|
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 ... |
26-380 |
0e+00 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 564.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 26 KAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGAS 105
Cdd:cd17654 107 PEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGAT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 106 LLIVPTSVKLLPSKLASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKT 185
Cdd:cd17654 187 LLIVPTSVKVLPSKLADILFKRHRITVLQATPTLFRRFGSQSIKSTVLSATSSLRVLALGGEPFPSLVILSSWRGKGNRT 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 186 QIFNVYGITEVSSWATIYRIPEKtlnstlkcELPVQLGFPLLGTVVEVRDTNGFtiqEGSGQVFLGGRNRVCFLDDEVTV 265
Cdd:cd17654 267 RIFNIYGITEVSCWALAYKVPEE--------DSPVQLGSPLLGTVIEVRDQNGS---EGTGQVFLGGLNRVCILDDEVTV 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 266 PLGTMRATGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKdaSVKEYIF 345
Cdd:cd17654 336 PKGTMRATGDFVTVKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQRLIAFIVGE--SSSSRIH 413
|
330 340 350
....*....|....*....|....*....|....*.
gi 1021589396 346 KELQKY-LPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd17654 414 KELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
38-380 |
3.68e-94 |
|
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: 301.37 E-value: 3.68e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 38 CLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLP 117
Cdd:cd05930 94 DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVlsatTSLRVLALGGEAFPSlTVLRSWRGEGNKTQIFNVYGITEVS 197
Cdd:cd05930 174 EALAD-LLAEEGITVLHLTPSLLRLLLQELELAAL----PSLRLVLVGGEALPP-DLVRRWRELLPGARLVNLYGPTEAT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 198 SWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRN--RVCFLDDEVT---------V 265
Cdd:cd05930 248 VDATYYRVPPDDEEDG-----RVPIGRPIPNTRVYVLDENLRPVPPGvPGELYIGGAGlaRGYLNRPELTaerfvpnpfG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 266 PLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYN----QEKLILFMVSKDASV 340
Cdd:cd05930 323 PGERMYRTGDLVRWLpDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREdgdgEKRLVAYVVPDEGGE 402
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1021589396 341 --KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd05930 403 ldEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
39-321 |
4.38e-57 |
|
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: 200.95 E-value: 4.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:TIGR01733 122 LAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLFSHHRVTVLQATPTLLrrfgsQLIKSTVLSATTSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITEVSS 198
Cdd:TIGR01733 202 ALLAALIAEHPVTVLNLTPSLL-----ALLAAALPPALASLRLVILGGEALTPALVDR-WRARGPGARLINLYGPTETTV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYRIPEKTLNStlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG-------SG-QVFLG-----GRNRVCFLDDE-VT 264
Cdd:TIGR01733 276 WSTATLVDPDDAPR----ESPVPIGRPLANTRLYVLDDDLRPVPVGvvgelyiGGpGVARGylnrpELTAERFVPDPfAG 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 265 VPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAV 321
Cdd:TIGR01733 352 GDGARLYRTGDLVRYlPDGNLEFLGRIDDQVKIRGYR--IELgeIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
39-380 |
3.43e-50 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 182.83 E-value: 3.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:cd05945 99 NAYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLfSHHRVTVLQATPTLLRR-FGSQLIKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVS 197
Cdd:cd05945 179 QLFRFL-AEHGITVWVSTPSFAAMcLLSPTFTPESLP---SLRHFLFCGEVLP-HKTARALQQRFPDARIYNTYGPTEAT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 198 SWATIYRIPEKTLNStlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLG------GRNRVCFLDDEV 263
Cdd:cd05945 254 VAVTYIEVTPEVLDG----YDRLPIGYAKPGAKLVILDEDGRPVPPGekgelvisGPSVSKGylnnpeKTAAAFFPDEGQ 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 264 TVplgtmRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESC-AVTWYNQEK---LILFMVSKDA 338
Cdd:cd05945 330 RA-----YRTGDLVRLEaDGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAvVVPKYKGEKvteLIAFVVPKPG 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1021589396 339 S----VKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd05945 405 AeaglTKA-IKAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
39-322 |
9.31e-50 |
|
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: 190.07 E-value: 9.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:COG1020 619 LAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPA 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLfSHHRVTVLQATPTLLRrfgsQLIkSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITEVSS 198
Cdd:COG1020 699 ALAELL-ARHRVTVLNLTPSLLR----ALL-DAAPEALPSLRLVLVGGEALP-PELVRRWRARLPGARLVNLYGPTETTV 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGftiQ---EG-SGQVFLGG----------------RnrvcF 258
Cdd:COG1020 772 DSTYYEVTPPDADGG-----SVPIGRPIANTRVYVLDAHL---QpvpVGvPGELYIGGaglargylnrpeltaeR----F 839
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589396 259 LDDEVTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVT 322
Cdd:COG1020 840 VADPFGFPGARLYRTGDLARWlPDGNLEFLGRADDQVKIRGFR--IELgeIEAALLQHPGVREAVVV 904
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
39-380 |
6.66e-48 |
|
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: 176.71 E-value: 6.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:cd12116 128 LAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASvLFSHHRVTVLQATPTLLRrfgsqLIKSTVLSATTSLRVLAlGGEAFPS-------LTVLRSWrgegnktqifNVY 191
Cdd:cd12116 208 ALAR-LIEAHSITVMQATPATWR-----MLLDAGWQGRAGLTALC-GGEALPPdlaarllSRVGSLW----------NLY 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 192 GITEVSSWATIYRI-PEKTlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGG-------RNR-----VC 257
Cdd:cd12116 271 GPTETTIWSTAARVtAAAG---------PIPIGRPLANTQVYVLDAALRPVPPGvPGELYIGGdgvaqgyLGRpaltaER 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 258 FLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWYNQE---KLIL 331
Cdd:cd12116 342 FVPDPFAGPGSRLYRTGDLVRRRaDGRLEYLGRADGQVKIRGHR--IELgeIEAALAAHPGVAQAAVVVREDGgdrRLVA 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1021589396 332 FMVSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd12116 420 YVVLKAGAApdAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
39-376 |
5.17e-47 |
|
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: 173.65 E-value: 5.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:cd17643 95 LAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLfSHHRVTVLQATPTLLRRFGSQLIKSTvlSATTSLRVLALGGEAFPsLTVLRSWRG--EGNKTQIFNVYGITEV 196
Cdd:cd17643 175 DFARLL-RDEGVTVLNQTPSAFYQLVEAADRDG--RDPLALRYVIFGGEALE-AAMLRPWAGrfGLDRPQLVNMYGITET 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 197 SSWATIYRIpektLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGG---------RNRVC---FLDDEV 263
Cdd:cd17643 251 TVHVTFRPL----DAADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVvGELYVSGagvargylgRPELTaerFVANPF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 264 TVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWYNQE----KLILFMVSK 336
Cdd:cd17643 327 GGPGSRMYRTGDLARrLPDGELEYLGRADEQVKIRGFR--IELgeIEAALATHPSVRDAAVIVREDEpgdtRLVAYVVAD 404
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1021589396 337 D------ASVKEYIfKELqkyLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd17643 405 DgaaadiAELRALL-KEL---LPDYMVPARYVPLDALPLTVNGKLD 446
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
39-380 |
2.06e-46 |
|
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: 172.77 E-value: 2.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVpniqhfRVLFD-----ITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSV 113
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGVV------RLVKNtnyvtLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGT 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 114 KLLPSKLASVLfSHHRVTVLQATPTLLRrfgsqLIKSTVLSATTSLRVLALGGEAFPSLTVlRSWRGEGNKTQIFNVYGI 193
Cdd:cd12117 212 LLDPDALGALI-AEEGVTVLWLTAALFN-----QLADEDPECFAGLRELLTGGEVVSPPHV-RRVLAACPGLRLVNGYGP 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 194 TEVSSWATIYRIPEKTLNstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGG-------RNRVCfLDDEVTV 265
Cdd:cd12117 285 TENTTFTTSHVVTELDEV-----AGSIPIGRPIANTRVYVLDEDGRPVPPGvPGELYVGGdglalgyLNRPA-LTAERFV 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 266 PL-----GTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWYNQE----KLILFM 333
Cdd:cd12117 359 ADpfgpgERLYRTGDLARWLpDGRLEFLGRIDDQVKIRGFR--IELgeIEAALRAHPGVREAVVVVREDAggdkRLVAYV 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1021589396 334 VSK----DASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd12117 437 VAEgaldAAELRAF----LRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
27-484 |
2.89e-45 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 176.51 E-value: 2.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 27 AEEHMDLRLK-HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGAS 105
Cdd:PRK12467 645 SGHNPEVALDpDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGAT 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 106 LLIVPTSVKLLPSKLASVLfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGNKT 185
Cdd:PRK12467 725 LHLLPPDCARDAEAFAALM-ADQGVTVLKIVPSHLQ----ALLQASRVALPRPQRALVCGGEALQ-VDLLARVRALGPGA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 186 QIFNVYGITEVSSWATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGR----------- 253
Cdd:PRK12467 799 RLINHYGPTETTVGVSTYELSDEERDFG-----NVPIGQPLANLGLYILDHYLNPVPVGVvGELYIGGAglargyhrrpa 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 254 ---NRvcFLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRL---NIELVQQVAEELQQVESCAVTWYNQ 326
Cdd:PRK12467 874 ltaER--FVPDPFGADGGRLYRTGDLARyRADGVIEYLGRMDHQVKIRGFRIelgEIEARLLAQPGVREAVVLAQPGDAG 951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 327 EKLILFMV-------SKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiylNYINLKSENKLSGK 399
Cdd:PRK12467 952 LQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPK---PDASAVQATFVAPQ 1028
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 400 EDLWEKLQYLWKSTLnlpeDLLRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVPglLEIILSSSILEIYnhiLQTVVP 479
Cdd:PRK12467 1029 TELEKRLAAIWADVL----KVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVP--LRTLFEHQTLAGF---AQAVAA 1099
|
....*
gi 1021589396 480 DEDVT 484
Cdd:PRK12467 1100 QQQGA 1104
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
34-385 |
8.06e-44 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 164.60 E-value: 8.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 34 RLKHCL----------AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFD-PSVVEIFLALSS 102
Cdd:COG0318 87 ELAYILedsgaralvtALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVfGLTVGLLAPLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 103 GASLLIVPtsvKLLPSKLASvLFSHHRVTVLQATPTLLRRfgsqLIKSTVLSAT--TSLRVLALGGEAFPSlTVLRSWRG 180
Cdd:COG0318 167 GATLVLLP---RFDPERVLE-LIERERVTVLFGVPTMLAR----LLRHPEFARYdlSSLRLVVSGGAPLPP-ELLERFEE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 181 EGNkTQIFNVYGITEvSSWATIYRIPEKTLnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLG- 251
Cdd:COG0318 238 RFG-VRIVEGYGLTE-TSPVVTVNPEDPGE------RRPGSVGRPLPGVEVRIVDEDGRELPPGevgeivvrGPNVMKGy 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 252 ----GRNRVCFLDdevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNIEL--VQQVAEELQQVESCAVT-- 322
Cdd:COG0318 310 wndpEATAEAFRD-------GWLR-TGDLGRLdEDGYLYIVGRKKDMIISGG--ENVYPaeVEEVLAAHPGVAEAAVVgv 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 323 ----WynQEKLILFMVSKD---ASVKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYL 385
Cdd:COG0318 380 pdekW--GERVVAFVVLRPgaeLDAEE-LRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYA 446
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
39-376 |
5.65e-43 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 162.71 E-value: 5.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFDPSVVEIFLALSSGASLLIvpTSVKLLP 117
Cdd:cd05918 108 AAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSESrVLQFASY-TFDVSILEIFTTLAAGGCLCI--PSEEDRL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASVLfSHHRVTVLQATPTLLRrfgsqLIKstvLSATTSLRVLALGGEAfPSLTVLRSWrgeGNKTQIFNVYGITEvs 197
Cdd:cd05918 185 NDLAGFI-NRLRVTWAFLTPSVAR-----LLD---PEDVPSLRTLVLGGEA-LTQSDVDTW---ADRVRLINAYGPAE-- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 198 swATIYRipekTLNSTLKCELPVQLGFPLLGT--VVEVRDTN-----GFTiqegsGQVFLGG------------RNRVCF 258
Cdd:cd05918 250 --CTIAA----TVSPVVPSTDPRNIGRPLGATcwVVDPDNHDrlvpiGAV-----GELLIEGpilargylndpeKTAAAF 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 259 LDDEVTVPLGTMRA------TGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL------VQQVAEELQQVESCAVT--- 322
Cdd:cd05918 319 IEDPAWLKQEGSGRgrrlyrTGDLVRyNPDGSLEYVGRKDTQVKIRGQR--VELgeiehhLRQSLPGAKEVVVEVVKpkd 396
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021589396 323 WYNQEKLILFMVSKDASVK-------------------EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd05918 397 GSSSPQLVAFVVLDGSSSGsgdgdslflepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKID 469
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
39-380 |
1.96e-42 |
|
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: 161.73 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:cd17655 139 LAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVlFSHHRVTVLQATPTLLrrfgsQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYGITEVSS 198
Cdd:cd17655 219 ALTQY-IRQNRITIIDLTPAHL-----KLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGR-------NR-----VCFLDDEVtV 265
Cdd:cd17655 293 DASIYQYEPETDQQV-----SVPIGKPLGNTRIYILDQYGRPQPVGVaGELYIGGEgvargylNRpeltaEKFVDDPF-V 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 266 PLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY----NQEKLILFMVS-KDAS 339
Cdd:cd17655 367 PGERMYRTGDLARwLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARkdeqGQNYLCAYIVSeKELP 446
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1021589396 340 VKEyIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd17655 447 VAQ-LREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKAL 486
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
39-376 |
2.73e-42 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 157.06 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPtsvKLLPS 118
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASvLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGITEVS 197
Cdd:cd04433 79 AALE-LIEREKVTILLGVPTLLARLLKAPeSAGYDLS---SLRALVSGGAPLPP-ELLERFE-EAPGIKLVNGYGLTETG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 198 SWATIYRIPEKTlnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRVcFLDDEVTVPlGT 269
Cdd:cd04433 153 GTVATGPPDDDA-------RKPGSVGRPVPGVEVRIVDPDGGELPPGeigelvvrGPSVMKGYWNNP-EATAAVDED-GW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 270 MRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNIEL--VQQVAEELQQVESCAV------TWynQEKLILFMVSKDAS- 339
Cdd:cd04433 224 YR-TGDLGRLdEDGYLYIVGRLKDMIKSGGE--NVYPaeVEAVLLGHPGVAEAAVvgvpdpEW--GERVVAVVVLRPGAd 298
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1021589396 340 -----VKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd04433 299 ldaeeLRAH----VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
36-380 |
2.91e-41 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341308 [Multi-domain] Cd Length: 433 Bit Score: 156.70 E-value: 2.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 36 KHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFDPSVVEIFLALSSGASLLIVPTSvk 114
Cdd:cd17653 104 PDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVGPGSrVAQVLSI-AFDACIGEIFSTLCNGGTLVLADPS-- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 115 llpSKLASVLFShhrVTVLQATPTLLrrfgsqliksTVLSATT--SLRVLALGGEAfPSLTVLRSWRGEgnkTQIFNVYG 192
Cdd:cd17653 181 ---DPFAHVART---VDALMSTPSIL----------STLSPQDfpNLKTIFLGGEA-VPPSLLDRWSPG---RRLYNAYG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 193 ITEVSSWATIYRI-PEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGG------------RNRVCF 258
Cdd:cd17653 241 PTECTISSTMTELlPGQ----------PVTIGKPIPNSTCYILDADLQPVPEGvVGEICISGvqvargylgnpaLTASKF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 259 LDDEVtVPLGTMRATGD--FVTvKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSK 336
Cdd:cd17653 311 VPDPF-WPGSRMYRTGDygRWT-EDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNGRLVAFVTPE 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1021589396 337 DASVkEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd17653 389 TVDV-DGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
39-380 |
7.88e-41 |
|
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: 155.94 E-value: 7.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVpTSVKLLPS 118
Cdd:cd12115 107 LAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLA-DNVLALPD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 klasvLFSHHRVTVLQATPTLLRrfgsQLIKSTVLSatTSLRVLALGGEAFPSlTVLRSWRGEGNKTQIFNVYGITEVSS 198
Cdd:cd12115 186 -----LPAAAEVTLINTVPSAAA----ELLRHDALP--ASVRVVNLAGEPLPR-DLVQRLYARLQVERVVNLYGPSEDTT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYRIPEKTLNstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRN-RVCFLDDE-------VTVPLGT 269
Cdd:cd12115 254 YSTVAPVPPGASG-------EVSIGRPLANTQAYVLDRALQPVPLGvPGELYIGGAGvARGYLGRPgltaerfLPDPFGP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 270 ---MRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQV-ESCAVTW---YNQEKLILFMVSKD--AS 339
Cdd:cd12115 327 garLYRTGDLVRWRpDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVrEAVVVAIgdaAGERRLVAYIVAEPgaAG 406
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1021589396 340 VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd12115 407 LVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
39-380 |
8.56e-41 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 156.67 E-value: 8.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPA 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASvLFSHHRVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGnkTQIFNVYGITE--- 195
Cdd:cd17646 220 YLAA-LIREHGVTTCHFVPSMLRVF----LAEPAAGSCASLRRVFCSGEALPPELAARFLALPG--AELHNLYGPTEaai 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 -VSSWAtiYRIPEKTlnstlkceLPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------NRVC-----FLDD 261
Cdd:cd17646 293 dVTHWP--VRGPAET--------PSVPIGRPVPNTRLYVLDDALRPVPVGvPGELYLGGVqlargylGRPAltaerFVPD 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 262 evtvPLGT---MRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFM 333
Cdd:cd17646 363 ----PFGPgsrMYRTGDLARWRpDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAApagaARLVGYV 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1021589396 334 VSK-------DASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd17646 439 VPAagaagpdTAALRAH----LAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
39-380 |
2.68e-40 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 153.95 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED-VLFLASPlTFDPSVVEIFLALSSGASLLIVPTSVKLLP 117
Cdd:cd17652 95 LAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVGPGSrVLQFASP-SFDASVWELLMALLAGATLVLAPAEELLPG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASVLfSHHRVTVLQATPTLLRrfgsqlikstVLSATT--SLRVLALGGEAfPSLTVLRSWrgeGNKTQIFNVYGITE 195
Cdd:cd17652 174 EPLADLL-REHRITHVTLPPAALA----------ALPPDDlpDLRTLVVAGEA-CPAELVDRW---APGRRMINAYGPTE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 VSSWATIYRIPEKtlnstlkcELPVQLGFPLLGTVVEVRDTN------GFTiqegsGQVFLGGR-------NR-----VC 257
Cdd:cd17652 239 TTVCATMAGPLPG--------GGVPPIGRPVPGTRVYVLDARlrpvppGVP-----GELYIAGAglargylNRpgltaER 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 258 FLDDEVTVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWYNQE----KLI 330
Cdd:cd17652 306 FVADPFGAPGSRMYRTGDLARwRADGQLEFLGRADDQVKIRGFR--IELgeVEAALTEHPGVAEAVVVVRDDRpgdkRLV 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1021589396 331 LFMV--SKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd17652 384 AYVVpaPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
37-376 |
6.53e-40 |
|
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: 154.04 E-value: 6.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 37 HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLL 116
Cdd:cd17651 136 DDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTD 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASVLfSHHRVTVLQATPTLLRRFGSQLIKSTVLSAttSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYGITEv 196
Cdd:cd17651 216 PPALAAWL-DEQRISRVFLPTVALRALAEHGRPLGVRLA--ALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTE- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 197 SSWATIYRIPektlNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGG-------RNR-----VCFLDDEV 263
Cdd:cd17651 292 THVVTALSLP----GDPAAWPAPPPIGRPIDNTRVYVLDAALRPVPPGvPGELYIGGaglargyLNRpeltaERFVPDPF 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 264 tVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVT----WYNQEKLILFMVSK 336
Cdd:cd17651 368 -VPGARMYRTGDLARwLPDGELEFLGRADDQVKIRGFR--IELgeIEAALARHPGVREAVVLaredRPGEKRLVAYVVGD 444
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1021589396 337 DASVK--EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd17651 445 PEAPVdaAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLD 486
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
39-380 |
2.86e-39 |
|
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: 152.04 E-value: 2.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:cd12114 128 LAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLfSHHRVTVLQATPTLLrrfgsQLIKSTVLSATT---SLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITE 195
Cdd:cd12114 208 HWAELI-ERHGVTLWNSVPALL-----EMLLDVLEAAQAllpSLRLVLLSGDWIP-LDLPARLRALAPDARLISLGGATE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 VSSWATIYRI--PEKTLNStlkcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRN--RVCFLDDEVT----VP 266
Cdd:cd12114 281 ASIWSIYHPIdeVPPDWRS-------IPYGRPLANQRYRVLDPRGRDCPDWvPGELWIGGRGvaLGYLGDPELTaarfVT 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 267 LGTMRA---TGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIEL--VQQVAEELQQVESCAVTWY---NQEKLILFMVSKD 337
Cdd:cd12114 354 HPDGERlyrTGDLGRYRpDGTLEFLGRRDGQVKVRGYR--IELgeIEAALQAHPGVARAVVVVLgdpGGKRLAAFVVPDN 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1021589396 338 -------ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd12114 432 dgtpiapDALRAF----LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
39-444 |
5.41e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 153.78 E-value: 5.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:PRK12467 1720 LAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPE 1799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLfSHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITE--- 195
Cdd:PRK12467 1800 QLIQLI-ERQQVTTLHFVPSMLQQL---LQMDEQVEHPLSLRRVVCGGEALE-VEALRPWLERLPDTGLFNLYGPTEtav 1874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 -VSSWATIYRIPEKTLNStlkcelPVQLGFPLLGTVVEVRDTNGFTIQEgSGQVFLGG-------RNRVC-----FLDDE 262
Cdd:PRK12467 1875 dVTHWTCRRKDLEGRDSV------PIGQPIANLSTYILDASLNPVPIGV-AGELYLGGvglargyLNRPAltaerFVADP 1947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 263 VTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIELVQQVAEELQQ--VESCAVT---WYNQEKLILFMVSK 336
Cdd:PRK12467 1948 FGTVGSRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFR--IELGEIEARLREQggVREAVVIaqdGANGKQLVAYVVPT 2025
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 337 DASVKEY---------IFKE-LQKYLPSHAVPDELVLIDSLPFTSHGKI--------DVSELNKIYlnyinlksenkLSG 398
Cdd:PRK12467 2026 DPGLVDDdeaqvalraILKNhLKASLPEYMVPAHLVFLARMPLTPNGKLdrkalpapDASELQQAY-----------VAP 2094
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1021589396 399 KEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 444
Cdd:PRK12467 2095 QSELEQRLAAIWQDVLGLE----QVGLHDNFFELGGDSIISIQVVS 2136
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-444 |
6.57e-38 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 153.57 E-value: 6.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:PRK12316 657 LAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASvLFSHHRVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSWrGEGNKTQIFNVYGITEVSS 198
Cdd:PRK12316 737 KLVE-LINREGVDTLHFVPSMLQAF----LQDEDVASCTSLRRIVCSGEALPADAQEQVF-AKLPQAGLYNLYGPTEAAI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYripekTLNSTLKCELPVqlGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRN------RVCFLDDE--VTVPLGT 269
Cdd:PRK12316 811 DVTHW-----TCVEEGGDSVPI--GRPIANLACYILDANLEPVPVGvLGELYLAGRGlargyhGRPGLTAErfVPSPFVA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 270 ---MRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKD--ASVKEY 343
Cdd:PRK12316 884 gerMYRTGDLARYRaDGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQLVGYVVLESegGDWREA 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 344 IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLWEKLQYLWKSTLNLPedllRV 423
Cdd:PRK12316 964 LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAP---EASVAQQGYVAPRNALERTLAAIWQDVLGVE----RV 1036
|
410 420
....*....|....*....|.
gi 1021589396 424 PDESLFLNSGGDSLKSIRLLS 444
Cdd:PRK12316 1037 GLDDNFFELGGDSIVSIQVVS 1057
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
39-380 |
7.15e-38 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 147.55 E-value: 7.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQED---VLFLASpLTFDPSVVEIFLALSSGASLLIVPTSVKL 115
Cdd:cd17648 96 LAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGdeaVLFFSN-YVFDFFVEQMTLALLNGQKLVVPPDEMRF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 116 LPSKLASvLFSHHRVTVLQATPTLLRRFGsqlikstvLSATTSLRVLALGGEAF--PSLTVLRSwrgeGNKTQIFNVYGI 193
Cdd:cd17648 175 DPDRFYA-YINREKVTYLSGTPSVLQQYD--------LARLPHLKRVDAAGEEFtaPVFEKLRS----RFAGLIINAYGP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 194 TEVSSWATIYRIP--EKTLNStlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGG-------RNRvcfldDEV 263
Cdd:cd17648 242 TETTVTNHKRFFPgdQRFDKS---------LGRPVRNTKCYVLNDAMKRVPVGAvGELYLGGdgvargyLNR-----PEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 264 T----VP-------------LGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---- 321
Cdd:cd17648 308 TaerfLPnpfqteqerargrNARLYKTGDLVRwLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVvake 387
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021589396 322 -----TWYNQEKLILFMVSKDASVKEY-IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd17648 388 dasqaQSRIQKYLVGYYLPEPGHVPESdLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
37-376 |
7.41e-38 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 147.58 E-value: 7.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 37 HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTsvKLL 116
Cdd:cd17644 106 ENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPE--EMR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASVLFSHH-RVTVLQATPTLLRRFGSQLIKSTvLSATTSLRVLALGGEAF-PSLtvLRSWR-GEGNKTQIFNVYGI 193
Cdd:cd17644 184 SSLEDFVQYIQQwQLTVLSLPPAYWHLLVLELLLST-IDLPSSLRLVIVGGEAVqPEL--VRQWQkNVGNFIQLINVYGP 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 194 TEVSSWATIYRIPEKTLNSTLKcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------NRvcfldDEVTV 265
Cdd:cd17644 261 TEATIAATVCRLTQLTERNITS----VPIGRPIANTQVYILDENLQPVPVGvPGELHIGGVglargylNR-----PELTA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 266 -----------PLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVT----WYNQEKL 329
Cdd:cd17644 332 ekfishpfnssESERLYKTGDLARyLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIvredQPGNKRL 411
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1021589396 330 ILFMVSKdaSVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd17644 412 VAYIVPH--YEESPSTVELRQFlkakLPDYMIPSAFVVLEELPLTPNGKID 460
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
39-376 |
2.02e-36 |
|
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: 143.28 E-value: 2.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:cd17649 96 LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASAD 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASvLFSHHRVTVLQATPTLLRRFgSQLIKSTVLSATTSLRVLALGGEAfpsLTVLRSWRGEGNKTQIFNVYGITEVSS 198
Cdd:cd17649 176 ELAE-MVRELGVTVLDLPPAYLQQL-AEEADRTGDGRPPSLRLYIFGGEA---LSPELLRRWLKAPVRLFNAYGPTEATV 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYRIPEKtlNSTLKCELPvqLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------NRVC-----FLDDEVTV 265
Cdd:cd17649 251 TPLVWKCEAG--AARAGASMP--IGRPLGGRSAYILDADLNPVPVGvTGELYIGGEglargylGRPEltaerFVPDPFGA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 266 PLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---TWYNQEKLILFMVSKDASV- 340
Cdd:cd17649 327 PGSRLYRTGDLARWRdDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVvalDGAGGKQLVAYVVLRAAAAq 406
|
330 340 350
....*....|....*....|....*....|....*....
gi 1021589396 341 ---KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd17649 407 pelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLD 445
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-455 |
3.70e-35 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 145.10 E-value: 3.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKlLPS 118
Cdd:PRK12316 4696 LAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPE 4774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLfSHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNkTQIFNVYGITEVSS 198
Cdd:PRK12316 4775 RLYAEI-HEHRVTVLVFPPVYLQQL---AEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKP-VYLFNGYGPTETTV 4849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYripeKTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR--------------NRvcFLDDEV 263
Cdd:PRK12316 4850 TVLLW----KARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGvAGELYLGGEgvargylerpaltaER--FVPDPF 4923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 264 TVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLnielvqqvaeELQQVESC-------------AVTWYNQEKL 329
Cdd:PRK12316 4924 GAPGGRLYRTGDLARYRaDGVIDYLGRVDHQVKIRGFRI----------ELGEIEARlrehpavreavviAQEGAVGKQL 4993
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 330 ILFMVSKDASVKEYIFKE----------LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIylnYINLKSENKLSGK 399
Cdd:PRK12316 4994 VGYVVPQDPALADADEAQaelrdelkaaLRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP---DASLLQQAYVAPR 5070
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589396 400 EDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 455
Cdd:PRK12316 5071 SELEQQVAAIWAEVLQLE----RVGLDDNFFELGGHSLLAIQVTSRIQLELGLELP 5122
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
39-376 |
2.53e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 137.19 E-value: 2.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVklLPS 118
Cdd:cd05922 119 LALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV--LDD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASvLFSHHRVTVLQATPT---LLRRFGSQLIKstvlsaTTSLRVLALGGEAFPSLTVlRSWRGEGNKTQIFNVYGITE 195
Cdd:cd05922 197 AFWE-DLREHGATGLAGVPStyaMLTRLGFDPAK------LPSLRYLTQAGGRLPQETI-ARLRELLPGAQVYVMYGQTE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 VSSWATiYRIPEKTLNStlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRVCFLDDEVTVpl 267
Cdd:cd05922 269 ATRRMT-YLPPERILEK------PGSIGLAIPGGEFEILDDDGTPTPPGepgeivhrGPNVMKGYWNDPPYRRKEGRG-- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 268 GTMRATGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVT---WYNQEKLILFMVSKDASVKEY 343
Cdd:cd05922 340 GGVLHTGDLaRRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVglpDPLGEKLALFVTAPDKIDPKD 419
|
330 340 350
....*....|....*....|....*....|...
gi 1021589396 344 IFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd05922 420 VLRSLAERLPPYKVPATVRVVDELPLTASGKVD 452
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
20-444 |
1.69e-33 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 139.71 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 20 EHVNEEKAEEHMDLR-LKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFL 98
Cdd:PRK12316 3178 DRGDENYAEANPAIRtMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFW 3257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 99 ALSSGASLLIVPTSVKLLPSKLASVLFShHRVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSLTVLRSW 178
Cdd:PRK12316 3258 PLMSGARVVLAGPEDWRDPALLVELINS-EGVDVLHAYPSMLQAF----LEEEDAHRCTSLKRIVCGGEALPADLQQQVF 3332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 179 RGEgnktQIFNVYGITEVSSWATIYRIPEKTlnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRN--R 255
Cdd:PRK12316 3333 AGL----PLYNLYGPTEATITVTHWQCVEEG-------KDAVPIGRPIANRACYILDGSLEPVPVGAlGELYLGGEGlaR 3401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 256 VCFLDDEVT---------VPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYN 325
Cdd:PRK12316 3402 GYHNRPGLTaerfvpdpfVPGERLYRTGDLARYRaDGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVD 3481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 326 QEKLILFMVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIylnYINLKSENKLSGKEDLW 403
Cdd:PRK12316 3482 GRQLVAYVVPEDEAgdLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP---DAALLQQDYVAPVNELE 3558
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1021589396 404 EKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 444
Cdd:PRK12316 3559 RRLAAIWADVLKLE----QVGLTDNFFELGGDSIISLQVVS 3595
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
37-454 |
3.23e-33 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 138.25 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 37 HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLL 116
Cdd:PRK10252 598 HHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRD 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSlTVLRSWRGEGNkTQIFNVYGITE- 195
Cdd:PRK10252 678 PLAMQQ-FFAEYGVTTTHFVPSMLAAFVASLTPEGARQSCASLRQVFCSGEALPA-DLCREWQQLTG-APLHNLYGPTEa 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 ---VSSWATiyrIPEKTLNSTlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR--------------NRvc 257
Cdd:PRK10252 755 avdVSWYPA---FGEELAAVR---GSSVPIGYPVWNTGLRILDARMRPVPPGvAGDLYLTGIqlaqgylgrpdltaSR-- 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 258 FLDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRlnIEL------------VQQVAEELQQVESCAVTWY 324
Cdd:PRK10252 827 FIADPF-APGERMYRTGDVARwLDDGAVEYLGRSDDQLKIRGQR--IELgeidramqalpdVEQAVTHACVINQAAATGG 903
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 325 NQEKLILFMVSKD------ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiylnyINLKSENKLSG 398
Cdd:PRK10252 904 DARQLVGYLVSQSglpldtSALQAQ----LRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPL-----PELKAQVPGRA 974
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589396 399 KEDLWEK-LQYLWKSTLNLPEdllrVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSV 454
Cdd:PRK10252 975 PKTGTETiIAAAFSSLLGCDV----VDADADFFALGGHSLLAMKLAAQLSRQFARQV 1027
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
37-444 |
3.29e-30 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 129.13 E-value: 3.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 37 HCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLL 116
Cdd:PRK05691 1273 DNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRD 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASVLFSHHrVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPS------LTVLrswrgegNKTQIFNV 190
Cdd:PRK05691 1353 PQRIAELVQQYG-VTTLHFVPPLLQLF----IDEPLAAACTSLRRLFSGGEALPAelrnrvLQRL-------PQVQLHNR 1420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 191 YGITEVSSWATIYRIP-EKTLNStlkcelPVqlGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------NRVCFLDD 261
Cdd:PRK05691 1421 YGPTETAINVTHWQCQaEDGERS------PI--GRPLGNVLCRVLDAELNLLPPGvAGELCIGGAglargylGRPALTAE 1492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 262 E-VTVPLGTMRA----TGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---TWYNQEKLILF 332
Cdd:PRK05691 1493 RfVPDPLGEDGArlyrTGDRARWNaDGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVlvrEGAAGAQLVGY 1572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 333 MVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKiylnyINLKSENKLSGKEDLWEKLQYLW 410
Cdd:PRK05691 1573 YTGEAGQeaEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPE-----PVWQQREHVEPRTELQQQIAAIW 1647
|
410 420 430
....*....|....*....|....*....|....
gi 1021589396 411 KSTLNLPEDLLRvpDEslFLNSGGDSLKSIRLLS 444
Cdd:PRK05691 1648 REVLGLPRVGLR--DD--FFALGGHSLLATQIVS 1677
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
39-380 |
3.40e-30 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 124.50 E-value: 3.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKcivpNIQHF------RVLFDITQEDVLFLASpLTFDPSVVEIFLALSSGASLLIVPTS 112
Cdd:cd17650 95 LAYVIYTSGTTGKPKGVMVEHR----NVAHAahawrrEYELDSFPVRLLQMAS-FSFDVFAGDFARSLLNGGTLVICPDE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 113 VKLLPSKLASVLFShHRVTVLQATPTLLRRFGSQLIKSTVlsATTSLRVLALGGEAFPSLTVLRSWRGEGNKTQIFNVYG 192
Cdd:cd17650 170 VKLDPAALYDLILK-SRITLMESTPALIRPVMAYVYRNGL--DLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYG 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 193 ITEVSSWATIYRIPEKTLNSTLKcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRNrVC-------------F 258
Cdd:cd17650 247 VTEATIDSTYYEEGRDPLGDSAN----VPIGRPLPNTAMYVLDERLQPQPVGvAGELYIGGAG-VArgylnrpeltaerF 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 259 LDDEVtVPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY---NQEK-LILFM 333
Cdd:cd17650 322 VENPF-APGERMYRTGDLARwRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVRedkGGEArLCAYV 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1021589396 334 VSKD----ASVKEYifkeLQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd17650 401 VAAAtlntAELRAF----LAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
39-296 |
3.69e-30 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 123.96 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVL----FDITQEDVLFLASPLTFDPSVV-EIFLALSSGASLLIVPTSV 113
Cdd:pfam00501 157 LAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVrprgFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFP 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 114 KLLPSKLASVLfSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYG 192
Cdd:pfam00501 237 ALDPAALLELI-ERYKVTVLYGVPTLLNMLlEAGAPKRALLS---SLRLVLSGGAPLPP-ELARRFR-ELFGGALVNGYG 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 193 ITEVSSWATIYRIPEKTLNSTLKCelpvqlGFPLLGTVVEVRD--TNGFTIQEGSGQVFLGGRNrV--CFLDD-----EV 263
Cdd:pfam00501 311 LTETTGVVTTPLPLDEDLRSLGSV------GRPLPGTEVKIVDdeTGEPVPPGEPGELCVRGPG-VmkGYLNDpeltaEA 383
|
250 260 270
....*....|....*....|....*....|....
gi 1021589396 264 TVPLGTMRaTGDFVTV-KDGEIFFLGRKDSQIKR 296
Cdd:pfam00501 384 FDEDGWYR-TGDLGRRdEDGYLEIVGRKKDQIKL 416
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
39-455 |
3.81e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 128.74 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKlLPS 118
Cdd:PRK12467 3239 LAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPE 3317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLFSHHrVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKtQIFNVYGITEVSS 198
Cdd:PRK12467 3318 ELWQAIHAHR-ISIACFPPAYLQ----QFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPR-GLTNGYGPTEAVV 3391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYRIPektlnSTLKCELP-VQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGrnrVC---------------FLDD 261
Cdd:PRK12467 3392 TVTLWKCG-----GDAVCEAPyAPIGRPVAGRSIYVLDGQLNPVPVGvAGELYIGG---VGlargyhqrpsltaerFVAD 3463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 262 EVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRlnIELVQQVAEELQQ--VESCAVTWYNQE---KLILFMVS 335
Cdd:PRK12467 3464 PFSGSGGRLYRTGDLARYRaDGVIEYLGRIDHQVKIRGFR--IELGEIEARLLQHpsVREAVVLARDGAggkQLVAYVVP 3541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 336 KD--ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNyinlKSENKLSGKEDLWEKLQYLWkst 413
Cdd:PRK12467 3542 ADpqGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAK----GSREYVAPRSEVEQQLAAIW--- 3614
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1021589396 414 lnlpEDLLRVPDESL---FLNSGGDSLKSIRLLSEIEKLVGTSVP 455
Cdd:PRK12467 3615 ----ADVLGVEQVGVtdnFFELGGDSLLALQVLSRIRQSLGLKLS 3655
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-455 |
8.70e-30 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.77 E-value: 8.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLlPS 118
Cdd:PRK12316 2148 LAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWD-PE 2226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASVLfSHHRVTVLQATPTLLRRFGSQLiksTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGnKTQIFNVYGITEVSS 198
Cdd:PRK12316 2227 QLYDEM-ERHGVTILDFPPVYLQQLAEHA---ERDGRPPAVRVYCFGGEAVPAASLRLAWEALR-PVYLFNGYGPTEAVV 2301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYripektlnstlKC--ELPVQLGFPLLGTVVEVRDT----NGFTI--QEGSGQVFLGGR-------NRVC-----F 258
Cdd:PRK12316 2302 TPLLW-----------KCrpQDPCGAAYVPIGRALGNRRAyildADLNLlaPGMAGELYLGGEglargylNRPGltaerF 2370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 259 LDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTwyNQE-----KLILF 332
Cdd:PRK12316 2371 VPDPFSASGERLYRTGDLARYRaDGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVV--AQDgasgkQLVAY 2448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 333 MVSKDAS--VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLnyiNLKSENKLSGKEDLWEKLQYLW 410
Cdd:PRK12316 2449 VVPDDAAedLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDV---SQLRQAYVAPQEGLEQRLAAIW 2525
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1021589396 411 KSTLNLPedllRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 455
Cdd:PRK12316 2526 QAVLKVE----QVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVP 2566
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
39-376 |
4.30e-29 |
|
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: 121.12 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPS 118
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLASvLFSHHRVTVlQATPTllrrfgsQLIKSTVLSATTSLRVLALGGEafpsltVLRswRGEGNKTQIFNVYGITEVSS 198
Cdd:cd17645 186 ALND-YFNQEGITI-SFLPT-------GAAEQFMQLDNQSLRVLLTGGD------KLK--KIERKGYKLVNNYGPTENTV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATIYRIPEKTLNstlkcelpVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGR-------NRvcfldDEVT------ 264
Cdd:cd17645 249 VATSFEIDKPYAN--------IPIGKPIDNTRVYILDEALQLQPIGvAGELCIAGEglargylNR-----PELTaekfiv 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 265 ---VPLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LILFMVSK 336
Cdd:cd17645 316 hpfVPGERMYRTGDLAKfLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADgrkyLVAYVTAP 395
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1021589396 337 DASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd17645 396 EEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVD 435
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
41-382 |
1.62e-27 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 117.30 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 41 YVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDItQEDVLFLA-SPLTFDPSVVEIFLALSSGASLLIVPTSVKLLPSK 119
Cdd:PRK04813 147 YIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFAL-PEGPQFLNqAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 120 LASVLFSHHrVTVLQATPT------LLRRFGSQLIkstvlsatTSLRVLALGGEAFPSLTVlRSWRGEGNKTQIFNVYGI 193
Cdd:PRK04813 226 LFETLPQLP-INVWVSTPSfadmclLDPSFNEEHL--------PNLTHFLFCGEELPHKTA-KKLLERFPSATIYNTYGP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 194 TEVSSWATIYRIPEKTLNstlKCE-LPVqlGFPLLGTVVEVRDTNG---FTIQEG----SGQ-VFLGgrnrvcFLD---- 260
Cdd:PRK04813 296 TEATVAVTSIEITDEMLD---QYKrLPI--GYAKPDSPLLIIDEEGtklPDGEQGeiviSGPsVSKG------YLNnpek 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 261 -DEVTVPLGTMRA--TGDFVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFM 333
Cdd:PRK04813 365 tAEAFFTFDGQPAyhTGDAGYLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDhkvqYLIAYV 444
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589396 334 VSKDASV-KEY-----IFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDV----SELNK 382
Cdd:PRK04813 445 VPKEEDFeREFeltkaIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRkaliEEVNK 503
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
18-380 |
5.47e-25 |
|
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: 109.49 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 18 SSEHVNEEKAEEHmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVpNIQHFRvlFDITQ----EDVLFLASPlTFDPSV 93
Cdd:cd17656 117 DTSNIDYINNSDD--------LLYIIYTSGTTGKPKGVQLEHKNMV-NLLHFE--REKTNinfsDKVLQFATC-SFDVCY 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 94 VEIFLALSSGASLLIVPTSVKLLPSKLASvLFSHHRVTVLQATPTLLRRFGSQliKSTVLSATTSLRVLALGGEAFPSLT 173
Cdd:cd17656 185 QEIFSTLLSGGTLYIIREETKRDVEQLFD-LVKRHNIEVVFLPVAFLKFIFSE--REFINRFPTCVKHIITAGEQLVITN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 174 VLRSWRGEGNKTqIFNVYGITEvSSWATIYRI-PEKTLNstlkcELPvQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLG 251
Cdd:cd17656 262 EFKEMLHEHNVH-LHNHYGPSE-THVVTTYTInPEAEIP-----ELP-PIGKPISNTWIYILDQEQQLQPQGIvGELYIS 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 252 GRN--RVCFLDDEVTV---------PLGTMRATGDFVT-VKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESC 319
Cdd:cd17656 334 GASvaRGYLNRQELTAekffpdpfdPNERMYRTGDLARyLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEA 413
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021589396 320 AV-TWYNQEK---LILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd17656 414 VVlDKADDKGekyLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
33-444 |
1.16e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 104.87 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 33 LRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASllIVPTS 112
Cdd:PRK05691 2329 LSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGAR--VVLRA 2406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 113 VKLLPSKLASVLFSHHRVTVLQATPTllrrFGSQLIKSTVLS-ATTSLRVLALGGEAfpsLTV--LRSWRGEGNKTQIFN 189
Cdd:PRK05691 2407 QGQWGAEEICQLIREQQVSILGFTPS----YGSQLAQWLAGQgEQLPVRMCITGGEA---LTGehLQRIRQAFAPQLFFN 2479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 190 VYGITEVSSWATIYRIPEKtlnstlkceLPVQLGFPLLGTVVEVR-----DTN-GFTIQEGSGQVFLGGR---------- 253
Cdd:PRK05691 2480 AYGPTETVVMPLACLAPEQ---------LEEGAASVPIGRVVGARvayilDADlALVPQGATGELYVGGAglaqgyhdrp 2550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 254 ----NRvcFLDDEVTVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE- 327
Cdd:PRK05691 2551 gltaER--FVADPFAADGGRLYRTGDLVRLRaDGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPs 2628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 328 --KLILFMVSKDAS--------VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNkiyLNYINLKSENKLS 397
Cdd:PRK05691 2629 gkQLAGYLVSAVAGqddeaqaaLREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP---APDPELNRQAYQA 2705
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1021589396 398 GKEDLWEKLQYLWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLS 444
Cdd:PRK05691 2706 PRSELEQQLAQIWREVLNVE----RVGLGDNFFELGGDSILSIQVVS 2748
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
40-386 |
1.30e-21 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 99.80 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVpnIQH---FRVLFDITQEDVLFLASPL---TFDPSVVeiFLALSSGASLLI---VP 110
Cdd:COG0365 187 LFILYTSGTTGKPKGVVHTHGGYL--VHAattAKYVLDLKPGDVFWCTADIgwaTGHSYIV--YGPLLNGATVVLyegRP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 111 TSVKllPSKLASVLfSHHRVTVLQATPTLLR---RFGSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQI 187
Cdd:COG0365 263 DFPD--PGRLWELI-EKYGVTVFFTAPTAIRalmKAGDEPLKKYDLS---SLRLLGSAGEPLNP-EVWEWWY-EAVGVPI 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 188 FNVYGITEVSSW--ATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFL----D 260
Cdd:COG0365 335 VDGWGQTETGGIfiSNLPGLPVK----------PGSMGKPVPGYDVAVVDEDGNPVPPGEeGELVIKGPWPGMFRgywnD 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 261 DEVTV------PLGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRL---NIE--LVQ--QVAEelqqvesCAVTWYNQ 326
Cdd:COG0365 405 PERYRetyfgrFPGWYR-TGDGARRdEDGYFWILGRSDDVINVSGHRIgtaEIEsaLVShpAVAE-------AAVVGVPD 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589396 327 E----KLILFMVSKD-ASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLN 386
Cdd:COG0365 477 EirgqVVKAFVVLKPgVEPSDELAKELQAHvreeLGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEG 545
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
39-455 |
5.48e-21 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 99.47 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNiQHFRVLF-DITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKLLP 117
Cdd:PRK05691 3871 LAYVIYTSGSTGLPKGVMVEQRGMLNN-QLSKVPYlALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDP 3949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLAsVLFSHHRVTVLQATPTLLRRFGSQlikstVLSATTSLRVLALGGEAFPSLtVLRSWRGEGNKTQIFNVYGITEVS 197
Cdd:PRK05691 3950 QGLL-AHVQAQGITVLESVPSLIQGMLAE-----DRQALDGLRWMLPTGEAMPPE-LARQWLQRYPQIGLVNAYGPAECS 4022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 198 SWATIYRIpekTLNSTLKCELPVqlGFPL----------------LGTVVE--VRDTngftiqeGSGQVFLGG--RNRVC 257
Cdd:PRK05691 4023 DDVAFFRV---DLASTRGSYLPI--GSPTdnnrlylldealelvpLGAVGElcVAGT-------GVGRGYVGDplRTALA 4090
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 258 FLDDEVTVPLGTMRATGDFV-TVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV---TWYNQEKLILFM 333
Cdd:PRK05691 4091 FVPHPFGAPGERLYRTGDLArRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVavqEGVNGKHLVGYL 4170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 334 VSKDASVK-----EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNyiNLKSENKLSGKEDLWEKLQY 408
Cdd:PRK05691 4171 VPHQTVLAqgallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIG--QLQSQAYLAPRNELEQTLAT 4248
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1021589396 409 LWKSTLNLPedllRVPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 455
Cdd:PRK05691 4249 IWADVLKVE----RVGVHDNFFELGGHSLLATQIASRVQKALQRNVP 4291
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
42-375 |
1.20e-20 |
|
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: 94.25 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 42 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRV-LFDITQEDVLFLASPLTFDPSVVEIFLALSSGAsLLIVPTSVKLLPSKL 120
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKeGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 121 ASVLFshHRVTVLQATPTLLRRFGSqLIKSTvLSATTSLRVLALGGE-AFPSLTVLRSWRGegnKTQIFNVYGITEVSSW 199
Cdd:cd17635 85 KILTT--NAVTTTCLVPTLLSKLVS-ELKSA-NATVPSLRLIGYGGSrAIAADVRFIEATG---LTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 200 ATI-YRIPEKTLNStlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS-GQ-VFLGGRNRVCFLDDEVTVP---LGTMRAT 273
Cdd:cd17635 158 LCLpTDDDSIEINA---------VGRPYPGVDVYLAATDGIAGPSASfGTiWIKSPANMLGYWNNPERTAevlIDGWVNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 274 GDFV-TVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFMVS---KDASVKEYIF 345
Cdd:cd17635 229 GDLGeRREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDeefgELVGLAVVAsaeLDENAIRALK 308
|
330 340 350
....*....|....*....|....*....|
gi 1021589396 346 KELQKYLPSHAVPDELVLIDSLPFTSHGKI 375
Cdd:cd17635 309 HTIRRELEPYARPSTIVIVTDIPRTQSGKV 338
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
41-376 |
1.44e-19 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 90.54 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 41 YVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIvptSVKLLPSKL 120
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 121 ASVLfSHHRVTVLQATPTLLRrfgsQLIKstVLSATTSLRVLALGGEAFPSLTvLRSWRGEGNKTQIFNVYGITEVSSWA 200
Cdd:cd17633 81 IRKI-NQYNATVIYLVPTMLQ----ALAR--TLEPESKIKSIFSSGQKLFEST-KKKLKNIFPKANLIEFYGTSELSFIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 201 tiYRIPEKTlnstlkcELPVQLGFPLLGTVVEVRDTNGF---TIQEGSGQVFLGgrnrvcFLDDEVTVPLGTMrATGDFV 277
Cdd:cd17633 153 --YNFNQES-------RPPNSVGRPFPNVEIEIRNADGGeigKIFVKSEMVFSG------YVRGGFSNPDGWM-SVGDIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 278 TVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK---LILFMVSKDASVKEYIFKELQKYLP 353
Cdd:cd17633 217 YVDeEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARfgeIAVALYSGDKLTYKQLKRFLKQKLS 296
|
330 340
....*....|....*....|...
gi 1021589396 354 SHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd17633 297 RYEIPKKIIFVDSLPYTSSGKIA 319
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
39-382 |
2.04e-19 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 92.39 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFlaSPLTFDPS---VVEIFLALSSGASLLIV--PTSV 113
Cdd:cd05909 149 PAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVF--GALPFFHSfglTGCLWLPLLSGIKVVFHpnPLDY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 114 KLLPSklasvLFSHHRVTVLQATPTLLRRFgsqlIKSTVLSATTSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGI 193
Cdd:cd05909 227 KKIPE-----LIYDKKATILLGTPTFLRGY----ARAAHPEDFSSLRLVVAGAEKLKD-TLRQEFQ-EKFGIRILEGYGT 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 194 TEVSswatiyriPEKTLNSTLKCELPVQLGFPLLGT---VVEVRDTNGFTIQEGsGQVFLGGRNRVC-FLDDE---VTVP 266
Cdd:cd05909 296 TECS--------PVISVNTPQSPNKEGTVGRPLPGMevkIVSVETHEEVPIGEG-GLLLVRGPNVMLgYLNEPeltSFAF 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 267 LGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEEL--QQVESCAVTWYNQ---EKLILFMVSKDASV 340
Cdd:cd05909 367 GDGWYDTGDIGKIdGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGrkgEKIVLLTTTTDTDP 446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1021589396 341 keyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:cd05909 447 -----SSLNDILKNAgisnlAKPSYIHQVEEIPLLGTGKPDYVTLKA 488
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
39-376 |
1.74e-18 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 88.82 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT-FDPSVVEIFLALSSGASLLIVPtsvKLLP 117
Cdd:cd17631 100 LALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVILR---KFDP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASvLFSHHRVTVLQATPTLLrrfgsQLIKSTVLSATT---SLRVLALGGEAFPSLtVLRSWRGEGnkTQIFNVYGIT 194
Cdd:cd17631 177 ETVLD-LIERHRVTSFFLVPTMI-----QALLQHPRFATTdlsSLRAVIYGGAPMPER-LLRALQARG--VKFVQGYGMT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 195 EVSSWATIYRiPEKTLnstlkcELPVQLGFPLLGTVVEVRDTNGFTIQEG--------SGQVFLGGRNRvcfldDEVTVP 266
Cdd:cd17631 248 ETSPGVTFLS-PEDHR------RKLGSAGRPVFFVEVRIVDPDGREVPPGevgeivvrGPHVMAGYWNR-----PEATAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 267 L---GTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNI---ElVQQVAEELQQVESCAV------TWynQEKLILFM 333
Cdd:cd17631 316 AfrdGWFH-TGDLGRLdEDGYLYIVDRKKDMIISGGE--NVypaE-VEDVLYEHPAVAEVAVigvpdeKW--GEAVVAVV 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1021589396 334 VSKDASV--KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd17631 390 VPRPGAEldEDELIAHCRERLARYKIPKSVEFVDALPRNATGKIL 434
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
39-375 |
4.00e-18 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 87.82 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT-FDPSVVEIFLALSSGASLLIVPTsvkLLP 117
Cdd:cd05903 95 VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKlASVLFSHHRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRVLALGGEAFPSLTVLRSWRGEGNKtqIFNVYGITE 195
Cdd:cd05903 172 DK-ALALMREHGVTFMMGATPFL----TDLLNAVEEAGEplSRLRTFVCGGATVPRSLARRAAELLGAK--VCSAYGSTE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 VSSWATIYRIPEKTLNSTLKcelpvqlGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVC-FLDDevtvPLGTMRA- 272
Cdd:cd05903 245 CPGAVTSITPAPEDRRLYTD-------GRPLPGVEIKVVDDTGATLAPGVeGELLSRGPSVFLgYLDR----PDLTADAa 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 273 ------TGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDASvk 341
Cdd:cd05903 314 pegwfrTGDLaRLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVALPDERLgeraCAVVVTKSGA-- 391
|
330 340 350
....*....|....*....|....*....|....*....
gi 1021589396 342 EYIFKELQKYLPSHAV-----PDELVLIDSLPFTSHGKI 375
Cdd:cd05903 392 LLTFDELVAYLDRQGVakqywPERLVHVDDLPRTPSGKV 430
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
39-380 |
5.94e-18 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 87.13 E-value: 5.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHF-RVLFDITQEDVLFLASPLTFDPSV-VEIFLALSSGASLLIVPTSVKll 116
Cdd:cd05919 93 IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWPT-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASVLfSHHRVTVLQATPTLLRRfgsqLIKSTVLS--ATTSLRVLALGGEAFPsltvlrswRGEGNK------TQIF 188
Cdd:cd05919 171 AERVLATL-ARFRPTVLYGVPTFYAN----LLDSCAGSpdALRSLRLCVSAGEALP--------RGLGERwmehfgGPIL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 189 NVYGITEVSSWATIYRIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGG--------RNRvcfl 259
Cdd:cd05919 238 DGIGATEVGHIFLSNRPGAWRLGST---------GRPVPGYEIRLVDEEGHTIPPGEeGDLLVRGpsaavgywNNP---- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 260 DDEVTVPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMV 334
Cdd:cd05919 305 EKSRATFNGGWYRTGDKFCRdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPEStglsRLTAFVV 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1021589396 335 SK-----DASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd05919 385 LKspaapQESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
40-376 |
1.32e-17 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 86.65 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHF-RVLFDITQEDVLFlaspltfdpSVVEIFLALSSGASL---LIVPTSVKL 115
Cdd:cd05959 166 AFWLYSSGSTGRPKGVVHLHADIYWTAELYaRNVLGIREDDVCF---------SAAKLFFAYGLGNSLtfpLSVGATTVL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 116 LPSKLASVLFSH----HRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRVLALGGEAFPSlTVLRSWRgegNKT--QI 187
Cdd:cd05959 237 MPERPTPAAVFKrirrYRPTVFFGVPTLY----AAMLAAPNLPSRdlSSLRLCVSAGEALPA-EVGERWK---ARFglDI 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 188 FNVYGITEVsswATIY---RIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTIQEG-SGQVFL-GGRNRVCFL--- 259
Cdd:cd05959 309 LDGIGSTEM---LHIFlsnRPGRVRYGTT---------GKPVPGYEVELRDEDGGDVADGePGELYVrGPSSATMYWnnr 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 260 DDEVTVPLGTMRATGD-FVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMV 334
Cdd:cd05959 377 DKTRDTFQGEWTRTGDkYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEdgltKPKAFVV 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1021589396 335 SKD-ASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd05959 457 LRPgYEDSEALEEELKEFvkdrLAPYKYPRWIVFVDELPKTATGKIQ 503
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
39-382 |
2.58e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 81.37 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL-TFDPSVVEIFLALSSGASLLIVPTSVKLLP 117
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPLfHVNGSVVTLLTPLASGAHVVLAGPAGYRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASV--LFSHHRVTVLQATPTLLrrfgSQLIKSTVLSATTSLRVLALGGEAFPslTVLRSWRGEGNKTQIFNVYGITE 195
Cdd:cd05944 84 GLFDNFwkLVERYRITSLSTVPTVY----AALLQVPVNADISSLRFAMSGAAPLP--VELRARFEDATGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 VSSWATI-YRIPEKTLNStlkcelpVQLGFPLLGTVVEVRDTNGFTIQE-GSGQVF---------LGG-----RNRVCFL 259
Cdd:cd05944 158 ATCLVAVnPPDGPKRPGS-------VGLRLPYARVRIKVLDGVGRLLRDcAPDEVGeicvagpgvFGGylyteGNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 260 DDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLILFM- 333
Cdd:cd05944 231 AD------GWLN-TGDLGRLdADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGqpdaHAGELPVAYVq 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1021589396 334 VSKDASVKEyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:cd05944 304 LKPGAVVEE---EELLAWARDHvperaAVPKHIEVLEELPVTAVGKVFKPALRA 354
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
39-380 |
4.36e-16 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 81.84 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQ--HFRVLFDITQEDVLFLASPL--TFDPSVVeIFLALSSGASLLIVPTSVk 114
Cdd:cd05936 127 VAVLQYTSGTTGVPKGAMLTHRNLVANALqiKAWLEDLLEGDDVVLAALPLfhVFGLTVA-LLLPLALGATIVLIPRFR- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 115 llpSKLASVLFSHHRVTVLQATPTLLrrfgSQLI--KSTVLSATTSLRVLALGGEAFPsLTVLRSWRgegnktQIFNV-- 190
Cdd:cd05936 205 ---PIGVLKEIRKHRVTIFPGVPTMY----IALLnaPEFKKRDFSSLRLCISGGAPLP-VEVAERFE------ELTGVpi 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 191 ---YGITEVSSWATIYRIPEKTLNSTlkcelpvqLGFPLLGTVVEVRDTNGFTIQEGS--------GQVFLGGRNRvcfl 259
Cdd:cd05936 271 vegYGLTETSPVVAVNPLDGPRKPGS--------IGIPLPGTEVKIVDDDGEELPPGEvgelwvrgPQVMKGYWNR---- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 260 ddevtvPLGTMRA-------TGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNI---ElVQQVAEELQQVESCAVTW----Y 324
Cdd:cd05936 339 ------PEETAEAfvdgwlrTGDIGYMdEDGYFFIVDRKKDMIIVGG--FNVyprE-VEEVLYEHPAVAEAAVVGvpdpY 409
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1021589396 325 NQEKLILFMVSKD-ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd05936 410 SGEAVKAFVVLKEgASLtEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
41-375 |
1.57e-14 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 77.23 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 41 YVLHTSGTTGIPK-IVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL---TFDPSVveIFLALSSGA-SLLIVPTSVKL 115
Cdd:cd17634 236 FILYTSGTTGKPKgVLHTTGGYLVYAATTMKYVFDYGPGDIYWCTADVgwvTGHSYL--LYGPLACGAtTLLYEGVPNWP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 116 LPSKLASVLfSHHRVTVLQATPTLLRRF---GSQLIKSTVLSattSLRVLALGGEAFPSLTVLRSWRG-EGNKTQIFNVY 191
Cdd:cd17634 314 TPARMWQVV-DKHGVNILYTAPTAIRALmaaGDDAIEGTDRS---SLRILGSVGEPINPEAYEWYWKKiGKEKCPVVDTW 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 192 GITEVsSWATIYRIPEKTlnsTLKCELPVQlgfPLLGTVVEVRDTNGFTIQEGS-GQVFLG----GRNRVCFLDDE---V 263
Cdd:cd17634 390 WQTET-GGFMITPLPGAI---ELKAGSATR---PVFGVQPAVVDNEGHPQPGGTeGNLVITdpwpGQTRTLFGDHErfeQ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 264 TV--PLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMVSK 336
Cdd:cd17634 463 TYfsTFKGMYFSGDGARRdEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAikgqAPYAYVVLN 542
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1021589396 337 D---------ASVKEYIFKELQKYlpshAVPDELVLIDSLPFTSHGKI 375
Cdd:cd17634 543 HgvepspelyAELRNWVRKEIGPL----ATPDVVHWVDSLPKTRSGKI 586
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
43-375 |
3.06e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 75.63 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 43 LHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASpltfDP-------SVVEIFLALSSGASLLIVPTSVKL 115
Cdd:cd05973 94 MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWNAA----DPgwayglyYAITGPLALGHPTILLEGGFSVES 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 116 LPSKLasvlfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATT---SLRVLALGGEafPSLTVLRSWRGEGNKTQIFNVYG 192
Cdd:cd05973 170 TWRVI-----ERLGVTNLAGSPTAYR----LLMAAGAEVPARpkgRLRRVSSAGE--PLTPEVIRWFDAALGVPIHDHYG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 193 ITEVSswatiyripeKTLNSTLKCELPVQ---LGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVC-----FLDDEV 263
Cdd:cd05973 239 QTELG----------MVLANHHALEHPVHagsAGRAMPGWRVAVLDDDGDELGPGEpGRLAIDIANSPLmwfrgYQLPDT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 264 TVPLGTMRATGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLILFMV---S 335
Cdd:cd05973 309 PAIDGGYYLTGDTVEFDpDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGvpdpERTEVVKAFVVlrgG 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1021589396 336 KDASvkEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKI 375
Cdd:cd05973 389 HEGT--PALADELQLHvkkrLSAHAYPRTIHFVDELPKTPSGKI 430
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
45-376 |
7.58e-14 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 74.44 E-value: 7.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 45 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASP---LTFDPSVVEIFlALSSGASLLIVPTSVkllPSKLA 121
Cdd:cd05958 105 TSGTTGAPKATMHFHRDPLASADRYAVNVLRLREDDRFVGSPplaFTFGLGGVLLF-PFGVGASGVLLEEAT---PDLLL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 122 SVLfSHHRVTVLQATPTLLR------RFGSQLIkstvlsatTSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVYGITE 195
Cdd:cd05958 181 SAI-ARYKPTVLFTAPTAYRamlahpDAAGPDL--------SSLRKCVSAGEALPA-ALHRAWK-EATGIPIIDGIGSTE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 vsswatIYRIpekTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDE--VTVPLGTMRA 272
Cdd:cd05958 250 ------MFHI---FISARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTiGRLAVRGPTGCRYLADKrqRTYVQGGWNI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 273 TGD-FVTVKDGEIFFLGRKDSQIKRHGkrLNIELVqQVAEELQQ---VESCAVTWY-NQEKLIL---FMVSK-DASVKEY 343
Cdd:cd05958 321 TGDtYSRDPDGYFRHQGRSDDMIVSGG--YNIAPP-EVEDVLLQhpaVAECAVVGHpDESRGVVvkaFVVLRpGVIPGPV 397
|
330 340 350
....*....|....*....|....*....|....*..
gi 1021589396 344 IFKELQKYLPSHAV----PDELVLIDSLPFTSHGKID 376
Cdd:cd05958 398 LARELQDHAKAHIApykyPRAIEFVTELPRTATGKLQ 434
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
40-375 |
7.76e-14 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 74.46 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFlaspLTFDPSVVE-----IFLALSSGASLLIVPTsvK 114
Cdd:cd05969 92 TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYW----CTADPGWVTgtvygIWAPWLNGVTNVVYEG--R 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 115 LLPSKLASVLfSHHRVTVLQATPTLLR---RFGSQLIKSTVLSattSLRVLALGGEAFPSLTVlrSWRGEGNKTQIFNVY 191
Cdd:cd05969 166 FDAESWYGII-ERVKVTVWYTAPTAIRmlmKEGDELARKYDLS---SLRFIHSVGEPLNPEAI--RWGMEVFGVPIHDTW 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 192 GITEVSSW--ATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFL--------------GGRN 254
Cdd:cd05969 240 WQTETGSImiANYPCMPIK----------PGSMGKPLPGVKAAVVDENGNELPPGTkGILALkpgwpsmfrgiwndEERY 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 255 RVCFLDDEVTvplgtmraTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTwyNQEKLIL-- 331
Cdd:cd05969 310 KNSFIDGWYL--------TGDLAYRdEDGYFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVI--GKPDPLRge 379
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1021589396 332 ----FMVSKDA-----SVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 375
Cdd:cd05969 380 iikaFISLKEGfepsdELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
17-384 |
1.00e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 74.45 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 17 ISSEHVNEEKAEEhmdlrlkhcLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEI 96
Cdd:cd05908 95 ITEEEVLCELADE---------LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 97 FLA-LSSGASLLIVPTSVKLLPSKLASVLFSHHRVTVLqATPTllrrFGSQLIKSTVLSAT------TSLRVLALGGEAF 169
Cdd:cd05908 166 HLApLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIV-SSPN----FGYKYFLKTLKPEKandwdlSSIRMILNGAEPI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 170 PS------LTVLRSWRgeGNKTQIFNVYGITEVSSWATIYRIPEKTLNSTL-------------------KCELPVQLGF 224
Cdd:cd05908 241 DYelchefLDHMSKYG--LKRNAILPVYGLAEASVGASLPKAQSPFKTITLgrrhvthgepepevdkkdsECLTFVEVGK 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 225 PLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNrvcflddeVTV-----PLGTMRA--------TGDFVTVKDGEIFFLGRK 290
Cdd:cd05908 319 PIDETDIRICDEDNKILPDGYiGHIQIRGKN--------VTPgyynnPEATAKVftddgwlkTGDLGFIRNGRLVITGRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 291 DSQIKRHGKRLNIELVQQVAEELQQVES-----CAV--TWYNQEKLILFMVSKDaSVKEYIfkELQKYLPSHAVP----- 358
Cdd:cd05908 391 KDIIFVNGQNVYPHDIERIAEELEGVELgrvvaCGVnnSNTRNEEIFCFIEHRK-SEDDFY--PLGKKIKKHLNKrggwq 467
|
410 420
....*....|....*....|....*..
gi 1021589396 359 -DELVLIDSLPFTSHGKIDVSELNKIY 384
Cdd:cd05908 468 iNEVLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
39-376 |
1.22e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 74.07 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdpsvveiF---------LALSSGASLLIV 109
Cdd:PRK06187 169 AAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM---------FhvhawglpyLALMAGAKQVIP 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 110 PtsvKLLPSKLASvLFSHHRVTVLQATPTLLRRFGSQLIKSTVlsATTSLRVLALGGEAFPsLTVLRSWRgEGNKTQIFN 189
Cdd:PRK06187 240 R---RFDPENLLD-LIETERVTFFFAVPTIWQMLLKAPRAYFV--DFSSLRLVIYGGAALP-PALLREFK-EKFGIDLVQ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 190 VYGITEVSSWATIYRIPEKTLNSTlkcELPVQLGFPLLGtvVEVR--DTNGFTI--QEGS-GQVFLGGRN--RVCFLDDE 262
Cdd:PRK06187 312 GYGMTETSPVVSVLPPEDQLPGQW---TKRRSAGRPLPG--VEARivDDDGDELppDGGEvGEIIVRGPWlmQGYWNRPE 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 263 VTVPL---GTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNI---ELvqqvaEEL----QQVESCAV------TWyn 325
Cdd:PRK06187 387 ATAETidgGWLH-TGDVGYIdEDGYLYITDRIKDVIISGGE--NIyprEL-----EDAlyghPAVAEVAVigvpdeKW-- 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589396 326 QEKLILFMVSKD-ASVKEyifKELQKYLPSH----AVPDELVLIDSLPFTSHGKID 376
Cdd:PRK06187 457 GERPVAVVVLKPgATLDA---KELRAFLRGRlakfKLPKRIAFVDELPRTSVGKIL 509
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
39-382 |
2.96e-13 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 72.75 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASpltfDPSvvEIFLALSSGASLLIVPTSV----- 113
Cdd:cd05972 83 PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNIA----DPG--WAKGAWSSFFGPWLLGATVfvyeg 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 114 -KLLPSKLASVLfSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEafpSLT--VLRSWRGEGNKTqIFNV 190
Cdd:cd05972 157 pRFDAERILELL-ERYGVTSFCGPPTAYRMLIKQDLSSYKFS---HLRLVVSAGE---PLNpeVIEWWRAATGLP-IRDG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 191 YGITEVSSwatiyripekTLNSTLKCEL-PVQLGFPLLGTVVEVRDTNG----------FTIQEGSGQVFLGgrnrvcFL 259
Cdd:cd05972 229 YGQTETGL----------TVGNFPDMPVkPGSMGRPTPGYDVAIIDDDGrelppgeegdIAIKLPPPGLFLG------YV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 260 DDEVtvplgTMRA--------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRL---NIE--LVQQVAeelqqVESCAVTWYN 325
Cdd:cd05972 293 GDPE-----KTEAsirgdyylTGDRAYRdEDGYFWFVGRADDIIKSSGYRIgpfEVEsaLLEHPA-----VAEAAVVGSP 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589396 326 QEkLILFMV------SKDASVKEYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:cd05972 363 DP-VRGEVVkafvvlTSGYEPSEELAEELQGHvkkvLAPYKYPREIEFVEELPKTISGKIRRVELRD 428
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
39-382 |
2.99e-13 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 73.24 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLT----FDPSVVEIFLAlsSGASLLIvptsvK 114
Cdd:PRK06087 189 LAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGhatgFLHGVTAPFLI--GARSVLL-----D 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 115 LLPSKLASVLFSHHRVT-VLQATP------TLLRRFGSQLikstvlsatTSLRVLALGGEAFPSLTVLRSWRgegNKTQI 187
Cdd:PRK06087 262 IFTPDACLALLEQQRCTcMLGATPfiydllNLLEKQPADL---------SALRFFLCGGTTIPKKVARECQQ---RGIKL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 188 FNVYGITEVSSWAtiYRIPEKTLNSTLKCElpvqlGFPLLGTVVEVRDTNGFTI------QEGS--GQVFLGgrnrvcFL 259
Cdd:PRK06087 330 LSVYGSTESSPHA--VVNLDDPLSRFMHTD-----GYAAAGVEIKVVDEARKTLppgcegEEASrgPNVFMG------YL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 260 DDevtvPLGTMRA--------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL- 329
Cdd:PRK06087 397 DE----PELTARAldeegwyySGDLCRMdEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLg 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 330 ---ILFMVSKDA----SVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:PRK06087 473 ersCAYVVLKAPhhslTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
39-380 |
4.12e-13 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 72.08 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIV---PNIQHFRVLFDITqEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVKL 115
Cdd:cd05971 90 PALIIYTSGTTGPPKGALHAHRVLLghlPGVQFPFNLFPRD-GDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 116 LPSKLASVLfSHHRVTVLQATPTLLRRFGSQliKSTVLSATTSLRVLALGGEafPSLTVLRSWRGEGNKTQIFNVYGITE 195
Cdd:cd05971 169 DPKAALDLM-SRYGVTTAFLPPTALKMMRQQ--GEQLKHAQVKLRAIATGGE--SLGEELLGWAREQFGVEVNEFYGQTE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 ----VSSWATIYRIPektlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFL----DDEVTV- 265
Cdd:cd05971 244 cnlvIGNCSALFPIK------------PGSMGKPIPGHRVAIVDDNGTPLPPGEvGEIAVELPDPVAFLgywnNPSATEk 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 266 -PLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWY----NQEKLILFMVSKDAS 339
Cdd:cd05971 312 kMAGDWLLTGDLGRKdSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpdpiRGEIVKAFVVLNPGE 391
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1021589396 340 VK-EYIFKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd05971 392 TPsDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
39-376 |
4.54e-13 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 72.35 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLA-LSSGASLLIVPtsvKLLP 117
Cdd:cd05926 151 LALILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLStLAAGGSVVLPP---RFSA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASvLFSHHRVTVLQATPT----LLRRFgsqliKSTVLSATTSLRVLALGGEAFPsLTVLRSWRgEGNKTQIFNVYGI 193
Cdd:cd05926 228 STFWP-DVRDYNATWYTAVPTihqiLLNRP-----EPNPESPPPKLRFIRSCSASLP-PAVLEALE-ATFGAPVLEAYGM 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 194 TEVSSWATIYRIPEktlnstlKCELPVQLGFPllgTVVEVR--DTNGFTIQEG-SGQVFLGGRNrVC--FLDD-----EV 263
Cdd:cd05926 300 TEAAHQMTSNPLPP-------GPRKPGSVGKP---VGVEVRilDEDGEILPPGvVGEICLRGPN-VTrgYLNNpeanaEA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 264 TVPLGTMRaTGDF-VTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV-----TWYNQEKLILFMVSKD 337
Cdd:cd05926 369 AFKDGWFR-TGDLgYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAfgvpdEKYGEEVAAAVVLREG 447
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1021589396 338 ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd05926 448 ASVtEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQ 487
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
42-380 |
1.45e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 70.94 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 42 VLHTSGTTGIPKIVRVPHKcivPNIQHFRVLFDIT---QEDVLFLASPLTFDPSVVEIFLALSSGASLLivpTSVKLLPS 118
Cdd:PRK13382 201 ILLTSGTTGTPKGARRSGP---GGIGTLKAILDRTpwrAEEPTVIVAPMFHAWGFSQLVLAASLACTIV---TRRRFDPE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 klASV-LFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNktQIFNVYGITEVS 197
Cdd:PRK13382 275 --ATLdLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGD--VIYNNYNATEAG 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 198 sWATIyRIPEktlnstlkcEL---PVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLggRNRVCFldDEVTVplGT---- 269
Cdd:PRK13382 351 -MIAT-ATPA---------DLraaPDTAGRPAEGTEIRILDQDFREVPTGEvGTIFV--RNDTQF--DGYTS--GStkdf 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 270 ---MRATGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVK 341
Cdd:PRK13382 414 hdgFMASGDVGYLDEnGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQygqrLAAFVVLKPGASA 493
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1021589396 342 --EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:PRK13382 494 tpETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRREL 534
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
39-376 |
2.63e-12 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 68.51 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASlLIVPTSVKLLPS 118
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAE-LVLLERNQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 KLAsvlfsHHRVTVLQATPTLLRRFgsqLIKSTVLSATTSLRVLALGGEAFPS-LT---VLRSWRgegnktqIFNVYGIT 194
Cdd:cd17630 81 DLA-----PPGVTHVSLVPTQLQRL---LDSGQGPAALKSLRAVLLGGAPIPPeLLeraADRGIP-------LYTTYGMT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 195 EVSSWATIYRIPEKTLNStlkcelpvqLGFPLLGtvVEVRDTNGFTIQEGSGQVFLGGRNRVC---FLDDevtvplGTMR 271
Cdd:cd17630 146 ETASQVATKRPDGFGRGG---------VGVLLPG--RELRIVEDGEIWVGGASLAMGYLRGQLvpeFNED------GWFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 272 aTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW-----YNQeKLILFMVSKDASVKEYIF 345
Cdd:cd17630 209 -TKDLGELhADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGvpdeeLGQ-RPVAVIVGRGPADPAELR 286
|
330 340 350
....*....|....*....|....*....|.
gi 1021589396 346 KELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd17630 287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVD 317
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
39-375 |
2.72e-12 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 70.08 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdpsvveiflALSSG-ASLLIVPTSVK--- 114
Cdd:PRK13295 199 VTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPM-----------AHQTGfMYGLMMPVMLGata 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 115 ----LLPSKLASVLFSHHRVT-VLQATPtllrrFGSQLIKSTVLSATT--SLRVLALGGEAFPSLTVLRSWRGEGnkTQI 187
Cdd:PRK13295 268 vlqdIWDPARAAELIRTEGVTfTMASTP-----FLTDLTRAVKESGRPvsSLRTFLCAGAPIPGALVERARAALG--AKI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 188 FNVYGITEVSSWATIY--RIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTI---QEGSGQV-----FLG--GRNR 255
Cdd:PRK13295 341 VSAWGMTENGAVTLTKldDPDERASTTD---------GCPLPGVEVRVVDADGAPLpagQIGRLQVrgcsnFGGylKRPQ 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 256 VCFLDDEvtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----I 330
Cdd:PRK13295 412 LNGTDAD-----GWFD-TGDLARIdADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLgeraC 485
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1021589396 331 LFMVSKDASvkEYIFKELQKYLPSHAV-----PDELVLIDSLPFTSHGKI 375
Cdd:PRK13295 486 AFVVPRPGQ--SLDFEEMVEFLKAQKVakqyiPERLVVRDALPRTPSGKI 533
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
39-375 |
1.16e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 67.70 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtF--DPSVVEIFLALSSGASLLIVPtsvKLL 116
Cdd:cd05934 83 PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLTVLPL-FhiNAQAVSVLAALSVGATLVLLP---RFS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASVLFSHHrVTVLQATPTLLrrfgSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGnkTQIFNVYGITEV 196
Cdd:cd05934 159 ASRFWSDVRRYG-ATVTNYLGAML----SYLLAQPPSPDDRAHRLRAAYGAPNPPELHEEFEERFG--VRLLEGYGMTET 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 197 SSwATIYRIPEKTlnstlkceLPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDEVTVPLGTMRA--- 272
Cdd:cd05934 232 IV-GVIGPRDEPR--------RPGSIGRPAPGYEVRIVDDDGQELPAGEpGELVIRGLRGWGFFKGYYNMPEATAEAmrn 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 273 ----TGD-FVTVKDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV----TWYNQEKLILFMVSKDASV--K 341
Cdd:cd05934 303 gwfhTGDlGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVvavpDEVGEDEVKAVVVLRPGETldP 382
|
330 340 350
....*....|....*....|....*....|....
gi 1021589396 342 EYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 375
Cdd:cd05934 383 EELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKV 416
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
42-380 |
1.20e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 68.03 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 42 VLHTSGTTGIPKIVRVPHkciVPNIQHFRVLFD---ITQEDVLFLASPLTFDPSVVEIFLALSSGASLLivpTSVKLLPS 118
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPE---PSPLAPLAGLLSrvpFRAGETTLLPAPMFHATGWAHLTLAMALGSTVV---LRRRFDPE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 119 K-LASVlfSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRSWRGEGNKtqIFNVYGITEVS 197
Cdd:PRK07788 286 AtLEDI--AKHKATALVVVPVMLSRILDLGPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPV--LYNLYGSTEVA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 198 sWATIYRIPEKTLNSTLkcelpvqLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLG----------GRNRVCflddevtvp 266
Cdd:PRK07788 362 -FATIATPEDLAEAPGT-------VGRPPKGVTVKILDENGNEVPRGvVGRIFVGngfpfegytdGRDKQI--------- 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 267 LGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV------TWYnqEKLILFMVSKDAS 339
Cdd:PRK07788 425 IDGLLSSGDVGYFdEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVigvddeEFG--QRLRAFVVKAPGA 502
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1021589396 340 ------VKEYIFKELQKylpsHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:PRK07788 503 aldedaIKDYVRDNLAR----YKVPRDVVFLDELPRNPTGKVLKREL 545
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
42-383 |
1.23e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 67.96 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 42 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtFDPSVVEIFL--ALSSGAsLLIVPTsvKLLPSK 119
Cdd:PRK06839 154 ICYTSGTTGKPKGAVLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGG-VIIVPR--KFEPTK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 120 lASVLFSHHRVTVLQATPTLlrrfgSQLIKSTVLSATTSL---RVLALGGEAFPsLTVLRSWR------GEGnktqifnv 190
Cdd:PRK06839 230 -ALSMIEKHKVTVVMGVPTI-----HQALINCSKFETTNLqsvRWFYNGGAPCP-EELMREFIdrgflfGQG-------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 191 YGITEVSswATIYRIPEKTLNSTlkcelPVQLGFPLLGTVVEVRDTNGFTIQEGS-GQVFLGGRNRVCFLDDEVTVPLGT 269
Cdd:PRK06839 295 FGMTETS--PTVFMLSEEDARRK-----VGSIGKPVLFCDYELIDENKNKVEVGEvGELLIRGPNVMKEYWNRPDATEET 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 270 MR----ATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDASV 340
Cdd:PRK06839 368 IQdgwlCTGDLARVdEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWgeipIAFIVKKSSSV 447
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1021589396 341 --KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKI 383
Cdd:PRK06839 448 liEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
42-385 |
2.52e-11 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 67.13 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 42 VLHTSGTTGIPK-IVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLI---VPTSVKllP 117
Cdd:cd05968 241 IIYTSGTTGKPKgTVHVHAGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgAPDHPK--A 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLaSVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPsltvLRSW------RGEGNKTqIFNVY 191
Cdd:cd05968 319 DRL-WRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLRVLGSTGEPWN----PEPWnwlfetVGKGRNP-IINYS 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 192 GITEVSswATIYRipektlNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFL----GGRNRVCFLDDEVTVPL 267
Cdd:cd05968 393 GGTEIS--GGILG------NVLIKPIKPSSFNGPVPGMKADVLDESGKPARPEVGELVLlapwPGMTRGFWRDEDRYLET 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 268 GTMR-----ATGDFVTVKDGEIFF-LGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ----EKLILFMVSKD 337
Cdd:cd05968 465 YWSRfdnvwVHGDFAYYDEEGYFYiLGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHpvkgEAIVCFVVLKP 544
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1021589396 338 A-SVKEYIFKELQKYLPSHA----VPDELVLIDSLPFTSHGKIDVSELNKIYL 385
Cdd:cd05968 545 GvTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRAAYL 597
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
45-382 |
2.91e-11 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 66.50 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 45 TSGTTGIPKIVRVPHKCIVpnIQHFRVL----FDITQEDVLFLASPLtFD------PsvveiFLALSSGASLliVPTSVK 114
Cdd:cd12119 171 TSGTTGNPKGVVYSHRSLV--LHAMAALltdgLGLSESDVVLPVVPM-FHvnawglP-----YAAAMVGAKL--VLPGPY 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 115 LLPSKLASvLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSlTVLRSWRGEGnkTQIFNVYGI 193
Cdd:cd12119 241 LDPASLAE-LIEREGVTFAAGVPTVWQGLLDHLeANGRDLS---SLRRVVIGGSAVPR-SLIEAFEERG--VRVIHAWGM 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 194 TEVSSWATIYRIPEKTLNSTLKCELPVQL--GFPLLGTVVEVRDTNGFTIQ---EGSGQVFLGGrNRVC---FLDDEVTV 265
Cdd:cd12119 314 TETSPLGTVARPPSEHSNLSEDEQLALRAkqGRPVPGVELRIVDDDGRELPwdgKAVGELQVRG-PWVTksyYKNDEESE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 266 PL---GTMRaTGDFVTV-KDGEIFFLGR-KDSqIKRHGKRL-NIELvQQVAEELQQVESCAV------TWynQEKLILFM 333
Cdd:cd12119 393 ALtedGWLR-TGDVATIdEDGYLTITDRsKDV-IKSGGEWIsSVEL-ENAIMAHPAVAEAAVigvphpKW--GERPLAVV 467
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1021589396 334 VSKD-ASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:cd12119 468 VLKEgATVtAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALRE 518
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
40-376 |
3.01e-11 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 66.58 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFD-----PSVVEIFLAlssGASLLIVPTsvk 114
Cdd:cd05920 142 ALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNfplacPGVLGTLLA---GGRVVLAPD--- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 115 llPSKLASV-LFSHHRVTVLQATPTLLRRFGSQLIKSTvlSATTSLRVLALGGEAFPSlTVLRSWRGE-GNKTQifNVYG 192
Cdd:cd05920 216 --PSPDAAFpLIEREGVTVTALVPALVSLWLDAAASRR--ADLSSLRLLQVGGARLSP-ALARRVPPVlGCTLQ--QVFG 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 193 ITEvsSWATIYRI--PEKTLNSTlkcelpvQlGFPLL-GTVVEVRDTNGFTIQEGS-GQVFLGG------------RNRV 256
Cdd:cd05920 289 MAE--GLLNYTRLddPDEVIIHT-------Q-GRPMSpDDEIRVVDEEGNPVPPGEeGELLTRGpytirgyyrapeHNAR 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 257 CFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLIL 331
Cdd:cd05920 359 AFTPD------GFYR-TGDLVRRtPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAmpdeLLGERSCA 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1021589396 332 FMVSKDASVKeyiFKELQKYL-----PSHAVPDELVLIDSLPFTSHGKID 376
Cdd:cd05920 432 FVVLRDPPPS---AAQLRRFLrerglAAYKLPDRIEFVDSLPLTAVGKID 478
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
17-383 |
3.28e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 66.34 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 17 ISSEHVNE----EKAEEHMDLRLKHCLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtfdps 92
Cdd:PRK07638 119 IEIDEWKRmiekYLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMKREDSVLIAGTL----- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 93 VVEIFL-----ALSSGASLLIVPtsvKLLPSKLASVLfSHHRVTVLQATPTLLRRFGSQlikstvlsattslrvlalggE 167
Cdd:PRK07638 194 VHSLFLygaisTLYVGQTVHLMR---KFIPNQVLDKL-ETENISVMYTVPTMLESLYKE--------------------N 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 168 AFP--SLTVLRS---WRGEGNK--------TQIFNVYGITEVSSWAtiYRIPEktlNSTLKcelPVQLGFPLLGTVVEVR 234
Cdd:PRK07638 250 RVIenKMKIISSgakWEAEAKEkiknifpyAKLYEFYGASELSFVT--ALVDE---ESERR---PNSVGRPFHNVQVRIC 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 235 DTNGFTIQEG--------SGQVFLGGRNRVCFLDDEVTVPLGTMRATGdFVTvKDGEIFFLGRKDSQIKRHGkrLNI--E 304
Cdd:PRK07638 322 NEAGEEVQKGeigtvyvkSPQFFMGYIIGGVLARELNADGWMTVRDVG-YED-EEGFIYIVGREKNMILFGG--INIfpE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 305 LVQQVAEELQQVESCAVT------WYNQEKLILfmvsKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVS 378
Cdd:PRK07638 398 EIESVLHEHPAVDEIVVIgvpdsyWGEKPVAII----KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARM 473
|
....*
gi 1021589396 379 ELNKI 383
Cdd:PRK07638 474 EAKSW 478
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
40-393 |
4.54e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 66.53 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFdpsvveiflALSSGASLLIVpTSVK--L 115
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVfhSF---------GLTGGLVLPLL-SGVKvfL 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 116 LPSKLasvlfsHHRVT---VLQATPTLLrrFGSqlikSTVLS--ATT-------SLRVLALGGEAFPSLTvlRSWRGEGN 183
Cdd:PRK06814 866 YPSPL------HYRIIpelIYDTNATIL--FGT----DTFLNgyARYahpydfrSLRYVFAGAEKVKEET--RQTWMEKF 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 184 KTQIFNVYGITEVSswatiyriPEKTLNSTLKCELpvqlgfpllGTV------VEVR--DTNGftIQEGsGQVFLGGRNr 255
Cdd:PRK06814 932 GIRILEGYGVTETA--------PVIALNTPMHNKA---------GTVgrllpgIEYRlePVPG--IDEG-GRLFVRGPN- 990
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 256 vcflddevtVPLGTMRA---------------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEEL-QQVES 318
Cdd:PRK06814 991 ---------VMLGYLRAenpgvleppadgwydTGDIVTIdEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALH 1061
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021589396 319 CAVTWYNQ---EKLILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNYINLKSE 393
Cdd:PRK06814 1062 AAVSIPDArkgERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKIDYVAVTKLAEEAAAKPEA 1139
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
40-380 |
1.68e-10 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 63.90 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVrvphkcivpnIQHFRVLF----------DITQEDVLFLASPLtFDPSVVEIFL-ALSSGASLLI 108
Cdd:cd05912 80 ATIMYTSGTTGKPKGV----------QQTFGNHWwsaigsalnlGLTEDDNWLCALPL-FHISGLSILMrSVIYGMTVYL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 109 VPtsvKLLPSKLASVLFSHhRVTVLQATPTLLRRfgsqLIKSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGnkTQIF 188
Cdd:cd05912 149 VD---KFDAEQVLHLINSG-KVTIISVVPTMLQR----LLEILGEGYPNNLRCILLGGGPAP-KPLLEQCKEKG--IPVY 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 189 NVYGITEVSSWATiyripekTLNSTLKCELPVQLGFPLLGTVVEVRDTNGftIQEGSGQVFLGGRNRV-CFL---DDEVT 264
Cdd:cd05912 218 QSYGMTETCSQIV-------TLSPEDALNKIGSAGKPLFPVELKIEDDGQ--PPYEVGEILLKGPNVTkGYLnrpDATEE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 265 VPLGTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDAS 339
Cdd:cd05912 289 SFENGWFKTGDIGYLdEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWgqvpVAFVVSERPI 368
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1021589396 340 VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd05912 369 SEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
39-321 |
1.74e-10 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 64.15 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDV--LFLasPLTfdpSVVE----IFLALSSGASLLIVPtS 112
Cdd:cd05907 89 LATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRhlSFL--PLA---HVFErragLYVPLLAGARIYFAS-S 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 113 VKLLPSKLASVlfshhRVTVLQATPTLLRRF--GSQLIKST-------VLSATTSLRVLALGGEAFPsLTVLRSWRGEGn 183
Cdd:cd05907 163 AETLLDDLSEV-----RPTVFLAVPRVWEKVyaAIKVKAVPglkrklfDLAVGGRLRFAASGGAPLP-AELLHFFRALG- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 184 kTQIFNVYGITEVSSWATIyripektlnSTLKCELPVQLGFPLLGTVVEVRDTNgfTIQEGSGQVFLGGRNrvcflDDEV 263
Cdd:cd05907 236 -IPVYEGYGLTETSAVVTL---------NPPGDNRIGTVGKPLPGVEVRIADDG--EILVRGPNVMLGYYK-----NPEA 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021589396 264 TVPLGTMR---ATGDFVTVK-DGEIFFLGR-KDSQIKRHGKrlNIELvQQVAEELQQ---VESCAV 321
Cdd:cd05907 299 TAEALDADgwlHTGDLGEIDeDGFLHITGRkKDLIITSGGK--NISP-EPIENALKAsplISQAVV 361
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
39-382 |
4.61e-10 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 63.05 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtF--DPSVVEIFLALSSGASLLiVPTSVKLL 116
Cdd:PRK07529 215 VAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL-FhvNALLVTGLAPLARGAHVV-LATPQGYR 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 -PSKLASV--LFSHHRVTVLQATPTLLrrfgSQLIKSTVLSA-TTSLRVlALGGEAFPSLTVLRSWRgEGNKTQIFNVYG 192
Cdd:PRK07529 293 gPGVIANFwkIVERYRINFLSGVPTVY----AALLQVPVDGHdISSLRY-ALCGAAPLPVEVFRRFE-AATGVRIVEGYG 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 193 ITEVSSWATI-YRIPEKTLNStlkcelpvqLGFPLLGTVVEV--RDTNGFTIQE------------GSGqVFLG----GR 253
Cdd:PRK07529 367 LTEATCVSSVnPPDGERRIGS---------VGLRLPYQRVRVviLDDAGRYLRDcavdevgvlciaGPN-VFSGyleaAH 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 254 NRVCFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlNIElVQQVAEEL---QQVESCAVTW------ 323
Cdd:PRK07529 437 NKGLWLED------GWLN-TGDLGRIdADGYFWLTGRAKDLIIRGGH--NID-PAAIEEALlrhPAVALAAAVGrpdaha 506
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 324 ------YNQEKlilfmvsKDASVKEyifKELQKYLPSH-----AVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:PRK07529 507 gelpvaYVQLK-------PGASATE---AELLAFARDHiaeraAVPKHVRILDALPKTAVGKIFKPALRR 566
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
39-376 |
1.16e-09 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 62.25 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVlfLASPLTFDPS---VVEIFLALSSGASLLIVPTsvkl 115
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDV--ILSSLPFFHSfglTVTLWLPLLEGIKVVYHPD---- 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 116 lPSKLASV--LFSHHRVTVLQATPTLLRRFgsqlIKSTVLSAT--TSLRVLALGGEAFPslTVLRSWRGEGNKTQIFNVY 191
Cdd:PRK08633 858 -PTDALGIakLVAKHRATILLGTPTFLRLY----LRNKKLHPLmfASLRLVVAGAEKLK--PEVADAFEEKFGIRILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 192 GITEVSSWATIyRIP--EKTLNSTLKCELPVQLGFPLLGTVVEVRDTNGFT---------IQEGSGQVFLGgrnrvcFLD 260
Cdd:PRK08633 931 GATETSPVASV-NLPdvLAADFKRQTGSKEGSVGMPLPGVAVRIVDPETFEelppgedglILIGGPQVMKG------YLG 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 261 D-----EVTVPLGTMR--ATGD--------FVTVKD---------GEIFFLGRkdsqikrhgkrlnielvqqVAEELQQV 316
Cdd:PRK08633 1004 DpektaEVIKDIDGIGwyVTGDkghldedgFLTITDrysrfakigGEMVPLGA-------------------VEEELAKA 1064
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589396 317 -----ESCAVTWYNQEK----LILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKID 376
Cdd:PRK08633 1065 lggeeVVFAVTAVPDEKkgekLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
45-455 |
1.18e-09 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 62.00 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 45 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLiVPTSVKL-LPSKLASV 123
Cdd:TIGR03443 423 TSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLL-VPTADDIgTPGRLAEW 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 124 LfSHHRVTVLQATPTLlrrfgSQLikstvLSATTSlrvlalggEAFPSL-------TVL-----RSWRGEGNKTQIFNVY 191
Cdd:TIGR03443 502 M-AKYGATVTHLTPAM-----GQL-----LSAQAT--------TPIPSLhhaffvgDILtkrdcLRLQTLAENVCIVNMY 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 192 GITEVSSWATIYRIPEKTLNST----LKCELP-------VQLgfpL------------LGTVVE--VRD----------- 235
Cdd:TIGR03443 563 GTTETQRAVSYFEIPSRSSDSTflknLKDVMPagkgmknVQL---LvvnrndrtqtcgVGEVGEiyVRAgglaegylglp 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 236 --------TNGFT-----------IQEGSGQVFLGGRNRvcflddevtvplgtMRATGDF-VTVKDGEIFFLGRKDSQIK 295
Cdd:TIGR03443 640 elnaekfvNNWFVdpshwidldkeNNKPEREFWLGPRDR--------------LYRTGDLgRYLPDGNVECCGRADDQVK 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 296 RHGKRL-----------------NIELVQQVAEELQQVESCAVTWYNQEKLILFMVSKDASV-KEYIFKELQKY------ 351
Cdd:TIGR03443 706 IRGFRIelgeidthlsqhplvreNVTLVRRDKDEEPTLVSYIVPQDKSDELEEFKSEVDDEEsSDPVVKGLIKYrklikd 785
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 352 --------LPSHAVPDELVLIDSLPFTSHGKID--------VSELNKIYLNYINLKSENKLSGKE----DLWEKLqylwk 411
Cdd:TIGR03443 786 ireylkkkLPSYAIPTVIVPLKKLPLNPNGKVDkpalpfpdTAQLAAVAKNRSASAADEEFTETEreirDLWLEL----- 860
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1021589396 412 stlnLPEDLLRV-PDESlFLNSGGDSLKSIRLLSEIEKLVGTSVP 455
Cdd:TIGR03443 861 ----LPNRPATIsPDDS-FFDLGGHSILATRMIFELRKKLNVELP 900
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
39-321 |
1.51e-09 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 61.07 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLF--DITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPtsvkll 116
Cdd:cd05911 148 TAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLygNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMP------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 psKLASVLF----SHHRVTVLQATPTLLrrfgSQLIKSTVLSATT--SLRVLALGGEAFpSLTVLRSWRGEGNKTQIFNV 190
Cdd:cd05911 222 --KFDSELFldliEKYKITFLYLVPPIA----AALAKSPLLDKYDlsSLRVILSGGAPL-SKELQELLAKRFPNATIKQG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 191 YGITEVSSWATIYRIPEKTLNSTlkcelpvqlGFPLLGTVVEVRDTNGFTI----QEG-----SGQVFLG--GR---NRV 256
Cdd:cd05911 295 YGMTETGGILTVNPDGDDKPGSV---------GRLLPNVEAKIVDDDGKDSlgpnEPGeicvrGPQVMKGyyNNpeaTKE 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021589396 257 CFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKrlnielvqQV--AE------ELQQVESCAV 321
Cdd:cd05911 366 TFDED------GWLH-TGDIGYFdEDGYLYIVDRKKELIKYKGF--------QVapAEleavllEHPGVADAAV 424
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
39-401 |
1.71e-09 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 60.84 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLaLSSGASllIVPTSVKLL 116
Cdd:cd17640 90 LATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRFLSILPIwhSYERS-AEYFI-FACGCS--QAYTSIRTL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASVlfshhRVTVLQATPTLLRRFGSQLIKSTVLSATTS------------LRVLALGGEAFPSlTVLRSWRGEGnk 184
Cdd:cd17640 166 KDDLKRV-----KPHYIVSVPRLWESLYSGIQKQVSKSSPIKqflflfflsggiFKFGISGGGALPP-HVDTFFEAIG-- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 185 TQIFNVYGITEVSSWATIYRIPEKTLNStlkcelpvqLGFPLLGTVVEVRD--TNGFTIQEGSGQVFLGGrnrvcfldDE 262
Cdd:cd17640 238 IEVLNGYGLTETSPVVSARRLKCNVRGS---------VGRPLPGTEIKIVDpeGNVVLPPGEKGIVWVRG--------PQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 263 VTV-----PLGTMRA--------TGDFVT-VKDGEIFFLGR-KDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE 327
Cdd:cd17640 301 VMKgyyknPEATSKVldsdgwfnTGDLGWlTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVGQDQK 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021589396 328 KLILFMVSKdasvkeyiFKELQKYLPSHAVpdelvlidSLPFTSHGKIDVSELNKIYLNYINLKSENKLSGKED 401
Cdd:cd17640 381 RLGALIVPN--------FEELEKWAKESGV--------KLANDRSQLLASKKVLKLYKNEIKDEISNRPGFKSF 438
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
39-382 |
2.66e-09 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 60.00 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLA-LSSGAsllivptSVKLLP 117
Cdd:cd05941 91 PALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWTEDDVLLHVLPLHHVHGLVNALLCpLFAGA-------SVEFLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 ---SKLASVLFSHHRVTVLQATPTLLRR------FGSQLIKSTVLSATTSLRVLALGGEAFPsLTVLRSWRGEGNKTqIF 188
Cdd:cd05941 164 kfdPKEVAISRLMPSITVFMGVPTIYTRllqyyeAHFTDPQFARAAAAERLRLMVSGSAALP-VPTLEEWEAITGHT-LL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 189 NVYGITEVSswatiyripeKTLNSTLKCE-LPVQLGFPLLGtvVEVR--DTNGFT---------IQEGSGQVFLGGRNRV 256
Cdd:cd05941 242 ERYGMTEIG----------MALSNPLDGErRPGTVGMPLPG--VQARivDEETGEplprgevgeIQVRGPSVFKEYWNKP 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 257 CFLDDEVTvPLGTMRaTGDFVTVK-DGEIFFLGR-KDSQIKRHGKRLNIELVQQVAEELQQVESCAV------TWynQEK 328
Cdd:cd05941 310 EATKEEFT-DDGWFK-TGDLGVVDeDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVigvpdpDW--GER 385
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589396 329 LILFMVSKD--ASVKEYIFKE-LQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:cd05941 386 VVAVVVLRAgaAALSLEELKEwAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
41-375 |
2.88e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 60.36 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 41 YVLHTSGTTGIPKivrvphkCIVPN-----IQH---FRVLFDITQEDVLF------------LASpltfdpsvveiflAL 100
Cdd:cd05943 253 YILYSSGTTGLPK-------CIVHGaggtlLQHlkeHILHCDLRPGDRLFyyttcgwmmwnwLVS-------------GL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 101 SSGASLLIVPTSvKLLPSKLASV-LFSHHRVTVLQATPTL---LRRFGSQLIKSTVLSattSLRVLALGGEAFPSLTVLR 176
Cdd:cd05943 313 AVGATIVLYDGS-PFYPDTNALWdLADEEGITVFGTSAKYldaLEKAGLKPAETHDLS---SLRTILSTGSPLKPESFDY 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 177 SWRGEGNKTQIFNVYGITEVSSwATIYRIPEktlnstlkceLPVQLG---FPLLGTVVEVRDTNGFTIQEGSGQVflggr 253
Cdd:cd05943 389 VYDHIKPDVLLASISGGTDIIS-CFVGGNPL----------LPVYRGeiqCRGLGMAVEAFDEEGKPVWGEKGEL----- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 254 nrVCflddevTVPLGTM-------------RAT-----------GDFVTV-KDGEIFFLGRKDSQIKRHGKRL-NIELVQ 307
Cdd:cd05943 453 --VC------TKPFPSMpvgfwndpdgsryRAAyfakypgvwahGDWIEItPRGGVVILGRSDGTLNPGGVRIgTAEIYR 524
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589396 308 QVaEELQQV-ESCAVTWYNQ---EKLILFMVSK-----DASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 375
Cdd:cd05943 525 VV-EKIPEVeDSLVVGQEWKdgdERVILFVKLRegvelDDELRKRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
41-375 |
4.67e-09 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 59.81 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 41 YVLHTSGTTGIPKivrvphkCIVPN-----IQHFRVL---FDITQEDVLF------------LASpltfdpsvveiflAL 100
Cdd:PRK03584 267 WILYSSGTTGLPK-------CIVHGhggilLEHLKELglhCDLGPGDRFFwyttcgwmmwnwLVS-------------GL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 101 SSGASLLIVPTSvkllPSKL-ASVLF---SHHRVTVLQATP---TLLRRFGSQLIKSTVLSAttsLRVLALGG-----EA 168
Cdd:PRK03584 327 LVGATLVLYDGS----PFYPdPNVLWdlaAEEGVTVFGTSAkylDACEKAGLVPGETHDLSA---LRTIGSTGsplppEG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 169 FpsltvlrSW--RGEGNKTQIFNVYGITEVSSwatiyripektlnstlkC------ELPV---QLGFPLLGTVVEVRDTN 237
Cdd:PRK03584 400 F-------DWvyEHVKADVWLASISGGTDICS-----------------CfvggnpLLPVyrgEIQCRGLGMAVEAWDED 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 238 GFTIQEGSGQVflggrnrVCflddevTVPLGTM-------------RAT-----------GDFVTV-KDGEIFFLGRKDS 292
Cdd:PRK03584 456 GRPVVGEVGEL-------VC------TKPFPSMplgfwndpdgsryRDAyfdtfpgvwrhGDWIEItEHGGVVIYGRSDA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 293 QIKRHGKRLNI-ELVQQVaEELQQV-ESCAV--TWYNQ-EKLILFMVSK-----DASVKEYIFKELQKYL-PSHaVPDEL 361
Cdd:PRK03584 523 TLNRGGVRIGTaEIYRQV-EALPEVlDSLVIgqEWPDGdVRMPLFVVLAegvtlDDALRARIRTTIRTNLsPRH-VPDKI 600
|
410
....*....|....
gi 1021589396 362 VLIDSLPFTSHGKI 375
Cdd:PRK03584 601 IAVPDIPRTLSGKK 614
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
39-375 |
7.08e-09 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 59.30 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFD---ITQEDVLFLASPL--TFDPSVVEIFLALSSGASLLI----- 108
Cdd:PRK08974 208 LAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpllHPGKELVVTALPLyhIFALTVNCLLFIELGGQNLLItnprd 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 109 VPTSVKLLpsklasvlfSHHRVTVLQATPTLLrrfgSQLIKSTVLSAT--TSLRvLALGGEAFPSLTVLRSWRgEGNKTQ 186
Cdd:PRK08974 288 IPGFVKEL---------KKYPFTAITGVNTLF----NALLNNEEFQELdfSSLK-LSVGGGMAVQQAVAERWV-KLTGQY 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 187 IFNVYGITEVSSWATIYRIPEKTLNSTLkcelpvqlGFPLLGTVVEVRDTNGFTIQEGSG--------QVFLGGRNRvcf 258
Cdd:PRK08974 353 LLEGYGLTECSPLVSVNPYDLDYYSGSI--------GLPVPSTEIKLVDDDGNEVPPGEPgelwvkgpQVMLGYWQR--- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 259 ldDEVTVPL---GTMrATGDFVTV-KDGEIFFLGRKDSQIKRHGkrLNI---ELVQQVAEELQQVESCAVTWYNQ---EK 328
Cdd:PRK08974 422 --PEATDEVikdGWL-ATGDIAVMdEEGFLRIVDRKKDMILVSG--FNVypnEIEDVVMLHPKVLEVAAVGVPSEvsgEA 496
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1021589396 329 LILFMVSKDASV-KEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 375
Cdd:PRK08974 497 VKIFVVKKDPSLtEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
39-290 |
1.23e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 58.38 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSVVeIFLALSSGASLLIVPtsvKLL 116
Cdd:PRK07656 168 VADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAANPFfhVFGYKAG-VNAPLMRGATILPLP---VFD 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASvLFSHHRVTVLQATPTLLRrfgsQLIKSTVLSAT--TSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGIT 194
Cdd:PRK07656 244 PDEVFR-LIETERITVLPGPPTMYN----SLLQHPDRSAEdlSSLRLAVTGAASMP-VALLERFESELGVDIVLTGYGLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 195 EVSSWATIYRI--PEKTLNSTlkcelpvqLGFPLLGTVVEVRDTNGFTIQEG-SGQVFLGGRNrVC--FLDDevtvPLGT 269
Cdd:PRK07656 318 EASGVTTFNRLddDRKTVAGT--------IGTAIAGVENKIVNELGEEVPVGeVGELLVRGPN-VMkgYYDD----PEAT 384
|
250 260 270
....*....|....*....|....*....|
gi 1021589396 270 MRA--------TGDFVTV-KDGEIFFLGRK 290
Cdd:PRK07656 385 AAAidadgwlhTGDLGRLdEEGYLYIVDRK 414
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
45-380 |
4.45e-08 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 56.37 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 45 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLiVPTSVKL-LPSKLASV 123
Cdd:cd17647 117 TSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLL-VPTQDDIgTPGRLAEW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 124 LfSHHRVTVLQATPTLlrrfgSQLIKSTVLSATTSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITEVSSWATIY 203
Cdd:cd17647 196 M-AKYGATVTHLTPAM-----GQLLTAQATTPFPKLHHAFFVGDILTKRDCLR-LQTLAENVRIVNMYGTTETQRAVSYF 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 204 RIPEKTLNST----LKCELPVQLGF---PLLgtVVEVRDTNGFTIQEGSGQVFL--GGR----------NRVCFLDD--- 261
Cdd:cd17647 269 EVPSRSSDPTflknLKDVMPAGRGMlnvQLL--VVNRNDRTQICGIGEVGEIYVraGGLaegyrglpelNKEKFVNNwfv 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 262 ------EVTVPLGT------------MRATGDF-VTVKDGEIFFLGRKDSQIKRHGKRL-----------------NIEL 305
Cdd:cd17647 347 epdhwnYLDKDNNEpwrqfwlgprdrLYRTGDLgRYLPNGDCECCGRADDQVKIRGFRIelgeidthisqhplvreNITL 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 306 VQQVAEElqqvESCAVTWY-----NQEKLILFMVSKDASVK-EYIFKELQKY--------------LPSHAVPDELVLID 365
Cdd:cd17647 427 VRRDKDE----EPTLVSYIvprfdKPDDESFAQEDVPKEVStDPIVKGLIGYrklikdireflkkrLASYAIPSLIVVLD 502
|
410
....*....|....*
gi 1021589396 366 SLPFTSHGKIDVSEL 380
Cdd:cd17647 503 KLPLNPNGKVDKPKL 517
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
42-380 |
7.85e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 55.77 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 42 VLHTSGTTGIPKIV-RVPHkcIVPNIQHFRVLFDITQEDV---LFLASPLTFDPSVVEIFLALSSGASLLivptSVKLLP 117
Cdd:PRK13383 179 VLLTSGTTGKPKGVpRAPQ--LRSAVGVWVTILDRTRLRTgsrISVAMPMFHGLGLGMLMLTIALGGTVL----THRHFD 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAF-PSLTvLRSWRGEGNKtqIFNVYGITEV 196
Cdd:PRK13383 253 AEAALAQASLHRADAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLdPTLG-QRFMDTYGDI--LYNGYGSTEV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 197 SswatiyrIPEKTLNSTLKcELPVQLGFPLLGTVVEVRDTNGFTI-QEGSGQVFLGGR-NRVCFLDDEVTVPLGTMRATG 274
Cdd:PRK13383 330 G-------IGALATPADLR-DAPETVGKPVAGCPVRILDRNNRPVgPRVTGRIFVGGElAGTRYTDGGGKAVVDGMTSTG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 275 DFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQE----KLILFMVSKD------ASVKEY 343
Cdd:PRK13383 402 DMGYLDNaGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErfghRLAAFVVLHPgsgvdaAQLRDY 481
|
330 340 350
....*....|....*....|....*....|....*..
gi 1021589396 344 IFKELQKYlpshAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:PRK13383 482 LKDRVSRF----EQPRDINIVSSIPRNPTGKVLRKEL 514
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
39-375 |
9.06e-08 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 55.18 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVV-EIFLALSSGASLLIVPTSVKllp 117
Cdd:cd05935 86 LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILACLPLFHVTGFVgSLNTAVYVGGTYVLMARWDR--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 sKLASVLFSHHRVTVLQATPTLLRRFGSQL-IKSTVLSattSLRVLALGGEAFPSLTVLRSWRgegnKTQIFNV--YGIT 194
Cdd:cd05935 163 -ETALELIEKYKVTFWTNIPTMLVDLLATPeFKTRDLS---SLKVLTGGGAPMPPAVAEKLLK----LTGLRFVegYGLT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 195 EVsswatiyrIPEKTLNSTLKCELPVqLGFPLLGTVVEVRD-TNGFTIQEG-SGQVFLGG------------RNRVCFLD 260
Cdd:cd05935 235 ET--------MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPPNeVGEIVVRGpqifkgywnrpeETEESFIE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 261 DE-----VTVPLGTMRAtgdfvtvkDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTW----YNQEKLIL 331
Cdd:cd05935 306 IKgrrffRTGDLGYMDE--------EGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVISvpdeRVGEEVKA 377
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1021589396 332 FMVSKDA----SVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 375
Cdd:cd05935 378 FIVLRPEyrgkVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKI 425
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
44-387 |
1.05e-07 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 55.14 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 44 HTSGTTGIPKIVRVPHKcivPNIQHFRVlfdITQEDVLFLASPLTFDPsVVEIFLALSSGASLLIVPTSVKL-LP-SKL- 120
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHR---SNVLHALM---ANNGDALGTSAADTMLP-VVPLFHANSWGIAFSAPSMGTKLvMPgAKLd 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 121 -ASV--LFSHHRVTVLQATPT----LLrrfgsQLIKSTVLSATTsLRVLALGGEAFPSlTVLRSWRGEGnkTQIFNVYGI 193
Cdd:PRK06018 257 gASVyeLLDTEKVTFTAGVPTvwlmLL-----QYMEKEGLKLPH-LKMVVCGGSAMPR-SMIKAFEDMG--VEVRHAWGM 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 194 TEVSSWATIYRIPEKTLNSTLKCELPVQL--GFPLLGTVVEVRDTNGFTIQEgSGQVFlgGRNRVC-------------- 257
Cdd:PRK06018 328 TEMSPLGTLAALKPPFSKLPGDARLDVLQkqGYPPFGVEMKITDDAGKELPW-DGKTF--GRLKVRgpavaaayyrvdge 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 258 FLDDEvtvplgTMRATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLN-IELvQQVAEELQQVESCAVT------WYNQEKL 329
Cdd:PRK06018 405 ILDDD------GFFDTGDVATIdAYGYMRITDRSKDVIKSGGEWISsIDL-ENLAVGHPKVAEAAVIgvyhpkWDERPLL 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1021589396 330 ILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNKIYLNY 387
Cdd:PRK06018 478 IVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREQFKDY 535
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
39-384 |
1.13e-07 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 55.37 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFL-ALSSGASLLIVPTSVKLLP 117
Cdd:cd05906 169 LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELHLrAVYLGCQQVHVPTEEILAD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASVLFSHHRVTVLQAtP----TLLRRFGSQLIKSTV-LSattSLRVLALGGEAFPSLTV---LRSWRGEGNKTQIFN 189
Cdd:cd05906 249 PLRWLDLIDRYRVTITWA-PnfafALLNDLLEEIEDGTWdLS---SLRYLVNAGEAVVAKTIrrlLRLLEPYGLPPDAIR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 190 -VYGITEVSSWATIYRIPEkTLNSTLKCELpVQLGFPLLGTVVEVRDTNGFTIQEG-------SGQVFLGG------RNR 255
Cdd:cd05906 325 pAFGMTETCSGVIYSRSFP-TYDHSQALEF-VSLGRPIPGVSMRIVDDEGQLLPEGevgrlqvRGPVVTKGyynnpeANA 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 256 VCFLDDevtvplGTMRaTGDFVTVKDGEIFFLGRKDSQIKRHG-KRLNIELvQQVAEELQQVES-----CAVTWYNQ--E 327
Cdd:cd05906 403 EAFTED------GWFR-TGDLGFLDNGNLTITGRTKDTIIVNGvNYYSHEI-EAAVEEVPGVEPsftaaFAVRDPGAetE 474
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021589396 328 KLILFMVSkdASVKEYIFKELQKYLPSHAV------PDELVLI--DSLPFTSHGKIDVSELNKIY 384
Cdd:cd05906 475 ELAIFFVP--EYDLQDALSETLRAIRSVVSrevgvsPAYLIPLpkEEIPKTSLGKIQRSKLKAAF 537
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
45-321 |
1.21e-07 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 55.19 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 45 TSGTTGIPKIVRVPHKCIVpnIQHFRVLFDI--TQEDVLFLASPLtfdpsvVEIFlALSSGASLLIVPTSVKLLP---SK 119
Cdd:PLN02860 180 TSGTTGRPKGVTISHSALI--VQSLAKIAIVgyGEDDVYLHTAPL------CHIG-GLSSALAMLMVGACHVLLPkfdAK 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 120 LASVLFSHHRVTVLQATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPSLtVLRSWRGEGNKTQIFNVYGITEVSSW 199
Cdd:PLN02860 251 AALQAIKQHNVTSMITVPAMMADLISLTRKSMTWKVFPSVRKILNGGGSLSSR-LLPDAKKLFPNAKLFSAYGMTEACSS 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 200 ATIYRIPEKTLNS----TLKCELPVQLGFPLLGTV--------VEVRDtnGFTIQEGSGQVFLGGRNRVCFLDDEVTVPL 267
Cdd:PLN02860 330 LTFMTLHDPTLESpkqtLQTVNQTKSSSVHQPQGVcvgkpaphVELKI--GLDESSRVGRILTRGPHVMLGYWGQNSETA 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 268 GTMRA-----TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV 321
Cdd:PLN02860 408 SVLSNdgwldTGDIGWIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
25-382 |
2.41e-07 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 54.01 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 25 EKAEEHMDLRLKHCLAYVLH-TSGTTGIPKIVRVPHKCI-VPNIQHFRVLFDITQEDVLFLASPLTFDPSVV-EIFLALS 101
Cdd:cd05928 161 EASTEHHCVETGSQEPMAIYfTSGTTGSPKMAEHSHSSLgLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 102 SGASLLivptsVKLLPSKLASVL---FSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEAF-PSltVLRS 177
Cdd:cd05928 241 QGACVF-----VHHLPRFDPLVIlktLSSYPITTFCGAPTVYRMLVQQDLSSYKFP---SLQHCVTGGEPLnPE--VLEK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 178 WRgegNKT--QIFNVYGITEVSSWATIYRipektlnsTLKCElPVQLGFPLLGTVVEVRDTNGFTI---QEGSGQVFLGG 252
Cdd:cd05928 311 WK---AQTglDIYEGYGQTETGLICANFK--------GMKIK-PGSMGKASPPYDVQIIDDNGNVLppgTEGDIGIRVKP 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 253 RNRVCFLDDEVTVPLGTMRA-TGDF-------VTVKDGEIFFLGRKDSQIKRHGKRLN-IELVQQVAEELQQVESCAVTW 323
Cdd:cd05928 379 IRPFGLFSGYVDNPEKTAATiRGDFyltgdrgIMDEDGYFWFMGRADDVINSSGYRIGpFEVESALIEHPAVVESAVVSS 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021589396 324 YNQ---EKLILFMV------SKDasvKEYIFKELQKYLPS----HAVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:cd05928 459 PDPirgEVVKAFVVlapqflSHD---PEQLTKELQQHVKSvtapYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
45-213 |
3.92e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 53.05 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 45 TSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDpSVVEIFLALSSGASLLIVPTSVKLLPSkLAS 122
Cdd:cd05917 10 TSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPSFDPLAV-LEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 123 VlfSHHRVTVLQATPTL-LRRFGSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRGEGNKTQIFNVYGITEVSSWAT 201
Cdd:cd05917 88 I--EKEKCTALHGVPTMfIAELEHPDFDKFDLS---SLRTGIMAGAPCPP-ELMKRVIEVMNMKDVTIAYGMTETSPVST 161
|
170
....*....|....*
gi 1021589396 202 IYRI---PEKTLNST 213
Cdd:cd05917 162 QTRTddsIEKRVNTV 176
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
39-291 |
4.02e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 53.43 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVlFLAspltfdpsVVEIF----------LALSSGASLLI 108
Cdd:PRK08314 192 LAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESV-VLA--------VLPLFhvtgmvhsmnAPIYAGATVVL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 109 VPTSVKllpsKLASVLFSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLALGGEAFPS--------LTVLRSWR 179
Cdd:PRK08314 263 MPRWDR----EAAARLIERYRVTHWTNIPTMVVDFlASPGLAERDLS---SLRYIGGGGAAMPEavaerlkeLTGLDYVE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 180 GegnktqifnvYGITEVSSwATIYRIPEKTlnsTLKCelpvqLGFPLLGTVVEVRDTNgfTIQE-GSG----------QV 248
Cdd:PRK08314 336 G----------YGLTETMA-QTHSNPPDRP---KLQC-----LGIPTFGVDARVIDPE--TLEElPPGevgeivvhgpQV 394
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1021589396 249 FLGGRNRvcflddevtvPLGTMRAtgdFVTVkDGEIFF----LGRKD 291
Cdd:PRK08314 395 FKGYWNR----------PEATAEA---FIEI-DGKRFFrtgdLGRMD 427
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
40-380 |
4.33e-07 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 53.28 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPniqhfRVLFDITQEDVLFLAS-------PLTFDPSVVEIFLALSSGASLLIVPTS 112
Cdd:cd05923 153 AFVFYTSGTTGLPKGAVIPQRAAES-----RVLFMSTQAGLRHGRHnvvlglmPLYHVIGFFAVLVAALALDGTYVVVEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 113 VKllpSKLASVLFSHHRVTVLQATPTLLRRF-GSQLIKSTVLSattSLRVLALGGEAFPSlTVLRSWRgEGNKTQIFNVY 191
Cdd:cd05923 228 FD---PADALKLIEQERVTSLFATPTHLDALaAAAEFAGLKLS---SLRHVTFAGATMPD-AVLERVN-QHLPGEKVNIY 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 192 GITEVSSwATIYRIPekTLNSTLKCELPVQLGF-PLLGTVVE---VRDTNGFTIQEGSGQVFLGGRNRvcFLDDEVTVPL 267
Cdd:cd05923 300 GTTEAMN-SLYMRDA--RTGTEMRPGFFSEVRIvRIGGSPDEalaNGEEGELIVAAAADAAFTGYLNQ--PEATAKKLQD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 268 GTMRaTGDFVTVK-DGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVKE 342
Cdd:cd05923 375 GWYR-TGDVGYVDpSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwgqsVTACVVPREGTLSA 453
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1021589396 343 yifKELQKY-----LPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:cd05923 454 ---DELDQFcraseLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
40-320 |
8.23e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 52.46 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvveifLALSSgasllIVPtsvKLLP 117
Cdd:cd05910 88 AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLfaLFGPA-----LGLTS-----VIP---DMDP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASV----LFS---HHRVTVLQATPTLLR---RFGSQLIKStvlsaTTSLRVLALGGEAFPSLTVLRSWRGEGNKTQI 187
Cdd:cd05910 155 TRPARAdpqkLVGairQYGVSIVFGSPALLErvaRYCAQHGIT-----LPSLRRVLSAGAPVPIALAARLRKMLSDEAEI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 188 FNVYGITE---VSSwatiyrIPEKTLNSTlKCELPVQ-----LGFPLLGTVVEVRDTNGFTIQE--GSGQVFLGGRNRVC 257
Cdd:cd05910 230 LTPYGATEalpVSS------IGSRELLAT-TTAATSGgagtcVGRPIPGVRVRIIEIDDEPIAEwdDTLELPRGEIGEIT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 258 FLDDEVTV-----PLGTMRA------------TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESC 319
Cdd:cd05910 303 VTGPTVTPtyvnrPVATALAkiddnsegfwhrMGDLGYLDDeGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRS 382
|
.
gi 1021589396 320 A 320
Cdd:cd05910 383 A 383
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
38-384 |
9.12e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 52.24 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 38 CLAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPLtFDPSVVEIFL--ALSSGASLLIV--PTSV 113
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPL-YHCAQLDVFLgpYLYVGATNVILdaPDPE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 114 KLLPsklasvLFSHHRVTVLQATPT----LLRrfgSQLIKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFN 189
Cdd:PRK08316 251 LILR------TIEAERITSFFAPPTvwisLLR---HPDFDTRDLS---SLRKGYYGASIMP-VEVLKELRERLPGLRFYN 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 190 VYGITEVSSWATIYRiPEKTLnstlkcELPVQLGFPLLGtvVEVR--DTNGFTIQEG--------SGQVFLGgrnrvcFL 259
Cdd:PRK08316 318 CYGQTEIAPLATVLG-PEEHL------RRPGSAGRPVLN--VETRvvDDDGNDVAPGevgeivhrSPQLMLG------YW 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 260 DD-EVTVP-----------LGTMRATGdFVTVKDgeifflgRKDSQIKRHGkrlniELV--QQVAEELQQ---VESCAVT 322
Cdd:PRK08316 383 DDpEKTAEafrggwfhsgdLGVMDEEG-YITVVD-------RKKDMIKTGG-----ENVasREVEEALYThpaVAEVAVI 449
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021589396 323 WYNQEKLI----LFMVSKD-ASVKEyifKELQKY----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKIY 384
Cdd:PRK08316 450 GLPDPKWIeavtAVVVPKAgATVTE---DELIAHcrarLAGFKVPKRVIFVDELPRNPSGKILKRELRERY 517
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
141-382 |
1.06e-06 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 51.58 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 141 RRFGS----QLIKS-TVLSATTSLRVLA---LGGEAFPSlTVLRSWRGEGnkTQIFNVYGITEVSSwatiyripektlns 212
Cdd:PRK07824 127 RRYTSlvpmQLAKAlDDPAATAALAELDavlVGGGPAPA-PVLDAAAAAG--INVVRTYGMSETSG-------------- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 213 tlKCelpVQLGFPLLGTVVEVRDtngftiqegsGQVFLGG-------RNRVcflDDEVTVPLGTMRaTGDFVTVKDGEIF 285
Cdd:PRK07824 190 --GC---VYDGVPLDGVRVRVED----------GRIALGGptlakgyRNPV---DPDPFAEPGWFR-TDDLGALDDGVLT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 286 FLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL---ILFMVSKDASVKEYIfKELQKY----LPSHAVP 358
Cdd:PRK07824 251 VLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLgqrVVAAVVGDGGPAPTL-EALRAHvartLDRTAAP 329
|
250 260
....*....|....*....|....
gi 1021589396 359 DELVLIDSLPFTSHGKIDVSELNK 382
Cdd:PRK07824 330 RELHVVDELPRRGIGKVDRRALVR 353
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
157-383 |
3.31e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 50.59 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 157 TSLRVLALGGEAFPSLTVLRsWRGEGNKTqIFNVYGITEVSSWATIYRIPEKTLNSTLkcelpvqlGFPLLGTVVEVRDT 236
Cdd:PRK12492 333 SALKLTNSGGTALVKATAER-WEQLTGCT-IVEGYGLTETSPVASTNPYGELARLGTV--------GIPVPGTALKVIDD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 237 NGFtiqegsgQVFLGGRNRVCFLDDEV-----TVPLGTMRA--------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLN 302
Cdd:PRK12492 403 DGN-------ELPLGERGELCIKGPQVmkgywQQPEATAEAldaegwfkTGDIAVIdPDGFVRIVDRKKDLIIVSGFNVY 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 303 IELVQQVAEELQQVESCAVTWYNQEK----LILFMVSKDASVKeyiFKELQKY----LPSHAVPDELVLIDSLPFTSHGK 374
Cdd:PRK12492 476 PNEIEDVVMAHPKVANCAAIGVPDERsgeaVKLFVVARDPGLS---VEELKAYckenFTGYKVPKHIVLRDSLPMTPVGK 552
|
....*....
gi 1021589396 375 IDVSELNKI 383
Cdd:PRK12492 553 ILRRELRDI 561
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
38-380 |
6.24e-06 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 49.80 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 38 CLAYVlhTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDItQEDVLFLASPLTFDPSVV--EIFLALSSGASLLIVPTSvKL 115
Cdd:cd05970 188 LLVYF--SSGTTGMPKMVEHDFTYPLGHIVTAKYWQNV-REGGLHLTVADTGWGKAVwgKIYGQWIAGAAVFVYDYD-KF 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 116 LPSKLASVLfSHHRVTVLQATPTLLRRFGSQLIKSTVLSattSLRVLALGGEAFpSLTVLRSWRgEGNKTQIFNVYGITE 195
Cdd:cd05970 264 DPKALLEKL-SKYGVTTFCAPPTIYRFLIREDLSRYDLS---SLRYCTTAGEAL-NPEVFNTFK-EKTGIKLMEGFGQTE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 -VSSWATIYRIPEKtlnstlkcelPVQLGFPLLGTVVEVRDTNGFTIQEG-SGQVflggrnrVCFLDDEVtvPLGTMRA- 272
Cdd:cd05970 338 tTLTIATFPWMEPK----------PGSMGKPAPGYEIDLIDREGRSCEAGeEGEI-------VIRTSKGK--PVGLFGGy 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 273 -----------------TGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK----LI 330
Cdd:cd05970 399 ykdaektaevwhdgyyhTGDAAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIrgqvVK 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1021589396 331 LFMV-SKDASVKEYIFKELQKYLPSHAVPDE----LVLIDSLPFTSHGKIDVSEL 380
Cdd:cd05970 479 ATIVlAKGYEPSEELKKELQDHVKKVTAPYKypriVEFVDELPKTISGKIRRVEI 533
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
42-375 |
7.10e-06 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 49.04 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 42 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLALSSGASllIVPTSVKLLPSK 119
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFfhTFGYK-AGIVACLLTGAT--VVPVAVFDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 120 LASVlfSHHRVTVLQATPTLlrrFGSQL----IKSTVLSattSLRVLALGGEAFPSLTVLRsWRGEGNKTQIFNVYGITE 195
Cdd:cd17638 82 LEAI--ERERITVLPGPPTL---FQSLLdhpgRKKFDLS---SLRAAVTGAATVPVELVRR-MRSELGFETVLTAYGLTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 196 VSSwATIYRI--PEKTLNSTlkcelpvqLGFPLLGTVVEVRDtngftiqegSGQVFLGGRN-RVCFLDDevtvPLGTMRA 272
Cdd:cd17638 153 AGV-ATMCRPgdDAETVATT--------CGRACPGFEVRIAD---------DGEVLVRGYNvMQGYLDD----PEATAEA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 273 --------TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEKL----ILFMVSKDAS 339
Cdd:cd17638 211 idadgwlhTGDVGELDErGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMgevgKAFVVARPGV 290
|
330 340 350
....*....|....*....|....*....|....*...
gi 1021589396 340 --VKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKI 375
Cdd:cd17638 291 tlTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
254-376 |
2.43e-05 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 47.83 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 254 NRVCFLDDevtvplGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNielvqqvAEELQ-------QVESCAVTWYN 325
Cdd:COG1021 401 NARAFTPD------GFYR-TGDLVRRtPDGYLVVEGRAKDQINRGGEKIA-------AEEVEnlllahpAVHDAAVVAMP 466
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 326 Q----EKLILFMVSKDASVKeyiFKELQKYL-----PSHAVPDELVLIDSLPFTSHGKID 376
Cdd:COG1021 467 DeylgERSCAFVVPRGEPLT---LAELRRFLrerglAAFKLPDRLEFVDALPLTAVGKID 523
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
399-455 |
6.24e-05 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 42.15 E-value: 6.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1021589396 399 KEDLWEKLQYLWKSTLNLPEDLLRvPDESLFLNSGGDSLKSIRLLSEIEKLVGTSVP 455
Cdd:COG0236 3 REELEERLAEIIAEVLGVDPEEIT-PDDSFFEDLGLDSLDAVELIAALEEEFGIELP 58
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
39-294 |
6.42e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 46.28 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFdPSVVEIFLALSSGAS--LLIVPTSVK 114
Cdd:cd05914 91 VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKILSILPLhhIY-PLTFTLLLPLLNGAHvvFLDKIPSAK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 115 LLPSKLASV----------LFSHHRVTVLQ------------ATPTLLRRFGSQLIKSTVLSATTSLRVLALGGEAFPsL 172
Cdd:cd05914 170 IIALAFAQVtptlgvpvplVIEKIFKMDIIpkltlkkfkfklAKKINNRKIRKLAFKKVHEAFGGNIKEFVIGGAKIN-P 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 173 TVLRSWRGEGNKTQIfnVYGITEVSSWATiYRIPEKT-LNSTlkcelpvqlGFPLLGTVVEVRDTNGFTiqeGSGQVFLG 251
Cdd:cd05914 249 DVEEFLRTIGFPYTI--GYGMTETAPIIS-YSPPNRIrLGSA---------GKVIDGVEVRIDSPDPAT---GEGEIIVR 313
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1021589396 252 GRN--RVCFLDDEVTV----PLGTMRaTGDFVT-VKDGEIFFLGRKDSQI 294
Cdd:cd05914 314 GPNvmKGYYKNPEATAeafdKDGWFH-TGDLGKiDAEGYLYIRGRKKEMI 362
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
40-202 |
9.72e-05 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 45.96 E-value: 9.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVL--FLASPLTFDPSVVEIFLALssgASLLIVPTSVKLLP 117
Cdd:PRK06334 186 AVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMmsFLPPFHAYGFNSCTLFPLL---SGVPVVFAYNPLYP 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASVLFSHHrVTVLQATPTllrrFGSQLIKSTVLSATT--SLRVLALGGEAFPSltvlrSWRGEGNKT----QIFNVY 191
Cdd:PRK06334 263 KKIVEMIDEAK-VTFLGSTPV----FFDYILKTAKKQESClpSLRFVVIGGDAFKD-----SLYQEALKTfphiQLRQGY 332
|
170
....*....|.
gi 1021589396 192 GITEVSSWATI 202
Cdd:PRK06334 333 GTTECSPVITI 343
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
40-383 |
1.50e-04 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 45.47 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvVEIFLALSSGAsllivptSVKLLP 117
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLT-VGLFTPLLTGA-------EVFLYP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLasvlfsHHRV----------TVLQATPTLL---RRFGSQLikstvlsATTSLRVLALGGEAFpSLTVLRSWRgEGNK 184
Cdd:PRK08043 440 SPL------HYRIvpelvydrncTVLFGTSTFLgnyARFANPY-------DFARLRYVVAGAEKL-QESTKQLWQ-DKFG 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 185 TQIFNVYGITEVSSWATIyRIPEKTLNSTLKCELPvqlgfpllgtVVEVRDTNGFTIQEGsGQVFLGGRN------RVcF 258
Cdd:PRK08043 505 LRILEGYGVTECAPVVSI-NVPMAAKPGTVGRILP----------GMDARLLSVPGIEQG-GRLQLKGPNimngylRV-E 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 259 LDDEVTVP-----LGTMRA----TGDFVTVKD-GEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQ-- 326
Cdd:PRK08043 572 KPGVLEVPtaenaRGEMERgwydTGDIVRFDEqGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDas 651
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021589396 327 --EKLILFmvSKDASVKEyifKELQKY-----LPSHAVPDELVLIDSLPFTSHGKIDVSELNKI 383
Cdd:PRK08043 652 kgEALVLF--TTDSELTR---EKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
40-382 |
1.55e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.16 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVL--FDITQEDVLFLASPLTFDPSVVEIFLALSSGASLliVPTSVKLLP 117
Cdd:PRK05620 184 AAICYSTGTTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLCCVPIYHVLSWGVPLAAFMSGTPL--VFPGPDLSA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 118 SKLASVL-FSHHRVTvlQATPTLLRRFGSQLIKSTvlSATTSLRVLALGGEAFPSLtVLRSWRgEGNKTQIFNVYGITEV 196
Cdd:PRK05620 262 PTLAKIIaTAMPRVA--HGVPTLWIQLMVHYLKNP--PERMSLQEIYVGGSAVPPI-LIKAWE-ERYGVDVVHVWGMTET 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 197 SSWATIYRIPEKTLNSTL------KCELPVQLGFPLL--GTVVEVRDTNGFTIQ----------------EGSGQVFLGG 252
Cdd:PRK05620 336 SPVGTVARPPSGVSGEARwayrvsQGRFPASLEYRIVndGQVMESTDRNEGEIQvrgnwvtasyyhspteEGGGAASTFR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 253 RNRVCFLDDEVTVPlGTMRaTGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAVTWYNQEK--- 328
Cdd:PRK05620 416 GEDVEDANDRFTAD-GWLR-TGDVGSVtRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwge 493
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 329 --LILFMVSKD----ASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSELNK 382
Cdd:PRK05620 494 rpLAVTVLAPGieptRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
42-197 |
2.78e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 44.38 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 42 VLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDpSVVEIFLALSSGASLLIVPTSVKLLPSk 119
Cdd:PRK12583 206 IQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCFG-MVLANLGCMTVGACLVYPNEAFDPLAT- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 120 LASVlfSHHRVTVLQATPTLlrrFGSQL----IKSTVLSattSLRVLALGGEAFPsLTVLRSWRGEGNKTQIFNVYGITE 195
Cdd:PRK12583 284 LQAV--EEERCTALYGVPTM---FIAELdhpqRGNFDLS---SLRTGIMAGAPCP-IEVMRRVMDEMHMAEVQIAYGMTE 354
|
..
gi 1021589396 196 VS 197
Cdd:PRK12583 355 TS 356
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
404-455 |
3.46e-04 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 39.47 E-value: 3.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1021589396 404 EKLQYLWKSTLNLPEDLLrVPDESLFlNSGGDSLKSIRLLSEIEKLVGTSVP 455
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEI-DPDTDLF-DLGLDSLLAVELIARLEEEFGVEIP 50
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
39-137 |
3.77e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 43.94 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDV--LFLasPL--TFDpSVVEIFlALSSGASlLIVPTSVK 114
Cdd:COG1022 185 LATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRtlSFL--PLahVFE-RTVSYY-ALAAGAT-VAFAESPD 259
|
90 100
....*....|....*....|...
gi 1021589396 115 LLPSKLASVlfshhRVTVLQATP 137
Cdd:COG1022 260 TLAEDLREV-----KPTFMLAVP 277
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
39-202 |
5.25e-04 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 43.36 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHF----RVLFDITQEDVLFLASPLT--FDPSVVEIFLA------LSSGASL 106
Cdd:cd05927 116 LATICYTSGTTGNPKGVMLTHGNIVSNVAGVfkilEILNKINPTDVYISYLPLAhiFERVVEALFLYhgakigFYSGDIR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 107 LIVPTSVKLLPSKLASV--LFS--HHRV-TVLQATPTLLRR---FGSQL----IKSTVLSATTSLRVL-------ALGGE 167
Cdd:cd05927 196 LLLDDIKALKPTVFPGVprVLNriYDKIfNKVQAKGPLKRKlfnFALNYklaeLRSGVVRASPFWDKLvfnkikqALGGN 275
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1021589396 168 -------AFPS----LTVLRSWRGegnkTQIFNVYGITEVSSWATI 202
Cdd:cd05927 276 vrlmltgSAPLspevLEFLRVALG----CPVLEGYGQTECTAGATL 317
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
39-196 |
6.14e-04 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 43.35 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL--TFDPSvveifLALSSgasllIVPtsvKLL 116
Cdd:PRK09274 176 MAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPLfaLFGPA-----LGMTS-----VIP---DMD 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 117 PSKLASV----LFS---HHRVTVLQATPTLLRRFGsQLIKSTVLSATTSLRVLALGGEAFPSLTV-LRSWRGEGnkTQIF 188
Cdd:PRK09274 243 PTRPATVdpakLFAaieRYGVTNLFGSPALLERLG-RYGEANGIKLPSLRRVISAGAPVPIAVIErFRAMLPPD--AEIL 319
|
....*...
gi 1021589396 189 NVYGITEV 196
Cdd:PRK09274 320 TPYGATEA 327
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
40-197 |
7.41e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 42.84 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPN-IQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIVPTSVkLLPS 118
Cdd:PRK07786 177 ALIMYTSGTTGRPKGAVLTHANLTGQaMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVIYPLGA-FDPG 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589396 119 KLASVLfSHHRVTVLQATPTllrRFGSQLIKSTVLSATTSLRVLALGGeAFPSLTVLRSWRGEGNKTQIFNVYGITEVS 197
Cdd:PRK07786 256 QLLDVL-EAEKVTGIFLVPA---QWQAVCAEQQARPRDLALRVLSWGA-APASDTLLRQMAATFPEAQILAAFGQTEMS 329
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
38-143 |
1.01e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 38 CLAYVLHTSGTTGIPKIVR--VPHKCI----VPNIQHFRVLFDITQEDVLFLASPLTFDPSVVEIFLALSSGASLLIvpt 111
Cdd:PRK13390 149 CGAVMLYSSGTTGFPKGIQpdLPGRDVdapgDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVL--- 225
|
90 100 110
....*....|....*....|....*....|..
gi 1021589396 112 sVKLLPSKLASVLFSHHRVTVLQATPTLLRRF 143
Cdd:PRK13390 226 -AKRFDAQATLGHVERYRITVTQMVPTMFVRL 256
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
45-321 |
1.13e-03 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 42.17 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 45 TSGTTGIPKIVRVPHKCiVPnIQHFRVLFDITQE--DV-LFLASPLTFDPSVVEIFLALSSGASLLIVpTSVKLLPSKLA 121
Cdd:cd05974 93 TSGTTSKPKLVEHTHRS-YP-VGHLSTMYWIGLKpgDVhWNISSPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 122 SVLfSHHRVTVLQATPTLLRrfgsQLIKSTVLSATTSLRVLALGGEAF-PSL--TVLRSWrgegNKTqIFNVYGITEVSS 198
Cdd:cd05974 170 AAL-VRYGVTTLCAPPTVWR----MLIQQDLASFDVKLREVVGAGEPLnPEVieQVRRAW----GLT-IRDGYGQTETTA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 199 WATiyripektlNSTLKCELPVQLGFPLLGTVVEVRDTNGFTIQEGSGQVFLGGRNRVCFL-----DDEVT--VPLGTMR 271
Cdd:cd05974 240 LVG---------NSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVALDLGDTRPVGLMkgyagDPDKTahAMRGGYY 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1021589396 272 ATGDFVTV-KDGEIFFLGRKDSQIKRHGKRLNIELVQQVAEELQQVESCAV 321
Cdd:cd05974 311 RTGDIAMRdEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
40-380 |
1.21e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 42.28 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL----------------------TFDPSVVEIF 97
Cdd:PRK07787 131 ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDVLVHGLPLfhvhglvlgvlgplrignrfvhTGRPTPEAYA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 98 LALSSGASLLI-VPTsvkllpsklasvlfSHHRVTvlqATPTLLRRFGSQ--LIK-STVLSATTSLRVLALGGEAfpslT 173
Cdd:PRK07787 211 QALSEGGTLYFgVPT--------------VWSRIA---ADPEAARALRGArlLVSgSAALPVPVFDRLAALTGHR----P 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 174 VLRswrgegnktqifnvYGITE----VSSWATIYRIPEktlnstlkcelpvQLGFPLLGTVVEVRDTNGFTIQE-----G 244
Cdd:PRK07787 270 VER--------------YGMTEtlitLSTRADGERRPG-------------WVGLPLAGVETRLVDEDGGPVPHdgetvG 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 245 SGQV-----FLGGRNR-----VCFLDDevtvplGTMRaTGDFVTVK-DGEIFFLGRKDSQ-IKRHGKRLNIELVQQVAEE 312
Cdd:PRK07787 323 ELQVrgptlFDGYLNRpdataAAFTAD------GWFR-TGDVAVVDpDGMHRIVGRESTDlIKSGGYRIGAGEIETALLG 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021589396 313 LQQVESCAVTWYNQEKL----ILFMVSKDASVKEYIFKELQKYLPSHAVPDELVLIDSLPFTSHGKIDVSEL 380
Cdd:PRK07787 396 HPGVREAAVVGVPDDDLgqriVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
45-141 |
1.43e-03 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 41.89 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 45 TSGTTGIPKIVRVPHKCIVpNIQHFRVLFDITQEDVLFLASPLTFDP-SVVEIFLALSSGASLlivptsvkLLPSKLASV 123
Cdd:cd05938 152 TSGTTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYITLPLYHSSgFLLGIGGCIELGATC--------VLKPKFSAS 222
|
90 100
....*....|....*....|..
gi 1021589396 124 LF----SHHRVTVLQATPTLLR 141
Cdd:cd05938 223 QFwddcRKHNVTVIQYIGELLR 244
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
43-111 |
2.87e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 41.17 E-value: 2.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021589396 43 LHTSGTTGIPKIVRVPhkcivpniqHFRVL---------FDITQEDVLFLASPLTFDPSVVEIF-LALSSGASLLIVPT 111
Cdd:PRK13388 156 IFTSGTTGAPKAVRCS---------HGRLAfagralterFGLTRDDVCYVSMPLFHSNAVMAGWaPAVASGAAVALPAK 225
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
45-99 |
2.97e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 41.13 E-value: 2.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021589396 45 TSGTTGIPKIVRVPHKCIVPNI--QHFRVLFDItQEDVL--------------FLASPLTFDPSVVEI----FLA 99
Cdd:PRK07768 160 TSGSTGSPKAVQITHGNLYANAeaMFVAAEFDV-ETDVMvswlplfhdmgmvgFLTVPMYFGAELVKVtpmdFLR 233
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
40-108 |
3.74e-03 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 40.63 E-value: 3.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021589396 40 AYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL------TFDPSVVeiflaLSSGASLLI 108
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCCLPLyhntggTVAWSSV-----LAAGATLAL 271
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
39-142 |
5.56e-03 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 40.24 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021589396 39 LAYVLHTSGTTGIPKIVRVPHKCIVPNIQHFRVLFDITQEDVLFLASPL-----TFdpsvVEIFLALSSGASLLIVPtsv 113
Cdd:PRK07514 158 LAAILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIfhthgLF----VATNVALLAGASMIFLP--- 230
|
90 100
....*....|....*....|....*....
gi 1021589396 114 KLLPSKLASVLfshHRVTVLQATPTLLRR 142
Cdd:PRK07514 231 KFDPDAVLALM---PRATVMMGVPTFYTR 256
|
|
| assembly_YfgL |
TIGR03300 |
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ... |
597-661 |
9.37e-03 |
|
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: 39.15 E-value: 9.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021589396 597 TQKMELHVRWRSDTGKCVDASPLVVIPTFDKSSttVYIGSHSHRMKAVDFYSGKVKWEQILGDRI 661
Cdd:TIGR03300 35 QPTVKVDQVWSASVGDGVGHYYLRLQPAVAGGK--VYAADADGTVAALDAETGKRLWRVDLDERL 97
|
|
| |
