-------KVERVGLTD 1052
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1720413180 398 VFLDSGGDSLKSMRLLSEIERLTGTAIPglLEVILSSSLLDVYnhiVQAV 447
Cdd:PRK12467 1053 NFFELGGHSLLATQVISRVRQRLGIQVP--LRTLFEHQTLAGF---AQAV 1097
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
17-343 |
3.78e-33 |
|
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: 134.10 E-value: 3.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 17 VYMKNNSIKNEVWAIHYEshrslFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTsvKVLPSKLADILFSRH- 95
Cdd:cd17644 124 VMIEHQSLVNLSHGLIKE-----YGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPE--EMRSSLEDFVQYIQQw 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 96 RVTVLQATPTLLRRFGSELIKSTVLSAHtSLRVLALGGEAF-PSLTILksWR-GKGNRTQIFNIYGITEVSSWATFYRIP 173
Cdd:cd17644 197 QLTVLSLPPAYWHLLVLELLLSTIDLPS-SLRLVIVGGEAVqPELVRQ--WQkNVGNFIQLINVYGPTEATIAATVCRLT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 174 EeiLNSAVKHESPVqlGSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGK-------NRvcfldDEMTV-----------PL 234
Cdd:cd17644 274 Q--LTERNITSVPI--GRPIANTQVYILDENLQPVPVGVpGELHIGGVglargylNR-----PELTAekfishpfnssES 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 235 GTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVT----WYNQERLILFIVSKVDLVKD 309
Cdd:cd17644 345 ERLYKTGDLARyLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIvredQPGNKRLVAYIVPHYEESPS 424
|
330 340 350
....*....|....*....|....*....|....*...
gi 1720413180 310 CifKELQKH----LPAHALPDDMVLIDTLPFTCHGKVD 343
Cdd:cd17644 425 T--VELRQFlkakLPDYMIPSAFVVLEELPLTPNGKID 460
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
50-347 |
1.72e-32 |
|
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: 132.45 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 50 LASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADIlFSRHRVTVLQATPTLLRrfgseLIKSTVLSAHTSLRVL 129
Cdd:cd17655 183 LFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQY-IRQNRITIIDLTPAHLK-----LLDAADDSEGLSLKHL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 130 ALGGEAFPSLTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEilnsAVKHESpVQLGSPLLGTVIEVRDQNGSPVL 209
Cdd:cd17655 257 IVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPE----TDQQVS-VPIGKPLGNTRIYILDQYGRPQP 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 210 EGT-GQVFLGGK-------NR-----VCFLDDEMtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIALVQQ 275
Cdd:cd17655 332 VGVaGELYIGGEgvargylNRpeltaEKFVDDPF-VPGERMYRTGDLARwLPDGNIEFLGRIDHQVKIRGYRIELGEIEA 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720413180 276 VAEELRQVESCAVTWY----NQERLILFIVSKVDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd17655 411 RLLQHPDIKEAVVIARkdeqGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
36-347 |
2.04e-32 |
|
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: 131.22 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 36 HRSLFDITQEDI-----------LFLASPlTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATP 104
Cdd:cd17652 115 HRGLANLAAAQIaafdvgpgsrvLQFASP-SFDASVWELLMALLAGATLVLAPAEELLPGEPLADLL-REHRITHVTLPP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 105 TLLRrfgselikstVLSAHT--SLRVLALGGEAfPSLTILKSWrGKGNRtqIFNIYGITEVSSWATFYRIPEEilnsavk 182
Cdd:cd17652 193 AALA----------ALPPDDlpDLRTLVVAGEA-CPAELVDRW-APGRR--MINAYGPTETTVCATMAGPLPG------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 183 hESPVQLGSPLLGTVIEVRDQNGSPVLEG-TGQVFLGGK-------NR-----VCFLDDEMTVPLGTMRATGDFVT-VKD 248
Cdd:cd17652 252 -GGVPPIGRPVPGTRVYVLDARLRPVPPGvPGELYIAGAglargylNRpgltaERFVADPFGAPGSRMYRTGDLARwRAD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 249 GEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQE----RLILFIVSKVDLVKDC--IFKELQKHLPAH 322
Cdd:cd17652 331 GQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRpgdkRLVAYVVPAPGAAPTAaeLRAHLAERLPGY 410
|
330 340
....*....|....*....|....*
gi 1720413180 323 ALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd17652 411 MVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
35-353 |
2.95e-32 |
|
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: 131.09 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSL----------FDITQEDILFLASPLTFD-PSVVEIFVSLSSGACLLIVPtsvKVLPSKLADiLFSRHRVTVLQAT 103
Cdd:COG0318 121 THRNLlanaaaiaaaLGLTPGDVVLVALPLFHVfGLTVGLLAPLLAGATLVLLP---RFDPERVLE-LIERERVTVLFGV 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 104 PTLLRRfgseLIKSTVLSAH--TSLRVLALGGEAFPSlTILKSWRGKGNrTQIFNIYGITEVSSWATFYriPEEILnsav 181
Cdd:COG0318 197 PTMLAR----LLRHPEFARYdlSSLRLVVSGGAPLPP-ELLERFEERFG-VRIVEGYGLTETSPVVTVN--PEDPG---- 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 182 kHESPVQLGSPLLGTVIEVRDQNGSPVLEGT--------GQVFLG-----GKNRVCFLDdemtvplGTMRaTGDFVTV-K 247
Cdd:COG0318 265 -ERRPGSVGRPLPGVEVRIVDEDGRELPPGEvgeivvrgPNVMKGywndpEATAEAFRD-------GWLR-TGDLGRLdE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 248 DGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVT------WynQERLILFIVSK--VDLVKDCIFKELQKHL 319
Cdd:COG0318 336 DGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVgvpdekW--GERVVAFVVLRpgAELDAEELRAFLRERL 413
|
330 340 350
....*....|....*....|....*....|....
gi 1720413180 320 PAHALPDDMVLIDTLPFTCHGKVDVSELNKIYLD 353
Cdd:COG0318 414 ARYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
40-347 |
5.38e-32 |
|
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: 131.24 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 40 FDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVLQATPTLLRRFGSELikstV 119
Cdd:cd17646 174 YPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAA-LIREHGVTTCHFVPSMLRVFLAEP----A 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 120 LSAHTSLRVLALGGEAFPSLTIlKSWRGKGNrTQIFNIYGITEVSSWATFYRIpeeilnSAVKHESPVQLGSPLLGTVIE 199
Cdd:cd17646 249 AGSCASLRRVFCSGEALPPELA-ARFLALPG-AELHNLYGPTEAAIDVTHWPV------RGPAETPSVPIGRPVPNTRLY 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 200 VRDQNGSPVLEGT-GQVFLGGK-------NRVC-----FLDDemtvPLGT---MRATGDFVTVK-DGEIFFLGRKDSQIK 262
Cdd:cd17646 321 VLDDALRPVPVGVpGELYLGGVqlargylGRPAltaerFVPD----PFGPgsrMYRTGDLARWRpDGALEFLGRSDDQVK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 263 RHGKRLNIALVQQVAEELRQVESCAVTWYNQ----ERLILFIVS---KVDLVKDCIFKELQKHLPAHALPDDMVLIDTLP 335
Cdd:cd17646 397 IRGFRVEPGEIEAALAAHPAVTHAVVVARAApagaARLVGYVVPaagAAGPDTAALRAHLAERLPEYMVPAAFVVLDALP 476
|
330
....*....|..
gi 1720413180 336 FTCHGKVDVSEL 347
Cdd:cd17646 477 LTANGKLDRAAL 488
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
36-343 |
6.35e-32 |
|
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: 130.93 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 36 HRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVLQATPTLLRRFGSELI 115
Cdd:cd17651 168 QARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAA-WLDEQRISRVFLPTVALRALAEHGR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 116 KSTVLSAhtSLRVLALGGEAFPSLTILKSWRGKGNRTQIFNIYGITEvSSWATFYRIPEEilnsAVKHESPVQLGSPLLG 195
Cdd:cd17651 247 PLGVRLA--ALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTE-THVVTALSLPGD----PAAWPAPPPIGRPIDN 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 196 TVIEVRDQNGSPVLEG-TGQVFLGGK-------NRvcfldDEMT---------VPLGTMRATGDFVT-VKDGEIFFLGRK 257
Cdd:cd17651 320 TRVYVLDAALRPVPPGvPGELYIGGAglargylNR-----PELTaerfvpdpfVPGARMYRTGDLARwLPDGELEFLGRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 258 DSQIKRHGKRLNIALVQQVAEELRQVESCAVT----WYNQERLILFIVSKVDLVKDC--IFKELQKHLPAHALPDDMVLI 331
Cdd:cd17651 395 DDQVKIRGFRIELGEIEAALARHPGVREAVVLaredRPGEKRLVAYVVGDPEAPVDAaeLRAALATHLPEYMVPSAFVLL 474
|
330
....*....|..
gi 1720413180 332 DTLPFTCHGKVD 343
Cdd:cd17651 475 DALPLTPNGKLD 486
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
40-347 |
6.42e-31 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 127.77 E-value: 6.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 40 FDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVLQATPTLLrrfgsELIKSTV 119
Cdd:cd12114 162 FAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAE-LIERHGVTLWNSVPALL-----EMLLDVL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 120 LSAHT---SLRVLALGGEAFPsLTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEIlnsavKHESPVQLGSPLLGT 196
Cdd:cd12114 236 EAAQAllpSLRLVLLSGDWIP-LDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVP-----PDWRSIPYGRPLANQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 197 VIEVRDQNGSPVLEG-TGQVFLGGKN--RVCFLDDEMT----VPLGTMRA---TGDFVTVK-DGEIFFLGRKDSQIKRHG 265
Cdd:cd12114 310 RYRVLDPRGRDCPDWvPGELWIGGRGvaLGYLGDPELTaarfVTHPDGERlyrTGDLGRYRpDGTLEFLGRRDGQVKVRG 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 266 KRLNIALVQQVAEELRQVESCAVTWY---NQERLILFIVSKVD---LVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCH 339
Cdd:cd12114 390 YRIELGEIEAALQAHPGVARAVVVVLgdpGGKRLAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTAN 469
|
....*...
gi 1720413180 340 GKVDVSEL 347
Cdd:cd12114 470 GKVDRAAL 477
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
29-343 |
1.55e-30 |
|
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: 123.55 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 29 WAIHYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPtsvKVLPSKLADiLFSRHRVTVLQATPTLLR 108
Cdd:cd04433 25 LLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPEAALE-LIEREKVTILLGVPTLLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 109 RFGSEL-IKSTVLSahtSLRVLALGGEAFPSlTILKSWRGKGNrTQIFNIYGITEVSSWATFYRIPEEilnsavkHESPV 187
Cdd:cd04433 101 RLLKAPeSAGYDLS---SLRALVSGGAPLPP-ELLERFEEAPG-IKLVNGYGLTETGGTVATGPPDDD-------ARKPG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 188 QLGSPLLGTVIEVRDQNGSPVLEG-TGQVFLGGKN-----------RVCFLDDemtvplGTMRaTGDFVTV-KDGEIFFL 254
Cdd:cd04433 169 SVGRPVPGVEVRIVDPDGGELPPGeIGELVVRGPSvmkgywnnpeaTAAVDED------GWYR-TGDLGRLdEDGYLYIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 255 GRKDSQIKRHGKrlNIAL--VQQVAEELRQVESCAV------TWynQERLILFIVSK--VDLVKDCIFKELQKHLPAHAL 324
Cdd:cd04433 242 GRLKDMIKSGGE--NVYPaeVEAVLLGHPGVAEAAVvgvpdpEW--GERVVAVVVLRpgADLDAEELRAHVRERLAPYKV 317
|
330
....*....|....*....
gi 1720413180 325 PDDMVLIDTLPFTCHGKVD 343
Cdd:cd04433 318 PRRVVFVDALPRTASGKID 336
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
47-347 |
8.20e-30 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 123.57 E-value: 8.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 47 ILFLASPlTFDPSVVEIFVSLSSGACLLIVPTSvkvlpSKLADILFSrhrVTVLQATPTLLrrfgselikSTV-LSAHTS 125
Cdd:cd17653 149 VAQVLSI-AFDACIGEIFSTLCNGGTLVLADPS-----DPFAHVART---VDALMSTPSIL---------STLsPQDFPN 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 126 LRVLALGGEAfPSLTILKSWRGkgNRTqIFNIYGITEVSSWATFYRipeeilnsaVKHESPVQLGSPLLGTVIEVRDQNG 205
Cdd:cd17653 211 LKTIFLGGEA-VPPSLLDRWSP--GRR-LYNAYGPTECTISSTMTE---------LLPGQPVTIGKPIPNSTCYILDADL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 206 SPVLEG-TGQVFLGG------------KNRVCFLDDEMtVPLGTMRATGD--FVTvKDGEIFFLGRKDSQIKRHGKRLNI 270
Cdd:cd17653 278 QPVPEGvVGEICISGvqvargylgnpaLTASKFVPDPF-WPGSRMYRTGDygRWT-EDGGLEFLGREDNQVKVRGFRINL 355
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720413180 271 ALVQQVAEELRQVESCAVTWYNQERLILFiVSKVDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd17653 356 EEIEEVVLQSQPEVTQAAAIVVNGRLVAF-VTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-414 |
2.96e-29 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 126.61 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 52 SPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVLQATPTLLRRFgselIKSTVLSAHTSLRVLAL 131
Cdd:PRK12316 703 TPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVE-LINREGVDTLHFVPSMLQAF----LQDEDVASCTSLRRIVC 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 132 GGEAFPsLTILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEilnsaVKHESPVqlGSPLLGTVIEVRDQNGSPVLEG 211
Cdd:PRK12316 778 SGEALP-ADAQEQVFAKLPQAGLYNLYGPTEAAIDVTHWTCVEE-----GGDSVPI--GRPIANLACYILDANLEPVPVG 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 212 -TGQVFLGGKN------RVCFLDDEMTVPL-----GTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIALVQQVAE 278
Cdd:PRK12316 850 vLGELYLAGRGlargyhGRPGLTAERFVPSpfvagERMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 279 ELRQVESCAVTWYNQERLILFIV--SKVDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVDVSELNKIylDYIS 356
Cdd:PRK12316 930 EHPWVREAAVLAVDGKQLVGYVVleSEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAP--EASV 1007
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720413180 357 SQ-----PRNELhgkEElwgKLQYLWKSILCLPedpedtlKVPANSVFLDSGGDSLKSMRLLS 414
Cdd:PRK12316 1008 AQqgyvaPRNAL---ER---TLAAIWQDVLGVE-------RVGLDDNFFELGGDSIVSIQVVS 1057
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
30-343 |
3.42e-29 |
|
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: 122.09 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 30 AIHYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATPTLLRR 109
Cdd:cd17649 120 AAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMV-RELGVTVLDLPPAYLQQ 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 110 FgSELIKSTVLSAHTSLRVLALGGEAFpSLTILKSWRGKGNRtqIFNIYGITEVSSWATFYRIPEEILNSAVKhespVQL 189
Cdd:cd17649 199 L-AEEADRTGDGRPPSLRLYIFGGEAL-SPELLRRWLKAPVR--LFNAYGPTEATVTPLVWKCEAGAARAGAS----MPI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 190 GSPLLGTVIEVRDQNGSPVLEG-TGQVFLGGK-------NRVC-----FLDDEMTVPLGTMRATGDFVTVK-DGEIFFLG 255
Cdd:cd17649 271 GRPLGGRSAYILDADLNPVPVGvTGELYIGGEglargylGRPEltaerFVPDPFGAPGSRLYRTGDLARWRdDGVIEYLG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 256 RKDSQIKRHGKRLNIALVQQVAEELRQVESCAV---TWYNQERLILFIVSKVDLVKDCIFKELQKH----LPAHALPDDM 328
Cdd:cd17649 351 RVDHQVKIRGFRIELGEIEAALLEHPGVREAAVvalDGAGGKQLVAYVVLRAAAAQPELRAQLRTAlrasLPDYMVPAHL 430
|
330
....*....|....*
gi 1720413180 329 VLIDTLPFTCHGKVD 343
Cdd:cd17649 431 VFLARLPLTPNGKLD 445
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-414 |
2.50e-28 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 123.91 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 20 KNNSIKNEVWAIHYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTV 99
Cdd:PRK12316 3212 KGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELI-NSEGVDV 3290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 100 LQATPTLLRRFgselIKSTVLSAHTSLRVLALGGEAFPSlTILKSWRGKGnrtQIFNIYGITEVSSWATFYRIPEEilns 179
Cdd:PRK12316 3291 LHAYPSMLQAF----LEEEDAHRCTSLKRIVCGGEALPA-DLQQQVFAGL---PLYNLYGPTEATITVTHWQCVEE---- 3358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 180 avkHESPVQLGSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGKN--RVCFLDDEMT---------VPLGTMRATGDFVTVK 247
Cdd:PRK12316 3359 ---GKDAVPIGRPIANRACYILDGSLEPVPVGAlGELYLGGEGlaRGYHNRPGLTaerfvpdpfVPGERLYRTGDLARYR 3435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 248 -DGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQERLILFIVSKVDL--VKDCIFKELQKHLPAHAL 324
Cdd:PRK12316 3436 aDGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAgdLREALKAHLKASLPEYMV 3515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 325 PDDMVLIDTLPFTCHGKVDVSELNKIYLDYISSQ---PRNELHgkeelwGKLQYLWKSILCLPEdpedtlkVPANSVFLD 401
Cdd:PRK12316 3516 PAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDyvaPVNELE------RRLAAIWADVLKLEQ-------VGLTDNFFE 3582
|
410
....*....|...
gi 1720413180 402 SGGDSLKSMRLLS 414
Cdd:PRK12316 3583 LGGDSIISLQVVS 3595
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
42-436 |
5.48e-28 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 122.07 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 42 ITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVLQATPTLLRRFGSELIKSTVLS 121
Cdd:PRK10252 636 LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQ-FFAEYGVTTTHFVPSMLAAFVASLTPEGARQ 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 122 AHTSLRVLALGGEAFPSlTILKSWRGKGNrTQIFNIYGITE----VSSWATFyriPEEILNSAvkhESPVQLGSPLLGTV 197
Cdd:PRK10252 715 SCASLRQVFCSGEALPA-DLCREWQQLTG-APLHNLYGPTEaavdVSWYPAF---GEELAAVR---GSSVPIGYPVWNTG 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 198 IEVRDQNGSPVLEGT-GQVFLGG--------------KNRvcFLDDEMtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQI 261
Cdd:PRK10252 787 LRILDARMRPVPPGVaGDLYLTGiqlaqgylgrpdltASR--FIADPF-APGERMYRTGDVARwLDDGAVEYLGRSDDQL 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 262 KRHGKR----------LNIALVQQVAEELRQVESCAVTWYNQERLILFIVSKVDLVKDC--IFKELQKHLPAHALPDDMV 329
Cdd:PRK10252 864 KIRGQRielgeidramQALPDVEQAVTHACVINQAAATGGDARQLVGYLVSQSGLPLDTsaLQAQLRERLPPHMVPVVLL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 330 LIDTLPFTCHGKVDVSELNK--IYLDYISSQPRNelhGKEELwgkLQYLWKSILCLPedpedtlKVPANSVFLDSGGDSL 407
Cdd:PRK10252 944 QLDQLPLSANGKLDRKALPLpeLKAQVPGRAPKT---GTETI---IAAAFSSLLGCD-------VVDADADFFALGGHSL 1010
|
410 420
....*....|....*....|....*....
gi 1720413180 408 KSMRLLSEIERLTGTAiPGLLEVILSSSL 436
Cdd:PRK10252 1011 LAMKLAAQLSRQFARQ-VTPGQVMVASTV 1038
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
40-414 |
3.74e-27 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 119.88 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 40 FDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATPTLLRRFgseLIKSTV 119
Cdd:PRK12467 1754 YQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLI-ERQQVTTLHFVPSMLQQL---LQMDEQ 1829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 120 LSAHTSLRVLALGGEAFPSLTILKSWRGKGNrTQIFNIYGITE----VSSWATFYRIPEEilnsavKHESPVqlGSPLLG 195
Cdd:PRK12467 1830 VEHPLSLRRVVCGGEALEVEALRPWLERLPD-TGLFNLYGPTEtavdVTHWTCRRKDLEG------RDSVPI--GQPIAN 1900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 196 TVIEVRDQNGSPVLEGT-GQVFLGGK-------NRVC-----FLDDEMTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQI 261
Cdd:PRK12467 1901 LSTYILDASLNPVPIGVaGELYLGGVglargylNRPAltaerFVADPFGTVGSRLYRTGDLARYRaDGVIEYLGRIDHQV 1980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 262 KRHGKRLNIA-----LVQQVAeeLRQVESCAVTWYNQERLILFIVSKVDLVKDCIFK------ELQKHLPAhALPDDMV- 329
Cdd:PRK12467 1981 KIRGFRIELGeiearLREQGG--VREAVVIAQDGANGKQLVAYVVPTDPGLVDDDEAqvalraILKNHLKA-SLPEYMVp 2057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 330 ----LIDTLPFTCHGKV--------DVSELNKIYldyisSQPRNELhgkEElwgKLQYLWKSILCLPedpedtlKVPANS 397
Cdd:PRK12467 2058 ahlvFLARMPLTPNGKLdrkalpapDASELQQAY-----VAPQSEL---EQ---RLAAIWQDVLGLE-------QVGLHD 2119
|
410
....*....|....*..
gi 1720413180 398 VFLDSGGDSLKSMRLLS 414
Cdd:PRK12467 2120 NFFELGGDSIISIQVVS 2136
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
45-347 |
7.58e-27 |
|
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: 114.80 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 45 EDILFLASpLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATPTLLRRFGselikstvLSAHT 124
Cdd:cd17648 138 EAVLFFSN-YVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYI-NREKVTYLSGTPSVLQQYD--------LARLP 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 125 SLRVLALGGEAF--PSLTILKSwrgkGNRTQIFNIYGITEVSSWA--TFYRIPEEILNSavkhespvqLGSPLLGTVIEV 200
Cdd:cd17648 208 HLKRVDAAGEEFtaPVFEKLRS----RFAGLIINAYGPTETTVTNhkRFFPGDQRFDKS---------LGRPVRNTKCYV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 201 RDQNGSPV-LEGTGQVFLGGK-------NRvcfldDEMT----VP-------------LGTMRATGDFVT-VKDGEIFFL 254
Cdd:cd17648 275 LNDAMKRVpVGAVGELYLGGDgvargylNR-----PELTaerfLPnpfqteqerargrNARLYKTGDLVRwLPSGELEYL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 255 GRKDSQIKRHGKRLNIALVQQVAEELRQVESCAV---------TWYNQERLILFIVSKVDLVKDC-IFKELQKHLPAHAL 324
Cdd:cd17648 350 GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVvakedasqaQSRIQKYLVGYYLPEPGHVPESdLLSFLRAKLPRYMV 429
|
330 340
....*....|....*....|...
gi 1720413180 325 PDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd17648 430 PARLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
34-343 |
1.52e-26 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 114.56 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 34 ESHRSLFDITQED-ILFLASPlTFDPSVVEIFVSLSSGACLLIvpTSVKVLPSKLADILfSRHRVTVLQATPTLLRrfgs 112
Cdd:cd05918 136 LAHGRALGLTSESrVLQFASY-TFDVSILEIFTTLAAGGCLCI--PSEEDRLNDLAGFI-NRLRVTWAFLTPSVAR---- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 113 eLIKSTVLsahTSLRVLALGGEAfPSLTILKSWrgkGNRTQIFNIYGITEVSSWATfyripeeiLNSAVKHESPVQLGSP 192
Cdd:cd05918 208 -LLDPEDV---PSLRTLVLGGEA-LTQSDVDTW---ADRVRLINAYGPAECTIAAT--------VSPVVPSTDPRNIGRP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 193 LLGT--VIEVRDQN-----GSP---VLEG-------------TGQVFLggkNRVCFLDDEMTVPLGTMRATGDFVT-VKD 248
Cdd:cd05918 272 LGATcwVVDPDNHDrlvpiGAVgelLIEGpilargylndpekTAAAFI---EDPAWLKQEGSGRGRRLYRTGDLVRyNPD 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 249 GEIFFLGRKDSQIKRHGKRLNI----ALVQQVAEELRQVESCAVT---WYNQERLILFIV------------SKVDLVKD 309
Cdd:cd05918 349 GSLEYVGRKDTQVKIRGQRVELgeieHHLRQSLPGAKEVVVEVVKpkdGSSSPQLVAFVVldgsssgsgdgdSLFLEPSD 428
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720413180 310 C---IFKELQKHLpAHALPDDMV-----LIDTLPFTCHGKVD 343
Cdd:cd05918 429 EfraLVAELRSKL-RQRLPSYMVpsvflPLSHLPLTASGKID 469
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
32-462 |
1.97e-26 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 117.75 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 32 HYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADIlfSRHRVTVLQATPTLLRRFg 111
Cdd:PRK12316 4722 HLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEI--HEHRVTVLVFPPVYLQQL- 4798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 112 seLIKSTVLSAHTSLRVLALGGEAFPSLTILKSWRGKGNrTQIFNIYGITEVSSWATFYRIPEEILNSAVKhespVQLGS 191
Cdd:PRK12316 4799 --AEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKP-VYLFNGYGPTETTVTVLLWKARDGDACGAAY----MPIGT 4871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 192 PLLGTVIEVRDQNGSPV-LEGTGQVFLGGK--------------NRvcFLDDEMTVPLGTMRATGDFVTVK-DGEIFFLG 255
Cdd:PRK12316 4872 PLGNRSGYVLDGQLNPLpVGVAGELYLGGEgvargylerpaltaER--FVPDPFGAPGGRLYRTGDLARYRaDGVIDYLG 4949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 256 RKDSQIKRHGKRLNIALVQQVAEE---LRQVESCAVTWYNQERLILFIVSKVDLVKDCIFKE----------LQKHLPAH 322
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREhpaVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQaelrdelkaaLRERLPEY 5029
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 323 ALPDDMVLIDTLPFTCHGKV--------DVSELNKIYLdyissQPRNELHgkeelwGKLQYLWKSILCLPedpedtlKVP 394
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLdrkalpqpDASLLQQAYV-----APRSELE------QQVAAIWAEVLQLE-------RVG 5091
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720413180 395 ANSVFLDSGGDSLKSMRLLSEIErltgtaipglLEVILSSSLLDVYNHIVQAVFTPEDRKANRSYTTK 462
Cdd:PRK12316 5092 LDDNFFELGGHSLLAIQVTSRIQ----------LELGLELPLRELFQTPTLAAFVELAAAAGSGDDEK 5149
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
29-347 |
3.37e-26 |
|
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: 112.95 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 29 WAIHYEshrslFDITQEDILFLASpLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATPTLLR 108
Cdd:cd17650 125 WRREYE-----LDSFPVRLLQMAS-FSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLI-LKSRITLMESTPALIR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 109 RFGSELIKSTVlsAHTSLRVLALGGEAFPSLTILKSWRGKGNRTQIFNIYGITEVSSWATFYripEEILNSAVKHESpVQ 188
Cdd:cd17650 198 PVMAYVYRNGL--DLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYY---EEGRDPLGDSAN-VP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 189 LGSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGKNrVC-------------FLDDEMtVPLGTMRATGDFVT-VKDGEIFF 253
Cdd:cd17650 272 IGRPLPNTAMYVLDERLQPQPVGVaGELYIGGAG-VArgylnrpeltaerFVENPF-APGERMYRTGDLARwRADGNVEL 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 254 LGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYN----QERLILFIVSKVDLVKDCIFKELQKHLPAHALPDDMV 329
Cdd:cd17650 350 LGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREdkggEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYV 429
|
330
....*....|....*...
gi 1720413180 330 LIDTLPFTCHGKVDVSEL 347
Cdd:cd17650 430 QLDALPLTPNGKVDRRAL 447
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
35-343 |
1.79e-25 |
|
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: 110.99 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSL----------FDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVkvLPSKLADiLFSRHRVTVLQATP 104
Cdd:cd05922 138 SHQNLlanarsiaeyLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV--LDDAFWE-DLREHGATGLAGVP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 105 T---LLRRFGSELIKSTvlsahtSLRVLALGGEAFPSLTIlKSWRGKGNRTQIFNIYGITEVSSWATfYRIPEEIlnsav 181
Cdd:cd05922 215 StyaMLTRLGFDPAKLP------SLRYLTQAGGRLPQETI-ARLRELLPGAQVYVMYGQTEATRRMT-YLPPERI----- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 182 kHESPVQLGSPLLGTVIEVRDQNGSPvlEGTGQ----------VFLGGKNRVCFLDDEMTVplGTMRATGDF-VTVKDGE 250
Cdd:cd05922 282 -LEKPGSIGLAIPGGEFEILDDDGTP--TPPGEpgeivhrgpnVMKGYWNDPPYRRKEGRG--GGVLHTGDLaRRDEDGF 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 251 IFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVT---WYNQERLILFIVSKVDLVKDCIFKELQKHLPAHALPDD 327
Cdd:cd05922 357 LFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVglpDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPAT 436
|
330
....*....|....*.
gi 1720413180 328 MVLIDTLPFTCHGKVD 343
Cdd:cd05922 437 VRVVDELPLTASGKVD 452
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
20-425 |
4.56e-24 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 109.87 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 20 KNNSIKNEVWAIHYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVlPSKLADILfSRHRVTV 99
Cdd:PRK12467 3253 KGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWD-PEELWQAI-HAHRISI 3330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 100 LQATPTLLRRFgseLIKSTVLSAHtSLRVLALGGEAFPSLTIlKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEeilnS 179
Cdd:PRK12467 3331 ACFPPAYLQQF---AEDAGGADCA-SLDIYVFGGEAVPPAAF-EQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGG----D 3401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 180 AVKHESPVQLGSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGK--------------NRvcFLDDEMTVPLGTMRATGDFV 244
Cdd:PRK12467 3402 AVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVaGELYIGGVglargyhqrpsltaER--FVADPFSGSGGRLYRTGDLA 3479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 245 TVK-DGEIFFLGRKDSQIKRHGKRLNIA-----LVQQVAeeLRQVESCAVTWYNQERLILFIVSKV---DLvKDCIFKEL 315
Cdd:PRK12467 3480 RYRaDGVIEYLGRIDHQVKIRGFRIELGeiearLLQHPS--VREAVVLARDGAGGKQLVAYVVPADpqgDW-RETLRDHL 3556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 316 QKHLPAHALPDDMVLIDTLPFTCHGKVDVSELNKIYL----DYISsqPRNELHgkeelwGKLQYLWKSILCLPedpedtl 391
Cdd:PRK12467 3557 AASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAkgsrEYVA--PRSEVE------QQLAAIWADVLGVE------- 3621
|
410 420 430
....*....|....*....|....*....|....
gi 1720413180 392 KVPANSVFLDSGGDSLKSMRLLSEIERLTGTAIP 425
Cdd:PRK12467 3622 QVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLS 3655
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
28-263 |
1.11e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 104.70 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 28 VWAIHYESHRsLFDITQEDILFLASPLTFDPSVV-EIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVLQATPTL 106
Cdd:pfam00501 184 VLSIKRVRPR-GFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDPAALLE-LIERYKVTVLYGVPTL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 107 LRRF-GSELIKSTVLSahtSLRVLALGGEAFPSlTILKSWRGKGnRTQIFNIYGITEVSSWATFYRIPEEilnsavKHES 185
Cdd:pfam00501 262 LNMLlEAGAPKRALLS---SLRLVLSGGAPLPP-ELARRFRELF-GGALVNGYGLTETTGVVTTPLPLDE------DLRS 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 186 PVQLGSPLLGTVIEVRDQN-GSPVLEG-TGQVFLGGKN--RVCFLDDEMT----VPLGTMRaTGDFVTV-KDGEIFFLGR 256
Cdd:pfam00501 331 LGSVGRPLPGTEVKIVDDEtGEPVPPGePGELCVRGPGvmKGYLNDPELTaeafDEDGWYR-TGDLGRRdEDGYLEIVGR 409
|
....*..
gi 1720413180 257 KDSQIKR 263
Cdd:pfam00501 410 KKDQIKL 416
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
36-343 |
1.13e-21 |
|
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: 99.17 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 36 HRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVlQATPTLLRRFGSELi 115
Cdd:cd17645 136 HRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALND-YFNQEGITI-SFLPTGAAEQFMQL- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 116 kstvlsAHTSLRVLALGGEafpsltILKswRGKGNRTQIFNIYGITEVSSWATFYRIPeeilnsavKHESPVQLGSPLLG 195
Cdd:cd17645 213 ------DNQSLRVLLTGGD------KLK--KIERKGYKLVNNYGPTENTVVATSFEID--------KPYANIPIGKPIDN 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 196 TVIEVRDQNGSPVLEG-TGQVFLGGK-------NRvcfldDEMT---------VPLGTMRATGDFVT-VKDGEIFFLGRK 257
Cdd:cd17645 271 TRVYILDEALQLQPIGvAGELCIAGEglargylNR-----PELTaekfivhpfVPGERMYRTGDLAKfLPDGNIEFLGRL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 258 DSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQ----ERLILFIVSKVDLVKDCIFKELQKHLPAHALPDDMVLIDT 333
Cdd:cd17645 346 DQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDadgrKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKA 425
|
330
....*....|
gi 1720413180 334 LPFTCHGKVD 343
Cdd:cd17645 426 LPLTANGKVD 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
30-425 |
5.54e-21 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 99.65 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 30 AIHYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKvLPSKLADILfSRHRVTVLQATPTLLRR 109
Cdd:PRK12316 2172 VAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELW-DPEQLYDEM-ERHGVTILDFPPVYLQQ 2249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 110 FGSELiksTVLSAHTSLRVLALGGEAFPSLTILKSWRGKGNrTQIFNIYGITE----VSSWATFYRIPEEilnsavkhES 185
Cdd:PRK12316 2250 LAEHA---ERDGRPPAVRVYCFGGEAVPAASLRLAWEALRP-VYLFNGYGPTEavvtPLLWKCRPQDPCG--------AA 2317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 186 PVQLGSPLLGTVIEVRDQNGSPV-LEGTGQVFLGGK-------NRVC-----FLDDEMTVPLGTMRATGDFVTVK-DGEI 251
Cdd:PRK12316 2318 YVPIGRALGNRRAYILDADLNLLaPGMAGELYLGGEglargylNRPGltaerFVPDPFSASGERLYRTGDLARYRaDGVV 2397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 252 FFLGRKDSQIKRHGKRLNIALVQ---QVAEELRQVESCAVTWYNQERLILFIV--SKVDLVKDCIFKELQKHLPAHALPD 326
Cdd:PRK12316 2398 EYLGRIDHQVKIRGFRIELGEIEarlQAHPAVREAVVVAQDGASGKQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPA 2477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 327 DMVLIDTLPFTCHGKVDVSELNKIYLdyiSSQPRNELHGKEELWGKLQYLWKSILCLPedpedtlKVPANSVFLDSGGDS 406
Cdd:PRK12316 2478 HWVVLERLPLNPNGKLDRKALPKPDV---SQLRQAYVAPQEGLEQRLAAIWQAVLKVE-------QVGLDDHFFELGGHS 2547
|
410
....*....|....*....
gi 1720413180 407 LKSMRLLSEIERLTGTAIP 425
Cdd:PRK12316 2548 LLATQVVSRVRQDLGLEVP 2566
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
38-349 |
1.01e-19 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 93.81 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 38 SLFDItQEDILFLA-SPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILFSRHrVTVLQATPT------LLRRF 110
Cdd:PRK04813 177 EDFAL-PEGPQFLNqAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLP-INVWVSTPSfadmclLDPSF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 111 GSELikstvlsaHTSLRVLALGGEAFPSLTIlKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEILNsavKHES-PVql 189
Cdd:PRK04813 255 NEEH--------LPNLTHFLFCGEELPHKTA-KKLLERFPSATIYNTYGPTEATVAVTSIEITDEMLD---QYKRlPI-- 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 190 GSPLLGTVIEVRDQNGSPVLEG-------TGQ-VFLGGKNrvcflDDEMT----VPLGTMRA--TGDFVTVKDGEIFFLG 255
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGeqgeiviSGPsVSKGYLN-----NPEKTaeafFTFDGQPAyhTGDAGYLEDGLLFYQG 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 256 RKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQE----RLILFIVSKVDLVKD------CIFKELQKHLPAHALP 325
Cdd:PRK04813 396 RIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDhkvqYLIAYVVPKEEDFERefeltkAIKKELKERLMEYMIP 475
|
330 340
....*....|....*....|....*...
gi 1720413180 326 DDMVLIDTLPFTCHGKVDV----SELNK 349
Cdd:PRK04813 476 RKFIYRDSLPLTPNGKIDRkaliEEVNK 503
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
30-342 |
1.47e-19 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 93.64 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 30 AIHYESHRSLFDITQEDILFLASPL---TFDPSVVeiFVSLSSGACLLI---VPTSVKvlPSKLADILfSRHRVTVLQAT 103
Cdd:COG0365 211 VHAATTAKYVLDLKPGDVFWCTADIgwaTGHSYIV--YGPLLNGATVVLyegRPDFPD--PGRLWELI-EKYGVTVFFTA 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 104 PTLLR---RFGSELIKSTVLSahtSLRVLALGGEAFPSLTILKsWR---GKgnrtQIFNIYGITEVSSWatfyripeeIL 177
Cdd:COG0365 286 PTAIRalmKAGDEPLKKYDLS---SLRLLGSAGEPLNPEVWEW-WYeavGV----PIVDGWGQTETGGI---------FI 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 178 NSAVKHesPVQLGS---PLLGTVIEVRDQNGSPVLEGT-GQVFLGGKNRVCFL----DDEMTV------PLGTMRaTGDF 243
Cdd:COG0365 349 SNLPGL--PVKPGSmgkPVPGYDVAVVDEDGNPVPPGEeGELVIKGPWPGMFRgywnDPERYRetyfgrFPGWYR-TGDG 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 244 VTV-KDGEIFFLGRKDSQIKRHGKRL---NI--ALVQ--QVAEelrqvesCAVTWYNQE----RLILFIVSK------VD 305
Cdd:COG0365 426 ARRdEDGYFWILGRSDDVINVSGHRIgtaEIesALVShpAVAE-------AAVVGVPDEirgqVVKAFVVLKpgvepsDE 498
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720413180 306 LVKDcIFKELQKHLPAHALPDDMVLIDTLPFTCHGKV 342
Cdd:COG0365 499 LAKE-LQAHVREELGPYAYPREIEFVDELPKTRSGKI 534
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
40-414 |
1.11e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 92.15 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 40 FDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADiLFSRHRVTVLQATPTLLRRFgselIKSTV 119
Cdd:PRK05691 1309 YALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAE-LVQQYGVTTLHFVPPLLQLF----IDEPL 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 120 LSAHTSLRVLALGGEAFPS------LTILKSwrgkgnrTQIFNIYGITEVSSWATFYRIpeeilNSAVKHESPVqlGSPL 193
Cdd:PRK05691 1384 AAACTSLRRLFSGGEALPAelrnrvLQRLPQ-------VQLHNRYGPTETAINVTHWQC-----QAEDGERSPI--GRPL 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 194 LGTVIEVRDQNGSPVLEGT-GQVFLGGK-------NRVCfLDDEMTV--PLGTMRA----TGDFVTVK-DGEIFFLGRKD 258
Cdd:PRK05691 1450 GNVLCRVLDAELNLLPPGVaGELCIGGAglargylGRPA-LTAERFVpdPLGEDGArlyrTGDRARWNaDGALEYLGRLD 1528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 259 SQIKRHGKRLNIALVQQVAEELRQVESCAV---TWYNQERLILFIVSKV--DLVKDCIFKELQKHLPAHALPDDMVLIDT 333
Cdd:PRK05691 1529 QQVKLRGFRVEPEEIQARLLAQPGVAQAAVlvrEGAAGAQLVGYYTGEAgqEAEAERLKAALAAELPEYMVPAQLIRLDQ 1608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 334 LPFTCHGKVDVSELNKIYLdyissQPRNELHGKEELWGKLQYLWKSILCLPedpedtlKVPANSVFLDSGGDSLKSMRLL 413
Cdd:PRK05691 1609 MPLGPSGKLDRRALPEPVW-----QQREHVEPRTELQQQIAAIWREVLGLP-------RVGLRDDFFALGGHSLLATQIV 1676
|
.
gi 1720413180 414 S 414
Cdd:PRK05691 1677 S 1677
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
25-347 |
3.93e-17 |
|
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: 85.22 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 25 KNEVWAIHYESHRSLFDiTQEDILFLASPlTFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILfSRHRVTVLQATP 104
Cdd:cd17656 151 KNMVNLLHFEREKTNIN-FSDKVLQFATC-SFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLV-KRHNIEVVFLPV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 105 TLLRRFGSEliKSTVLSAHTSLRVLALGGEAFPSLTILKSWRGKGNRTqIFNIYGITEvSSWATFYRIpeeilnsavKHE 184
Cdd:cd17656 228 AFLKFIFSE--REFINRFPTCVKHIITAGEQLVITNEFKEMLHEHNVH-LHNHYGPSE-THVVTTYTI---------NPE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 185 SPVQL----GSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGKN--RVCFLDDEMTV---------PLGTMRATGDFVT-VK 247
Cdd:cd17656 295 AEIPElppiGKPISNTWIYILDQEQQLQPQGIvGELYISGASvaRGYLNRQELTAekffpdpfdPNERMYRTGDLARyLP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 248 DGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAV-TWYNQER---LILFIVSKVDLVKDCIFKELQKHLPAHA 323
Cdd:cd17656 375 DGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVlDKADDKGekyLCAYFVMEQELNISQLREYLAKQLPEYM 454
|
330 340
....*....|....*....|....
gi 1720413180 324 LPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd17656 455 IPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
35-343 |
4.96e-16 |
|
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: 81.50 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSL----------FDITQEDILFLASPLT-FDPSVVEIFVSLSSGACLLIVPtsvKVLPSKLADiLFSRHRVTVLQAT 103
Cdd:cd17631 119 THRNLlwnavnalaaLDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVILR---KFDPETVLD-LIERHRVTSFFLV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 104 PTLLRRF-GSELIKSTVLSahtSLRVLALGGEAFPSLtILKSWRGKGnrTQIFNIYGITEVSSWATFYRiPEEILnsavk 182
Cdd:cd17631 195 PTMIQALlQHPRFATTDLS---SLRAVIYGGAPMPER-LLRALQARG--VKFVQGYGMTETSPGVTFLS-PEDHR----- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 183 hESPVQLGSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGKNRV-CFLDDE----MTVPLGTMRaTGDFVTV-KDGEIFFLG 255
Cdd:cd17631 263 -RKLGSAGRPVFFVEVRIVDPDGREVPPGEvGEIVVRGPHVMaGYWNRPeataAAFRDGWFH-TGDLGRLdEDGYLYIVD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 256 RKDSQIKRHGKrlNI--ALVQQVAEELRQVESCAV------TWynQERLILFIV--SKVDLVKDCIFKELQKHLPAHALP 325
Cdd:cd17631 341 RKKDMIISGGE--NVypAEVEDVLYEHPAVAEVAVigvpdeKW--GEAVVAVVVprPGAELDEDELIAHCRERLARYKIP 416
|
330
....*....|....*...
gi 1720413180 326 DDMVLIDTLPFTCHGKVD 343
Cdd:cd17631 417 KSVEFVDALPRNATGKIL 434
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
91-414 |
5.34e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 83.29 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 91 LFSRHRVTVLQATPTllrrFGSELIKSTVLSAHT-SLRVLALGGEAfpsLT--ILKSWRGKGNRTQIFNIYGITEVSSWA 167
Cdd:PRK05691 2418 LIREQQVSILGFTPS----YGSQLAQWLAGQGEQlPVRMCITGGEA---LTgeHLQRIRQAFAPQLFFNAYGPTETVVMP 2490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 168 TFYRIPEEILNSAvkheSPVQLGSPLLGTVIEVRDQNGSPVLEG-TGQVFLGGK--------------NRvcFLDDEMTV 232
Cdd:PRK05691 2491 LACLAPEQLEEGA----ASVPIGRVVGARVAYILDADLALVPQGaTGELYVGGAglaqgyhdrpgltaER--FVADPFAA 2564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 233 PLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQE---RLILFIVSKV---- 304
Cdd:PRK05691 2565 DGGRLYRTGDLVRLRaDGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPsgkQLAGYLVSAVagqd 2644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 305 ----DLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVDVS-------ELNKiyLDYIssQPRNELhgkEElwgKL 373
Cdd:PRK05691 2645 deaqAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRalpapdpELNR--QAYQ--APRSEL---EQ---QL 2714
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1720413180 374 QYLWKSILclpedpeDTLKVPANSVFLDSGGDSLKSMRLLS 414
Cdd:PRK05691 2715 AQIWREVL-------NVERVGLGDNFFELGGDSILSIQVVS 2748
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
29-343 |
8.46e-15 |
|
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: 76.29 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 29 WAIHYESHRSLFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLIvptSVKVLPSKLADILfSRHRVTVLQATPTLLR 108
Cdd:cd17633 25 WIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNPKSWIRKI-NQYNATVIYLVPTMLQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 109 rfgsELIKstVLSAHTSLRVLALGGEAFPSLTiLKSWRGKGNRTQIFNIYGITEVSSWAtfYRIPEEIlnsavkhESPVQ 188
Cdd:cd17633 101 ----ALAR--TLEPESKIKSIFSSGQKLFEST-KKKLKNIFPKANLIEFYGTSELSFIT--YNFNQES-------RPPNS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 189 LGSPLLGTVIEVRDQNGSPVlegtGQVFLGGKNRVCFLDDEMTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKR 267
Cdd:cd17633 165 VGRPFPNVEIEIRNADGGEI----GKIFVKSEMVFSGYVRGGFSNPDGWMSVGDIGYVDeEGYLYLVGRESDMIIIGGIN 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720413180 268 LNIALVQQVAEELRQVESCAVTWYNQER---LILFIVSKVDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVD 343
Cdd:cd17633 241 IFPTEIESVLKAIPGIEEAIVVGIPDARfgeIAVALYSGDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
545-696 |
2.34e-14 |
|
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: 75.62 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 545 DENLEKPPLFQQGSPVVgamamALRERWRSDTGKCVDASPLLVRAAVQDkpsTTVYIGSHSHTVKAVDLSSGETRWEQLL 624
Cdd:COG1520 14 EDDEPPPAPLPEFEPSV-----KVKQLWSASVGDGVGKGYSRLAPAVAG---DRVYAADADGRVAALDAATGKELWRVDL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720413180 625 GDRIesSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWTFTTEDAVKSSPAVDptTGLIYVGSHDQHAYALD 696
Cdd:COG1520 86 GEPL--SGGVGADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAPAVA--GGRVVVRTGDGRVYALD 153
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
607-827 |
5.85e-14 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 72.44 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 607 TVKAVDLSSGETRWEQLLGDRIESSACVSkcGNFIVVGCYNGLVYVLKSNSGEKYWTFTTEDAVKSSPAVDptTGLIYVG 686
Cdd:pfam13360 4 VVTALDAATGAELWRVDLETGLGGGVAVD--GGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVA--GGRVFVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 687 SHDQHAYALDIYEKKCVWKL---NCEGALFSSPCVSLSPHHLYCATLGGLLLALNPASGSTVWKRSCGKP---------- 753
Cdd:pfam13360 80 AGDGSLIALDAADGRRLWSYqrsGEPLALRSSGSPAVVGDTVVAGFSSGKLVALDPATGKVRWEAPLAAPrgtnelerlv 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720413180 754 -LFSSPRCYQQYICIGCVDGSLLCF-THSGEQVWRFAAGGPifSSPCVsaAEQEIFFGSHDCFIYCCS-KEGHLRWK 827
Cdd:pfam13360 160 dITGTPVVAGGRVFASAYQGRLVAFdAATGRRLWTREISGP--NGPIL--DGDLLYVVSDDGELYALDrATGAVVWK 232
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
35-342 |
7.47e-14 |
|
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: 73.83 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSLF-----------DITQEDILFLASPLTFDPSVVEIFVSL-SSGACllIVPTSVKVLPSKLADILFsrHRVTVLQA 102
Cdd:cd17635 22 ANKTFFavpdilqkeglNWVVGDVTYLPLPATHIGGLWWILTCLiHGGLC--VTGGENTTYKSLFKILTT--NAVTTTCL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 103 TPTLLRRFGSELiKSTvLSAHTSLRVLALGGE-AFPSLTILKSWRGKgnrTQIFNIYGITEVSSwATFYRIPEEILN-SA 180
Cdd:cd17635 98 VPTLLSKLVSEL-KSA-NATVPSLRLIGYGGSrAIAADVRFIEATGL---TNTAQVYGLSETGT-ALCLPTDDDSIEiNA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 181 VkhespvqlGSPLLGTVIEVRDQNGSPVLEGTGQVFLGGKNRVC---FLDDEMT--VPLGTMRATGDFV-TVKDGEIFFL 254
Cdd:cd17635 172 V--------GRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMlgyWNNPERTaeVLIDGWVNTGDLGeRREDGFLFIT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 255 GRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQ----ERLILFIVSKVDLVKDCI--FKE-LQKHLPAHALPDD 327
Cdd:cd17635 244 GRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDeefgELVGLAVVASAELDENAIraLKHtIRRELEPYARPST 323
|
330
....*....|....*
gi 1720413180 328 MVLIDTLPFTCHGKV 342
Cdd:cd17635 324 IVIVTDIPRTQSGKV 338
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
87-347 |
1.44e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 74.58 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 87 LADIlfSRHRVTVLQATPTLLRRF---GSELIKSTVLSahtSLRVLALGGEAF-PSLtilkswrgkGNRTQ------IFN 156
Cdd:PRK07788 288 LEDI--AKHKATALVVVPVMLSRIldlGPEVLAKYDTS---SLKIIFVSGSALsPEL---------ATRALeafgpvLYN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 157 IYGITEVSsWATFYRiPEEILnsavkhESPVQLGSPLLGTVIEVRDQNGSPVLEG-TGQVFLGG------------KNRV 223
Cdd:PRK07788 354 LYGSTEVA-FATIAT-PEDLA------EAPGTVGRPPKGVTVKILDENGNEVPRGvVGRIFVGNgfpfegytdgrdKQII 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 224 cflDDEMtvplgtmrATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAV------TWYnqERL 296
Cdd:PRK07788 426 ---DGLL--------SSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVigvddeEFG--QRL 492
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1720413180 297 ILFIVSK--VDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:PRK07788 493 RAFVVKApgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
39-353 |
7.00e-13 |
|
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: 72.52 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 39 LFDITQEDILFLASPLTFDPSVVEIFVSLSSGACLLI---VPTSVKvlPSKLADiLFSRHRVTVLQATPTLLRRF---GS 112
Cdd:cd05968 272 QFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgAPDHPK--ADRLWR-MVEDHEITHLGLSPTLIRALkprGD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 113 ELIKSTVLSahtSLRVLALGGEAFPsltiLKSW------RGKGnRTQIFNIYGITEVSSwatfyripeEIL-NSAVKHES 185
Cdd:cd05968 349 APVNAHDLS---SLRVLGSTGEPWN----PEPWnwlfetVGKG-RNPIINYSGGTEISG---------GILgNVLIKPIK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 186 PVQLGSPLLGTVIEVRDQNGSPVLEGTGQVFL----GGKNRVCFLDDEMTVPLGTMR-----ATGDFVTVKDGEIFF-LG 255
Cdd:cd05968 412 PSSFNGPVPGMKADVLDESGKPARPEVGELVLlapwPGMTRGFWRDEDRYLETYWSRfdnvwVHGDFAYYDEEGYFYiLG 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 256 RKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQ----ERLILFIVSKVDLVKDCIFKE-----LQKHLPAHALPD 326
Cdd:cd05968 492 RSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHpvkgEAIVCFVVLKPGVTPTEALAEelmerVADELGKPLSPE 571
|
330 340
....*....|....*....|....*..
gi 1720413180 327 DMVLIDTLPFTCHGKVDVSELNKIYLD 353
Cdd:cd05968 572 RILFVKDLPKTRNAKVMRRVIRAAYLG 598
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
545-696 |
4.05e-12 |
|
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: 68.81 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 545 DENLEKPPLFQQGSPVVgamamALRERWRSDTGKCVDASPLLVRAAVQDkpsTTVYIGSHSHTVKAVDLSSGETRWEQLL 624
Cdd:TIGR03300 22 EDDEPQPAELPEFQPTV-----KVDQVWSASVGDGVGHYYLRLQPAVAG---GKVYAADADGTVAALDAETGKRLWRVDL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720413180 625 GDRIesSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWTFTTEDAVKSSPAVDptTGLIYVGSHDQHAYALD 696
Cdd:TIGR03300 94 DERL--SGGVGADGGLVFVGTEKGEVIALDAEDGKELWRAKLSSEVLSPPLVA--NGLVVVRTNDGRLTALD 161
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
32-342 |
9.46e-12 |
|
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: 68.30 E-value: 9.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 32 HYESHRSLFDITQEDILFLasplTFDPSVVE-----IFVSLSSGACLLIVPTsvKVLPSKLADILfSRHRVTVLQATPTL 106
Cdd:cd05969 117 YYFTGKYVLDLHPDDIYWC----TADPGWVTgtvygIWAPWLNGVTNVVYEG--RFDAESWYGII-ERVKVTVWYTAPTA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 107 LR---RFGSELIKSTVLSahtSLRVLALGGEAFPSLTIlkSWRGKGNRTQIFNIYGITEVSSWAtfyripeeILNSAVKH 183
Cdd:cd05969 190 IRmlmKEGDELARKYDLS---SLRFIHSVGEPLNPEAI--RWGMEVFGVPIHDTWWQTETGSIM--------IANYPCMP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 184 ESPVQLGSPLLGTVIEVRDQNGSPVLEGT-GQVFL--------------GGKNRVCFLDDEMTvplgtmraTGDFVTV-K 247
Cdd:cd05969 257 IKPGSMGKPLPGVKAAVVDENGNELPPGTkGILALkpgwpsmfrgiwndEERYKNSFIDGWYL--------TGDLAYRdE 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 248 DGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTW----YNQERLILFIVSK-----VDLVKDCIFKELQKH 318
Cdd:cd05969 329 DGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGkpdpLRGEIIKAFISLKegfepSDELKEEIINFVRQK 408
|
330 340
....*....|....*....|....
gi 1720413180 319 LPAHALPDDMVLIDTLPFTCHGKV 342
Cdd:cd05969 409 LGAHVAPREIEFVDNLPKTRSGKI 432
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
37-347 |
1.10e-11 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 67.87 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 37 RSLFDITQEDILFLASPLTFDPSV-VEIFVSLSSGACLLIVPTSVKvlPSKLAdILFSRHRVTVLQATPTLLRRfgseLI 115
Cdd:cd05919 125 REALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWPT--AERVL-ATLARFRPTVLYGVPTFYAN----LL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 116 KSTVLSAH--TSLRVLALGGEAFPsLTILKSWRGKGNrTQIFNIYGITEVSSwaTFyripeeiLNSAVKHESPVQLGSPL 193
Cdd:cd05919 198 DSCAGSPDalRSLRLCVSAGEALP-RGLGERWMEHFG-GPILDGIGATEVGH--IF-------LSNRPGAWRLGSTGRPV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 194 LGTVIEVRDQNGSPVLEGT-GQVFLGG--------KNRvcflDDEMTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKR 263
Cdd:cd05919 267 PGYEIRLVDEEGHTIPPGEeGDLLVRGpsaavgywNNP----EKSRATFNGGWYRTGDKFCRdADGWYTHAGRADDMLKV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 264 HGKRLNIALVQQVAEELRQVESCAVTWY-NQERLI---LFIVSKVDLVKDCIFKE-----LQKHLPAHALPDDMVLIDTL 334
Cdd:cd05919 343 GGQWVSPVEVESLIIQHPAVAEAAVVAVpESTGLSrltAFVVLKSPAAPQESLARdihrhLLERLSAHKVPRRIAFVDEL 422
|
330
....*....|...
gi 1720413180 335 PFTCHGKVDVSEL 347
Cdd:cd05919 423 PRTATGKLQRFKL 435
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
91-347 |
1.21e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 68.25 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 91 LFSRHRVTVLQATPTLLRRFgSELIKStVLSAHT--SLRVLALGGEAFPSLTILKSWRGKGNrtQIFNIYGITEVSSWAT 168
Cdd:PRK13382 279 LIDRHRATGLAVVPVMFDRI-MDLPAE-VRNRYSgrSLRFAAASGSRMRPDVVIAFMDQFGD--VIYNNYNATEAGMIAT 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 169 fyRIPEEIlnsavkHESPVQLGSPLLGTVIEVRDQNGSPVLEG-TGQVFLggKNRVCFldDEMTVplGT-------MRAT 240
Cdd:PRK13382 355 --ATPADL------RAAPDTAGRPAEGTEIRILDQDFREVPTGeVGTIFV--RNDTQF--DGYTS--GStkdfhdgFMAS 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 241 GDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQE----RLILFIVSKVDLVK--DCIFK 313
Cdd:PRK13382 421 GDVGYLDEnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEqygqRLAAFVVLKPGASAtpETLKQ 500
|
250 260 270
....*....|....*....|....*....|....
gi 1720413180 314 ELQKHLPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:PRK13382 501 HVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
94-347 |
3.79e-11 |
|
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: 66.22 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 94 RHRVTVLQATPTLLRRfgseLIKSTVLSAHTSLRVLALGGEAFPsLTILKSWRGKGnrTQIFNIYGITEVSS-WATFYri 172
Cdd:cd05912 163 SGKVTIISVVPTMLQR----LLEILGEGYPNNLRCILLGGGPAP-KPLLEQCKEKG--IPVYQSYGMTETCSqIVTLS-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 173 PEEILN---SAvkhespvqlGSPLLGTVIEVRDQNGSPvlEGTGQVFLGGKNRV-CFL---DDEMTVPLGTMRATGDFVT 245
Cdd:cd05912 234 PEDALNkigSA---------GKPLFPVELKIEDDGQPP--YEVGEILLKGPNVTkGYLnrpDATEESFENGWFKTGDIGY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 246 V-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAV------TWynQERLILFIVSKVDLVKDCIFKELQKH 318
Cdd:cd05912 303 LdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVvgipddKW--GQVPVAFVVSERPISEEELIAYCSEK 380
|
250 260
....*....|....*....|....*....
gi 1720413180 319 LPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd05912 381 LAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
55-425 |
5.71e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.12 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 55 TFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADILFSRhRVTVLQATPTLLRRFGSElikstVLSAHTSLRVLALGGE 134
Cdd:PRK05691 3920 SFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQ-GITVLESVPSLIQGMLAE-----DRQALDGLRWMLPTGE 3993
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 135 AFPSLtILKSWRGKGNRTQIFNIYGITEVSSWATFYRIPEEILNSAVkhespVQLGSP-------LLGTVIEVRDQNGSP 207
Cdd:PRK05691 3994 AMPPE-LARQWLQRYPQIGLVNAYGPAECSDDVAFFRVDLASTRGSY-----LPIGSPtdnnrlyLLDEALELVPLGAVG 4067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 208 VL----EGTGQVFLGGKNRVC--FLDDEMTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEEL 280
Cdd:PRK05691 4068 ELcvagTGVGRGYVGDPLRTAlaFVPHPFGAPGERLYRTGDLARRrSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQ 4147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 281 RQVESCAV---TWYNQERLILFIV-SKVDLVKDCIFKELQKHLPAhALPDDMV-----LIDTLPFTCHGKVDVSELNKIY 351
Cdd:PRK05691 4148 AEVREAAVavqEGVNGKHLVGYLVpHQTVLAQGALLERIKQRLRA-ELPDYMVplhwlWLDRLPLNANGKLDRKALPALD 4226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 352 LDYISSQ----PRNELhgkEElwgKLQYLWKsilclpedpeDTLKVPANSV---FLDSGGDSLKSMRLLSEIERLTGTAI 424
Cdd:PRK05691 4227 IGQLQSQaylaPRNEL---EQ---TLATIWA----------DVLKVERVGVhdnFFELGGHSLLATQIASRVQKALQRNV 4290
|
.
gi 1720413180 425 P 425
Cdd:PRK05691 4291 P 4291
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
659-905 |
1.25e-10 |
|
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: 64.28 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 659 EKYWTFTTEDAVKSSPAVDptTGLIYVGSHDQHAYALDIYEKKCVWKLNCEGALFSSPCVSLSPHHLYCATLGGLLLALN 738
Cdd:cd10276 19 SKSVGNGGMAGIDLTPVVA--GDMVYAADANGQVSAFNATTGKIIWETSLSGKGFLGGTPAVGNGKIFVGTESGYLYALD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 739 PASGSTVWKRSCGKPLFSSPRCYQQ-YICIGCVDGSLLCF-THSGEQVWRFAAGGPIFSSPCVSA---AEQEIFFGSHDC 813
Cdd:cd10276 97 AKDGSELWRTEVSDSQLLSPPTYADgKIYVGTGDGRLYYCnAETGKVVWNRTSTAPELSLRGGAApvgAYDVVFVGDGNG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 814 FIYCCSKE-GHLRWKFETTARVYATP----FAFSNHPRSDDALLAAASTDGKLWVLESRSGELRSVYELpGEVFSSPVVW 888
Cdd:cd10276 177 TVVALNTGtGVDIWEFSVSEPRGRTElprmIDSSVTYVVVGGYLYSTSYQGYLVALDFESGQFLWSRKA-SGGTSTSTDA 255
|
250
....*....|....*..
gi 1720413180 889 ESMLVIGCRNNYIYCLD 905
Cdd:cd10276 256 NGRVYVGDGEGSLYCLD 272
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
84-342 |
1.44e-10 |
|
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: 64.91 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 84 PSKLADILfSRHRVTVLQATPTLLRRF---GSELIKSTVLSahtSLRVLALGGEAFPSLTILKSWR--GKGNRTQIfNIY 158
Cdd:cd17634 315 PARMWQVV-DKHGVNILYTAPTAIRALmaaGDDAIEGTDRS---SLRILGSVGEPINPEAYEWYWKkiGKEKCPVV-DTW 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 159 GITEVSsWATFYRIPEEIlnsAVKHESPVQlgsPLLGTVIEVRDQNGSPVLEGT-GQVFLG----GKNRVCFLDDE--MT 231
Cdd:cd17634 390 WQTETG-GFMITPLPGAI---ELKAGSATR---PVFGVQPAVVDNEGHPQPGGTeGNLVITdpwpGQTRTLFGDHErfEQ 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 232 VPLGT---MRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQE----RLILFIVSK 303
Cdd:cd17634 463 TYFSTfkgMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAikgqAPYAYVVLN 542
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720413180 304 V-----DLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKV 342
Cdd:cd17634 543 HgvepsPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
84-347 |
2.07e-10 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 63.99 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 84 PSKLADILfSRHRVTVLQATPTLLR--RFGSELIKSTVLSahtsLRVLALGGEafPSLTILKSWRGKGNRTQIFNIYGIT 161
Cdd:cd05971 170 PKAALDLM-SRYGVTTAFLPPTALKmmRQQGEQLKHAQVK----LRAIATGGE--SLGEELLGWAREQFGVEVNEFYGQT 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 162 E----VSSwatfyripeeilNSAVKHESPVQLGSPLLGTVIEVRDQNGSPVLEG-TGQVFLGGKNRVCFL----DDEMTV 232
Cdd:cd05971 243 EcnlvIGN------------CSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGeVGEIAVELPDPVAFLgywnNPSATE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 233 --PLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWY----NQERLILFIVSKVD 305
Cdd:cd05971 311 kkMAGDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdpiRGEIVKAFVVLNPG 390
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720413180 306 LVK-DCIFKELQKH----LPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd05971 391 ETPsDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
63-349 |
2.87e-10 |
|
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: 63.51 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 63 IFVSLSSGACLlIVPTSVKVLPSKLADILfSRHRVTVLQATPTLLRRFGSELIKSTVLSahtSLRVLALGGEafpSLT-- 140
Cdd:cd05972 141 FFGPWLLGATV-FVYEGPRFDAERILELL-ERYGVTSFCGPPTAYRMLIKQDLSSYKFS---HLRLVVSAGE---PLNpe 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 141 ILKSWRGKGNRTqIFNIYGITEVS-SWATFYRIPeeilnsaVKhesPVQLGSPLLGTVIEVRDQNGSPVLEGT-G----- 213
Cdd:cd05972 213 VIEWWRAATGLP-IRDGYGQTETGlTVGNFPDMP-------VK---PGSMGRPTPGYDVAIIDDDGRELPPGEeGdiaik 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 214 ----QVFLGgknrvcFLDDEMtvplgTMRA--------TGDFVTV-KDGEIFFLGRKDSQIKRHGKR-----LNIALVQQ 275
Cdd:cd05972 282 lpppGLFLG------YVGDPE-----KTEAsirgdyylTGDRAYRdEDGYFWFVGRADDIIKSSGYRigpfeVESALLEH 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 276 VAeelrqVESCAVtwynqerlilfiVSKVD-----LVK------------DCIFKELQKH----LPAHALPDDMVLIDTL 334
Cdd:cd05972 351 PA-----VAEAAV------------VGSPDpvrgeVVKafvvltsgyepsEELAEELQGHvkkvLAPYKYPREIEFVEEL 413
|
330
....*....|....*
gi 1720413180 335 PFTCHGKVDVSELNK 349
Cdd:cd05972 414 PKTISGKIRRVELRD 428
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
35-343 |
2.90e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 63.67 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSLF----------DITQEDILFLASPLtfdpsvveiFVSLSSGACLLIVPTSVKVL------PSKLADiLFSRHRVT 98
Cdd:PRK06187 188 SHRNLFlhslavcawlKLSRDDVYLVIVPM---------FHVHAWGLPYLALMAGAKQViprrfdPENLLD-LIETERVT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 99 VLQATPTLLRRFGSELIKSTV-LSahtSLRVLALGGEAFPsLTILKSWRGKgNRTQIFNIYGITEVSSWATFYRIPEEIL 177
Cdd:PRK06187 258 FFFAVPTIWQMLLKAPRAYFVdFS---SLRLVIYGGAALP-PALLREFKEK-FGIDLVQGYGMTETSPVVSVLPPEDQLP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 178 NSAVKHESpvqLGSPLLGTVIEVRDQNGSPVLEGTGQV-------------FLGGKNrvcflDDEMTVPLGTMRaTGDFV 244
Cdd:PRK06187 333 GQWTKRRS---AGRPLPGVEARIVDDDGDELPPDGGEVgeiivrgpwlmqgYWNRPE-----ATAETIDGGWLH-TGDVG 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 245 TV-KDGEIFFLGRKDSQIKRHGKrlNI--ALVQQVAEELRQVESCAV------TWynQERLILFIVSKVDlvKDCIFKEL 315
Cdd:PRK06187 404 YIdEDGYLYITDRIKDVIISGGE--NIypRELEDALYGHPAVAEVAVigvpdeKW--GERPVAVVVLKPG--ATLDAKEL 477
|
330 340 350
....*....|....*....|....*....|..
gi 1720413180 316 QKHLPAH----ALPDDMVLIDTLPFTCHGKVD 343
Cdd:PRK06187 478 RAFLRGRlakfKLPKRIAFVDELPRTSVGKIL 509
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
91-343 |
6.00e-10 |
|
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: 62.73 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 91 LFSRHRVTVLQATPTLLRRFGSELIKSTvlSAHTSLRVLALGGEAFPSLTILKSWRGKGNRTQifNIYGITEvsSWATFY 170
Cdd:cd05920 224 LIEREGVTVTALVPALVSLWLDAAASRR--ADLSSLRLLQVGGARLSPALARRVPPVLGCTLQ--QVFGMAE--GLLNYT 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 171 RI---PEEILNSAVKHESPvqlgspllGTVIEVRDQNGSPVLEG-TGQVFLGG------------KNRVCFLDDemtvpl 234
Cdd:cd05920 298 RLddpDEVIIHTQGRPMSP--------DDEIRVVDEEGNPVPPGeEGELLTRGpytirgyyrapeHNARAFTPD------ 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 235 GTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTW----YNQERLILFIVSK---VDL 306
Cdd:cd05920 364 GFYR-TGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAmpdeLLGERSCAFVVLRdppPSA 442
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720413180 307 VkdcifkELQKHL-----PAHALPDDMVLIDTLPFTCHGKVD 343
Cdd:cd05920 443 A------QLRRFLrerglAAYKLPDRIEFVDSLPLTAVGKID 478
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
37-343 |
1.50e-09 |
|
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: 61.62 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 37 RSLFDITQEDILFLASPLTFDPSVVE-IFVSLSSGACLLIVPTSVKvlPSKLADILfSRHRVTVLQATPTL----LRrfg 111
Cdd:cd05959 197 RNVLGIREDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLMPERPT--PAAVFKRI-RRYRPTVFFGVPTLyaamLA--- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 112 SELIKSTVLSahtSLRVLALGGEAFPSlTILKSWRgkgNRT--QIFNIYGITEVSswatfyripeEILNSAVKHES-PVQ 188
Cdd:cd05959 271 APNLPSRDLS---SLRLCVSAGEALPA-EVGERWK---ARFglDILDGIGSTEML----------HIFLSNRPGRVrYGT 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 189 LGSPLLGTVIEVRDQNGSPVLEG-TGQVFL-GGKNRVCFL---DDEMTVPLGTMRATGD-FVTVKDGEIFFLGRKDSQIK 262
Cdd:cd05959 334 TGKPVPGYEVELRDEDGGDVADGePGELYVrGPSSATMYWnnrDKTRDTFQGEWTRTGDkYVRDDDGFYTYAGRADDMLK 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 263 RHGKRLNIALVQQVAEELRQVESCAVT-WYNQERLI---LFIVSKVDL-VKDCIFKELQKH----LPAHALPDDMVLIDT 333
Cdd:cd05959 414 VSGIWVSPFEVESALVQHPAVLEAAVVgVEDEDGLTkpkAFVVLRPGYeDSEALEEELKEFvkdrLAPYKYPRWIVFVDE 493
|
330
....*....|
gi 1720413180 334 LPFTCHGKVD 343
Cdd:cd05959 494 LPKTATGKIQ 503
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
35-347 |
2.92e-09 |
|
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: 60.27 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSLF------------DITQEDILFLASPL--TFDPSVVeIFVSLSSGACLLIVPTSVkvLPSKLADIlfSRHRVTVL 100
Cdd:cd05936 146 THRNLVanalqikawledLLEGDDVVLAALPLfhVFGLTVA-LLLPLALGATIVLIPRFR--PIGVLKEI--RKHRVTIF 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 101 QATPTLLrrfgSELIKSTVLSAH--TSLRVLALGGEAFPsLTILKSWRGKgNRTQIFNIYGITEVSSWATFyripeeilN 178
Cdd:cd05936 221 PGVPTMY----IALLNAPEFKKRdfSSLRLCISGGAPLP-VEVAERFEEL-TGVPIVEGYGLTETSPVVAV--------N 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 179 SAVKHESPVQLGSPLLGTVIEVRDQNGSPVLEG-TG-------QVFLGGKNRvcflddemtvPLGTMRA-------TGDF 243
Cdd:cd05936 287 PLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGeVGelwvrgpQVMKGYWNR----------PEETAEAfvdgwlrTGDI 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 244 VTV-KDGEIFFLGRKDSQIKRHGkrLNI--ALVQQVAEELRQVESCAVTW----YNQERLILFIVSK--VDLVKDCIFKE 314
Cdd:cd05936 357 GYMdEDGYFFIVDRKKDMIIVGG--FNVypREVEEVLYEHPAVAEAAVVGvpdpYSGEAVKAFVVLKegASLTEEEIIAF 434
|
330 340 350
....*....|....*....|....*....|...
gi 1720413180 315 LQKHLPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd05936 435 CREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
647-870 |
6.40e-09 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 57.41 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 647 NGLVYVLKSNSGEKYWTFTTEDAVKSSPAVDptTGLIYVGSHDQHAYALDIYEKKCVWKLNCEGALFSSPCVslSPHHLY 726
Cdd:pfam13360 2 DGVVTALDAATGAELWRVDLETGLGGGVAVD--GGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLV--AGGRVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 727 CATLGGLLLALNPASGSTVWKRSCGKPLF-----SSPRCYQQYICIGCVDGSLLCF-THSGEQVW-----------RFAA 789
Cdd:pfam13360 78 VVAGDGSLIALDAADGRRLWSYQRSGEPLalrssGSPAVVGDTVVAGFSSGKLVALdPATGKVRWeaplaaprgtnELER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 790 GGPIFSSPCVsaAEQEIFFGSHdcfiyccsKEGHLRWKFETTARVYATPFAFSNHPRSDDALLAAASTDGKLWVLESRSG 869
Cdd:pfam13360 158 LVDITGTPVV--AGGRVFASAY--------QGRLVAFDAATGRRLWTREISGPNGPILDGDLLYVVSDDGELYALDRATG 227
|
.
gi 1720413180 870 E 870
Cdd:pfam13360 228 A 228
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
93-347 |
3.31e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 57.31 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 93 SRHRVTVLQATPTLLRRFGSELIKSTVLSAHTSLRVLALGGEAF-PSLtilkswrgkGNRTQ------IFNIYGITEVSS 165
Cdd:PRK13383 261 SLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLdPTL---------GQRFMdtygdiLYNGYGSTEVGI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 166 WAtfYRIPEEIlnsavkHESPVQLGSPLLGTVIEVRDQNGSPV-LEGTGQVFLGGK-NRVCFLDDEMTVPLGTMRATGDF 243
Cdd:PRK13383 332 GA--LATPADL------RDAPETVGKPVAGCPVRILDRNNRPVgPRVTGRIFVGGElAGTRYTDGGGKAVVDGMTSTGDM 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 244 VTVKD-GEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQE----RLILFIVSK--VDLVKDCIFKELQ 316
Cdd:PRK13383 404 GYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErfghRLAAFVVLHpgSGVDAAQLRDYLK 483
|
250 260 270
....*....|....*....|....*....|.
gi 1720413180 317 KHLPAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:PRK13383 484 DRVSRFEQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
35-349 |
7.38e-08 |
|
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: 55.80 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSL----------FDITQEDILFLASPL--TFDPSVVEIFVSLSSGAcllIV----PTSVKVLPSKLADIlfsrhRVT 98
Cdd:cd05909 168 SHKNLlanveqitaiFDPNPEDVVFGALPFfhSFGLTGCLWLPLLSGIK---VVfhpnPLDYKKIPELIYDK-----KAT 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 99 VLQATPTLLRRFgselIKSTVLSAHTSLRVLALGGEAFPSlTILKSWRGK-GNRtqIFNIYGITEVSswatfyriPEEIL 177
Cdd:cd05909 240 ILLGTPTFLRGY----ARAAHPEDFSSLRLVVAGAEKLKD-TLRQEFQEKfGIR--ILEGYGTTECS--------PVISV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 178 NSAVKHESPVQLGSPLLGtvIEVR---DQNGSPVLEG-TGQVFLGGKNRVC-FLDDE---MTVPLGTMRATGDFVTV-KD 248
Cdd:cd05909 305 NTPQSPNKEGTVGRPLPG--MEVKivsVETHEEVPIGeGGLLLVRGPNVMLgYLNEPeltSFAFGDGWYDTGDIGKIdGE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 249 GEIFFLGRKDSQIKRHGKRLNIALVQQVAEEL--RQVESCAVTWYNQ---ERLILFIVSKvDLVKDcifkELQKHLPAH- 322
Cdd:cd05909 383 GFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGrkgEKIVLLTTTT-DTDPS----SLNDILKNAg 457
|
330 340 350
....*....|....*....|....*....|.
gi 1720413180 323 ----ALPDDMVLIDTLPFTCHGKVDVSELNK 349
Cdd:cd05909 458 isnlAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
91-351 |
1.45e-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: 54.98 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 91 LFSRHRVTVLQAtP----TLLRRFGSELIKSTV-LSahtSLRVLALGGEAFPSLTI---LKSWRGKGNRTQIFN-IYGIT 161
Cdd:cd05906 255 LIDRYRVTITWA-PnfafALLNDLLEEIEDGTWdLS---SLRYLVNAGEAVVAKTIrrlLRLLEPYGLPPDAIRpAFGMT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 162 EVSSWATFYRIPEEiLNSAVKHESpVQLGSPLLGTVIEVRDQNGSPVLEGT-------GQVFLGG------KNRVCFLDD 228
Cdd:cd05906 331 ETCSGVIYSRSFPT-YDHSQALEF-VSLGRPIPGVSMRIVDDEGQLLPEGEvgrlqvrGPVVTKGyynnpeANAEAFTED 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 229 emtvplGTMRaTGDFVTVKDGEIFFLGRKDSQIKRHGkrLNIAL--VQQVAEELRQVES-----CAVTWYNQ--ERLILF 299
Cdd:cd05906 409 ------GWFR-TGDLGFLDNGNLTITGRTKDTIIVNG--VNYYSheIEAAVEEVPGVEPsftaaFAVRDPGAetEELAIF 479
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720413180 300 IVSKVDLVKDC--IFKELQKHL-------PAHALPDDMvliDTLPFTCHGKVDVSELNKIY 351
Cdd:cd05906 480 FVPEYDLQDALseTLRAIRSVVsrevgvsPAYLIPLPK---EEIPKTSLGKIQRSKLKAAF 537
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
94-342 |
1.54e-07 |
|
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: 54.83 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 94 RHRVTVLQATPTLLRRfgseLIKSTVLSAHT---SLRVLALGGEAFPSLTIlkSWRGKGNRTQIFNIYGITEVSSwatfy 170
Cdd:cd05973 176 RLGVTNLAGSPTAYRL----LMAAGAEVPARpkgRLRRVSSAGEPLTPEVI--RWFDAALGVPIHDHYGQTELGM----- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 171 ripeeILNSAVKHESPVQLGS---PLLGTVIEVRDQNGSPVLEGT-GQVFLGGKNRVC-----FLDDEMTVPLGTMRATG 241
Cdd:cd05973 245 -----VLANHHALEHPVHAGSagrAMPGWRVAVLDDDGDELGPGEpGRLAIDIANSPLmwfrgYQLPDTPAIDGGYYLTG 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 242 DFVTVK-DGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTW----YNQERLILFIV------SKVDLVkdc 310
Cdd:cd05973 320 DTVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGvpdpERTEVVKAFVVlrggheGTPALA--- 396
|
250 260 270
....*....|....*....|....*....|....*.
gi 1720413180 311 ifKELQKH----LPAHALPDDMVLIDTLPFTCHGKV 342
Cdd:cd05973 397 --DELQLHvkkrLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| BamB_YfgL |
cd10276 |
Beta-barrel assembly machinery (Bam) complex component B and related proteins; BamB (YflG) is ... |
599-906 |
2.62e-07 |
|
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: 53.87 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 599 VYIGSHSHTVKAVDLSSGETRWEQLLGDRIESSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWTFTTEDAVKSSPavdP 678
Cdd:cd10276 41 VYAADANGQVSAFNATTGKIIWETSLSGKGFLGGTPAVGNGKIFVGTESGYLYALDAKDGSELWRTEVSDSQLLSP---P 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 679 TT--GLIYVGSHDQHAYALDIYEKKCVWKLNC---EGALFSSPCVSLSPHHLYCATLGGLLLALNPASGSTVWKRSCGKP 753
Cdd:cd10276 118 TYadGKIYVGTGDGRLYYCNAETGKVVWNRTStapELSLRGGAAPVGAYDVVFVGDGNGTVVALNTGTGVDIWEFSVSEP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 754 LFSSPRCYQQYICIGCVDGSLLCFT------------HSGEQVWRFAAGGpIFSSPCVsaAEQEIFFGSHDCFIYCCSKE 821
Cdd:cd10276 198 RGRTELPRMIDSSVTYVVVGGYLYStsyqgylvaldfESGQFLWSRKASG-GTSTSTD--ANGRVYVGDGEGSLYCLDAS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 822 -GHLRWKFETTARVYATPFAFSnhprSDDALLAAASTDGKLWVLESRSGEL-------RSVYELPGevfssPVVWESMLV 893
Cdd:cd10276 275 tGDELWSQTVLLGRVLSSPAIY----VGVYIYVTDNAEGYLYCLKDNDGLTvarvevdYSQYILQG-----PAVSDGWLY 345
|
330
....*....|...
gi 1720413180 894 IGCRNNYIYCLDL 906
Cdd:cd10276 346 YGTDDGYLYALTR 358
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
42-349 |
3.81e-07 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 53.98 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 42 ITQEDILFLASPLT----FDPSVVeifvslssgACLLIVPTSV---KVLPSKLADILfSRHRVT-VLQATP------TLL 107
Cdd:PRK06087 225 LTWQDVFMMPAPLGhatgFLHGVT---------APFLIGARSVlldIFTPDACLALL-EQQRCTcMLGATPfiydllNLL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 108 RRFGSELikstvlsahTSLRVLALGGEAFPSLTILKSWRgkgNRTQIFNIYGITEvSSWATFYRiPEEILnSAVKHESpv 187
Cdd:PRK06087 295 EKQPADL---------SALRFFLCGGTTIPKKVARECQQ---RGIKLLSVYGSTE-SSPHAVVN-LDDPL-SRFMHTD-- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 188 qlGSPLLGTVIEVRDQNGSPVLEGTG--------QVFLGgknrvcFLDDemtvPLGTMRA--------TGDFVTV-KDGE 250
Cdd:PRK06087 358 --GYAAAGVEIKVVDEARKTLPPGCEgeeasrgpNVFMG------YLDE----PELTARAldeegwyySGDLCRMdEAGY 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 251 IFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQERLILFIVSKVDLVKDCIFKELQ--------KHLPAH 322
Cdd:PRK06087 426 IKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAPHHSLTLEevvaffsrKRVAKY 505
|
330 340
....*....|....*....|....*..
gi 1720413180 323 ALPDDMVLIDTLPFTCHGKVDVSELNK 349
Cdd:PRK06087 506 KYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
41-351 |
4.08e-07 |
|
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: 53.65 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 41 DITQEDILFLASPLTFDPSVVEIFVS-LSSGACLLIVPTSVKVLPSKLADILFSRHRVTVLQ----ATPTLLRRFGSELI 115
Cdd:cd05908 143 EWKTKDRILSWMPLTHDMGLIAFHLApLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVSspnfGYKYFLKTLKPEKA 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 116 KSTVLSahtSLRVLALGGEAFPS------LTILKSWrgKGNRTQIFNIYGITEVSSWATFYRIPEE-----ILNSAVKHE 184
Cdd:cd05908 223 NDWDLS---SIRMILNGAEPIDYelchefLDHMSKY--GLKRNAILPVYGLAEASVGASLPKAQSPfktitLGRRHVTHG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 185 SP--------------VQLGSPLLGTVIEVRDQNGSPVLEGT-GQVFLGGKNRVC--FLDDEMT----VPLGTMRaTGDF 243
Cdd:cd05908 298 EPepevdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYiGHIQIRGKNVTPgyYNNPEATakvfTDDGWLK-TGDL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 244 VTVKDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVES-----CAV--TWYNQERLILFIV---SKVDLVKdcIFK 313
Cdd:cd05908 377 GFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELgrvvaCGVnnSNTRNEEIFCFIEhrkSEDDFYP--LGK 454
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1720413180 314 ELQKHLPAHA--LPDDMVLIDTLPFTCHGKVDVSELNKIY 351
Cdd:cd05908 455 KIKKHLNKRGgwQINEVLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
780-895 |
1.00e-06 |
|
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: 52.12 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 780 SGEQVWRFAAGGPIfSSPcVSAAEQEIFFGSHDCFIYCCSKE-GHLRWKFETTARVYATPfafsnhpRSDDALLAAASTD 858
Cdd:COG1520 76 TGKELWRVDLGEPL-SGG-VGADGGLVVVGTEDGEVIALDADdGEELWRARLSSEVLAAP-------AVAGGRVVVRTGD 146
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1720413180 859 GKLWVLESRSGELRSVYELPGEVF-----SSPVVWESMLVIG 895
Cdd:COG1520 147 GRVYALDAATGERLWSYQRPVPALtlrgtSSPVIVGGAVLVG 188
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
82-343 |
1.14e-06 |
|
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: 51.56 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 82 VLPSKLADILFSRHR--VTVLQATPTLLRRFgseLIKSTVLSAHTSLRVLALGGEAFPS-LTIlkswRGKGNRTQIFNIY 158
Cdd:cd17630 70 VLLERNQALAEDLAPpgVTHVSLVPTQLQRL---LDSGQGPAALKSLRAVLLGGAPIPPeLLE----RAADRGIPLYTTY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 159 GITEVSSWATFYRIPEEILNSavkhespvqLGSPLLGtvIEVRDQNGSPVLEGTGQVFLGGKNRVC---FLDDemtvplG 235
Cdd:cd17630 143 GMTETASQVATKRPDGFGRGG---------VGVLLPG--RELRIVEDGEIWVGGASLAMGYLRGQLvpeFNED------G 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 236 TMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNIalvqqVAEELRQ-------VESCAVTW-----YNQeRLILFIVS 302
Cdd:cd17630 206 WFT-TKDLGELhADGRLTVLGRADNMIISGG--ENI-----QPEEIEAalaahpaVRDAFVVGvpdeeLGQ-RPVAVIVG 276
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1720413180 303 KVDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVD 343
Cdd:cd17630 277 RGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVD 317
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
26-349 |
1.45e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 51.33 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 26 NEVWAIHYESHRSLFDITqeDILFLASPL-TFDPSVVEIFVSLSSGACLLIVPTSVKVLPSKLADI--LFSRHRVTVLQA 102
Cdd:cd05944 26 NEVYNAWMLALNSLFDPD--DVLLCGLPLfHVNGSVVTLLTPLASGAHVVLAGPAGYRNPGLFDNFwkLVERYRITSLST 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 103 TPTLLrrfgSELIKSTVLSAHTSLRVLALGGEAFPSLTIlkswRGKGNRT--QIFNIYGITEVSSwatfyripeeiLNSA 180
Cdd:cd05944 104 VPTVY----AALLQVPVNADISSLRFAMSGAAPLPVELR----ARFEDATglPVVEGYGLTEATC-----------LVAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 181 VKHESPVQLGS-----PLLGTVIEVRDQNGSPVLE-GTGQVF---------LGG-----KNRVCFLDDemtvplGTMRaT 240
Cdd:cd05944 165 NPPDGPKRPGSvglrlPYARVRIKVLDGVGRLLRDcAPDEVGeicvagpgvFGGylyteGNKNAFVAD------GWLN-T 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 241 GDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQERLILFIVSKVDLVKDCIFK--ELQK 317
Cdd:cd05944 238 GDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEeeELLA 317
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720413180 318 HLPAH-----ALPDDMVLIDTLPFTCHGKVDVSELNK 349
Cdd:cd05944 318 WARDHvperaAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
81-347 |
1.94e-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: 51.34 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 81 KVLPSKLADILfSRHRVTVLQATPTLLRRFGSELIKSTVLSahtSLRVLALGGEAFpSLTILKSWRGKGNrTQIFNIYGI 160
Cdd:cd05970 262 KFDPKALLEKL-SKYGVTTFCAPPTIYRFLIREDLSRYDLS---SLRYCTTAGEAL-NPEVFNTFKEKTG-IKLMEGFGQ 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 161 TE-VSSWATFyripeeilnsAVKHESPVQLGSPLLGTVIEVRDQNGSPVLEG-TGQVflggknrVCFLDDEmtVPLGTMR 238
Cdd:cd05970 336 TEtTLTIATF----------PWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGeEGEI-------VIRTSKG--KPVGLFG 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 239 A------------------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWYNQERLILF 299
Cdd:cd05970 397 GyykdaektaevwhdgyyhTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQV 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720413180 300 IVSKVDLVKD-----CIFKELQKHL----PAHALPDDMVLIDTLPFTCHGKVDVSEL 347
Cdd:cd05970 477 VKATIVLAKGyepseELKKELQDHVkkvtAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PRK11138 |
PRK11138 |
outer membrane biogenesis protein BamB; Provisional |
588-707 |
2.64e-06 |
|
outer membrane biogenesis protein BamB; Provisional
Pssm-ID: 236857 [Multi-domain] Cd Length: 394 Bit Score: 50.70 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 588 RAAVQDkpsTTVYIGSHSHTVKAVDLSSGETRWEQLLGDRIES---------SACVSKCGNFIVVGCYNGLVYVLKSNSG 658
Cdd:PRK11138 64 HPAVAY---NKVYAADRAGLVKALDADTGKEIWSVDLSEKDGWfsknksallSGGVTVAGGKVYIGSEKGQVYALNAEDG 140
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720413180 659 EKYWTFTTEDAVKSSPAVDptTGLIYVGSHDQHAYALDIYEKKCVWKLN 707
Cdd:PRK11138 141 EVAWQTKVAGEALSRPVVS--DGLVLVHTSNGMLQALNESDGAVKWTVN 187
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
41-353 |
3.03e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 51.01 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 41 DITQEDILFLASPLtFDPSVVEIFV--SLSSGAcLLIVPTsvKVLPSKlADILFSRHRVTVLQATPTLLRRF-GSELIKS 117
Cdd:PRK06839 186 DLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGG-VIIVPR--KFEPTK-ALSMIEKHKVTVVMGVPTIHQALiNCSKFET 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 118 TVLSahtSLRVLALGGEAFPsLTILKSWRGKGNRtqIFNIYGITEVSswATFYRIPEEilNSAVKhesPVQLGSPLLGTV 197
Cdd:PRK06839 261 TNLQ---SVRWFYNGGAPCP-EELMREFIDRGFL--FGQGFGMTETS--PTVFMLSEE--DARRK---VGSIGKPVLFCD 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 198 IEVRDQNGSPVLEG-TGQVFLGGKNrvcFLDDEMTVPLGTMRA-------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRL 268
Cdd:PRK06839 328 YELIDENKNKVEVGeVGELLIRGPN---VMKEYWNRPDATEETiqdgwlcTGDLARVdEDGFVYIVGRKKEMIISGGENI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 269 NIALVQQVAEELRQVESCAVTWYNQERL----ILFIVSKVDLVkdCIFKELQKH----LPAHALPDDMVLIDTLPFTCHG 340
Cdd:PRK06839 405 YPLEVEQVINKLSDVYEVAVVGRQHVKWgeipIAFIVKKSSSV--LIEKDVIEHcrlfLAKYKIPKEIVFLKELPKNATG 482
|
330
....*....|...
gi 1720413180 341 KVDVSELNKIYLD 353
Cdd:PRK06839 483 KIQKAQLVNQLKS 495
|
|
| PQQ_3 |
pfam13570 |
PQQ-like domain; |
658-695 |
9.31e-06 |
|
PQQ-like domain;
Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 43.35 E-value: 9.31e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1720413180 658 GEKYWTFTTEDAVKSSPAVDptTGLIYVGSHDQHAYAL 695
Cdd:pfam13570 1 GEVLWRFETGGPIVSSPAVA--GGLVYVGTGDGTLYAL 36
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
184-341 |
1.47e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 48.64 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 184 ESPV---QLGSPLLGTVIEVRDQNGSPVLEGTGQVflggknrVCflddemTVPLGTM-------------RAT------- 240
Cdd:PRK03584 432 LLPVyrgEIQCRGLGMAVEAWDEDGRPVVGEVGEL-------VC------TKPFPSMplgfwndpdgsryRDAyfdtfpg 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 241 ----GDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQV-ESCAV--TWYNQ-ERLILFIVSK--VDL--- 306
Cdd:PRK03584 499 vwrhGDWIEItEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVlDSLVIgqEWPDGdVRMPLFVVLAegVTLdda 578
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720413180 307 VKDCIFKELQKHL-PAHaLPDDMVLIDTLPFTCHGK 341
Cdd:PRK03584 579 LRARIRTTIRTNLsPRH-VPDKIIAVPDIPRTLSGK 613
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
186-341 |
1.71e-05 |
|
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: 48.42 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 186 PVQLG---SPLLGTVIEVRDQNGSPVLEGTGQVflggknrVCflddemTVPLGTM-------------RAT--------- 240
Cdd:cd05943 420 PVYRGeiqCRGLGMAVEAFDEEGKPVWGEKGEL-------VC------TKPFPSMpvgfwndpdgsryRAAyfakypgvw 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 241 --GDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQV-ESCAVTWYNQ---ERLILFIV--SKVDL---VK 308
Cdd:cd05943 487 ahGDWIEItPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVeDSLVVGQEWKdgdERVILFVKlrEGVELddeLR 566
|
170 180 190
....*....|....*....|....*....|...
gi 1720413180 309 DCIFKELQKHLPAHALPDDMVLIDTLPFTCHGK 341
Cdd:cd05943 567 KRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
572-866 |
2.29e-05 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 47.98 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 572 WRSDTGKCV---DASPLLVRAAVQDKPSTTVYIGSHSHTVKAVDLSSGETRWEqLLGDRIE-SSACVSKCGNFIVVGCYN 647
Cdd:COG2319 147 WDLATGKLLrtlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGHTGAvRSVAFSPDGKLLASGSAD 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 648 GLVYVLKSNSGEKYWTFTTEDAVKSSPAVDPTTGLIYVGSHDQHAYALDIYEKKCVWKLncEGALFSSPCVSLSP--HHL 725
Cdd:COG2319 226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTL--TGHSGGVNSVAFSPdgKLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 726 ycatlgglllalnpASGS-----TVWKRSCGKPLfssprcyqqyicigcvdgsllcFTHSGEQVWRFAAggpifsspCVS 800
Cdd:COG2319 304 --------------ASGSddgtvRLWDLATGKLL----------------------RTLTGHTGAVRSV--------AFS 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720413180 801 AAEQEIFFGSHDcfiyccskeGHLR-WKFET----------TARVYAtpFAFSnhprSDDALLAAASTDG--KLWVLES 866
Cdd:COG2319 340 PDGKTLASGSDD---------GTVRlWDLATgellrtltghTGAVTS--VAFS----PDGRTLASGSADGtvRLWDLAT 403
|
|
| PQQ_2 |
pfam13360 |
PQQ-like domain; This domain contains several repeats of the PQQ repeat. |
598-705 |
2.40e-05 |
|
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
Pssm-ID: 433144 [Multi-domain] Cd Length: 233 Bit Score: 46.63 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 598 TVYIGSHSHTVKAVDLSSGETRWEQLL-----GDRIE-----SSACVSKCGNFIVVGcYNGLVYVLKSNSGEKYWTftte 667
Cdd:pfam13360 120 TVVAGFSSGKLVALDPATGKVRWEAPLaaprgTNELErlvdiTGTPVVAGGRVFASA-YQGRLVAFDAATGRRLWT---- 194
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720413180 668 DAVKSSPAVDPTTGLIYVGSHDQHAYALDIYEKKCVWK 705
Cdd:pfam13360 195 REISGPNGPILDGDLLYVVSDDGELYALDRATGAVVWK 232
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
553-862 |
3.38e-05 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 47.21 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 553 LFQQGSPVVGAMAMALRERWRSDTGKCVDASPLL---VRAAVQDKPSTTVYIGSHSHTVKAVDLSSGETRWEQLLGDRIE 629
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHtaaVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 630 SSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWTFTTEDAVKSSPAVDPTTGLIYVGSHDQHAYALDIYEKKCVWKLNCE 709
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 710 GALFSSpcVSLSP--HHLycatlgglllalnpASGST-----VWKRSCGKPLFS-------------SPrcYQQYICIGC 769
Cdd:COG2319 204 TGAVRS--VAFSPdgKLL--------------ASGSAdgtvrLWDLATGKLLRTltghsgsvrsvafSP--DGRLLASGS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 770 VDGSLLCF-THSGEQVWRFAAGGPIFSSPCVSAAEQEIFFGSHDcfiyccskeGHLR-WKFET----------TARVYAt 837
Cdd:COG2319 266 ADGTVRLWdLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDD---------GTVRlWDLATgkllrtltghTGAVRS- 335
|
330 340
....*....|....*....|....*..
gi 1720413180 838 pFAFSnhprSDDALLAAASTDG--KLW 862
Cdd:COG2319 336 -VAFS----PDGKTLASGSDDGtvRLW 357
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
66-343 |
4.29e-05 |
|
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: 46.92 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 66 SLSSGACLLIVPtsvKVLPSKLADiLFSRHRVTVLQATPT----LLRRFGSELIKstvlsAHTSLRVLALGGEAFPsLTI 141
Cdd:cd05926 212 TLAAGGSVVLPP---RFSASTFWP-DVRDYNATWYTAVPTihqiLLNRPEPNPES-----PPPKLRFIRSCSASLP-PAV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 142 LKSWRgKGNRTQIFNIYGITEVSSWATFYRIPEeilnsavkheSPVQLGSPLLGTVIEVR--DQNGSPVLEG-TGQVFLG 218
Cdd:cd05926 282 LEALE-ATFGAPVLEAYGMTEAAHQMTSNPLPP----------GPRKPGSVGKPVGVEVRilDEDGEILPPGvVGEICLR 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 219 GKNrVC--FLDD-----EMTVPLGTMRaTGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAV-- 288
Cdd:cd05926 351 GPN-VTrgYLNNpeanaEAAFKDGWFR-TGDLgYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfg 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 289 ---TWYNQErLILFIVSKVD--LVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVD 343
Cdd:cd05926 429 vpdEKYGEE-VAAAVVLREGasVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQ 487
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
376-425 |
4.41e-05 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 42.17 E-value: 4.41e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720413180 376 LWKSILCLPEDPedtlkVPANSVFLDSGGDSLKSMRLLSEIERLTGTAIP 425
Cdd:pfam00550 6 LLAEVLGVPAEE-----IDPDTDLFDLGLDSLLAVELIARLEEEFGVEIP 50
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
67-343 |
5.26e-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: 47.06 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 67 LSSGACLLIVPTsvkvlPSklADILFS---RHRVTVLQATPTLLRRF-GSELIKSTVLSahtSLRVLALGGEAF-PSLT- 140
Cdd:COG1021 249 LYAGGTVVLAPD-----PS--PDTAFPlieRERVTVTALVPPLALLWlDAAERSRYDLS---SLRVLQVGGAKLsPELAr 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 141 -ILKSWrgkGNRTQifNIYGITE--VSswatFYRI--PEEILNSAVkhespvqlGSPllgtvI----EVR--DQNGSPVL 209
Cdd:COG1021 319 rVRPAL---GCTLQ--QVFGMAEglVN----YTRLddPEEVILTTQ--------GRP-----IspddEVRivDEDGNPVP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 210 EG-TGQ-------VFLG-----GKNRVCFLDDemtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNIAlvqq 275
Cdd:COG1021 377 PGeVGElltrgpyTIRGyyrapEHNARAFTPD------GFYR-TGDLVRRtPDGYLVVEGRAKDQINRGGE--KIA---- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 276 vAEELR-------QVESCAVTWYNQERLI----LFIVSKVDLVKdciFKELQKHL-----PAHALPDDMVLIDTLPFTCH 339
Cdd:COG1021 444 -AEEVEnlllahpAVHDAAVVAMPDEYLGerscAFVVPRGEPLT---LAELRRFLrerglAAFKLPDRLEFVDALPLTAV 519
|
....
gi 1720413180 340 GKVD 343
Cdd:COG1021 520 GKID 523
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
35-360 |
6.61e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 46.88 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 35 SHRSLF----------DITQEDILFLASPLtfdpsvveiFVS--LSSGACLLIVpTSVKVL--PSKL------------- 87
Cdd:PRK06814 814 SHRNLLanraqvaariDFSPEDKVFNALPV---------FHSfgLTGGLVLPLL-SGVKVFlyPSPLhyriipeliydtn 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 88 ADILFSrhrvtvlqaTPTLLRRFGSelikstvlSAHT----SLRVLALGGEAFPSLTiLKSWRGK-GNRtqIFNIYGITE 162
Cdd:PRK06814 884 ATILFG---------TDTFLNGYAR--------YAHPydfrSLRYVFAGAEKVKEET-RQTWMEKfGIR--ILEGYGVTE 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 163 VSswatfyripeeilnsavkhesPV-QLGSPL---LGTV------IEVRDQNGSPVLEGtGQVFLGGKNrvcflddemtV 232
Cdd:PRK06814 944 TA---------------------PViALNTPMhnkAGTVgrllpgIEYRLEPVPGIDEG-GRLFVRGPN----------V 991
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 233 PLGTMRA---------------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELR-QVESCAVTWYNQ-- 293
Cdd:PRK06814 992 MLGYLRAenpgvleppadgwydTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWpDALHAAVSIPDArk 1071
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720413180 294 -ERLILFIVSKvdlvkDCIFKELQKHLPAH-----ALPDDMVLIDTLPFTCHGKVDVSELNKIYLDYISSQPR 360
Cdd:PRK06814 1072 gERIILLTTAS-----DATRAAFLAHAKAAgaselMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
64-288 |
9.48e-05 |
|
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: 46.02 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 64 FVSLSSGACLLIVpTSVKVLPSKLADILfSRHRVTVLQATPTLLRRfgseLIKSTVLSAHTSLRVLALGGEAF-PSL--T 140
Cdd:cd05974 146 FAPWNAGATVFLF-NYARFDAKRVLAAL-VRYGVTTLCAPPTVWRM----LIQQDLASFDVKLREVVGAGEPLnPEVieQ 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 141 ILKSWrgkgNRTqIFNIYGITEVSSwatfyripeEILNSAVKHESPVQLGSPLLGTVIEVRDQNGSPVLEGTGQVFLGGK 220
Cdd:cd05974 220 VRRAW----GLT-IRDGYGQTETTA---------LVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVALDLGDT 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720413180 221 NRVCFL-----DDEMT--VPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAV 288
Cdd:cd05974 286 RPVGLMkgyagDPDKTahAMRGGYYRTGDIAMRdEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
738-909 |
1.18e-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: 45.31 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 738 NPASGSTVWKRSCGKplfsSPRCYQQYICIGCVDGSLlcFT------------HSGEQVWRFAAGGPIfsSPCVSAAEQE 805
Cdd:TIGR03300 36 PTVKVDQVWSASVGD----GVGHYYLRLQPAVAGGKV--YAadadgtvaaldaETGKRLWRVDLDERL--SGGVGADGGL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 806 IFFGSHDCFIYCCSKE-GHLRWKFETTARVYATPFafsnhprSDDALLAAASTDGKLWVLESRSGELRSVYELPGEVF-- 882
Cdd:TIGR03300 108 VFVGTEKGEVIALDAEdGKELWRAKLSSEVLSPPL-------VANGLVVVRTNDGRLTALDAATGERLWTYSRVTPPLtl 180
|
170 180 190
....*....|....*....|....*....|
gi 1720413180 883 ---SSPVVWESMLVIGCRNNYIYCLDLLCG 909
Cdd:TIGR03300 181 rgsASPVIADGGVLVGFAGGKLVALDLQTG 210
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
190-349 |
1.45e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 45.04 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 190 GSPLLGTVIEVRDqngspvlegtGQVFLGG-------KNRVcfLDDEMTVPlGTMRaTGDFVTVKDGEIFFLGRKDSQIK 262
Cdd:PRK07824 195 GVPLDGVRVRVED----------GRIALGGptlakgyRNPV--DPDPFAEP-GWFR-TDDLGALDDGVLTVLGRADDAIS 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 263 RHGKRLNIALVQQVAEELRQVESCAVTWYNQERLILFIVSKV--DLVKDCIFKELQKH----LPAHALPDDMVLIDTLPF 336
Cdd:PRK07824 261 TGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVvgDGGPAPTLEALRAHvartLDRTAAPRELHVVDELPR 340
|
170
....*....|...
gi 1720413180 337 TCHGKVDVSELNK 349
Cdd:PRK07824 341 RGIGKVDRRALVR 353
|
|
| PQQ_DH_like |
cd00216 |
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
576-686 |
1.57e-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: 45.29 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 576 TGKCVDASPLLVRAAVQDkpsTTVYIGSHSHTVKAVDLSSGETRWEQLLGDRIESSAcVSKCGNFIVVGCYNGLVYVLKS 655
Cdd:cd00216 296 NGELVSARPLVPDSYDPD---RELFYVPANGRIMALDPVTGVVVWEKSELHPLLGGP-LSTAGNLVFVGTSDGYLKAYNA 371
|
90 100 110
....*....|....*....|....*....|.
gi 1720413180 656 NSGEKYWTFTTEDAVKSSPAVDPTTGLIYVG 686
Cdd:cd00216 372 DTGEKLWQQKVPSGFQAEPVTYEVDGEQYVL 402
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
63-342 |
4.87e-04 |
|
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: 43.26 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 63 IFVSLSSGACllIVPTSVKVLPSKLADIlfSRHRVTVLQATPTLLRR-FGSELIKSTVLSahtSLRVLALGGEAFPsLTI 141
Cdd:cd17638 60 IVACLLTGAT--VVPVAVFDVDAILEAI--ERERITVLPGPPTLFQSlLDHPGRKKFDLS---SLRAAVTGAATVP-VEL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 142 LKSWRGKGNRTQIFNIYGITEVSSwATFYRiPEEilnSAVKHESPVqlGSPLLGTviEVRdqngspvLEGTGQVFLGGKN 221
Cdd:cd17638 132 VRRMRSELGFETVLTAYGLTEAGV-ATMCR-PGD---DAETVATTC--GRACPGF--EVR-------IADDGEVLVRGYN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 222 -RVCFLDDemtvPLGTMRA--------TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTWY 291
Cdd:cd17638 196 vMQGYLDD----PEATAEAidadgwlhTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGV 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720413180 292 NQERL----ILFIVSK--VDLVKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKV 342
Cdd:cd17638 272 PDERMgevgKAFVVARpgVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| Luminal_IRE1_like |
cd09213 |
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The ... |
770-875 |
7.71e-04 |
|
The Luminal domain, a dimerization domain, of Inositol-requiring protein 1-like proteins; The Luminal domain is a dimerization domain present in Inositol-requiring protein 1 (IRE1), eukaryotic translation Initiation Factor 2-Alpha Kinase 3 (EIF2AK3), and similar proteins. IRE1 and EIF2AK3 are serine/threonine protein kinases (STKs) and are type I transmembrane proteins that are localized in the endoplasmic reticulum (ER). They are kinase receptors that are activated through the release of BiP, a chaperone bound to their luminal domains under unstressed conditions. This results in dimerization through their luminal domains, allowing trans-autophosphorylation of their kinase domains and activation. They play roles in the signaling of the unfolded protein response (UPR), which is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), contains an endoribonuclease domain in its cytoplasmic side and acts as an ER stress sensor. It is the oldest and most conserved component of the UPR in eukaryotes. Its activation results in the cleavage of its mRNA substrate, HAC1 in yeast and Xbp1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. EIF2AK3, also called PKR-like Endoplasmic Reticulum Kinase (PERK), phosphorylates the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. It functions as the central regulator of translational control during the UPR pathway. In addition to the eIF-2 alpha subunit, EIF2AK3 also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR.
Pssm-ID: 188873 [Multi-domain] Cd Length: 312 Bit Score: 42.48 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 770 VDGSLLCF-THSGEQVWRFAAGGPIFSSPcVSAAEQEIFFGSHDCFI--------YCCSKEGHLRWKFETTAR--VYATP 838
Cdd:cd09213 7 LDGTIYAVdASSGEIQWSFDGGGPLYSSY-QSSRDGNAESSSTMLIPsldgdgnlYQHDKGHGSLQRLPLTIEdlVEASP 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720413180 839 FAFsnHPRSDDALLaAASTDGKLWVLESRSGELRSVY 875
Cdd:cd09213 86 LVS--DTNEDDVVV-VGSKRTSVFALDAKTGKIIKTY 119
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-342 |
1.10e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 42.28 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 29 WAIHYESHRslFDITQEDILFLASPLtF--DPSVVEIFVSLSSGACLLIVPtsvKVLPSK-LADILfsRHRVTVLQATPT 105
Cdd:cd05934 108 FAGYYSARR--FGLGEDDVYLTVLPL-FhiNAQAVSVLAALSVGATLVLLP---RFSASRfWSDVR--RYGATVTNYLGA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 106 LLrrfgselikSTVLS--------AHTsLRVlALGGEAFPSLtilksWRGKGNR--TQIFNIYGITEVSSwatfyripeE 175
Cdd:cd05934 180 ML---------SYLLAqppspddrAHR-LRA-AYGAPNPPEL-----HEEFEERfgVRLLEGYGMTETIV---------G 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 176 ILNSAVKHESPVQLGSPLLGTVIEVRDQNGSPVLEG-TGQVFLGGKNRVCFLDDEMTVPLGTMRA-------TGD-FVTV 246
Cdd:cd05934 235 VIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGePGELVIRGLRGWGFFKGYYNMPEATAEAmrngwfhTGDlGYRD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 247 KDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAV----TWYNQERLILFIVSKVD--LVKDCIFKELQKHLP 320
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVvavpDEVGEDEVKAVVVLRPGetLDPEELFAFCEGQLA 394
|
330 340
....*....|....*....|..
gi 1720413180 321 AHALPDDMVLIDTLPFTCHGKV 342
Cdd:cd05934 395 YFKVPRYIRFVDDLPKTPTEKV 416
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
66-257 |
1.42e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 42.20 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 66 SLSSGACLLIVPtsvKVLPSKLADiLFSRHRVTVLQATPTLLRrfgsELIKSTVLSAH--TSLRVLALGGEAFPsLTILK 143
Cdd:PRK07656 229 PLMRGATILPLP---VFDPDEVFR-LIETERITVLPGPPTMYN----SLLQHPDRSAEdlSSLRLAVTGAASMP-VALLE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 144 SWRGKGNRTQIFNIYGITEVSSWATFYRI---PEEILNSAvkhespvqlGSPLLGTVIEVRDQNGSPVLEG-TGQVFLGG 219
Cdd:PRK07656 300 RFESELGVDIVLTGYGLSEASGVTTFNRLdddRKTVAGTI---------GTAIAGVENKIVNELGEEVPVGeVGELLVRG 370
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1720413180 220 KNrVC--FLDDemtvPLGTMRA--------TGDFVTV-KDGEIFFLGRK 257
Cdd:PRK07656 371 PN-VMkgYYDD----PEATAAAidadgwlhTGDLGRLdEEGYLYIVDRK 414
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
153-350 |
1.53e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 42.07 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 153 QIFNIYGITEVSSWAtfYRIPEEilnSAVKhesPVQLGSPLLGTVIEVRDQNGSPVLEG-TGQVF----------LGGKN 221
Cdd:PRK07638 281 KLYEFYGASELSFVT--ALVDEE---SERR---PNSVGRPFHNVQVRICNEAGEEVQKGeIGTVYvkspqffmgyIIGGV 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 222 RVCFLDDE--MTVplgtmratGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNI--ALVQQVAEELRQVESCAVTW----YN 292
Cdd:PRK07638 353 LARELNADgwMTV--------RDVGYEdEEGFIYIVGREKNMILFGG--INIfpEEIESVLHEHPAVDEIVVIGvpdsYW 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720413180 293 QERLILFIVSKVDlvKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKVDVSELNKI 350
Cdd:PRK07638 423 GEKPVAIIKGSAT--KQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEAKSW 478
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
37-349 |
1.75e-03 |
|
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: 42.07 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 37 RSLFDITQEDILFLASPLTFDPSVV-EIFVSLSSGACLLivptsVKVLPSKLADIL---FSRHRVTVLQATPTLLRRFGS 112
Cdd:cd05928 208 RYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVF-----VHHLPRFDPLVIlktLSSYPITTFCGAPTVYRMLVQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 113 ELIKSTVLSahtSLRVLALGGEAF-PSltILKSWRgkgNRT--QIFNIYGITEVSSWATFYRiPEEIlnsavkheSPVQL 189
Cdd:cd05928 283 QDLSSYKFP---SLQHCVTGGEPLnPE--VLEKWK---AQTglDIYEGYGQTETGLICANFK-GMKI--------KPGSM 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 190 GSPLLGTVIEVRDQNGS---PVLEGTGQVFLGGKNRVCFLDDEMTVPLGTMRAT-GDF-------VTVKDGEIFFLGRKD 258
Cdd:cd05928 346 GKASPPYDVQIIDDNGNvlpPGTEGDIGIRVKPIRPFGLFSGYVDNPEKTAATIrGDFyltgdrgIMDEDGYFWFMGRAD 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 259 SQIKRHGKRLNIALVQQ-VAEELRQVESCAVTWYNQER---LILFIVSKVDLV---KDCIFKELQKHLPA----HALPDD 327
Cdd:cd05928 426 DVINSSGYRIGPFEVESaLIEHPAVVESAVVSSPDPIRgevVKAFVVLAPQFLshdPEQLTKELQQHVKSvtapYKYPRK 505
|
330 340
....*....|....*....|..
gi 1720413180 328 MVLIDTLPFTCHGKVDVSELNK 349
Cdd:cd05928 506 VEFVQELPKTVTGKIQRNELRD 527
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
240-343 |
1.76e-03 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 41.90 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 240 TGDFVTV-KDGEIFFLGRKDSQIKRHGKR----------------LNIALVQqVAEELRQVESCAvtwynqerlilFIVS 302
Cdd:PRK10946 413 SGDLVSIdPDGYITVVGREKDQINRGGEKiaaeeienlllrhpavIHAALVS-MEDELMGEKSCA-----------FLVV 480
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720413180 303 KVDLvkdcifK--ELQKHLPAHA-----LPDDMVLIDTLPFTCHGKVD 343
Cdd:PRK10946 481 KEPL------KavQLRRFLREQGiaefkLPDRVECVDSLPLTAVGKVD 522
|
|
| PQQ |
smart00564 |
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ... |
634-665 |
1.89e-03 |
|
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.
Pssm-ID: 128836 [Multi-domain] Cd Length: 33 Bit Score: 36.74 E-value: 1.89e-03
10 20 30
....*....|....*....|....*....|..
gi 1720413180 634 VSKCGNFIVVGCYNGLVYVLKSNSGEKYWTFT 665
Cdd:smart00564 2 VVLSDGTVYVGSTDGTLYALDAKTGEILWTYK 33
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
598-697 |
2.30e-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: 41.34 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 598 TVYIGSHSHTVKAVDLSSGETRWEQ--LLGDRIESSACVskcGNFIVVGCYNGLVYVLKSNSGEkywtF-----TTEDAV 670
Cdd:COG1520 273 NLYVTDDDGRVWALDRRNGAELWKQdaLLYRGLTAPVVL---GDYVVVGDFEGYLHWLSRDDGS----LvarlrVDGSGI 345
|
90 100
....*....|....*....|....*..
gi 1720413180 671 KSSPAVDPTTglIYVGSHDQHAYALDI 697
Cdd:COG1520 346 RAAPVVVGDT--LYVQTRDGTLAALRL 370
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
187-352 |
3.40e-03 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 41.14 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 187 VQLGSPLLGTVIEVRDQNGSPVLE-GTGQVFLGGKNRVC--FLDDEMTvplGTMRA-----TGDFVTVKDGEIFFLGRKD 258
Cdd:PRK09192 385 VNCGKALPGHEIEIRNEAGMPLPErVVGHICVRGPSLMSgyFRDEESQ---DVLAAdgwldTGDLGYLLDGYLYITGRAK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 259 SQIKRHGKrlNI--ALVQQVAE---ELRQVESCA--VTWYNQERLILFI---VSKVDLVKDCIFKELQKHLPAHALPDDM 328
Cdd:PRK09192 462 DLIIINGR--NIwpQDIEWIAEqepELRSGDAAAfsIAQENGEKIVLLVqcrISDEERRGQLIHALAALVRSEFGVEAAV 539
|
170 180
....*....|....*....|....*.
gi 1720413180 329 VLI--DTLPFTCHGKVDVSELNKIYL 352
Cdd:PRK09192 540 ELVppHSLPRTSSGKLSRAKAKKRYL 565
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
91-342 |
3.47e-03 |
|
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: 40.93 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 91 LFSRHRVTVLQATPTLLRRFGSEL-IKSTVLSahtSLRVLALGGEAFPSLTILKSWRGKGNRtqiFN-IYGITEVsswat 168
Cdd:cd05935 168 LIEKYKVTFWTNIPTMLVDLLATPeFKTRDLS---SLKVLTGGGAPMPPAVAEKLLKLTGLR---FVeGYGLTET----- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 169 fyrIPEEILNSAVKHESPVqLGSPLLGT---VIEVRD-------QNGSPVLEGTgQVFLG-----GKNRVCFLDDE---- 229
Cdd:cd05935 237 ---MSQTHTNPPLRPKLQC-LGIP*FGVdarVIDIETgrelppnEVGEIVVRGP-QIFKGywnrpEETEESFIEIKgrrf 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 230 -MTVPLGTMRAtgdfvtvkDGEIFFLGRKDSQIKRHGKRLNIALVQQVAEELRQVESCAVTW----YNQERLILFIV--- 301
Cdd:cd05935 312 fRTGDLGYMDE--------EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISvpdeRVGEEVKAFIVlrp 383
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720413180 302 ---SKVDlvKDCIFKELQKHLPAHALPDDMVLIDTLPFTCHGKV 342
Cdd:cd05935 384 eyrGKVT--EEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| PQQ_3 |
pfam13570 |
PQQ-like domain; |
781-817 |
3.89e-03 |
|
PQQ-like domain;
Pssm-ID: 463925 [Multi-domain] Cd Length: 36 Bit Score: 35.64 E-value: 3.89e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1720413180 781 GEQVWRFAAGGPIFSSPCVsaAEQEIFFGSHDCFIYC 817
Cdd:pfam13570 1 GEVLWRFETGGPIVSSPAV--AGGLVYVGTGDGTLYA 35
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
597-691 |
6.21e-03 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 39.29 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 597 TTVYI-GSHSHTVKAVDLSSGETRWEQLLGDRIESSACVSKCGNFIVVGCYNGLVYVLKSNSGEKYWTFTTEDavksSP- 674
Cdd:COG3391 80 RRLYVaNSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVVATIPVGA----GPh 155
|
90
....*....|....*....
gi 1720413180 675 --AVDPTTGLIYVGSHDQH 691
Cdd:COG3391 156 giAVDPDGKRLYVANSGSN 174
|
|
| PQQ_DH_like |
cd00216 |
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ... |
662-792 |
6.58e-03 |
|
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: 39.90 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 662 WTFTTEDA----VKSSPAVdpTTGLIYVGSHDQHAYALDIYEKKCVWKLNCE--GALFSSPC------VSLSPHHLYCAT 729
Cdd:cd00216 11 WSFSTGDGgnrgSELTPIV--VDGVMYATTSFSRVFALDADDGKEIWSYDPAlkDGWFEACCdlvnrgVAVWGGKVYIGV 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720413180 730 LGGLLLALNPASGSTVWKRS-----CGKPLFSSPRCYQQYICIGC------VDGSLLCF-THSGEQVWRFAAGGP 792
Cdd:cd00216 89 LDGRVYALNAETGKVAWKVKnadvlGGYTATSAPVVVDGLVIIGSsgdefgVRGYLTAYdVATGEEKWRFYLVMP 163
|
|
| PQQ_ADH_I |
cd10277 |
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ... |
589-674 |
6.59e-03 |
|
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller.
Pssm-ID: 199835 [Multi-domain] Cd Length: 529 Bit Score: 39.97 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 589 AAVQDKPSTTVYIGShshtVKAVDLSSGETRWEQllgdRIESSAC---VSKCGNFIVVGCYNGLVYVLKSNSGEKYWTFT 665
Cdd:cd10277 403 AGFTIKPPFEDHIGE----LQAIDPTTGKKVWEH----KTPLPLWggvLTTAGGLVFTGTPDGYFRAFDAKTGKELWEFQ 474
|
....*....
gi 1720413180 666 TEDAVKSSP 674
Cdd:cd10277 475 TGSGIIGPP 483
|
|
| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
738-872 |
7.70e-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: 39.80 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 738 NPASGSTVWKRSCGKPLFSSPRCYQQYICIGCVDGSLLCF-THSGEQVWRFAAGGPIFSSPCVsaAEQEIFFGSHDCFIY 816
Cdd:COG1520 73 DAATGKELWRVDLGEPLSGGVGADGGLVVVGTEDGEVIALdADDGEELWRARLSSEVLAAPAV--AGGRVVVRTGDGRVY 150
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720413180 817 CCSKE-GHLRWKFETTA-----RVYATPFAfsnhprSDDALLAAAStDGKLWVLESRSGELR 872
Cdd:COG1520 151 ALDAAtGERLWSYQRPVpaltlRGTSSPVI------VGGAVLVGFA-NGKLVALDLANGQPL 205
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| PQQ |
COG1520 |
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ... |
847-905 |
8.05e-03 |
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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: 39.41 E-value: 8.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720413180 847 SDDALLAAASTDGKLWVLESRSGELRSVYELPGEVFSSPVVWESMLVIGCRNNYIYCLD 905
Cdd:COG1520 95 ADGGLVVVGTEDGEVIALDADDGEELWRARLSSEVLAAPAVAGGRVVVRTGDGRVYALD 153
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| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
572-703 |
8.20e-03 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 39.24 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720413180 572 WRSDTGKCVDA-----SPllVRAAVQDKPSTTVYIGSHSHTVKAVDLSSGETRWeQLLG--DRIeSSACVSKCGNFIVVG 644
Cdd:cd00200 120 WDVETGKCLTTlrghtDW--VNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVA-TLTGhtGEV-NSVAFSPDGEKLLSS 195
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720413180 645 CYNGLVYVLKSNSGEKYWTFTTEDAVKSSPAVDPTTGLIYVGSHDQHAYALDIYEKKCV 703
Cdd:cd00200 196 SSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECV 254
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