|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
9-406 |
0e+00 |
|
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: 527.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLL 88
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 89 TVGEVRVQVTQPGLTQLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINE 168
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 169 RFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRM 248
Cdd:cd12114 161 RFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 249 SYPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVESTWTSIPYGRGLRNQPVYVLNAQLE 328
Cdd:cd12114 241 LLPSLRLVLLSGDWIPLDLPARLRALAPDA-RLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPRGR 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535686385 329 ECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVwREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd12114 320 DCPDWVPGELWIGGRGVALGYLGDPELTAARFV-THPDGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGE 396
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3-406 |
4.63e-151 |
|
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: 460.86 E-value: 4.63e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:COG1020 484 AQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVTQPGLTQL--EPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:COG1020 564 RLAYMLEDAGARLVLTQSALAARlpELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLC 240
Cdd:COG1020 644 NLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALL 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 241 EYHSGDRmsyPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVESTWTSIPYGRGLRNQPV 320
Cdd:COG1020 724 DAAPEAL---PSLRLVLVGGEALPPELVRRWRARLPGA-RLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRV 799
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 321 YVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVN 398
Cdd:COG1020 800 YVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVadPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIR 879
|
....*...
gi 535686385 399 GYRIELGE 406
Cdd:COG1020 880 GFRIELGE 887
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
22-406 |
1.87e-144 |
|
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: 416.67 E-value: 1.87e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 22 TYRQLSTAADHVARALLAL-GVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTQP 100
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 101 GLTQLEPSLPVLIIDDGML------DTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNA 174
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLelaaldDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 175 QDRVFGLSSLSFDLSVYDAFAPFMVGAALVL-PEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEyhsGDRMSYPTL 253
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVpPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA---ALPPALASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 254 RLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVESTWTS-IPYGRGLRNQPVYVLNAQLEECPV 332
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGPGA-RLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535686385 333 GVEGEICIGGMGLAQGYLNDAEKTAASFV---WREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERFVpdpFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
9-406 |
4.46e-132 |
|
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: 386.50 E-value: 4.46e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLL 88
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 89 TVGEVRVQVTQPGltqlepslpvliiddgmldtpaaplpevagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINE 168
Cdd:cd05930 81 EDSGAKLVLTDPD---------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 169 RFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYhsGDRM 248
Cdd:cd05930 128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE--LELA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 249 SYPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVESTWTSIPYGRGLRNQPVYVLNAQLE 328
Cdd:cd05930 206 ALPSLRLVLVGGEALPPDLVRRWRELLPGA-RLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLR 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535686385 329 ECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV-WREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVpNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGE 363
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
3-406 |
1.66e-111 |
|
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: 335.40 E-value: 1.66e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:cd17646 6 EQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVTQPGLT-QLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMN 161
Cdd:cd17646 86 RLAYMLADAGPAVVLTTADLAaRLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 162 TLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCE 241
Cdd:cd17646 166 RLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 242 yhSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETMdiISLGGATECAIWSVYYPIGEVESTwTSIPYGRGLRNQPVY 321
Cdd:cd17646 246 --EPAAGSCASLRRVFCSGEALPPELAARFLALPGAEL--HNLYGPTEAAIDVTHWPVRGPAET-PSVPIGRPVPNTRLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 322 VLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE-ASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGY 400
Cdd:cd17646 321 VLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPfGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGF 400
|
....*.
gi 535686385 401 RIELGE 406
Cdd:cd17646 401 RVEPGE 406
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
3-406 |
3.56e-106 |
|
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: 321.46 E-value: 3.56e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:cd12117 5 EQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVTQPGLTQLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNT 162
Cdd:cd12117 85 RLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 163 LEDINERfGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEY 242
Cdd:cd12117 165 VKNTNYV-TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALFNQLADE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 243 HSGdrmSYPTLRLALLSGDWIPltlPEQMRERLNETMD--IISLGGATECAIWSVYYPIGEVESTWTSIPYGRGLRNQPV 320
Cdd:cd12117 244 DPE---CFAGLRELLTGGEVVS---PPHVRRVLAACPGlrLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGRPIANTRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 321 YVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE-ASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNG 399
Cdd:cd12117 318 YVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPfGPGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRG 397
|
....*..
gi 535686385 400 YRIELGE 406
Cdd:cd12117 398 FRIELGE 404
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1-397 |
2.15e-103 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 312.32 E-value: 2.15e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETAL-ISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVL 79
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 80 PPQRRQLLLTVGEVRVQVTQ---------PGLTQLEPSLPVLIIDDGMLDT-----------PAAPLPEVAGDVTDLAYI 139
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDdalkleellEALGKLEVVKLVLVLDRDPVLKeeplpeeakpaDVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 140 IFTSGSTGTPKGVMIDHRAAMNTLEDI----NERFGLNAQDRVFGLSSLSFDLSV-YDAFAPFMVGAALVLPEAGREKDP 214
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 215 RHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETmdIISLGGATECAIWS 294
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA--LVNGYGLTETTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 295 VYYPIGEVEstWTSIP-YGRGLRNQPVYVLNAQ-LEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVwreasGERIYR 372
Cdd:pfam00501 319 TTPLPLDED--LRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD-----EDGWYR 391
|
410 420
....*....|....*....|....*
gi 535686385 373 TGDRGRYFADGQVAFLGRNDTQVKV 397
Cdd:pfam00501 392 TGDLGRRDEDGYLEIVGRKKDQIKL 416
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
9-406 |
8.44e-98 |
|
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: 299.59 E-value: 8.44e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLL 88
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 89 TVGEVRVQVTQPGLTQLEPSLPVLIIDDGMLD--TPAAPLPEVAGDvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDI 166
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAaaAPAAPRTPVSPD--DLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 167 NERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHW-QTVMAHGhVSVWNAVPALMQMLCEYHSG 245
Cdd:cd12116 159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALaRLIEAHS-ITVMQATPATWRMLLDAGWQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 246 DRmsyPTLRlALLSGDWIPLTLPEQMRERlneTMDIISLGGATECAIWSVyypIGEVESTWTSIPYGRGLRNQPVYVLNA 325
Cdd:cd12116 238 GR---AGLT-ALCGGEALPPDLAARLLSR---VGSLWNLYGPTETTIWST---AARVTAAAGPIPIGRPLANTQVYVLDA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 326 QLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIE 403
Cdd:cd12116 308 ALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVpdPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIE 387
|
...
gi 535686385 404 LGE 406
Cdd:cd12116 388 LGE 390
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
4-406 |
1.75e-96 |
|
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: 296.93 E-value: 1.75e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:cd17655 6 QAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQPGLTQLEPSLP-VLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNT 162
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQPPIAFIGlIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 163 LEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLpeaGREKDPRHWQTVMAH---GHVSVWNAVPALMQML 239
Cdd:cd17655 166 VEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYI---VRKETVLDGQALTQYirqNRITIIDLTPAHLKLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 240 CEyhsGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETMDIISLGGATECAIWSVYYPIGEVESTWTSIPYGRGLRNQP 319
Cdd:cd17655 243 DA---ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 320 VYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE-ASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVN 398
Cdd:cd17655 320 IYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPfVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIR 399
|
....*...
gi 535686385 399 GYRIELGE 406
Cdd:cd17655 400 GYRIELGE 407
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
3-406 |
6.28e-95 |
|
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: 293.10 E-value: 6.28e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVTQPGLT--QLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAgeLAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRSLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLC 240
Cdd:cd17651 163 NLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 241 EY--HSGDRMsyPTLRLALLSGDwiPLTLPEQMRERLNET--MDIISLGGATECAIWSVYYPIGEVeSTWTSIP-YGRGL 315
Cdd:cd17651 243 EHgrPLGVRL--AALRYLLTGGE--QLVLTEDLREFCAGLpgLRLHNHYGPTETHVVTALSLPGDP-AAWPAPPpIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 316 RNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWREAS-GERIYRTGDRGRYFADGQVAFLGRNDTQ 394
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVpGARMYRTGDLARWLPDGELEFLGRADDQ 397
|
410
....*....|..
gi 535686385 395 VKVNGYRIELGE 406
Cdd:cd17651 398 VKIRGFRIELGE 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
5-406 |
2.79e-91 |
|
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: 282.21 E-value: 2.79e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRR 84
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 85 QLLLTVGEvrvqvtqpgltqlepslPVLIIDDGmldtpaaplpevagdvTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLE 164
Cdd:cd05945 81 REILDAAK-----------------PALLIADG----------------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 165 DINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHS 244
Cdd:cd05945 128 WMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 245 GDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETMdIISLGGATECAIWSVYYPI-GEVESTWTSIPYGRGLRNQPVYVL 323
Cdd:cd05945 208 FTPESLPSLRHFLFCGEVLPHKTARALQQRFPDAR-IYNTYGPTEATVAVTYIEVtPEVLDGYDRLPIGYAKPGAKLVIL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 324 NAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWREasGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIE 403
Cdd:cd05945 287 DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE--GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIE 364
|
...
gi 535686385 404 LGE 406
Cdd:cd05945 365 LEE 367
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1-406 |
2.38e-90 |
|
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: 279.97 E-value: 2.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPgltqlepslpvliiddgmldtpaaplpevagdvTDLAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:cd12115 85 PERLRFILEDAQARLVLTDP---------------------------------DDLAYVIYTSGSTGRPKGVAIEHRNAA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEagrekDPRHWQTVMAHGHVSVWNAVPALMQMLC 240
Cdd:cd12115 132 AFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPSAAAELL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 241 EyHSGdrmSYPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVESTWTSIpyGRGLRNQPV 320
Cdd:cd12115 207 R-HDA---LPASVRVVNLAGEPLPRDLVQRLYARLQVE-RVVNLYGPSEDTTYSTVAPVPPGASGEVSI--GRPLANTQA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 321 YVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVW-REASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNG 399
Cdd:cd12115 280 YVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPdPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRG 359
|
....*..
gi 535686385 400 YRIELGE 406
Cdd:cd12115 360 FRIELGE 366
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-406 |
5.78e-87 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 288.78 E-value: 5.78e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:PRK12316 520 QVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAER 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQPGLTQLEP---SLPVLIIDDGMLDTPAAP--LPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRA 158
Cdd:PRK12316 600 LAYMLEDSGVQLLLSQSHLGRKLPlaaGVQVLDLDRPAAWLEGYSeeNPGTELNPENLAYVIYTSGSTGKPKGAGNRHRA 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 159 AMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDP-RHWQTVMAHGhVSVWNAVPALMQ 237
Cdd:PRK12316 680 LSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPaKLVELINREG-VDTLHFVPSMLQ 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 238 MLceYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIgeVESTWTSIPYGRGLRN 317
Cdd:PRK12316 759 AF--LQDEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQA-GLYNLYGPTEAAIDVTHWTC--VEEGGDSVPIGRPIAN 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 318 QPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE-ASGERIYRTGDRGRYFADGQVAFLGRNDTQVK 396
Cdd:PRK12316 834 LACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPfVAGERMYRTGDLARYRADGVIEYAGRIDHQVK 913
|
410
....*....|
gi 535686385 397 VNGYRIELGE 406
Cdd:PRK12316 914 LRGLRIELGE 923
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
3-406 |
9.77e-86 |
|
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: 269.03 E-value: 9.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:cd05918 7 ERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLltvgevrVQVTQPGLTqlepslpvliiddgmldtpaaplpeVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNT 162
Cdd:cd05918 87 RLQEI-------LQDTGAKVV-------------------------LTSSPSDAAYVIFTSGSTGKPKGVVIEHRALSTS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 163 LEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLP-EAGREKDPrhwQTVMAHGHVSVWNAVPALMQMLce 241
Cdd:cd05918 135 ALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPsEEDRLNDL---AGFINRLRVTWAFLTPSVARLL-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 242 yhsgDRMSYPTLRLALLSGdwipltlpEQMRERLNET----MDIISLGGATECAIWSVYYPIGeveSTWTSIPYGRGLRN 317
Cdd:cd05918 210 ----DPEDVPSLRTLVLGG--------EALTQSDVDTwadrVRLINAYGPAECTIAATVSPVV---PSTDPRNIGRPLGA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 318 QpVYVLNAQLEE--CPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWREA--------SGERIYRTGDRGRYFADGQVAF 387
Cdd:cd05918 275 T-CWVVDPDNHDrlVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegsgRGRRLYRTGDLVRYNPDGSLEY 353
|
410
....*....|....*....
gi 535686385 388 LGRNDTQVKVNGYRIELGE 406
Cdd:cd05918 354 VGRKDTQVKIRGQRVELGE 372
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
3-406 |
1.10e-85 |
|
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: 267.25 E-value: 1.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:cd17653 5 RIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQllltvgevrvqvtqpglTQLEPSLPVLIIddgmldTPAAPlpevagdvTDLAYIIFTSGSTGTPKGVMIDHRAAMNT 162
Cdd:cd17653 85 RIQ-----------------AILRTSGATLLL------TTDSP--------DDLAYIIFTSGSTGIPKGVMVPHRGVLNY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 163 LEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLpeagreKDPRH-WQTVMAhgHVSVWNAVPALMQMLce 241
Cdd:cd17653 134 VSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL------ADPSDpFAHVAR--TVDALMSTPSILSTL-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 242 yhsgDRMSYPTLRLALLSGDWIPLTLPEQMRERlnetMDIISLGGATECAIWSVY---YPIgevestwTSIPYGRGLRNQ 318
Cdd:cd17653 204 ----SPQDFPNLKTIFLGGEAVPPSLLDRWSPG----RRLYNAYGPTECTISSTMtelLPG-------QPVTIGKPIPNS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 319 PVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV-WREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKV 397
Cdd:cd17653 269 TCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVpDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKV 348
|
....*....
gi 535686385 398 NGYRIELGE 406
Cdd:cd17653 349 RGFRINLEE 357
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-406 |
1.16e-84 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 282.05 E-value: 1.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:PRK12467 520 AQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQD 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVTQPGLTQLEP---SLPVLIIDDG--MLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:PRK12467 600 RLAYMLDDSGVRLLLTQSHLLAQLPvpaGLRSLCLDEPadLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHG 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 158 AAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQ 237
Cdd:PRK12467 680 ALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQ 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 238 MLCeyhSGDRMSYPT-LRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVESTWTSIPYGRGLR 316
Cdd:PRK12467 760 ALL---QASRVALPRpQRALVCGGEALQVDLLARVRALGPGA-RLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLA 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 317 NQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE--ASGERIYRTGDRGRYFADGQVAFLGRNDTQ 394
Cdd:PRK12467 836 NLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPfgADGGRLYRTGDLARYRADGVIEYLGRMDHQ 915
|
410
....*....|..
gi 535686385 395 VKVNGYRIELGE 406
Cdd:PRK12467 916 VKIRGFRIELGE 927
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
9-406 |
5.75e-84 |
|
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: 262.96 E-value: 5.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLL 88
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 89 TVGEVRVQVTQPGltqlepslpvliiddgmldtpaaplpevagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINE 168
Cdd:cd17652 81 ADARPALLLTTPD---------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 169 RFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLceyhsgDRM 248
Cdd:cd17652 128 AFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL------PPD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 249 SYPTLRLALLSGDWIPLTLPeqmrERLNETMDIISLGGATECAIWSVYYpigEVESTWTSIPYGRGLRNQPVYVLNAQLE 328
Cdd:cd17652 202 DLPDLRTLVVAGEACPAELV----DRWAPGRRMINAYGPTETTVCATMA---GPLPGGGVPPIGRPVPGTRVYVLDARLR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 329 ECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE--ASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd17652 275 PVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPfgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGE 354
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
9-406 |
4.62e-83 |
|
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: 261.15 E-value: 4.62e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLL 88
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 89 TVGEVRVQVTQPGLTqlepslpvliiddgmldtpaaplpevagdvtdLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINE 168
Cdd:cd17649 81 EDSGAGLLLTHHPRQ--------------------------------LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 169 RFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEY--HSGD 246
Cdd:cd17649 129 RYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEadRTGD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 247 RmSYPTLRLALLSGDWIPltlPEQMRERLNETMDIISLGGATECAIWSVYYPI-GEVESTWTSIPYGRGLRNQPVYVLNA 325
Cdd:cd17649 209 G-RPPSLRLYIFGGEALS---PELLRRWLKAPVRLFNAYGPTEATVTPLVWKCeAGAARAGASMPIGRPLGGRSAYILDA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 326 QLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE--ASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIE 403
Cdd:cd17649 285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPfgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIE 364
|
...
gi 535686385 404 LGE 406
Cdd:cd17649 365 LGE 367
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
4-406 |
7.34e-83 |
|
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: 261.22 E-value: 7.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:cd17644 9 QVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQPgltqlepslpvliiddgmldtpaaplpevagdvTDLAYIIFTSGSTGTPKGVMIDHRAAMNTL 163
Cdd:cd17644 89 LTYILEDAQISVLLTQP---------------------------------ENLAYVIYTSGSTGKPKGVMIEHQSLVNLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 164 EDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVL-PEAGREKDPRHWQTVMAHgHVSVWNAVPALMQMLCEY 242
Cdd:cd17644 136 HGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLrPEEMRSSLEDFVQYIQQW-QLTVLSLPPAYWHLLVLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 243 HSGDRMSYP-TLRLALLSGDWIPLTLPEQMRERLNETMDIISLGGATECAI-WSVYYPIGEVESTWTSIPYGRGLRNQPV 320
Cdd:cd17644 215 LLLSTIDLPsSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIaATVCRLTQLTERNITSVPIGRPIANTQV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 321 YVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV---WREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKV 397
Cdd:cd17644 295 YILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIshpFNSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKI 374
|
....*....
gi 535686385 398 NGYRIELGE 406
Cdd:cd17644 375 RGFRIELGE 383
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
9-406 |
1.01e-82 |
|
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: 260.32 E-value: 1.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLL 88
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 89 TVGEVRVQVTQPgltqlepslpvliiddgmldtpaaplpevagdvTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINE 168
Cdd:cd17643 81 ADSGPSLLLTDP---------------------------------DDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 169 RFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVP----ALMQMLCEYHS 244
Cdd:cd17643 128 WFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPsafyQLVEAADRDGR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 245 GDrmsyPTLRLALLSGDWIPLTLPEQMRERLNETM-DIISLGGATECAIWSVYYPIGEVE-STWTSIPYGRGLRNQPVYV 322
Cdd:cd17643 208 DP----LALRYVIFGGEALEAAMLRPWAGRFGLDRpQLVNMYGITETTVHVTFRPLDAADlPAAAASPIGRPLPGLRVYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 323 LNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWREAS--GERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGY 400
Cdd:cd17643 284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgpGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
|
....*.
gi 535686385 401 RIELGE 406
Cdd:cd17643 364 RIELGE 369
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
9-406 |
7.60e-82 |
|
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: 257.78 E-value: 7.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLL 88
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 89 TVGEVRVQVTQPgltqlepslpvliiddgmldtpaaplpevagdvTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINE 168
Cdd:cd17650 81 EDSGAKLLLTQP---------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 169 RFGLNAQD-RVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDR 247
Cdd:cd17650 128 EYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 248 MSYPTLRLALLSGDWIPLTLPEQMRERLNETMDIISLGGATECAIWSVYYPIGEVE-STWTSIPYGRGLRNQPVYVLNAQ 326
Cdd:cd17650 208 LDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPlGDSANVPIGRPLPNTAMYVLDER 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 327 LEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV-WREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELG 405
Cdd:cd17650 288 LQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVeNPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELG 367
|
.
gi 535686385 406 E 406
Cdd:cd17650 368 E 368
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-406 |
4.94e-81 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 271.65 E-value: 4.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:PRK12467 3103 AQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVTQPGLTQ---LEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAA 159
Cdd:PRK12467 3183 RLAYMIEDSGVKLLLTQAHLLEqlpAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGAL 3262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 160 MNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLpEAGREKDP-RHWQTVMAHgHVSVWNAVPALMQM 238
Cdd:PRK12467 3263 ANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDPeELWQAIHAH-RISIACFPPAYLQQ 3340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 239 LCEYHsgDRMSYPTLRLALLSGDWIPLTLPEQMRERLnETMDIISLGGATECAIWSVYYPI-GEVESTWTSIPYGRGLRN 317
Cdd:PRK12467 3341 FAEDA--GGADCASLDIYVFGGEAVPPAAFEQVKRKL-KPRGLTNGYGPTEAVVTVTLWKCgGDAVCEAPYAPIGRPVAG 3417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 318 QPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWR--EASGERIYRTGDRGRYFADGQVAFLGRNDTQV 395
Cdd:PRK12467 3418 RSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADpfSGSGGRLYRTGDLARYRADGVIEYLGRIDHQV 3497
|
410
....*....|.
gi 535686385 396 KVNGYRIELGE 406
Cdd:PRK12467 3498 KIRGFRIELGE 3508
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-406 |
2.80e-80 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 269.72 E-value: 2.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:PRK12467 1582 DQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRE 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVTQPGLTQLEPS---LPVLIID--DGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:PRK12467 1662 RLAYMIEDSGIELLLTQSHLQARLPLpdgLRSLVLDqeDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHG 1741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 158 AAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQ 237
Cdd:PRK12467 1742 ALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQ 1821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 238 MLCEyHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVEST-WTSIPYGRGLR 316
Cdd:PRK12467 1822 QLLQ-MDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDT-GLFNLYGPTETAVDVTHWTCRRKDLEgRDSVPIGQPIA 1899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 317 NQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWR--EASGERIYRTGDRGRYFADGQVAFLGRNDTQ 394
Cdd:PRK12467 1900 NLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADpfGTVGSRLYRTGDLARYRADGVIEYLGRIDHQ 1979
|
410
....*....|..
gi 535686385 395 VKVNGYRIELGE 406
Cdd:PRK12467 1980 VKIRGFRIELGE 1991
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-406 |
6.06e-80 |
|
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: 253.19 E-value: 6.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:COG0318 5 LRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTqpgltqlepslpvliiddgmldtpaaplpevagdvtdlAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:COG0318 85 AEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTHRNLL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFGLNAQDRVFGLSSLSFDLSVYDA-FAPFMVGAALVLPeagREKDPRHWQTVMAHGHVSVWNAVPALMQML 239
Cdd:COG0318 127 ANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGlLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGVPTMLARL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 240 CEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNetMDIISLGGATECAIWSVYYPIGEVESTWTSIpyGRGLRNQP 319
Cdd:COG0318 204 LRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPGERRPGSV--GRPLPGVE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 320 VYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriYRTGDRGRYFADGQVAFLGRNDTQVKV 397
Cdd:COG0318 280 VRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRdgW--------LRTGDLGRLDEDGYLYIVGRKKDMIIS 351
|
....*....
gi 535686385 398 NGYRIELGE 406
Cdd:COG0318 352 GGENVYPAE 360
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1-406 |
1.37e-79 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 266.91 E-value: 1.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGLTQLEPSLPVLIIDD-GMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAA 159
Cdd:PRK10252 544 DDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCyNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 160 MNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQ-M 238
Cdd:PRK10252 624 VNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAaF 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 239 LCEYHS-GDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETMDiiSLGGATECAIWSVYYPIG---EVESTWTSIPYGRG 314
Cdd:PRK10252 704 VASLTPeGARQSCASLRQVFCSGEALPADLCREWQQLTGAPLH--NLYGPTEAAVDVSWYPAFgeeLAAVRGSSVPIGYP 781
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 315 LRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE-ASGERIYRTGDRGRYFADGQVAFLGRNDT 393
Cdd:PRK10252 782 VWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPfAPGERMYRTGDVARWLDDGAVEYLGRSDD 861
|
410
....*....|...
gi 535686385 394 QVKVNGYRIELGE 406
Cdd:PRK10252 862 QLKIRGQRIELGE 874
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-406 |
4.72e-78 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 263.36 E-value: 4.72e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:PRK12316 2012 QAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQPGLTQLEP---SLPVLIIDDG--MLDTPA-APLPEVAGDvtDLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:PRK12316 2092 LAYMLEDSGAALLLTQRHLLERLPlpaGVARLPLDRDaeWADYPDtAPAVQLAGE--NLAYVIYTSGSTGLPKGVAVSHG 2169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 158 AAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGhVSVWNAVPALMQ 237
Cdd:PRK12316 2170 ALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHG-VTILDFPPVYLQ 2248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 238 MLCEYHSGDRMSyPTLRLALLSGDWIPLTLPEQMRERLnETMDIISLGGATECAIWSVYYPIGEVE-STWTSIPYGRGLR 316
Cdd:PRK12316 2249 QLAEHAERDGRP-PAVRVYCFGGEAVPAASLRLAWEAL-RPVYLFNGYGPTEAVVTPLLWKCRPQDpCGAAYVPIGRALG 2326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 317 NQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWR--EASGERIYRTGDRGRYFADGQVAFLGRNDTQ 394
Cdd:PRK12316 2327 NRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDpfSASGERLYRTGDLARYRADGVVEYLGRIDHQ 2406
|
410
....*....|..
gi 535686385 395 VKVNGYRIELGE 406
Cdd:PRK12316 2407 VKIRGFRIELGE 2418
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
4-406 |
2.67e-77 |
|
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: 245.93 E-value: 2.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:cd17645 7 QVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQPGltqlepslpvliiddgmldtpaaplpevagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTL 163
Cdd:cd17645 87 IAYMLADSSAKILLTNPD---------------------------------DLAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 164 EDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAAL-VLPEAGR---EKDPRHWQTvmaHGHVSVWNAVPALMQ-M 238
Cdd:cd17645 134 EWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALhVVPSERRldlDALNDYFNQ---EGITISFLPTGAAEQfM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 239 LCEYHSgdrmsyptLRLALLSGDwipltlpeQMRERLNETMDIISLGGATECAIWSVYYPIGEVEStwtSIPYGRGLRNQ 318
Cdd:cd17645 211 QLDNQS--------LRVLLTGGD--------KLKKIERKGYKLVNNYGPTENTVVATSFEIDKPYA---NIPIGKPIDNT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 319 PVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWR-EASGERIYRTGDRGRYFADGQVAFLGRNDTQVKV 397
Cdd:cd17645 272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHpFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKI 351
|
....*....
gi 535686385 398 NGYRIELGE 406
Cdd:cd17645 352 RGYRIEPGE 360
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-406 |
3.86e-77 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 260.66 E-value: 3.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:PRK12316 4560 RARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRER 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQpglTQLEPSLPV------LIID-DGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDH 156
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQ---SHLLQRLPIpdglasLALDrDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSH 4716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 157 RAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHgHVSVWNAVPALM 236
Cdd:PRK12316 4717 GSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEH-RVTVLVFPPVYL 4795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 237 QMLCEyHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPI-GEVESTWTSIPYGRGL 315
Cdd:PRK12316 4796 QQLAE-HAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPV-YLFNGYGPTETTVTVLLWKArDGDACGAAYMPIGTPL 4873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 316 RNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWR--EASGERIYRTGDRGRYFADGQVAFLGRNDT 393
Cdd:PRK12316 4874 GNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfGAPGGRLYRTGDLARYRADGVIDYLGRVDH 4953
|
410
....*....|...
gi 535686385 394 QVKVNGYRIELGE 406
Cdd:PRK12316 4954 QVKIRGFRIELGE 4966
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
9-406 |
2.49e-70 |
|
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: 228.44 E-value: 2.49e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGD-RVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLL 87
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 88 LTVGEVRVQVTqpgltqlepslpvliiddgmldtpaaplpevagDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDIN 167
Cdd:cd17648 81 LEDTGARVVIT---------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 168 ERFGLNAQD--RVFGLSSLSFDLSVYDAFAPFMVGAAL-VLPEAGREKDPRHWQTVMAHGhVSVWNAVPALMQMLceyhs 244
Cdd:cd17648 128 ERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLvVPPDEMRFDPDRFYAYINREK-VTYLSGTPSVLQQY----- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 245 gDRMSYPTLRLALLSGDwiPLTLP--EQMRERLNETmdIISLGGATECAIWSVYYPIGEVESTWTSIpyGRGLRNQPVYV 322
Cdd:cd17648 202 -DLARLPHLKRVDAAGE--EFTAPvfEKLRSRFAGL--IINAYGPTETTVTNHKRFFPGDQRFDKSL--GRPVRNTKCYV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 323 LNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV---------WREASGERIYRTGDRGRYFADGQVAFLGRNDT 393
Cdd:cd17648 275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLpnpfqteqeRARGRNARLYKTGDLVRWLPSGELEYLGRNDF 354
|
410
....*....|...
gi 535686385 394 QVKVNGYRIELGE 406
Cdd:cd17648 355 QVKIRGQRIEPGE 367
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-406 |
3.83e-66 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 228.69 E-value: 3.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:PRK12316 3066 QVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEER 3145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQPGLTQLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTL 163
Cdd:PRK12316 3146 LAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHL 3225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 164 EDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEyh 243
Cdd:PRK12316 3226 CWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLE-- 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 244 SGDRMSYPTLRLALLSGDwiplTLPEQMRERLNETMDIISLGGATECAIWSVYYPIgeVESTWTSIPYGRGLRNQPVYVL 323
Cdd:PRK12316 3304 EEDAHRCTSLKRIVCGGE----ALPADLQQQVFAGLPLYNLYGPTEATITVTHWQC--VEEGKDAVPIGRPIANRACYIL 3377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 324 NAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE-ASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:PRK12316 3378 DGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPfVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRI 3457
|
....
gi 535686385 403 ELGE 406
Cdd:PRK12316 3458 ELGE 3461
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-406 |
7.43e-66 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 227.74 E-value: 7.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYP 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGLTQLEPSLP---VLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:PRK05691 1217 AERLAYMLADSGVELLLTQSHLLERLPQAEgvsAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHA 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 158 AAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDP-RHWQTVMAHGhVSVWNAVPALM 236
Cdd:PRK05691 1297 ALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPqRIAELVQQYG-VTTLHFVPPLL 1375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 237 QMLCEyhSGDRMSYPTLRLALLSGDwiplTLPEQMRERLNETMDIISLG---GATECAIwSVYYPIGEVESTWTSiPYGR 313
Cdd:PRK05691 1376 QLFID--EPLAAACTSLRRLFSGGE----ALPAELRNRVLQRLPQVQLHnryGPTETAI-NVTHWQCQAEDGERS-PIGR 1447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 314 GLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWREAS--GERIYRTGDRGRYFADGQVAFLGRN 391
Cdd:PRK05691 1448 PLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGedGARLYRTGDRARWNADGALEYLGRL 1527
|
410
....*....|....*
gi 535686385 392 DTQVKVNGYRIELGE 406
Cdd:PRK05691 1528 DQQVKLRGFRVEPEE 1542
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
8-406 |
7.13e-63 |
|
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: 209.64 E-value: 7.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 8 TPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLL 87
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 88 LTVGEVRVQVTQPGLT-QLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDI 166
Cdd:cd17656 81 MLDSGVRVVLTQRHLKsKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 167 NERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAAL-VLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSG 245
Cdd:cd17656 161 REKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 246 DRmsYPT-LRLALLSGDWIPLTLPeqMRERLNE-TMDIISLGGATECAIWSVYYPIGEVEstWTSI-PYGRGLRNQPVYV 322
Cdd:cd17656 241 NR--FPTcVKHIITAGEQLVITNE--FKEMLHEhNVHLHNHYGPSETHVVTTYTINPEAE--IPELpPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 323 LNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE-ASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYR 401
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPfDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
....*
gi 535686385 402 IELGE 406
Cdd:cd17656 395 IELGE 399
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-406 |
2.23e-58 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 206.17 E-value: 2.23e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:PRK05691 3729 QVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQR 3808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQV-----TQPGLTQLE-------PSLpvLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKG 151
Cdd:PRK05691 3809 LQRIIELSRTPVLVcsaacREQARALLDelgcanrPRL--LVWEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKG 3886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 152 VMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPrhwQTVMAHGH---VSV 228
Cdd:PRK05691 3887 VMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDP---QGLLAHVQaqgITV 3963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 229 WNAVPALMQ-MLCEyhsgDRMSYPTLRLALLSGDWIPLTLPEQMRERLNEtMDIISLGGATECAIWSVYYPIGEVESTWT 307
Cdd:PRK05691 3964 LESVPSLIQgMLAE----DRQALDGLRWMLPTGEAMPPELARQWLQRYPQ-IGLVNAYGPAECSDDVAFFRVDLASTRGS 4038
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 308 SIPYGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWRE--ASGERIYRTGDRGRYFADGQV 385
Cdd:PRK05691 4039 YLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPfgAPGERLYRTGDLARRRSDGVL 4118
|
410 420
....*....|....*....|.
gi 535686385 386 AFLGRNDTQVKVNGYRIELGE 406
Cdd:PRK05691 4119 EYVGRIDHQVKIRGYRIELGE 4139
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
5-406 |
2.15e-51 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 179.57 E-value: 2.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRR 84
Cdd:TIGR01734 10 AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 85 QLLLTVGEVRVQVTQPGLTQLEPSLPVLIIDDGM-LDTPAAPL---PEVAGDvtDLAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:TIGR01734 90 EMIIEAAGPELVIHTAELSIDAVGTQIITLSALEqAETSGGPVsfdHAVKGD--DNYYIIYTSGSTGNPKGVQISHDNLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQM-- 238
Cdd:TIGR01734 168 SFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVDMcl 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 239 LCEYHSGDRmsYPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATEC--AIWSVYYpIGEVESTWTSIPYGRGLR 316
Cdd:TIGR01734 248 LDPNFNQEN--YPHLTHFLFCGEELPVKTAKALLERFPKA-TIYNTYGPTEAtvAVTSVKI-TQEILDQYPRLPIGFAKP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 317 NQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVwrEASGERIYRTGDRGrYFADGQVAFLGRNDTQVK 396
Cdd:TIGR01734 324 DMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF--SHEGQPAYRTGDAG-TITDGQLFYQGRLDFQIK 400
|
410
....*....|
gi 535686385 397 VNGYRIELGE 406
Cdd:TIGR01734 401 LHGYRIELED 410
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-406 |
5.15e-51 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 184.60 E-value: 5.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR 83
Cdd:PRK05691 2197 QAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLER 2276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQPGLTQLEPSLPVLII-----DDGML--DTPAAPLPEVAGDvTDLAYIIFTSGSTGTPKGVMIDH 156
Cdd:PRK05691 2277 LHYMIEDSGIGLLLSDRALFEALGELPAGVArwcleDDAAAlaAYSDAPLPFLSLP-QHQAYLIYTSGSTGKPKGVVVSH 2355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 157 -RAAMNTLEDInERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGhVSVWNAVPAL 235
Cdd:PRK05691 2356 gEIAMHCQAVI-ERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQ-VSILGFTPSY 2433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 236 MQMLCEYHSGDRMSYPtLRLALLSGDWIPLTLPEQMRERLNETMdIISLGGATECAIWSVYYPIGE-VESTWTSIPYGRG 314
Cdd:PRK05691 2434 GSQLAQWLAGQGEQLP-VRMCITGGEALTGEHLQRIRQAFAPQL-FFNAYGPTETVVMPLACLAPEqLEEGAASVPIGRV 2511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 315 LRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWR--EASGERIYRTGDRGRYFADGQVAFLGRND 392
Cdd:PRK05691 2512 VGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADpfAADGGRLYRTGDLVRLRADGLVEYVGRID 2591
|
410
....*....|....
gi 535686385 393 TQVKVNGYRIELGE 406
Cdd:PRK05691 2592 HQVKIRGFRIELGE 2605
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
16-406 |
5.44e-50 |
|
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: 176.17 E-value: 5.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 16 SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRv 95
Cdd:cd17647 16 SKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 96 qvtqpGLtqlepslpVLIIDDGMLDTPAApLPEVAgdvtdlayiiFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQ 175
Cdd:cd17647 95 -----GL--------IVIRAAGVVVGPDS-NPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 176 DRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCeyhSGDRMSYPTLRL 255
Cdd:cd17647 151 DKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLT---AQATTPFPKLHH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 256 ALLSGDWipLTLPEQMR-ERLNETMDIISLGGATECAIWSVYYPI-------GEVESTWTSIPYGRGLRNQPVYVLNA-- 325
Cdd:cd17647 228 AFFVGDI--LTKRDCLRlQTLAENVRIVNMYGTTETQRAVSYFEVpsrssdpTFLKNLKDVMPAGRGMLNVQLLVVNRnd 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 326 QLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--------------------WREAS---GERIYRTGDRGRYFAD 382
Cdd:cd17647 306 RTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvepdhwnyldkdnnepWRQFWlgpRDRLYRTGDLGRYLPN 385
|
410 420
....*....|....*....|....
gi 535686385 383 GQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd17647 386 GDCECCGRADDQVKIRGFRIELGE 409
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
8-406 |
7.96e-49 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 172.77 E-value: 7.96e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 8 TPQETALISPIRELTYRQLSTAADHVARALLALGVqhgDRVAVVMEKGWQQ---IAAVHGILRLGAVYLPVDPVLPPQRR 84
Cdd:PRK04813 15 QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKL---PDKSPIIVFGHMSpemLATFLGAVKAGHAYIPVDVSSPAERI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 85 QLLLTVGEVRVQVTQPGLTQLEPSLPVLIIDD----GMLDTPAAPLPEVAGDvtDLAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:PRK04813 92 EMIIEVAKPSLIIATEELPLEILGIPVITLDElkdiFATGNPYDFDHAVKGD--DNYYIIFTSGTTGKPKGVQISHDNLV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQM-- 238
Cdd:PRK04813 170 SFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVWVSTPSFADMcl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 239 ----LCEYHsgdrmsYPTLRLALLSGDWIPLTLPEQMRERLNETMdIISLGGATEC--AIWSVyyPI-GEVESTWTSIPY 311
Cdd:PRK04813 250 ldpsFNEEH------LPNLTHFLFCGEELPHKTAKKLLERFPSAT-IYNTYGPTEAtvAVTSI--EItDEMLDQYKRLPI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 312 GRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVwrEASGERIYRTGDRGrYFADGQVAFLGRN 391
Cdd:PRK04813 321 GYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF--TFDGQPAYHTGDAG-YLEDGLLFYQGRI 397
|
410
....*....|....*
gi 535686385 392 DTQVKVNGYRIELGE 406
Cdd:PRK04813 398 DFQIKLNGYRIELEE 412
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
8-406 |
8.14e-49 |
|
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: 177.95 E-value: 8.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 8 TPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLL 87
Cdd:TIGR03443 258 TPSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 88 LTVGEVRVQVTQPGLTQLEPS--------------LPVL-IIDDGML----------DTpAAPLPEVAGDVTDL------ 136
Cdd:TIGR03443 338 LSVAKPRALIVIEKAGTLDQLvrdyidkelelrteIPALaLQDDGSLvggsleggetDV-LAPYQALKDTPTGVvvgpds 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 137 -AYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPR 215
Cdd:TIGR03443 417 nPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPG 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 216 HWQTVMAHGHVSVWNAVPALMQMLCeyhSGDRMSYPTLRLALLSGDWipLTLPEQMR-ERLNETMDIISLGGATECAIWS 294
Cdd:TIGR03443 497 RLAEWMAKYGATVTHLTPAMGQLLS---AQATTPIPSLHHAFFVGDI--LTKRDCLRlQTLAENVCIVNMYGTTETQRAV 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 295 VYYPIGEVESTWT-------SIPYGRGLRNQPVYVLN----AQLeeCPVGVEGEICIGGMGLAQGYLNDAEKTAASFV-- 361
Cdd:TIGR03443 572 SYFEIPSRSSDSTflknlkdVMPAGKGMKNVQLLVVNrndrTQT--CGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnn 649
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535686385 362 ------------------WRE---ASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:TIGR03443 650 wfvdpshwidldkennkpEREfwlGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGE 715
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
28-406 |
3.67e-47 |
|
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: 167.23 E-value: 3.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 28 TAADHVARALLALGVQHGDRVAVVMEKG----WQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTQPGL- 102
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRftyiELSFAVAYAGGRLGLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 103 TQLEPSLPVLIIDDGMLDTPA-------APLPEVAGDvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQ 175
Cdd:cd05922 81 DRLRDALPASPDPGTVLDADGiraarasAPAHEVSHE--DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 176 DRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGReKDPRHWQTVMAHGhVSVWNAVPALMQMLCEYhSGDRMSYPTLRL 255
Cdd:cd05922 159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGV-LDDAFWEDLREHG-ATGLAGVPSTYAMLTRL-GFDPAKLPSLRY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 256 ALLSGDwiplTLPEQMRERLNETM---DIISLGGATECAIWSVYYPIGEVESTWTSIpyGRGLRNQPVYVLNAQLEECPV 332
Cdd:cd05922 236 LTQAGG----RLPQETIARLRELLpgaQVYVMYGQTEATRRMTYLPPERILEKPGSI--GLAIPGGEFEILDDDGTPTPP 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535686385 333 GVEGEICIGGMGLAQGYLNDAEKTAAsfvwrEASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd05922 310 GEPGEIVHRGPNVMKGYWNDPPYRRK-----EGRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTE 378
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1-402 |
5.63e-47 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 168.75 E-value: 5.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALIS-----PIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV 75
Cdd:COG0365 15 LDRHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 76 DPVLPPQ---------RRQLLLTVGE-VRVQVTQPGLTQLE------PSLPVLIIDDGM---------------LDTPAA 124
Cdd:COG0365 95 FPGFGAEaladriedaEAKVLITADGgLRGGKVIDLKEKVDealeelPSLEHVIVVGRTgadvpmegdldwdelLAAASA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 125 PLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHR----AAMNTLEDInerFGLNAQDRVFGLSSLSF--DLSvYDAFAPFM 198
Cdd:COG0365 175 EFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGgylvHAATTAKYV---LDLKPGDVFWCTADIGWatGHS-YIVYGPLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 199 VGAALVL-------PEAGrekdpRHWQTVMAHGhVSVWNAVPALMQMLCEYHSGDRMSY--PTLRLALLSGDwiPLTlPE 269
Cdd:COG0365 251 NGATVVLyegrpdfPDPG-----RLWELIEKYG-VTVFFTAPTAIRALMKAGDEPLKKYdlSSLRLLGSAGE--PLN-PE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 270 ---QMRERLNetMDIISLGGATE-CAIWSVYYPIGEVESTWTSIPyGRGLRnqpVYVLNAQLEECPVGVEGEICIGG--M 343
Cdd:COG0365 322 vweWWYEAVG--VPIVDGWGQTEtGGIFISNLPGLPVKPGSMGKP-VPGYD---VAVVDEDGNPVPPGEEGELVIKGpwP 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 535686385 344 GLAQGYLNDAEKTAASFvWREASGerIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:COG0365 396 GMFRGYWNDPERYRETY-FGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRI 451
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
135-406 |
1.43e-46 |
|
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: 162.84 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGrekDP 214
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 215 RHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNetMDIISLGGATECAIWS 294
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 295 VYYPIGEVESTWTSIpyGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreasGERIYRTG 374
Cdd:cd04433 156 ATGPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD------EDGWYRTG 227
|
250 260 270
....*....|....*....|....*....|..
gi 535686385 375 DRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAE 259
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-400 |
1.72e-46 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 166.62 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK07656 11 LARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGL----TQLEPSLPVL----IIDDGMLD----------------TPAAPLPEVAGDvtDL 136
Cdd:PRK07656 91 ADEAAYILARGDAKALFVLGLFlgvdYSATTRLPALehvvICETEEDDphtekmktftdflaagDPAERAPEVDPD--DV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 137 AYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfgLSSLSFdlsvYDAF-------APFMVGAAlVLPEAg 209
Cdd:PRK07656 169 ADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRY--LAANPF----FHVFgykagvnAPLMRGAT-ILPLP- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 210 rEKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNetMDIISLG-GAT 288
Cdd:PRK07656 241 -VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELG--VDIVLTGyGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 289 ECAIWSVYYPIGEVESTW-TSIpyGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSG 367
Cdd:PRK07656 318 EASGVTTFNRLDDDRKTVaGTI--GTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI-----DA 390
|
410 420 430
....*....|....*....|....*....|...
gi 535686385 368 ERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGY 400
Cdd:PRK07656 391 DGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGF 423
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1-383 |
2.24e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 161.12 E-value: 2.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK06187 12 LRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQrrQLLLTVG--EVRVQVTQPG----LTQLEPSLP----VLIIDDGMLDTPAA----------------PLPEVagDVT 134
Cdd:PRK06187 92 PE--EIAYILNdaEDRVVLVDSEfvplLAAILPQLPtvrtVIVEGDGPAAPLAPevgeyeellaaasdtfDFPDI--DEN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHR-AAMNTLEdINERFGLNAQDRvfGLSSL----SFDLSVydAFAPFMVGAALVLPeag 209
Cdd:PRK06187 168 DAAAMLYTSGTTGHPKGVVLSHRnLFLHSLA-VCAWLKLSRDDV--YLVIVpmfhVHAWGL--PYLALMAGAKQVIP--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 210 REKDPRH-WQTVMAHGhVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNetMDIISLGGAT 288
Cdd:PRK06187 240 RRFDPENlLDLIETER-VTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFG--IDLVQGYGMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 289 ECA-IWSVYYPIGEVESTWTsIPY--GRGLRNQPVYVLNAQLEECPVGVE--GEICIGGMGLAQGYLNDAEKTAASFV-- 361
Cdd:PRK06187 317 ETSpVVSVLPPEDQLPGQWT-KRRsaGRPLPGVEARIVDDDGDELPPDGGevGEIIVRGPWLMQGYWNRPEATAETIDgg 395
|
410 420
....*....|....*....|..
gi 535686385 362 WreasgeriYRTGDRGRYFADG 383
Cdd:PRK06187 396 W--------LHTGDVGYIDEDG 409
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1-383 |
1.15e-42 |
|
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: 155.41 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGLTQLepslpvliiddgmLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDL-------------LAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFG--LNAQDRVFGLsslsfdLSVYDAFA-------PFMVGAALVLpeagrEKDPRHWQTV--MAHGHVSVW 229
Cdd:cd05936 152 ANALQIKAWLEdlLEGDDVVLAA------LPLFHVFGltvalllPLALGATIVL-----IPRFRPIGVLkeIRKHRVTIF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 230 NAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERlneTMDIISLG-GATECA-------IWSVYYP--I 299
Cdd:cd05936 221 PGVPTMYIALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEEL---TGVPIVEGyGLTETSpvvavnpLDGPRKPgsI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 300 GevestwtsIPygrgLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriYRTGDRG 377
Cdd:cd05936 298 G--------IP----LPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVdgW--------LRTGDIG 357
|
....*.
gi 535686385 378 RYFADG 383
Cdd:cd05936 358 YMDEDG 363
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1-390 |
2.28e-42 |
|
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: 153.92 E-value: 2.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVdpvlp 80
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRrqllLTVGEVRVqvtqpgltQLEPSLPVLIIDdgmldtpaaplpevagdvtDLAYIIFTSGSTGTPKGVMIDHR--- 157
Cdd:cd17631 76 NFR----LTPPEVAY--------ILADSGAKVLFD-------------------DLALLMYTSGTTGRPKGAMLTHRnll 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 158 -AAMNTLEDinerFGLNAQDRVFGLSSLS--FDLSVYdAFAPFMVGAALVLPeagREKDPRH-WQTVMAHGHVSVWnAVP 233
Cdd:cd17631 125 wNAVNALAA----LDLGPDDVLLVVAPLFhiGGLGVF-TLPTLLRGGTVVIL---RKFDPETvLDLIERHRVTSFF-LVP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 234 ALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERlneTMDIISLGGATECAIWSVYYPIGEVESTWTSIpyGR 313
Cdd:cd17631 196 TMIQALLQHPRFATTDLSSLRAVIYGGAPMPERLLRALQAR---GVKFVQGYGMTETSPGVTFLSPEDHRRKLGSA--GR 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535686385 314 GLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriYRTGDRGRYFADGQVAFLGR 390
Cdd:cd17631 271 PVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRdgW--------FHTGDLGRLDEDGYLYIVDR 341
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
21-402 |
3.67e-39 |
|
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: 145.17 E-value: 3.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTqp 100
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 101 gltqlepslpvliiddgmldtpaaplpevagDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFG 180
Cdd:cd05972 79 -------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 181 LSSLSFDLSVYDAF-APFMVGAALVLPEaGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEY--HSGDRmsyPTLRLAL 257
Cdd:cd05972 128 IADPGWAKGAWSSFfGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIKQdlSSYKF---SHLRLVV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 258 LSGDwiPLTlPEQMRERLNET-MDIISLGGATECAIWSVYYPIGEVE--STWTSIPygrGLRnqpVYVLNAQLEECPVGV 334
Cdd:cd05972 204 SAGE--PLN-PEVIEWWRAATgLPIRDGYGQTETGLTVGNFPDMPVKpgSMGRPTP---GYD---VAIIDDDGRELPPGE 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 335 EGEICI--GGMGLAQGYLNDAEKTAASFVwreasgERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05972 275 EGDIAIklPPPGLFLGYVGDPEKTEASIR------GDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRI 338
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
19-402 |
1.80e-38 |
|
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: 144.28 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVT 98
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 QPGL---------------------TQLEPSLPVLIIDDGMLDTPAAPLPEVAGD-VTDLAYIIFTSGSTGTPKGVMIDH 156
Cdd:cd05911 89 DPDGlekvkeaakelgpkdkiivldDKPDGVLSIEDLLSPTLGEEDEDLPPPLKDgKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 157 RAAMNTLEDINERFGLNAQDRVFGLSSLSFdlsvYDAFAPFMVGAALVLpeaG------REKDPRHW-QTVMAHgHVSVW 229
Cdd:cd05911 169 RNLIANLSQVQTFLYGNDGSNDVILGFLPL----YHIYGLFTTLASLLN---GatviimPKFDSELFlDLIEKY-KITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 230 NAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVESTwtSI 309
Cdd:cd05911 241 YLVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNA-TIKQGYGMTETGGILTVNPDGDDKPG--SV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 310 pyGRGLRNQPVYVLNAQL-EECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV---WreasgeriYRTGDRGRYFADGQV 385
Cdd:cd05911 318 --GRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDedgW--------LHTGDIGYFDEDGYL 387
|
410
....*....|....*..
gi 535686385 386 AFLGRNDTQVKVNGYRI 402
Cdd:cd05911 388 YIVDRKKELIKYKGFQV 404
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
21-406 |
3.99e-38 |
|
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: 143.00 E-value: 3.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTQP 100
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 101 GLTQLEPSLPVLIIDDGMldtpaaPLPEvagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFG 180
Cdd:cd17654 97 ELDNAPLSFTPEHRHFNI------RTDE------CLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSEDILFL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 181 LSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGH-VSVWNAVPALMQMLCEYHSGDR-MSYPT-LRLAL 257
Cdd:cd17654 165 TSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHrITVLQATPTLFRRFGSQSIKSTvLSATSsLRVLA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 258 LSGDWIP-LTLPEQMRERLNETmDIISLGGATECAIWSVYYPIGEVESTwtsIPYGRGLRNQPVYVlnaqLEECPVGVEG 336
Cdd:cd17654 245 LGGEPFPsLVILSSWRGKGNRT-RIFNIYGITEVSCWALAYKVPEEDSP---VQLGSPLLGTVIEV----RDQNGSEGTG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 337 EICIGgmGLAQGYLNDAEKTAASFVWReASGERIYRTgdrgryfaDGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd17654 317 QVFLG--GLNRVCILDDEVTVPKGTMR-ATGDFVTVK--------DGELFFLGRKDSQIKRRGKRINLDL 375
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1-391 |
4.44e-38 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 144.43 E-value: 4.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISP------IRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLP 74
Cdd:PRK13295 30 LDACVASCPDKTAVTAVrlgtgaPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 75 VDPVLPPQRRQLLLTVGEVRVQVT---------QPGLTQLEPSLP----VLIID-------DGMLDTPA--------APL 126
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVpktfrgfdhAAMARRLRPELPalrhVVVVGgdgadsfEALLITPAweqepdapAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 127 PEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLS-VYDAFAPFMVGAALVL 205
Cdd:PRK13295 190 ARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVMLGATAVL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 206 PEAGrekDP-RHWQTVMAHGHVSVWNAVPALMQmLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETmdIISL 284
Cdd:PRK13295 270 QDIW---DPaRAAELIRTEGVTFTMASTPFLTD-LTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAK--IVSA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 285 GGATECAIWSVYYPIGEVESTWTSipYGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwre 364
Cdd:PRK13295 344 WGMTENGAVTLTKLDDPDERASTT--DGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA---- 417
|
410 420
....*....|....*....|....*..
gi 535686385 365 asgERIYRTGDRGRYFADGQVAFLGRN 391
Cdd:PRK13295 418 ---DGWFDTGDLARIDADGYIRISGRS 441
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1-399 |
2.51e-36 |
|
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: 138.66 E-value: 2.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:cd05959 10 DLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRV--------QVTQPGLTQLEPSLPVLIIDDGMLDTPAAP-----LPEVAGDVT-------DLAYII 140
Cdd:cd05959 90 PDDYAYYLEDSRARVvvvsgelaPVLAAALTKSEHTLVVLIVSGGAGPEAGALllaelVAAEAEQLKpaathadDPAFWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 141 FTSGSTGTPKGVMIDHRAAMNTLEDINER-FGLNAQDRVFGLSSLSFDLSVYDA-FAPFMVGAALVLpEAGREKDPRHWQ 218
Cdd:cd05959 170 YSSGSTGRPKGVVHLHADIYWTAELYARNvLGIREDDVCFSAAKLFFAYGLGNSlTFPLSVGATTVL-MPERPTPAAVFK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 219 TVMAHgHVSVWNAVPALM-QMLCEYHSGDRmSYPTLRLALLSGDWIPLTLPEQMRERLNetMDIISLGGATECA-IWSVY 296
Cdd:cd05959 249 RIRRY-RPTVFFGVPTLYaAMLAAPNLPSR-DLSSLRLCVSAGEALPAEVGERWKARFG--LDILDGIGSTEMLhIFLSN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 297 YPiGEVESTWTSIP---YGRGLRNQpvyvlnaQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriY 371
Cdd:cd05959 325 RP-GRVRYGTTGKPvpgYEVELRDE-------DGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQgeW--------T 388
|
410 420
....*....|....*....|....*...
gi 535686385 372 RTGDRGRYFADGQVAFLGRNDTQVKVNG 399
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSG 416
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
21-406 |
1.07e-35 |
|
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: 135.97 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTQP 100
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 101 GLTQLEPslpvliiddgmldtpaAPLPEvagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFG 180
Cdd:cd05903 82 RFRQFDP----------------AAMPD------AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 181 LSSLS-FDLSVYDAFAPFMVGAALVLPEAGrekDPRHWQTVMAHGHVSVWNAVPALMQMLC--EYHSGDRMsyPTLRLAL 257
Cdd:cd05903 140 ASPMAhQTGFVYGFTLPLLLGAPVVLQDIW---DPDKALALMREHGVTFMMGATPFLTDLLnaVEEAGEPL--SRLRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 258 LSGDWIPLTLPEQMRERLnETMdIISLGGATECAIWSVYYPIGEVESTWTSipYGRGLRNQPVYVLNAQLEECPVGVEGE 337
Cdd:cd05903 215 CGGATVPRSLARRAAELL-GAK-VCSAYGSTECPGAVTSITPAPEDRRLYT--DGRPLPGVEIKVVDDTGATLAPGVEGE 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535686385 338 ICIGGMGLAQGYLNDAEKTAasfvwrEASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd05903 291 LLSRGPSVFLGYLDRPDLTA------DAAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLE 353
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
13-390 |
3.60e-34 |
|
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: 132.44 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 13 ALISPIR--ELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTV 90
Cdd:cd05926 5 ALVVPGStpALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 91 GEVRVQVTQPG-------------LTQLEPSLPVLIIDD--------GMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTP 149
Cdd:cd05926 85 LGSKLVLTPKGelgpasraasklgLAILELALDVGVLIRapsaeslsNLLADKKNAKSEGVPLPDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 150 KGVMIDHRAAMNTLEDINERFGLNAQDRVF---------GLsslsfdlsVYDAFAPFMVGAALVLPEAGREKdpRHWQTV 220
Cdd:cd05926 165 KGVPLTHRNLAASATNITNTYKLTPDDRTLvvmplfhvhGL--------VASLLSTLAAGGSVVLPPRFSAS--TFWPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 221 MAHgHVSVWNAVPALMQMLCEYHSGDRMS-YPTLRLALLSGDWIPLTLPEQMRERLN----ETMdiislgGATECAIWSV 295
Cdd:cd05926 235 RDY-NATWYTAVPTIHQILLNRPEPNPESpPPKLRFIRSCSASLPPAVLEALEATFGapvlEAY------GMTEAAHQMT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 296 YYPIGEVESTWTSIPYGRGLRnqpVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSGERIYRTGD 375
Cdd:cd05926 308 SNPLPPGPRKPGSVGKPVGVE---VRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA-----FKDGWFRTGD 379
|
410
....*....|....*
gi 535686385 376 RGRYFADGQVAFLGR 390
Cdd:cd05926 380 LGYLDADGYLFLTGR 394
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
19-399 |
8.18e-33 |
|
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: 127.79 E-value: 8.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLppqRRQLLLTVgevrVQVT 98
Cdd:cd05934 2 RRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTAL---RGDELAYI----IDHS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 QPGLTqlepslpvliiddgmldtpaaplpevagdVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRV 178
Cdd:cd05934 75 GAQLV-----------------------------VVDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 179 fgLSSLSF---DLSVYDAFAPFMVGAALVLPEagREKDPRHWQTVMAHGhVSVWNAVPALMQMLCEYHSGDRMSYPTLRL 255
Cdd:cd05934 126 --LTVLPLfhiNAQAVSVLAALSVGATLVLLP--RFSASRFWSDVRRYG-ATVTNYLGAMLSYLLAQPPSPDDRAHRLRA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 256 ALLSGdwIPLTLPEQMRERLNetMDIISLGGATE--CAIWS-VYYPIGevestWTSIpyGRGLRNQPVYVLNAQLEECPV 332
Cdd:cd05934 201 AYGAP--NPPELHEEFEERFG--VRLLEGYGMTEtiVGVIGpRDEPRR-----PGSI--GRPAPGYEVRIVDDDGQELPA 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 333 GVEGEICI---GGMGLAQGYLNDAEKTAAsfVWREAsgerIYRTGDRGRYFADGQVAFLGRNDTQVKVNG 399
Cdd:cd05934 270 GEPGELVIrglRGWGFFKGYYNMPEATAE--AMRNG----WFHTGDLGYRDADGFFYFVDRKKDMIRRRG 333
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1-390 |
1.25e-32 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 128.86 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISP----------IRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGA 70
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPggrgadgklaYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 71 VYLPVDPVLppQRRQLLLTVGEVRVQ--VTQPgLTQL--------EPSLPVLI------------IDDGMLDTPAAPLPE 128
Cdd:PRK09274 92 VPVLVDPGM--GIKNLKQCLAEAQPDafIGIP-KAHLarrlfgwgKPSVRRLVtvggrllwggttLATLLRDGAAAPFPM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 129 VAGDVTDLAYIIFTSGSTGTPKGVMIDHR--AAMntLEDINERFGLNAQDRvfglsslsfDLSVYDAFAPF--MVGAALV 204
Cdd:PRK09274 169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGmfEAQ--IEALREDYGIEPGEI---------DLPTFPLFALFgpALGMTSV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 205 LPEAGREK----DPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETMD 280
Cdd:PRK09274 238 IPDMDPTRpatvDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLPSLRRVISAGAPVPIAVIERFRAMLPPDAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 281 IISLGGATECaiwsvyYPIGEVES------TWTSIPYGRG----------------LRNQPVYVLNAQLeECPVGVEGEI 338
Cdd:PRK09274 318 ILTPYGATEA------LPISSIESreilfaTRAATDNGAGicvgrpvdgvevriiaISDAPIPEWDDAL-RLATGEIGEI 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 535686385 339 CIGGMGLAQGYLNDAEKTAASFVWREASGERiYRTGDRGRYFADGQVAFLGR 390
Cdd:PRK09274 391 VVAGPMVTRSYYNRPEATRLAKIPDGQGDVW-HRMGDLGYLDAQGRLWFCGR 441
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
11-399 |
1.60e-32 |
|
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: 127.19 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 11 ETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTV 90
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 91 GEVRVqvtqpgltqlepslpvLIIDDgmldtpaaplpevagdvTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDI-NER 169
Cdd:cd05919 81 CEARL----------------VVTSA-----------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMaREA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 170 FGLNAQDRVFGLSSLSFDLSVYDA-FAPFMVGAALVLPEAGREKDpRHWQTVMAHGHvSVWNAVPALMQMLCEYHSGDRM 248
Cdd:cd05919 128 LGLTPGDRVFSSAKMFFGYGLGNSlWFPLAVGASAVLNPGWPTAE-RVLATLARFRP-TVLYGVPTFYANLLDSCAGSPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 249 SYPTLRLALLSGDwiplTLPEQMRERLNET--MDIISLGGATECAIWSVYYPIGEVESTWTsipyGRGLRNQPVYVLNAQ 326
Cdd:cd05919 206 ALRSLRLCVSAGE----ALPRGLGERWMEHfgGPILDGIGATEVGHIFLSNRPGAWRLGST----GRPVPGYEIRLVDEE 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535686385 327 LEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriYRTGDRGRYFADGQVAFLGRNDTQVKVNG 399
Cdd:cd05919 278 GHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNggW--------YRTGDKFCRDADGWYTHAGRADDMLKVGG 344
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
9-402 |
1.08e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 126.23 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALL-ALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPV--------- 78
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMnreeelahy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 79 --------------LPPQRRQLLLTVGEVRVQVTQ-------------PGLTQLEPSLPVLIIDDGM-----LDTPAAPL 126
Cdd:PRK08314 104 vtdsgarvaivgseLAPKVAPAVGNLRLRHVIVAQysdylpaepeiavPAWLRAEPPLQALAPGGVVawkeaLAAGLAPP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 127 PEVAGdVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfgLSSLS-FDLS--VYDAFAPFMVGAAL 203
Cdd:PRK08314 184 PHTAG-PDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVV--LAVLPlFHVTgmVHSMNAPIYAGATV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 204 VL-PEAGREKDPRhwqtVMAHGHVSVWNAVPALMQmlceyhsgDRMSYPTLR------LALLSGDWIPltLPEQMRERLN 276
Cdd:PRK08314 261 VLmPRWDREAAAR----LIERYRVTHWTNIPTMVV--------DFLASPGLAerdlssLRYIGGGGAA--MPEAVAERLK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 277 ETMDIISLGGatecaiwsvyYPIGEVESTWTSIPYGRGlRNQ----PVYVLNAQ------LEECPVGVEGEICIGGMGLA 346
Cdd:PRK08314 327 ELTGLDYVEG----------YGLTETMAQTHSNPPDRP-KLQclgiPTFGVDARvidpetLEELPPGEVGEIVVHGPQVF 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 535686385 347 QGYLNDAEKTAASFVwrEASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:PRK08314 396 KGYWNRPEATAEAFI--EIDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKV 449
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
3-390 |
1.67e-31 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 125.81 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALI------SPIRELTYRQLSTAADHVARALLALGvQHGDRVAVVMEKGWQQIAAVHGILRLGAVylPVd 76
Cdd:cd05931 1 RRAAARPDRPAYTflddegGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAI--AV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 77 PVLPPQRRQ---------------LLLTVGEVRVQVTQPGLTQLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIF 141
Cdd:cd05931 77 PLPPPTPGRhaerlaailadagprVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 142 TSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRV---------FGLsslsfdlsVYDAFAPFMVGAALVL--PEAgR 210
Cdd:cd05931 157 TSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVvswlplyhdMGL--------IGGLLTPLYSGGPSVLmsPAA-F 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 211 EKDPRHW-QTVMAHGhvSVWNAVP--ALmQMLCEYHSGDRMSY------------------PTLR--------------- 254
Cdd:cd05931 228 LRRPLRWlRLISRYR--ATISAAPnfAY-DLCVRRVRDEDLEGldlsswrvalngaepvrpATLRrfaeafapfgfrpea 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 255 ------LA----LLSGDWI--PLTLPEQMRERLNETMDIISLGGATECAIWSvyypigevestwtsipYGRGLRNQPVYV 322
Cdd:cd05931 305 frpsygLAeatlFVSGGPPgtGPVVLRVDRDALAGRAVAVAADDPAARELVS----------------CGRPLPDQEVRI 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 323 LNAQ-LEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWREASGERIY-RTGDRGrYFADGQVAFLGR 390
Cdd:cd05931 369 VDPEtGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWlRTGDLG-FLHDGELYITGR 437
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-390 |
2.27e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 124.69 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK03640 8 LKQRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGLTQLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMI---DHR 157
Cdd:PRK03640 88 REELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQtygNHW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 158 A-AMNTLEDInerfGLNAQDR------VFGLSSLSFdlsvydAFAPFMVGAALVLPEAGREKDPRHWqtvMAHGHVSVWN 230
Cdd:PRK03640 168 WsAVGSALNL----GLTEDDCwlaavpIFHISGLSI------LMRSVIYGMRVVLVEKFDAEKINKL---LQTGGVTIIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 231 AVPA-LMQMLCEYHSGdrmSYP-TLRLALLSGDWIPLTLPEQMRERlneTMDIISLGGATECAIWSVYYP-------IGE 301
Cdd:PRK03640 235 VVSTmLQRLLERLGEG---TYPsSFRCMLLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETASQIVTLSpedaltkLGS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 302 VestwtsipyGRGLRnqPVYV-LNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriYRTGDRGR 378
Cdd:PRK03640 309 A---------GKPLF--PCELkIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQdgW--------FKTGDIGY 369
|
410
....*....|..
gi 535686385 379 YFADGQVAFLGR 390
Cdd:PRK03640 370 LDEEGFLYVLDR 381
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1-383 |
4.56e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 121.19 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK08316 17 LRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGLTQ---------------LEPSLPVLIIDDGMLD------TPAAPLPEVAGDVTDLAYI 139
Cdd:PRK08316 97 GEELAYILDHSGARAFLVDPALAPtaeaalallpvdtliLSLVLGGREAPGGWLDfadwaeAGSVAEPDVELADDDLAQI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 140 IFTSGSTGTPKGVMIDHRAAM----NTLEDInerfGLNAQDRVfgLSSL----SFDLSVYdaFAP-FMVGAALVLPEAgr 210
Cdd:PRK08316 177 LYTSGTESLPKGAMLTHRALIaeyvSCIVAG----DMSADDIP--LHALplyhCAQLDVF--LGPyLYVGATNVILDA-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 211 eKDP-RHWQTVMAHGHVS------VWNAV---PALmqmlceyhsgDRMSYPTLRLALLSGDWIPLTLPEQMRERLNEtMD 280
Cdd:PRK08316 247 -PDPeLILRTIEAERITSffapptVWISLlrhPDF----------DTRDLSSLRKGYYGASIMPVEVLKELRERLPG-LR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 281 IISLGGATECA-IWSVYYPiGEVESTWTSIpyGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAAS 359
Cdd:PRK08316 315 FYNCYGQTEIApLATVLGP-EEHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEA 391
|
410 420
....*....|....*....|....*.
gi 535686385 360 FV--WreasgeriYRTGDRGRYFADG 383
Cdd:PRK08316 392 FRggW--------FHSGDLGVMDEEG 409
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
5-399 |
5.07e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 121.69 E-value: 5.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRR 84
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 85 QLLLTVGEVRVQVTQPGLTQL------------------------EPSLPV-------LIIDDGMLD------TPAAPLP 127
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLAPVveqvraetslrhvivtsladvlpaEPTLPLpdslrapRLAAAGAIDllpalrACTAPVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 128 EVAGDVTDLAYIIFTSGSTGTPKGVMIDHR-----AAMNTLEDINERfglnaQDRVFglssLSF---------DLSVyda 193
Cdd:PRK06178 203 LPPPALDALAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAVVGG-----EDSVF----LSFlpefwiageNFGL--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 194 FAPFMVGAALVL-----PEAGREKDPRHWQTVMAhghVSVWNAVpALMQmlceyHSG-DRMSYPTLRLALLSGDWIPLTl 267
Cdd:PRK06178 271 LFPLFSGATLVLlarwdAVAFMAAVERYRVTRTV---MLVDNAV-ELMD-----HPRfAEYDLSSLRQVRVVSFVKKLN- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 268 PEqMRERLNEtmdiislggATECAIWSVYYPIGEvesTWTSIPYGRG-------LRNQPVY----VLNAQLEEC------ 330
Cdd:PRK06178 341 PD-YRQRWRA---------LTGSVLAEAAWGMTE---THTCDTFTAGfqdddfdLLSQPVFvglpVPGTEFKICdfetge 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535686385 331 --PVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriYRTGDRGRYFADGQVAFLGRNDTQVKVNG 399
Cdd:PRK06178 408 llPLGAEGEIVVRTPSLLKGYWNKPEATAEALRdgW--------LHTGDIGKIDEQGFLHYLGRRKEMLKVNG 472
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
19-390 |
4.92e-29 |
|
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: 117.70 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVT 98
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 qpgltqlepslpvliiddgmldtpaaplpevaGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRv 178
Cdd:cd05907 84 --------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDR- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 179 fglsSLSF-DLS-----VYDAFAPFMVGAALVLPEagREKD----------------PRHWQTVMAHGHVSvwnAVPALM 236
Cdd:cd05907 131 ----HLSFlPLAhvferRAGLYVPLLAGARIYFAS--SAETllddlsevrptvflavPRVWEKVYAAIKVK---AVPGLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 237 QMLCEYHSGDRmsyptLRLALLSGDWIPLTLPEQMRerlnetmdiiSLG-------GATECAiwsvyyPIGEVeSTWTSI 309
Cdd:cd05907 202 RKLFDLAVGGR-----LRFAASGGAPLPAELLHFFR----------ALGipvyegyGLTETS------AVVTL-NPPGDN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 310 PYGR-GLRNQPVyvlnaqleECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV---WreasgeriYRTGDRGRYFADGQV 385
Cdd:cd05907 260 RIGTvGKPLPGV--------EVRIADDGEILVRGPNVMLGYYKNPEATAEALDadgW--------LHTGDLGEIDEDGFL 323
|
....*
gi 535686385 386 AFLGR 390
Cdd:cd05907 324 HITGR 328
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
19-390 |
7.20e-29 |
|
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: 117.18 E-value: 7.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLppQRRQLLLTVGEVrvqvt 98
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGM--GRKNLKQCLQEA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 qpgltqlEPslpvliidDGMLDTPAAPLPevagdvtdlAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRv 178
Cdd:cd05910 74 -------EP--------DAFIGIPKADEP---------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 179 fglsslsfDLSVYDAFAPF--MVGAALVLPEAGREK----DPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPT 252
Cdd:cd05910 129 --------DLATFPLFALFgpALGLTSVIPDMDPTRparaDPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 253 LRLALLSGDWIPLTLPEQMRERLNETMDIISLGGATECAIWSVyypIG--EVESTWTSIP-------YGRGLRNQPVYVL 323
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEALPVSS---IGsrELLATTTAATsggagtcVGRPIPGVRVRII 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535686385 324 NA---------QLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWREASGERiYRTGDRGRYFADGQVAFLGR 390
Cdd:cd05910 278 EIddepiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFW-HRMGDLGYLDDEGRLWFCGR 352
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
22-390 |
1.11e-28 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 117.54 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 22 TYRQLSTAADHVARALLALGVQHGDRVAVVMeKGWQQIAAVH-GILRLGAVYLPVD----------------------PV 78
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQL-PGWCEFTIIYlACLKVGAVSVPLLpswreaelvwvlnkcqakmffaPT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 79 LPPQRRQLLLTVgEVRVQVTQ----PGLTQLEPSLPVL----IIDDGmldTPAAPLPEVAGDvtDLAYIIFTSGSTGTPK 150
Cdd:PRK06087 130 LFKQTRPVDLIL-PLQNQLPQlqqiVGVDKLAPATSSLslsqIIADY---EPLTTAITTHGD--ELAAVLFTSGTEGLPK 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 151 GVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAF-APFMVGAALVLPEAGRekdPRHWQTVMAHGHVS-V 228
Cdd:PRK06087 204 GVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVtAPFLIGARSVLLDIFT---PDACLALLEQQRCTcM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 229 WNAVPALMQMLCEYHSgDRMSYPTLRLALLSGDWIPLTLPEQMRERlneTMDIISLGGATEcAIWSVYYPIGEVEStWTS 308
Cdd:PRK06087 281 LGATPFIYDLLNLLEK-QPADLSALRFFLCGGTTIPKKVARECQQR---GIKLLSVYGSTE-SSPHAVVNLDDPLS-RFM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 309 IPYGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAasfvwREASGERIYRTGDRGRYFADGQVAFL 388
Cdd:PRK06087 355 HTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-----RALDEEGWYYSGDLCRMDEAGYIKIT 429
|
..
gi 535686385 389 GR 390
Cdd:PRK06087 430 GR 431
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
3-392 |
6.35e-28 |
|
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: 114.91 E-value: 6.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIR--ELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:cd05923 9 RAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGLTQLEPS----LPVLIIDD----GMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGV 152
Cdd:cd05923 89 AAELAELIERGEMTAAVIAVDAQVMDAIfqsgVRVLALSDlvglGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 153 MIDHRAA------MNTLEDIneRFGlnAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEagREKDPRHWQTVMAHGHV 226
Cdd:cd05923 169 VIPQRAAesrvlfMSTQAGL--RHG--RHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVV--EEFDPADALKLIEQERV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 227 SVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGdwipLTLPEQMRERLNETM--DIISLGGATEcAIWSVYYPIGEVES 304
Cdd:cd05923 243 TSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAG----ATMPDAVLERVNQHLpgEKVNIYGTTE-AMNSLYMRDARTGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 305 TWTSipyGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLA--QGYLNDAEKTAASFVwreasgERIYRTGDRGRYFAD 382
Cdd:cd05923 318 EMRP---GFFSEVRIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQ------DGWYRTGDVGYVDPS 388
|
410
....*....|
gi 535686385 383 GQVAFLGRND 392
Cdd:cd05923 389 GDVRILGRVD 398
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
12-406 |
1.11e-27 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 113.54 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 12 TALISPIRELTYRQLSTAADHVARALLALG-VQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPqrRQLLLTv 90
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPL--AELEYV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 91 gevrvqvtqpgLTQLEPSLpvliiddgmldtpaaplpevagdVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERF 170
Cdd:cd05941 80 -----------ITDSEPSL-----------------------VLDPALILYTSGTTGRPKGVVLTHANLAANVRALVDAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 171 GLNAQDR---------VFGLsslsfdlsVYDAFAPFMVGAALV-LPEAgrekDPRHWQTVMAHGHVSVWNAVPALMQMLC 240
Cdd:cd05941 126 RWTEDDVllhvlplhhVHGL--------VNALLCPLFAGASVEfLPKF----DPKEVAISRLMPSITVFMGVPTIYTRLL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 241 EYHsgDRMSYPT----------LRLaLLSGDwipLTLPEQMRERLNETMD--IISLGGATEcaiwsvyypIGEVestwTS 308
Cdd:cd05941 194 QYY--EAHFTDPqfaraaaaerLRL-MVSGS---AALPVPTLEEWEAITGhtLLERYGMTE---------IGMA----LS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 309 IPY---------GRGLRNQPVYVL-NAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVwreasGERIYRTGDRGR 378
Cdd:cd05941 255 NPLdgerrpgtvGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFT-----DDGWFKTGDLGV 329
|
410 420
....*....|....*....|....*....
gi 535686385 379 YFADGQVAFLGR-NDTQVKVNGYRIELGE 406
Cdd:cd05941 330 VDEDGYYWILGRsSVDIIKSGGYKVSALE 358
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
20-402 |
1.41e-27 |
|
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: 113.34 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 20 ELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTq 99
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 100 pgLTQLEpslpvliiddgmldtpaaplpevagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVF 179
Cdd:cd05935 80 --GSELD----------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVIL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 180 GLSSLsFDLS--VYDAFAPFMVGAALVL-----PEAGREKDPRHwqtvmahgHVSVWNAVPALMQMLCEYHSGDRMSYPT 252
Cdd:cd05935 130 ACLPL-FHVTgfVGSLNTAVYVGGTYVLmarwdRETALELIEKY--------KVTFWTNIPTMLVDLLATPEFKTRDLSS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 253 LRLaLLSGDWiplTLPEQMRERLNET--MDIISLGGATECAIWSVYYPIGEVESTWTSIP-YGRGLRnqpvyVLNAQ-LE 328
Cdd:cd05935 201 LKV-LTGGGA---PMPPAVAEKLLKLtgLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDAR-----VIDIEtGR 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535686385 329 ECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVwrEASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05935 272 ELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI--EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKV 343
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
21-402 |
1.91e-27 |
|
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: 112.98 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTQP 100
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 101 GLTQlepslpvliiddgmldtpaaplpevAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFG 180
Cdd:cd05969 81 ELYE-------------------------RTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWC 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 181 LSSLSFDL-SVYDAFAPFMVGAALVLPEAgrEKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYhsGDRM--SY--PTLRL 255
Cdd:cd05969 136 TADPGWVTgTVYGIWAPWLNGVTNVVYEG--RFDAESWYGIIERVKVTVWYTAPTAIRMLMKE--GDELarKYdlSSLRF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 256 ALLSGDwiPLTlPEQMR---ERLNetMDIISLGGATECAiwsvyypiGEVESTWTSIPYGRGLRNQPV-----YVLNAQL 327
Cdd:cd05969 212 IHSVGE--PLN-PEAIRwgmEVFG--VPIHDTWWQTETG--------SIMIANYPCMPIKPGSMGKPLpgvkaAVVDENG 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535686385 328 EECPVGVEGEICI--GGMGLAQGYLNDAEKTAASFV--WreasgeriYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05969 279 NELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFIdgW--------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRV 349
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1-390 |
1.30e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 111.29 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAA-LTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVL 79
Cdd:PRK07470 12 FLRQAArRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 80 PPQRRQLLLTVGEVR--------------VQVTQPGLTQ---LEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFT 142
Cdd:PRK07470 92 TPDEVAYLAEASGARamichadfpehaaaVRAASPDLTHvvaIGGARAGLDYEALVARHLGARVANAAVDHDDPCWFFFT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 143 SGSTGTPKGVMIDHrAAM-----NTLEDINErfGLNAQDRVFGLSSLSFDLSVYdAFAPFMVGAALVLPEAGREKDPRHW 217
Cdd:PRK07470 172 SGTTGRPKAAVLTH-GQMafvitNHLADLMP--GTTEQDASLVVAPLSHGAGIH-QLCQVARGAATVLLPSERFDPAEVW 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 218 QTVMAHGhVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGdwIPLTLPEQMRERLnetmdiiSLGgatecAIWSVYY 297
Cdd:PRK07470 248 ALVERHR-VTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAG--APMYRADQKRALA-------KLG-----KVLVQYF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 298 PIGEVESTWTSIP-YGRGLRNQP---------------VYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV 361
Cdd:PRK07470 313 GLGEVTGNITVLPpALHDAEDGPdarigtcgfertgmeVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR 392
|
410 420 430
....*....|....*....|....*....|.
gi 535686385 362 --WreasgeriYRTGDRGRYFADGQVAFLGR 390
Cdd:PRK07470 393 dgW--------FRTGDLGHLDARGFLYITGR 415
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-390 |
1.77e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 111.35 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPI----RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVD 76
Cdd:COG1022 17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 77 PVLPPQRRQLLLTVGEVRVQVTQpGLTQLE---------PSLPVLIIDD--GMLDTP-------------AAPLPE---- 128
Cdd:COG1022 97 PTSSAEEVAYILNDSGAKVLFVE-DQEQLDkllevrdelPSLRHIVVLDprGLRDDPrllsldellalgrEVADPAelea 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 129 --VAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfglssLSF-DLS-VYD---AFAPFMVGA 201
Cdd:COG1022 176 rrAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRT-----LSFlPLAhVFErtvSYYALAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 202 ALVLPEAGRE--KD------------PRHW----QTVMAHGHVSVWN-------AVPALMQMLCEYHSGDRMSyPTLRLA 256
Cdd:COG1022 251 TVAFAESPDTlaEDlrevkptfmlavPRVWekvyAGIQAKAEEAGGLkrklfrwALAVGRRYARARLAGKSPS-LLLRLK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 257 LLSGDWI---PLtlpeqmRERLNETMDIISLGGAtecaiwsvyyPIG-EVESTWTSIpygrGLrnqPVYVLNAQLEECPV 332
Cdd:COG1022 330 HALADKLvfsKL------REALGGRLRFAVSGGA----------ALGpELARFFRAL----GI---PVLEGYGLTETSPV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 333 -------------------GVE------GEICIGGMGLAQGYLNDAEKTAASFV---WreasgeriYRTGDRGRYFADGQ 384
Cdd:COG1022 387 itvnrpgdnrigtvgpplpGVEvkiaedGEILVRGPNVMKGYYKNPEATAEAFDadgW--------LHTGDIGELDEDGF 458
|
....*.
gi 535686385 385 VAFLGR 390
Cdd:COG1022 459 LRITGR 464
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
17-385 |
1.69e-25 |
|
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: 108.10 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 17 PIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQrrQLLLTV--GEVR 94
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPE--QIAYIInhAEDR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 95 VQVT----QPGLTQLEPSLPVLIIDDGMLDTPAAPLPevaGDVTDLAY-----------------------IIFTSGSTG 147
Cdd:cd12119 100 VVFVdrdfLPLLEAIAPRLPTVEHVVVMTDDAAMPEP---AGVGVLAYeellaaespeydwpdfdentaaaICYTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 148 TPKGVMIDHRAA-MNTLedinerfGLNAQDrVFGLSSLSFDLSVYD---------AFAPFMVGAALVLPeaGREKDPRHW 217
Cdd:cd12119 177 NPKGVVYSHRSLvLHAM-------AALLTD-GLGLSESDVVLPVVPmfhvnawglPYAAAMVGAKLVLP--GPYLDPASL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 218 QTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERlneTMDIISLGGATE-CAIWSV- 295
Cdd:cd12119 247 AELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER---GVRVIHAWGMTEtSPLGTVa 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 296 YYPIGEVESTWTSIPYGRGLRNQPVYVLNAQLEEcPVGVE--------GEICIGGMGLAQGYLNDAEKTAASFV--Wrea 365
Cdd:cd12119 324 RPPSEHSNLSEDEQLALRAKQGRPVPGVELRIVD-DDGRElpwdgkavGELQVRGPWVTKSYYKNDEESEALTEdgW--- 399
|
410 420
....*....|....*....|
gi 535686385 366 sgeriYRTGDRGRYFADGQV 385
Cdd:cd12119 400 -----LRTGDVATIDEDGYL 414
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
20-406 |
4.85e-25 |
|
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: 105.98 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 20 ELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTq 99
Cdd:cd05971 6 KVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 100 pgltqlepslpvliidDGmldtpaaplpevagdVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGL--NAQDR 177
Cdd:cd05971 85 ----------------DG---------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLfpRDGDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 178 VFGLSSLSFDLSVYDAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEyhSGDRMSYPTLRLAL 257
Cdd:cd05971 134 YWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQ--QGEQLKHAQVKLRA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 258 LSGDWIPL--TLPEQMRERLNetMDIISLGGATECAIW----SVYYPIGEvestwTSIpyGRGLRNQPVYVLNAQLEECP 331
Cdd:cd05971 212 IATGGESLgeELLGWAREQFG--VEVNEFYGQTECNLVigncSALFPIKP-----GSM--GKPIPGHRVAIVDDNGTPLP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 332 VGVEGEICI----GGMGLaqGYLNDAEKTAASFV--WreasgeriYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELG 405
Cdd:cd05971 283 PGEVGEIAVelpdPVAFL--GYWNNPSATEKKMAgdW--------LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPA 352
|
.
gi 535686385 406 E 406
Cdd:cd05971 353 E 353
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
5-390 |
1.20e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 105.74 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRR 84
Cdd:PRK07798 13 ADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 85 QLLLTVGEVRVQVTQ----PGLTQLEPSLP----VLIIDDG--------------MLDTPAAPLPEVAGDVTDLaYIIFT 142
Cdd:PRK07798 93 RYLLDDSDAVALVYErefaPRVAEVLPRLPklrtLVVVEDGsgndllpgavdyedALAAGSPERDFGERSPDDL-YLLYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 143 SGSTGTPKGVMIDH----RAAMN-----------TLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPE 207
Cdd:PRK07798 172 GGTTGMPKGVMWRQedifRVLLGgrdfatgepieDEEELAKRAAAGPGMRRFPAPPLMHGAGQWAAFAALFSGQTVVLLP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 208 aGREKDPRH-WQTVMAHGhVSVwnavpalMQMLceyhsGDRMSYPTLR------------LALLSGDWIPLTlpEQMRER 274
Cdd:PRK07798 252 -DVRFDADEvWRTIEREK-VNV-------ITIV-----GDAMARPLLDaleargpydlssLFAIASGGALFS--PSVKEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 275 LNETM------DIIslgGATEC-AIWSVYYPIGEVESTWTSIPYGRGlrnqpVYVLNAQLEECPVG--VEGEICIGGMgL 345
Cdd:PRK07798 316 LLELLpnvvltDSI---GSSETgFGGSGTVAKGAVHTGGPRFTIGPR-----TVVLDEDGNPVEPGsgEIGWIARRGH-I 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 535686385 346 AQGYLNDAEKTAASFvwREASGERIYRTGDRGRYFADGQVAFLGR 390
Cdd:PRK07798 387 PLGYYKDPEKTAETF--PTIDGVRYAIPGDRARVEADGTITLLGR 429
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1-402 |
1.82e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 105.23 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVL- 79
Cdd:PRK06155 27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 80 PPQRRQLLLTVGEVRVQVTQPGLTQLEPSLP-------VLIIDDGMLDTPAA-----PLPEVAGDVT-------DLAYII 140
Cdd:PRK06155 107 GPQLEHILRNSGARLLVVEAALLAALEAADPgdlplpaVWLLDAPASVSVPAgwstaPLPPLDAPAPaaavqpgDTAAIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 141 FTSGSTGTPKGVMIDHRA----AMNTLEDInerfGLNAQDRVFGLSSLsFDLSVYDAFAPFMV-GAALVLPEagREKDPR 215
Cdd:PRK06155 187 YTSGTTGPSKGVCCPHAQfywwGRNSAEDL----EIGADDVLYTTLPL-FHTNALNAFFQALLaGATYVLEP--RFSASG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 216 HWQTVMAHGhVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGdwIPLTLPEQMRERLNetMDIISLGGATEcAIWSV 295
Cdd:PRK06155 260 FWPAVRRHG-ATVTYLLGAMVSILLSQPARESDRAHRVRVALGPG--VPAALHAAFRERFG--VDLLDGYGSTE-TNFVI 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 296 YYPIGEVESTWTsipyGRGLRNQPVYVLNAQLEECPVGVEGEICIGG---MGLAQGYLNDAEKTAASfvWREAsgerIYR 372
Cdd:PRK06155 334 AVTHGSQRPGSM----GRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFGMPEKTVEA--WRNL----WFH 403
|
410 420 430
....*....|....*....|....*....|
gi 535686385 373 TGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:PRK06155 404 TGDRVVRDADGWFRFVDRIKDAIRRRGENI 433
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
21-402 |
2.48e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 101.06 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTQp 100
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 101 gltqlepslpvliiddgmldtpAAPLPEVAgdvTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFG 180
Cdd:cd05973 80 ----------------------AANRHKLD---SDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSFWN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 181 LSSLSFDLSVYDAF-APFMVGAALVLPEAGREKdPRHWQTVMAHGhVSVWNAVPALMQMLCEyHSGDRMSYPTLRLALLS 259
Cdd:cd05973 135 AADPGWAYGLYYAItGPLALGHPTILLEGGFSV-ESTWRVIERLG-VTNLAGSPTAYRLLMA-AGAEVPARPKGRLRRVS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 260 GDWIPLTlPEQMR-ERLNETMDIISLGGATE-----CAIWSVYYPIGEVEStwtsipyGRGLRNQPVYVLNAQLEECPVG 333
Cdd:cd05973 212 SAGEPLT-PEVIRwFDAALGVPIHDHYGQTElgmvlANHHALEHPVHAGSA-------GRAMPGWRVAVLDDDGDELGPG 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535686385 334 VEGEICI----GGMGLAQGYLNDAEKTAASfvwreasgeRIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05973 284 EPGRLAIdianSPLMWFRGYQLPDTPAIDG---------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1-390 |
2.81e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 101.81 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIREL--TYRQLSTAADHVARALLALGVQHGDRVAV----VMEkgW--QQIAAVhgilRLGAVY 72
Cdd:PRK08315 22 LDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIwapnVPE--WvlTQFATA----KIGAIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 73 LPVDPVLPPQRRQLLLTVGEVRVQVTQPG---------LTQLEP-------------SLP----VLIIDD----GMLDTP 122
Cdd:PRK08315 96 VTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamLYELAPelatcepgqlqsaRLPelrrVIFLGDekhpGMLNFD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 123 AapLPEVAGDVTDLAY--------------IIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRV---------F 179
Cdd:PRK08315 176 E--LLALGRAVDDAELaarqatldpddpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLcipvplyhcF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 180 G-----LSSLSfdlsvydafapfmVGAALVLPeaGREKDPrhwQTVMA----------HGhvsvwnaVPAL-MQMLcEYH 243
Cdd:PRK08315 254 GmvlgnLACVT-------------HGATMVYP--GEGFDP---LATLAaveeerctalYG-------VPTMfIAEL-DHP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 244 SGDRMSYPTLRLALLSGDwiplTLPEQMRERLNETM---DIISLGGATECAiwsvyyPIgeveSTWTSI--PY------- 311
Cdd:PRK08315 308 DFARFDLSSLRTGIMAGS----PCPIEVMKRVIDKMhmsEVTIAYGMTETS------PV----STQTRTddPLekrvttv 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 312 GRGLRNQPVYVLNAQL-EECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSGERIYRTGDRGRYFADGQVAFLGR 390
Cdd:PRK08315 374 GRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI-----DADGWMHTGDLAVMDEEGYVNIVGR 448
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
12-402 |
4.04e-23 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 101.16 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 12 TALISPI--RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPvlppqrrqlLLT 89
Cdd:cd05904 22 PALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP---------LST 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 90 VGEVRVQV----------TQPGLTQLEP-SLPVLIIDD----------GMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGT 148
Cdd:cd05904 93 PAEIAKQVkdsgaklaftTAELAEKLASlALPVVLLDSaefdslsfsdLLFEADEAEPPVVVIKQDDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 149 PKGVMIDHRAAMNTLEDINERFGLNA--QDR---------VFGLSSLsfdlsvydAFAPFMVGAALV------LPEAGRe 211
Cdd:cd05904 173 SKGVMLTHRNLIAMVAQFVAGEGSNSdsEDVflcvlpmfhIYGLSSF--------ALGLLRLGATVVvmprfdLEELLA- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 212 kdprhwqTVMAHGhVSVWNAVPALMQMLCEYHSGDRMSYPTLRlALLSGDwIPLT--LPEQMRERLnETMDIISLGGATE 289
Cdd:cd05904 244 -------AIERYK-VTHLPVVPPIVLALVKSPIVDKYDLSSLR-QIMSGA-APLGkeLIEAFRAKF-PNVDLGQGYGMTE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 290 -CAIWSVYYPIGEVESTWTSIpyGRGLRNQPVYVLNAQLEEC-PVGVEGEICIGGMGLAQGYLNDAEKTAASFVwreasG 367
Cdd:cd05904 313 sTGVVAMCFAPEKDRAKYGSV--GRLVPNVEAKIVDPETGESlPPNQTGELWIRGPSIMKGYLNNPEATAATID-----K 385
|
410 420 430
....*....|....*....|....*....|....*
gi 535686385 368 ERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05904 386 EGWLHTGDLCYIDEDGYLFIVDRLKELIKYKGFQV 420
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1-406 |
5.67e-23 |
|
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: 100.48 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVylpvdPV-- 78
Cdd:cd05920 21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAV-----PVla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 79 LPPQRRQLLLTVgevrVQVTQPGLtqlepslpvLIIDDGMLDTPAAPLP-EVAGDVTDLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:cd05920 96 LPSHRRSELSAF----CAHAEAVA---------YIVPDRHAGFDHRALArELAESIPEVALFLLSGGTTGTPKLIPRTHN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 158 AAMNTLEDINERFGLNAQDRVfgLSSLS----FDLSVYDAFAPFMVGAALVLpeaGREKDPRHWQTVMAHGHVSVWNAVP 233
Cdd:cd05920 163 DYAYNVRASAEVCGLDQDTVY--LAVLPaahnFPLACPGVLGTLLAGGRVVL---APDPSPDAAFPLIEREGVTVTALVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 234 ALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNetmdiislggateCAIWSVYypiGEVES--TWTSI-- 309
Cdd:cd05920 238 ALVSLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLG-------------CTLQQVF---GMAEGllNYTRLdd 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 310 -------PYGRGL-RNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSGERIYRTGDRGRYFA 381
Cdd:cd05920 302 pdeviihTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF-----TPDGFYRTGDLVRRTP 376
|
410 420
....*....|....*....|....*
gi 535686385 382 DGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd05920 377 DGYLVVEGRIKDQINRGGEKIAAEE 401
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
19-383 |
9.06e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 100.46 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAV-------YLP----------------- 74
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVvvehnplYTAhelehpfedhgarvaiv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 75 ---VDPVLPPQRRQLLL-TVGEVRVQVTQPGLTQLEPSLPV----------------------LIIDDGMLDTPAAPLPE 128
Cdd:PRK05605 136 wdkVAPTVERLRRTTPLeTIVSVNMIAAMPLLQRLALRLPIpalrkaraaltgpapgtvpwetLVDAAIGGDGSDVSHPR 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 129 VAGDvtDLAYIIFTSGSTGTPKGVMIDHR----------AAMNTLEDINERFglnaqdrvfgLSSL----SFDLSVYDAF 194
Cdd:PRK05605 216 PTPD--DVALILYTSGTTGKPKGAQLTHRnlfanaaqgkAWVPGLGDGPERV----------LAALpmfhAYGLTLCLTL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 195 APFMvGAALVLPEAgreKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLAlLSGdwiPLTLPEQMRER 274
Cdd:PRK05605 284 AVSI-GGELVLLPA---PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNA-FSG---AMALPVSTVEL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 275 LNE-TMDIISLG-GATECAIWSVYYPIGEV-ESTWTSIPYgrglRNQPVYVLNAQ--LEECPVGVEGEICIGGMGLAQGY 349
Cdd:PRK05605 356 WEKlTGGLLVEGyGLTETSPIIVGNPMSDDrRPGYVGVPF----PDTEVRIVDPEdpDETMPDGEEGELLVRGPQVFKGY 431
|
410 420 430
....*....|....*....|....*....|....*.
gi 535686385 350 LNDAEKTAASFV--WreasgeriYRTGDRGRYFADG 383
Cdd:PRK05605 432 WNRPEETAKSFLdgW--------FRTGDVVVMEEDG 459
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
9-406 |
1.56e-22 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 99.57 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALI------SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:cd17634 67 GDRTAIIyegddtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVT-----QPGLT---------QLEPSLP----VLIID-----------------DGMLDTPAAPLP 127
Cdd:cd17634 147 AVAGRIIDSSSRLLITadggvRAGRSvplkknvddALNPNVTsvehVIVLKrtgsdidwqegrdlwwrDLIAKASPEHQP 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 128 EvAGDVTDLAYIIFTSGSTGTPKGVMIDHRA-AMNTLEDINERFGLNAQDRVFGLSSLSFDLS-VYDAFAPFMVGAALVL 205
Cdd:cd17634 227 E-AMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 206 PEaGREKDP---RHWQTVMAHGhVSVWNAVPALMQMLCEyhSGD----RMSYPTLRLALLSGD-WIPLTLPEQMRERLNE 277
Cdd:cd17634 306 YE-GVPNWPtpaRMWQVVDKHG-VNILYTAPTAIRALMA--AGDdaieGTDRSSLRILGSVGEpINPEAYEWYWKKIGKE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 278 TMDIISLGGATE-----CAIWSVYYPIgEVESTWTSIPygrGLRNQpvyVLNAQLEECPVGVEGEICIGGM--GLAQGYL 350
Cdd:cd17634 382 KCPVVDTWWQTEtggfmITPLPGAIEL-KAGSATRPVF---GVQPA---VVDNEGHPQPGGTEGNLVITDPwpGQTRTLF 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 535686385 351 NDAEKTAASFvWREASGerIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd17634 455 GDHERFEQTY-FSTFKG--MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAE 507
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
16-402 |
4.05e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 98.43 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 16 SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV------DPVLppQRrqllLT 89
Cdd:PRK04319 69 SRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafmeEAVR--DR----LE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 90 VGEVRVQVTQPGLTQLEP--SLP----VLIIDD------GMLDTPAA------PLPEVAGDVTDLAYIIFTSGSTGTPKG 151
Cdd:PRK04319 143 DSEAKVLITTPALLERKPadDLPslkhVLLVGEdveegpGTLDFNALmeqasdEFDIEWTDREDGAILHYTSGSTGKPKG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 152 VMIDHRAAmnTLEDINERFGLNAQDR-----------VFGLSslsfdlsvYDAFAPFMVGAALVLPEAgrEKDPRHWQTV 220
Cdd:PRK04319 223 VLHVHNAM--LQHYQTGKYVLDLHEDdvywctadpgwVTGTS--------YGIFAPWLNGATNVIDGG--RFSPERWYRI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 221 MAHGHVSVWNAVPALMQMLCEyhSGD----RMSYPTLRLALLSGDwiPLTlPEQMR-------ERLNET--Mdiislgga 287
Cdd:PRK04319 291 LEDYKVTVWYTAPTAIRMLMG--AGDdlvkKYDLSSLRHILSVGE--PLN-PEVVRwgmkvfgLPIHDNwwM-------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 288 TEC-AIWSVYYPIGEVEstwtsiP--YGRGLRNQPVYVLNAQLEECPVGVEGEICI--GGMGLAQGYLNDAEKTAASFV- 361
Cdd:PRK04319 358 TETgGIMIANYPAMDIK------PgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAg 431
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 535686385 362 -WreasgeriYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:PRK04319 432 dW--------YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERV 465
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
139-390 |
4.95e-22 |
|
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: 96.19 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 139 IIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRV---------FGLsslsfdlsVYDAFAPFMVGAALVLPEAG 209
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcipvplfhcFGS--------VLGVLACLTHGATMVFPSPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 210 -----------REKdprhwQTVMaHGhvsvwnaVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNET 278
Cdd:cd05917 79 fdplavleaieKEK-----CTAL-HG-------VPTMFIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 279 mDIISLGGATECA-IWSVYYPIGEVESTWTSIpyGRGLRNQPVYVLNAQ-LEECPVGVEGEICIGGMGLAQGYLNDAEKT 356
Cdd:cd05917 146 -DVTIAYGMTETSpVSTQTRTDDSIEKRVNTV--GRIMPHTEAKIVDPEgGIVPPVGVPGELCIRGYSVMKGYWNDPEKT 222
|
250 260 270
....*....|....*....|....*....|....
gi 535686385 357 AasfvwREASGERIYRTGDRGRYFADGQVAFLGR 390
Cdd:cd05917 223 A-----EAIDGDGWLHTGDLAVMDEDGYCRIVGR 251
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
3-393 |
1.03e-21 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 97.25 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVylpVDPVLPPQ 82
Cdd:PRK08279 45 EAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAV---VALLNTQQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLL-----------LTVGE--------VRVQVTQPG----LTQLEPSLPVLIID-DGMLDTPAAPLPEVAGDVT--DL 136
Cdd:PRK08279 122 RGAVLahslnlvdakhLIVGEelveafeeARADLARPPrlwvAGGDTLDDPEGYEDlAAAAAGAPTTNPASRSGVTakDT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 137 AYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVF----------GLSSLSfdlSVydafapFMVGAALVLp 206
Cdd:PRK08279 202 AFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYcclplyhntgGTVAWS---SV------LAAGATLAL- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 207 eagREK--DPRHWQTVMAHGhvsvwnavpALMQM----LCEY------HSGDRMSypTLRLAL---LSGD-WipltlpEQ 270
Cdd:PRK08279 272 ---RRKfsASRFWDDVRRYR---------ATAFQyigeLCRYllnqppKPTDRDH--RLRLMIgngLRPDiW------DE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 271 MRERLNEtMDIISLGGATECAIwsVYYPIGEVEST------WTSIPY---------GRGLRNQpvyvlNAQLEECPVGVE 335
Cdd:PRK08279 332 FQQRFGI-PRILEFYAASEGNV--GFINVFNFDGTvgrvplWLAHPYaivkydvdtGEPVRDA-----DGRCIKVKPGEV 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535686385 336 GEiCIGGMGLAQ---GYlNDAEKTAASfVWREA--SGERIYRTGDRGRYFADGQVAFLGR-NDT 393
Cdd:PRK08279 404 GL-LIGRITDRGpfdGY-TDPEASEKK-ILRDVfkKGDAWFNTGDLMRDDGFGHAQFVDRlGDT 464
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
3-390 |
1.12e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 97.15 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIREL--TYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK12583 26 ATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPG---------LTQLEPSLP-----------------VLIID----DGMLDTPA------- 123
Cdd:PRK12583 106 ASELEYALGQSGVRWVICADAfktsdyhamLQELLPGLAegqpgalacerlpelrgVVSLApappPGFLAWHElqarget 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 124 ---APLPEVAGDVT--DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRvfglssLSFDLSVYDAFAPFM 198
Cdd:PRK12583 186 vsrEALAERQASLDrdDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDR------LCVPVPLYHCFGMVL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 199 -------VGAALVLPeaGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPltlPEQM 271
Cdd:PRK12583 260 anlgcmtVGACLVYP--NEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCP---IEVM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 272 RERLNET-MDIISLG-GATECAiwsvyyPIGEVESTWTSIP-----YGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMG 344
Cdd:PRK12583 335 RRVMDEMhMAEVQIAyGMTETS------PVSLQTTAADDLErrvetVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYS 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 535686385 345 LAQGYLNDAEKTAASFvwreaSGERIYRTGDRGRYFADGQVAFLGR 390
Cdd:PRK12583 409 VMKGYWNNPEATAESI-----DEDGWMHTGDLATMDEQGYVRIVGR 449
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
135-383 |
1.87e-21 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 96.92 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfgLSSL----SFDLSVyDAFAPFMVGAALVLpeagr 210
Cdd:PRK08633 783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVI--LSSLpffhSFGLTV-TLWLPLLEGIKVVY----- 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 211 EKDPRHWQTV---MAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNetMDIISLGGA 287
Cdd:PRK08633 855 HPDPTDALGIaklVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKFG--IRILEGYGA 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 288 TECA-IWSVYYPIGEVESTWTSIPYGRGLRNQP-----VYVLNAQ-LEECPVGVEGEICIGGMGLAQGYLNDAEKTAAsf 360
Cdd:PRK08633 933 TETSpVASVNLPDVLAADFKRQTGSKEGSVGMPlpgvaVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-- 1010
|
250 260
....*....|....*....|...
gi 535686385 361 VWREASGERIYRTGDRGRYFADG 383
Cdd:PRK08633 1011 VIKDIDGIGWYVTGDKGHLDEDG 1033
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
20-390 |
2.96e-21 |
|
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: 94.72 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 20 ELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVylpvdpVLPPQRRqllLTVGEVRVQvtq 99
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAE------AVLLNTR---LTPNELAFQ--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 100 pgltqlepslpvliiddgmldtpaapLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDR-- 177
Cdd:cd05912 69 --------------------------LKDSDVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNwl 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 178 ----VFGLSSLSFDL-SVYDAFAPFMVgaalvlpeagrEK-DPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGdrmSYP 251
Cdd:cd05912 123 calpLFHISGLSILMrSVIYGMTVYLV-----------DKfDAEQVLHLINSGKVTIISVVPTMLQRLLEILGE---GYP 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 252 -TLRLALLSGDWIPLTLPEQMRERlneTMDIISLGGATECAIWSVYYPIGEVESTWTSIpyGRGLRnqPVYVLNAQLEEC 330
Cdd:cd05912 189 nNLRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETCSQIVTLSPEDALNKIGSA--GKPLF--PVELKIEDDGQP 261
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535686385 331 PVGVeGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriYRTGDRGRYFADGQVAFLGR 390
Cdd:cd05912 262 PYEV-GEILLKGPNVTKGYLNRPDATEESFEngW--------FKTGDIGYLDEEGFLYVLDR 314
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
12-406 |
1.11e-20 |
|
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: 93.31 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 12 TALISPIRELTYRQLSTAADHVARALL-ALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTV 90
Cdd:cd05958 2 TCLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 91 GEVRVQVTQPGLTQLEpslpvliiddgmldtpaaplpevagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINER- 169
Cdd:cd05958 82 ARITVALCAHALTASD----------------------------DICILAFTSGTTGAPKATMHFHRDPLASADRYAVNv 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 170 FGLNAQDRVFGLSSLSFDLSV-YDAFAPFMVGAALVLPEagrEKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRM 248
Cdd:cd05958 134 LRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLE---EATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 249 SYPTLRLALLSGDwiplTLPEQMRERLNET--MDIISLGGATEcaIWSVYYPIGE----VESTWTSIPygrGLRNQpvyV 322
Cdd:cd05958 211 DLSSLRKCVSAGE----ALPAALHRAWKEAtgIPIIDGIGSTE--MFHIFISARPgdarPGATGKPVP---GYEAK---V 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 323 LNAQLEECPVGVEGEICIGGmglAQGYLNDAEKTAASFVwreaSGERIYrTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05958 279 VDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYV----QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNI 350
|
....
gi 535686385 403 ELGE 406
Cdd:cd05958 351 APPE 354
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
3-402 |
1.46e-20 |
|
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: 93.71 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALI-----SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKG---WQQIAAVHgilRLGAVYLP 74
Cdd:cd05970 25 AMAKEYPDKLALVwcddaGEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRyefWYSLLALH---KLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 75 VDPVLPP-------QRRQL--LLTVGEVRVQVTQPGLTQLEPSLPVLI-----IDDGMLD--------TPAAPLP----E 128
Cdd:cd05970 102 ATHQLTAkdivyriESADIkmIVAIAEDNIPEEIEKAAPECPSKPKLVwvgdpVPEGWIDfrkliknaSPDFERPtansY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 129 VAGDvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLedINERFGLNAQDRvfglsslSFDLSVYDA----------FAPFM 198
Cdd:cd05970 182 PCGE--DILLVYFSSGTTGMPKMVEHDFTYPLGHI--VTAKYWQNVREG-------GLHLTVADTgwgkavwgkiYGQWI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 199 VGAALVLPEAGReKDPRHWQTVMAHGHVSVWNAVPALMQMLCEyHSGDRMSYPTLRLALLSGDwiplTLPEQMRERLNET 278
Cdd:cd05970 251 AGAAVFVYDYDK-FDPKALLEKLSKYGVTTFCAPPTIYRFLIR-EDLSRYDLSSLRYCTTAGE----ALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 279 MDI-ISLG-GATECAIWSVYYPIGEVESTwtSIpyGRGLRNQPVYVLNAQLEECPVGVEGEICIGGM-----GLAQGYLN 351
Cdd:cd05970 325 TGIkLMEGfGQTETTLTIATFPWMEPKPG--SM--GKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 535686385 352 DAEKTAAsfVWREAsgerIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05970 401 DAEKTAE--VWHDG----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRI 445
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2-399 |
1.81e-20 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 93.21 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 2 LRQ-----AALTPQETALI-----SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAV 71
Cdd:PRK08008 9 LRQmwddlADVYGHKTALIfessgGVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 72 YLPVDPVLPPQRRQLLLTVGEVRVQVTQ----PGLTQLEPSLP-----VLIID------DGMLD-------TPAAPLPEV 129
Cdd:PRK08008 89 MVPINARLLREESAWILQNSQASLLVTSaqfyPMYRQIQQEDAtplrhICLTRvalpadDGVSSftqlkaqQPATLCYAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 130 AGDVTDLAYIIFTSGSTGTPKGVMIDHraamntledINERFG---------LNAQDRVFG-LSSLSFDLSVYDAFAPFMV 199
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITH---------YNLRFAgyysawqcaLRDDDVYLTvMPAFHIDCQCTAAMAAFSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 200 GAALVLPE--AGRekdpRHWQTVMAHgHVSVWNAVPALMQ--MLCEYHSGDRMSypTLRLALLSgdwipLTLPEQMRERL 275
Cdd:PRK08008 240 GATFVLLEkySAR----AFWGQVCKY-RATITECIPMMIRtlMVQPPSANDRQH--CLREVMFY-----LNLSDQEKDAF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 276 NETMDIISLG--GATECAIWSVYYPIGEvESTWTSIpyGR-GLRNQpVYVLNAQLEECPVGVEGEICIGGM---GLAQGY 349
Cdd:PRK08008 308 EERFGVRLLTsyGMTETIVGIIGDRPGD-KRRWPSI--GRpGFCYE-AEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEY 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 535686385 350 LNDAEKTAASFvwrEASGerIYRTGDRGRYFADGQVAFLGRNDTQVKVNG 399
Cdd:PRK08008 384 YLDPKATAKVL---EADG--WLHTGDTGYVDEEGFFYFVDRRCNMIKRGG 428
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
19-405 |
2.07e-20 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 92.78 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARaLLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVylPV--------------------DPV 78
Cdd:cd05909 6 TSLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKV--PVmlnytaglrelraciklagiKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 79 LPPQRRQLLLTVGEVRVQVTQPGLTQLEPSLPVLIIDDGMLDTPAAPLPEVAGDV---------TDLAYIIFTSGSTGTP 149
Cdd:cd05909 83 LTSKQFIEKLKLHHLFDVEYDARIVYLEDLRAKISKADKCKAFLAGKFPPKWLLRifgvapvqpDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 150 KGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSL--SFDLSVyDAFAPFMVGAALVLpeagrEKDPRHWQTVMAHGH-- 225
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTG-CLWLPLLSGIKVVF-----HPNPLDYKKIPELIYdk 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 226 -VSVWNAVPA-LMQMLCEYHSGDrmsYPTLRLALLSGDwiplTLPEQMRERLNETMDI-ISLG-GATECA-IWSVYYPI- 299
Cdd:cd05909 237 kATILLGTPTfLRGYARAAHPED---FSSLRLVVAGAE----KLKDTLRQEFQEKFGIrILEGyGTTECSpVISVNTPQs 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 300 GEVESTwtsipYGRGLRNQPVYVLN-AQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAasfvwrEASGERIYRTGDRGR 378
Cdd:cd05909 310 PNKEGT-----VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS------FAFGDGWYDTGDIGK 378
|
410 420
....*....|....*....|....*..
gi 535686385 379 YFADGQVAFLGRNDTQVKVNGYRIELG 405
Cdd:cd05909 379 IDGEGFLTITGRLSRFAKIAGEMVSLE 405
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1-390 |
1.73e-19 |
|
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: 90.20 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVylpvdPV-- 78
Cdd:COG1021 31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAI-----PVfa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 79 LPPQRRQ------------LLLTVGEVR----------VQVTQPGLTQlepslpVLIIDDGM-------LDTPAAPLPEV 129
Cdd:COG1021 106 LPAHRRAeishfaeqseavAYIIPDRHRgfdyralareLQAEVPSLRH------VLVVGDAGeftsldaLLAAPADLSEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 130 AGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfgLSSL----SFDLSVYDAFAPFMVGAALVL 205
Cdd:COG1021 180 RPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVY--LAALpaahNFPLSSPGVLGVLYAGGTVVL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 206 PEAGrekDP--------RHwqtvmahgHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDwiplTLPEQMRERLNE 277
Cdd:COG1021 258 APDP---SPdtafplieRE--------RVTVTALVPPLALLWLDAAERSRYDLSSLRVLQVGGA----KLSPELARRVRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 278 TmdiisLGgateCAIWSVYypiGEVEstwtsipygrGLRNQ----------------P------VYVLNAQLEECPVGVE 335
Cdd:COG1021 323 A-----LG----CTLQQVF---GMAE----------GLVNYtrlddpeevilttqgrPispddeVRIVDEDGNPVPPGEV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 535686385 336 GEICIGGMGLAQGYLNDAEKTAASFvwrEASGerIYRTGDRGRYFADGQVAFLGR 390
Cdd:COG1021 381 GELLTRGPYTIRGYYRAPEHNARAF---TPDG--FYRTGDLVRRTPDGYLVVEGR 430
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
17-264 |
7.38e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 88.27 E-value: 7.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 17 PIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQ 96
Cdd:PRK06018 36 PIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 97 VTQ----PGLTQLEPSLP-----VLIIDDGMLdtPAAPLP----------EVAGDVT-------DLAYIIFTSGSTGTPK 150
Cdd:PRK06018 116 ITDltfvPILEKIADKLPsveryVVLTDAAHM--PQTTLKnavayeewiaEADGDFAwktfdenTAAGMCYTSGTTGDPK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 151 GVMIDHRA-AMNTLEDIN-ERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPeaGREKDPRHWQTVMAHGHVSV 228
Cdd:PRK06018 194 GVLYSHRSnVLHALMANNgDALGTSAADTMLPVVPLFHANSWGIAFSAPSMGTKLVMP--GAKLDGASVYELLDTEKVTF 271
|
250 260 270
....*....|....*....|....*....|....*.
gi 535686385 229 WNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIP 264
Cdd:PRK06018 272 TAGVPTVWLMLLQYMEKEGLKLPHLKMVVCGGSAMP 307
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
5-394 |
1.14e-18 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 87.62 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVmekGWQQIAAVHGIL---RLGAVYLPVDPVLPP 81
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALR---GKNSPETLLAYLallQCGARVLPLNPQLPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 82 QRRQLLLTVGEVRVQVTqpgltqLEPSLPVLIIDDGMLDTPAAPlPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMN 161
Cdd:PRK09029 90 PLLEELLPSLTLDFALV------LEGENTFSALTSLHLQLVEGA-HAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAHLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 162 TLEDINERFGLNAQDRvfGLSSLS-FDLS----VYDAFApfmVGAALVLPEAGrekdpRHWQTVMAHGHVSVwnaVPALM 236
Cdd:PRK09029 163 SAEGVLSLMPFTAQDS--WLLSLPlFHVSgqgiVWRWLY---AGATLVVRDKQ-----PLEQALAGCTHASL---VPTQL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 237 QMLCEYHSGdrmsYPTLRLALLSGDWIPLTLPEQMRERLNETMdiisLG-GATECAiwsvyypigeveSTWTSIPY---- 311
Cdd:PRK09029 230 WRLLDNRSE----PLSLKAVLLGGAAIPVELTEQAEQQGIRCW----CGyGLTEMA------------STVCAKRAdgla 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 312 --GRGLRNQPVyvlnaQLeecpvgVEGEICIGGMGLAQGYlndaektaasfvWREasGERI--------YRTGDRGRyFA 381
Cdd:PRK09029 290 gvGSPLPGREV-----KL------VDGEIWLRGASLALGY------------WRQ--GQLVplvndegwFATRDRGE-WQ 343
|
410
....*....|...
gi 535686385 382 DGQVAFLGRNDTQ 394
Cdd:PRK09029 344 NGELTILGRLDNL 356
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1-399 |
1.67e-18 |
|
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: 87.34 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAAlTPQETALISPIRE------LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLP 74
Cdd:cd05906 15 LLLRAA-ERGPTKGITYIDAdgseefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 75 VdPVLPPQR---------RQLLLTVGEVRVqVTQPGLTQ---------LEPSLPVLIIDDgmLDTPAAPLPEVAGDVTDL 136
Cdd:cd05906 94 L-TVPPTYDepnarlrklRHIWQLLGSPVV-LTDAELVAefagletlsGLPGIRVLSIEE--LLDTAADHDLPQSRPDDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 137 AYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRvfGLSSLSFD----------LSVYDAFAPFMVGAALVLp 206
Cdd:cd05906 170 ALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDV--FLNWVPLDhvgglvelhlRAVYLGCQQVHVPTEEIL- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 207 eagreKDPRHWQTVMAHGHVSV-W--NAVPALMQMLCEYHSGDRMSYPTLRLALLSGDwiplTLPEQMRERLNETM---- 279
Cdd:cd05906 247 -----ADPLRWLDLIDRYRVTItWapNFAFALLNDLLEEIEDGTWDLSSLRYLVNAGE----AVVAKTIRRLLRLLepyg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 280 ---DIISLG-GATE-CA--IWSV---YYPIGEvESTWTSI--PY-GRGLRnqpvyVLNAQLEECPVGVEGEICIGGMGLA 346
Cdd:cd05906 318 lppDAIRPAfGMTEtCSgvIYSRsfpTYDHSQ-ALEFVSLgrPIpGVSMR-----IVDDEGQLLPEGEVGRLQVRGPVVT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 535686385 347 QGYLNDAEKTAASFV---WreasgeriYRTGDRGrYFADGQVAFLGRNDTQVKVNG 399
Cdd:cd05906 392 KGYYNNPEANAEAFTedgW--------FRTGDLG-FLDNGNLTITGRTKDTIIVNG 438
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
5-377 |
2.43e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 86.86 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVL-PPQR 83
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLaADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQLLLTVGEVRVQVTQPGLTQLEPSLPVLIIDDG------MLDTPAAPLPEVAGDV-TDLAYIIFTSGSTGTPKGVM--- 153
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAaqadsrRLAQGGLEIPPQAAVApTDLVRLMYTSGTTDRPKGVMhsy 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 154 -------IDHRAAMntledinerfGLNAQDRVFGLSSL----SFDLSvydAFAPFMVGAALVLPeagREKDPrhwQTVMA 222
Cdd:PRK06145 172 gnlhwksIDHVIAL----------GLTASERLLVVGPLyhvgAFDLP---GIAVLWVGGTLRIH---REFDP---EAVLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 223 ----HGHVSVWNAvPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPltlPEQMRE--RLNETMDIISLGGATECAIWSVY 296
Cdd:PRK06145 233 aierHRLTCAWMA-PVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTP---ESRIRDftRVFTRARYIDAYGLTETCSGDTL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 297 YPIG-EVESTWTSipyGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--WreasgeriYRT 373
Cdd:PRK06145 309 MEAGrEIEKIGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYgdW--------FRS 377
|
....
gi 535686385 374 GDRG 377
Cdd:PRK06145 378 GDVG 381
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
8-406 |
2.60e-18 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 86.99 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 8 TPQETALI--SP----IRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAV---------- 71
Cdd:cd05967 64 RGDQIALIydSPvtgtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIhsvvfggfaa 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 72 -----------------------------YLP-VDPVL-----PPqRRQLLLTVGEVRVQVTQPGLTqlepslpvLIIDD 116
Cdd:cd05967 144 kelasriddakpklivtascgiepgkvvpYKPlLDKALelsghKP-HHVLVLNRPQVPADLTKPGRD--------LDWSE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 117 GMLD-TPAAPLPeVAGdvTDLAYIIFTSGSTGTPKGVMID---HRAAMN-TLEDInerFGLNAQDRVFGLSSLSF----D 187
Cdd:cd05967 215 LLAKaEPVDCVP-VAA--TDPLYILYTSGTTGKPKGVVRDnggHAVALNwSMRNI---YGIKPGDVWWAASDVGWvvghS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 188 LSVYdafAPFMVGAALVLPEAG--REKDPRHWQTVMA-HGHVSVWNAVPALMQMLCEYHSGDRMS-YP--TLRLALLSGd 261
Cdd:cd05967 289 YIVY---GPLLHGATTVLYEGKpvGTPDPGAFWRVIEkYQVNALFTAPTAIRAIRKEDPDGKYIKkYDlsSLRTLFLAG- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 262 wipltlpeqmrERLN-ETMDIISlgGATECAIWSVYYpigEVESTW--TSIPYGRGLR-------NQPVY-----VLNAQ 326
Cdd:cd05967 365 -----------ERLDpPTLEWAE--NTLGVPVIDHWW---QTETGWpiTANPVGLEPLpikagspGKPVPgyqvqVLDED 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 327 LEECPVGVEGEICIGG---MGLAQGYLNDAEKTAASFvWREASGerIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIE 403
Cdd:cd05967 429 GEPVGPNELGNIVIKLplpPGCLLTLWKNDERFKKLY-LSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLS 505
|
...
gi 535686385 404 LGE 406
Cdd:cd05967 506 TGE 508
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1-390 |
8.00e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 85.32 E-value: 8.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALT-PQETALISPIRE--LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDP 77
Cdd:PRK05852 21 LVEVAATRlPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 78 VLP--PQR-RQLLLTVGEVRVQVTQPGlTQLEPSLPVLII------DDGM--------LDTPAAPLPEVAGDV---TDLA 137
Cdd:PRK05852 101 ALPiaEQRvRSQAAGARVVLIDADGPH-DRAEPTTRWWPLtvnvggDSGPsggtlsvhLDAATEPTPATSTPEglrPDDA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 138 YIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDA-FAPFMVGAALVLPEAGREKDPRH 216
Cdd:PRK05852 180 MIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAAlLATLASGGAVLLPARGRFSAHTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 217 WQTvMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLT--LPEQMRERLNETMdIISLG--GATECAI 292
Cdd:PRK05852 260 WDD-IKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTaeTAQALQTEFAAPV-VCAFGmtEATHQVT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 293 WSVYYPIGEVES-TWTSIPYGRGLRNQpVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV--Wreasger 369
Cdd:PRK05852 338 TTQIEGIGQTENpVVSTGLVGRSTGAQ-IRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTdgW------- 409
|
410 420
....*....|....*....|.
gi 535686385 370 iYRTGDRGRYFADGQVAFLGR 390
Cdd:PRK05852 410 -LRTGDLGSLSAAGDLSIRGR 429
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
5-406 |
9.63e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 85.18 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRR 84
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 85 QLLLTVGEVRVQVTQPGLTQLE-------------PSLP-VLIIDDGMLDTPA---------------APLP---EVAGD 132
Cdd:PRK06164 100 AHILGRGRARWLVVWPGFKGIDfaailaavppdalPPLRaIAVVDDAADATPApapgarvqlfalpdpAPPAaagERAAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 133 VTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDR---------VFGLSSLsfdlsvydaFAPFMVGAAL 203
Cdd:PRK06164 180 PDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVllaalpfcgVFGFSTL---------LGALAGGAPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 204 VLPEAgrEKDPRHWQTVMAHGHVSVWNAVPALMQMLCEyhSGDRMSYPTLRLaLLSGDWIPlTLPEQMRERLNETMDIIS 283
Cdd:PRK06164 251 VCEPV--FDAARTARALRRHRVTHTFGNDEMLRRILDT--AGERADFPSARL-FGFASFAP-ALGELAALARARGVPLTG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 284 LGGATEC-AIWSvyypIGEVESTWTSIPYGRGLRNQP---VYVLNAQLEE-CPVGVEGEICIGGMGLAQGYLNDAEKTAA 358
Cdd:PRK06164 325 LYGSSEVqALVA----LQPATDPVSVRIEGGGRPASPearVRARDPQDGAlLPDGESGEIEIRAPSLMRGYLDNPDATAR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 535686385 359 SFvwreaSGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:PRK06164 401 AL-----TDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAE 443
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1-391 |
1.02e-17 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 84.66 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:cd12118 10 LERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGLTQLEpslpVLIIDDGmldtpaAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:cd12118 90 AEEIAFILRHSEAKVLFVDREFEYED----LLAEGDP------DFEWIPPADEWDPIALNYTSGTTGRPKGVVYHHRGAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 -NTLEDINErfglnaqdrvFGLSSLSFDLSVYDAF---------APFMVGAALV-LpeagREKDPRHWQTVMAHGHVSVW 229
Cdd:cd12118 160 lNALANILE----------WEMKQHPVYLWTLPMFhcngwcfpwTVAAVGGTNVcL----RKVDAKAIYDLIEKHKVTHF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 230 NAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMrERLNetMDIISLGGATEcaiwsVYYPI--GEVESTWT 307
Cdd:cd12118 226 CGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPPPAAVLAKM-EELG--FDVTHVYGLTE-----TYGPAtvCAWKPEWD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 308 SIPYGR--------GLRN---QPVYVLNAQLEEcPV---GVE-GEICIGGMGLAQGYLNDAEKTAASFV--Wreasgeri 370
Cdd:cd12118 298 ELPTEErarlkarqGVRYvglEEVDVLDPETMK-PVprdGKTiGEIVFRGNIVMKGYLKNPEATAEAFRggW-------- 368
|
410 420
....*....|....*....|.
gi 535686385 371 YRTGDRGRYFADGQVAFLGRN 391
Cdd:cd12118 369 FHSGDLAVIHPDGYIEIKDRS 389
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
138-390 |
1.38e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 83.59 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 138 YIIFTSGSTGTPKGVMIDH----RAAMN----------TLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAAL 203
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifRMLMGgadfgtgeftPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 204 VLPeaGREKDPRH-WQTVMAHGHVS---VWNAVpaLMQMLCEYHSGDRMSYPTLRLALLSGdwipLTLPEQMRERLNETM 279
Cdd:cd05924 87 VLP--DDRFDPEEvWRTIEKHKVTSmtiVGDAM--ARPLIDALRDAGPYDLSSLFAISSGG----ALLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 280 D---IISLGGATECAIWSVYYPIGEVESTWTsipygRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGL-AQGYLNDAEK 355
Cdd:cd05924 159 PnitLVDAFGSSETGFTGSGHSAGSGPETGP-----FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAK 233
|
250 260 270
....*....|....*....|....*....|....*
gi 535686385 356 TAASFvwREASGERIYRTGDRGRYFADGQVAFLGR 390
Cdd:cd05924 234 TAETF--PEVDGVRYAVPGDRATVEADGTVTLLGR 266
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1-360 |
1.40e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 84.44 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRVQVTQPGLT-------QLEPSLPVLII-----DDGML--------DTPAAPLPEVAGDVTdlAYII 140
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALApvatavrDIVPLLSTVVVaggssDDSVLgyedllaeAGPAHAPVDIPNDSP--ALIM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 141 FTSGSTGTPKGVMIDHR----AAMNTLEDinerFGLNAQDRVFGLSSLSFDLSVYDAFAPF-MVGAALVLPEAGrEKDPR 215
Cdd:PRK07786 181 YTSGTTGRPKGAVLTHAnltgQAMTCLRT----NGADINSDVGFVGVPLFHIAGIGSMLPGlLLGAPTVIYPLG-AFDPG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 216 HWQTVMAHGHVSVWNAVPALMQMLCeyhsGDRMSYP-TLRLALLSGDWIPL--TLPEQMRERLNETMdIISLGGATECA- 291
Cdd:PRK07786 256 QLLDVLEAEKVTGIFLVPAQWQAVC----AEQQARPrDLALRVLSWGAAPAsdTLLRQMAATFPEAQ-ILAAFGQTEMSp 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 292 -------------IWSVYYPIGEVEstwtsipygrglrnqpVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAA 358
Cdd:PRK07786 331 vtcmllgedairkLGSVGKVIPTVA----------------ARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAE 394
|
..
gi 535686385 359 SF 360
Cdd:PRK07786 395 AF 396
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
19-393 |
2.80e-16 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 80.09 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVylpvdPVL--PPQRRQLLLTVgevrVQ 96
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV-----AALinYNLRGESLAHC----LN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 97 VTQPGltqlepslpVLIIddgmldtpaaplpevagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQD 176
Cdd:cd05940 73 VSSAK---------HLVV--------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 177 RVFGLSSLSFDLSVYDAF-APFMVGAALVLpeagREK--DPRHWQTVMAHgHVSVWNAVPALMQMLCEYHSGDRMSYPTL 253
Cdd:cd05940 124 VLYTCLPLYHSTALIVGWsACLASGATLVI----RKKfsASNFWDDIRKY-QATIFQYIGELCRYLLNQPPKPTERKHKV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 254 RLAL---LSGD-WipltlpEQMRERLNeTMDIISLGGATECAIWSVYYP--IGEVESTWTSIPYGRGLR--------NQP 319
Cdd:cd05940 199 RMIFgngLRPDiW------EEFKERFG-VPRIAEFYAATEGNSGFINFFgkPGAIGRNPSLLRKVAPLAlvkydlesGEP 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535686385 320 VYVLNAQLEECPVGVEGE-IC-IGGMGLAQGYLNDA--EKTAASFVWREasGERIYRTGDRGRYFADGQVAFLGR-NDT 393
Cdd:cd05940 272 IRDAEGRCIKVPRGEPGLlISrINPLEPFDGYTDPAatEKKILRDVFKK--GDAWFNTGDLMRLDGEGFWYFVDRlGDT 348
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
19-406 |
3.73e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 80.03 E-value: 3.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALgvqhgDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDP-VLPPQRRQLLLTVGEVRVQV 97
Cdd:PRK07787 24 RVLSRSDLAGAATAVAERVAGA-----RRVAVLATPTLATVLAVVGALIAGVPVVPVPPdSGVAERRHILADSGAQAWLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 98 TQPGLTQLEPSLPVLIIDDGmldtpAAPLPEVAGDVTdlAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDR 177
Cdd:PRK07787 99 PAPDDPAGLPHVPVRLHARS-----WHRYPEPDPDAP--ALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADDV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 178 -VFGLSSLSFDLSVYDAFAPFMVGAALVlpEAGREKDPRHWQTVMAHGhvSVWNAVPALMQMLCEyhsgDRMSYPTLRLA 256
Cdd:PRK07787 172 lVHGLPLFHVHGLVLGVLGPLRIGNRFV--HTGRPTPEAYAQALSEGG--TLYFGVPTVWSRIAA----DPEAARALRGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 257 --LLSGDwIPLTLPEQMRERLNETMDIISLGGATECAIWSVYYPIGEVESTWTSIPygrgLRNQPVYVLNAQLEECPVGV 334
Cdd:PRK07787 244 rlLVSGS-AALPVPVFDRLAALTGHRPVERYGMTETLITLSTRADGERRPGWVGLP----LAGVETRLVDEDGGPVPHDG 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535686385 335 E--GEICIGGMGLAQGYLNDAEKTAASFV---WreasgeriYRTGDRGRYFADGQVAFLGRNDTQ-VKVNGYRIELGE 406
Cdd:PRK07787 319 EtvGELQVRGPTLFDGYLNRPDATAAAFTadgW--------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGE 388
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
19-402 |
5.45e-16 |
|
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: 79.84 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVT 98
Cdd:cd05968 90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 QPGLTQ------LEPSL-----------PVLIIDDGMLDTPAAPL------PEVAG--------DVTDLAYIIFTSGSTG 147
Cdd:cd05968 170 ADGFTRrgrevnLKEEAdkacaqcptveKVVVVRHLGNDFTPAKGrdlsydEEKETagdgaertESEDPLMIIYTSGTTG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 148 TPKGVMIDH-----RAAMntleDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEA--GREKDPRHWQTV 220
Cdd:cd05968 250 KPKGTVHVHagfplKAAQ----DMYFQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGapDHPKADRLWRMV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 221 MAH--GHVSVW-NAVPALMQMLCEYHSGDRMSypTLRLALLSGD-WIPLTLPEQMRERLNETMDIISLGGATECA--IWS 294
Cdd:cd05968 326 EDHeiTHLGLSpTLIRALKPRGDAPVNAHDLS--SLRVLGSTGEpWNPEPWNWLFETVGKGRNPIINYSGGTEISggILG 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 295 VYY--PIGEVeSTWTSIPygrGL-------RNQPVyvlnaqleecpVGVEGEICIGG--MGLAQGYLNDAEKTAASFvWR 363
Cdd:cd05968 404 NVLikPIKPS-SFNGPVP---GMkadvldeSGKPA-----------RPEVGELVLLApwPGMTRGFWRDEDRYLETY-WS 467
|
410 420 430
....*....|....*....|....*....|....*....
gi 535686385 364 EASGERIYrtGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05968 468 RFDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRV 504
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
20-390 |
8.09e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 79.02 E-value: 8.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 20 ELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLtvgevrvqvtq 99
Cdd:cd05914 7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHIL----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 100 pgltqlEPSLPVLIIddgmldtpaaplpevAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVF 179
Cdd:cd05914 76 ------NHSEAKAIF---------------VSDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKIL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 180 GLSSLSFDLS-VYDAFAPFMVGAALVLpeagREKDPRHWQTVMAHGHVSVWNAVPALMQMLceyhsgdrMSYPTLRLALL 258
Cdd:cd05914 135 SILPLHHIYPlTFTLLLPLLNGAHVVF----LDKIPSAKIIALAFAQVTPTLGVPVPLVIE--------KIFKMDIIPKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 259 SGDWIPLTLP---------EQMRERLNET----MDIISLGGA-----------------------TECAIWSVYYPIGEV 302
Cdd:cd05914 203 TLKKFKFKLAkkinnrkirKLAFKKVHEAfggnIKEFVIGGAkinpdveeflrtigfpytigygmTETAPIISYSPPNRI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 303 ESTWTsipyGRGLRNQPVYVlnaqLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFV---WreasgeriYRTGDRGRY 379
Cdd:cd05914 283 RLGSA----GKVIDGVEVRI----DSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDkdgW--------FHTGDLGKI 346
|
410
....*....|.
gi 535686385 380 FADGQVAFLGR 390
Cdd:cd05914 347 DAEGYLYIRGR 357
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
4-390 |
1.59e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 77.92 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPI--RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPP 81
Cdd:PRK09088 4 HARLQPQRLAAVDLAlgRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 82 QRRQLLLTVGEVRVQVTQPGLTQLEP---SLPVLI--ID-DGMLDTPAAPLPEVagdvtdlAYIIFTSGSTGTPKGVMID 155
Cdd:PRK09088 84 SELDALLQDAEPRLLLGDDAVAAGRTdveDLAAFIasADaLEPADTPSIPPERV-------SLILFTSGTSGQPKGVMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 156 HRAAMNTLedINerFGLNAqdRVFGLSSLSFDLSVYDAFA-------PFMVGAALVLPEAGREKDPRHWQTVMAHGhVSV 228
Cdd:PRK09088 157 ERNLQQTA--HN--FGVLG--RVDAHSSFLCDAPMFHIIGlitsvrpVLAVGGSILVSNGFEPKRTLGRLGDPALG-ITH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 229 WNAVPALMQMLCEYHSGDRMSYPTLRlALLSG--------------DWIPLTLPEQMRERLNetmdiiSLGGATECAIWS 294
Cdd:PRK09088 230 YFCVPQMAQAFRAQPGFDAAALRHLT-ALFTGgaphaaedilgwldDGIPMVDGFGMSEAGT------VFGMSVDCDVIR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 295 vyypiGEVESTWTSIPyGRGLRnqpvyVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSGERIYRTG 374
Cdd:PRK09088 303 -----AKAGAAGIPTP-TVQTR-----VVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-----TGDGWFRTG 366
|
410
....*....|....*.
gi 535686385 375 DRGRYFADGQVAFLGR 390
Cdd:PRK09088 367 DIARRDADGFFWVVDR 382
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1-289 |
2.12e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 77.82 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALIS-----PIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV 75
Cdd:PRK07008 15 LIAHAARHAGDTEIVSrrvegDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 76 DPVLPPQrrQLLLTVGEVRVQVTQPGLT------QLEPSLP-----VLIIDDGMLDTPAAPL----------------PE 128
Cdd:PRK07008 95 NPRLFPE--QIAYIVNHAEDRYVLFDLTflplvdALAPQCPnvkgwVAMTDAAHLPAGSTPLlcyetlvgaqdgdydwPR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 129 VagDVTDLAYIIFTSGSTGTPKGVMIDHRAAM-----NTLEDInerFGLNAQDRVFGLSSLsFDLSVYD-AFAPFMVGAA 202
Cdd:PRK07008 173 F--DENQASSLCYTSGTTGNPKGALYSHRSTVlhaygAALPDA---MGLSARDAVLPVVPM-FHVNAWGlPYSAPLTGAK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 203 LVLPeaGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDwiplTLPEQMRERLNETMDI- 281
Cdd:PRK07008 247 LVLP--GPDLDGKSLYELIEAERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGS----ACPPAMIRTFEDEYGVe 320
|
....*....
gi 535686385 282 -ISLGGATE 289
Cdd:PRK07008 321 vIHAWGMTE 329
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
19-359 |
2.14e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 77.64 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVT 98
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 QPGL--------TQLEPSLPVLIIDDGMLDT-----------PAAPLP-EVAGDvtDLAYiifTSGSTGTPKGVmidhRA 158
Cdd:PRK08276 90 SAALadtaaelaAELPAGVPLLLVVAGPVPGfrsyeealaaqPDTPIAdETAGA--DMLY---SSGTTGRPKGI----KR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 159 AMNTLeDINERFGLNAqdRVFGLSSLSFDLSVYDAFAPFMVGAALvlpeagrekdpRHWQTVMAHGHVSV----WNAVPA 234
Cdd:PRK08276 161 PLPGL-DPDEAPGMML--ALLGFGMYGGPDSVYLSPAPLYHTAPL-----------RFGMSALALGGTVVvmekFDAEEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 235 LmqMLCEYHsgdRMSYptlrlallsGDWIP------LTLPEQMRERlnetMDIISL----GGATECAI--------W--- 293
Cdd:PRK08276 227 L--ALIERY---RVTH---------SQLVPtmfvrmLKLPEEVRAR----YDVSSLrvaiHAAAPCPVevkramidWwgp 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535686385 294 --SVYYPIGE------VES-TWTSIP--YGRGLRNQpVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAAS 359
Cdd:PRK08276 289 iiHEYYASSEgggvtvITSeDWLAHPgsVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA 364
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
9-390 |
2.76e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 77.33 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVA--------VVMEKGWQQIA-----AVHGILRL------- 68
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVAllslnrpeVLMAIGAAQLAglrrtALHPLGSLddhayvl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 69 ---GAVYLPVDPVLPPQRRQLLLTvgevRVqvtqPGLTQLEPSLPVLI-IDDGMLDTPAAPLPEVAGDV-TDLAYIIFTS 143
Cdd:PRK06188 106 edaGISTLIVDPAPFVERALALLA----RV----PSLKHVLTLGPVPDgVDLLAAAAKFGPAPLVAAALpPDIAGLAYTG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 144 GSTGTPKGVMIDHR--AAMNTLedINERFGLNAQDRVFGLSSLSFdlsvydafapfmVGAALVLPEAGR-------EK-D 213
Cdd:PRK06188 178 GTTGKPKGVMGTHRsiATMAQI--QLAEWEWPADPRFLMCTPLSH------------AGGAFFLPTLLRggtvivlAKfD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 214 PRHWQTVMAHGHVSVWNAVPALMQMLceyhsgdrMSYPTLRLALLSG-DWI-----PLTlPeqmrERLNETMDIISlgga 287
Cdd:PRK06188 244 PAEVLRAIEEQRITATFLVPTMIYAL--------LDHPDLRTRDLSSlETVyygasPMS-P----VRLAEAIERFG---- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 288 tecAIWSVYYPIGEVESTWTSIPYGRGLRNQP--------------VYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDA 353
Cdd:PRK06188 307 ---PIFAQYYGQTEAPMVITYLRKRDHDPDDPkrltscgrptpglrVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRP 383
|
410 420 430
....*....|....*....|....*....|....*....
gi 535686385 354 EKTAASFV--WreasgeriYRTGDRGRYFADGQVAFLGR 390
Cdd:PRK06188 384 EETAEAFRdgW--------LHTGDVAREDEDGFYYIVDR 414
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
135-390 |
5.64e-15 |
|
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: 75.23 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPEAgrEKDP 214
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVA--VFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 215 RHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNeTMDIISLGGATECAIWS 294
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELG-FETVLTAYGLTEAGVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 295 VYYPIGEVESTWTSIpyGRGLRNQpvyvlnaqleECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwrEASGerIYRTG 374
Cdd:cd17638 158 MCRPGDDAETVATTC--GRACPGF----------EVRIADDGEVLVRGYNVMQGYLDDPEATAEAI---DADG--WLHTG 220
|
250
....*....|....*.
gi 535686385 375 DRGRYFADGQVAFLGR 390
Cdd:cd17638 221 DVGELDERGYLRITDR 236
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-157 |
6.77e-15 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 76.07 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPI-RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVL 79
Cdd:PRK07514 8 ALRAAFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 80 PPQRRQLLLTVGEVRVQVTQPG-------LTQLEPSLPVLIIDD---GMLDTPAAPLPE----VAGDVTDLAYIIFTSGS 145
Cdd:PRK07514 88 TLAELDYFIGDAEPALVVCDPAnfawlskIAAAAGAPHVETLDAdgtGSLLEAAAAAPDdfetVPRGADDLAAILYTSGT 167
|
170
....*....|..
gi 535686385 146 TGTPKGVMIDHR 157
Cdd:PRK07514 168 TGRSKGAMLSHG 179
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
18-390 |
2.75e-14 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 74.43 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 18 IRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRV-- 95
Cdd:cd05932 4 VVEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKAlf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 96 -------QVTQPGL-----TQLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTD---LAYIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:cd05932 84 vgklddwKAMAPGVpegliSISLPPPSAANCQYQWDDLIAQHPPLEERPTRFpeqLATLIYTSGTTGQPKGVMLTFGSFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFGLNAQDRVFGLSSLSFDLS-VYDAFAPFMVGAALVLPEA--------GREKD------PRHWqTVMAHGh 225
Cdd:cd05932 164 WAAQAGIEHIGTEENDRMLSYLPLAHVTErVFVEGGSLYGGVLVAFAESldtfvedvQRARPtlffsvPRLW-TKFQQG- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 226 vsVWNAVPA----------LMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRerlNETMDIISLGGATE-CAIWS 294
Cdd:cd05932 242 --VQDKIPQqklnlllkipVVNSLVKRKVLKGLGLDQCRLAGCGSAPVPPALLEWYR---SLGLNILEAYGMTEnFAYSH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 295 VYYPigevestwtsipygrgLRNQPVYVLNA-QLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwrEASGerIYRT 373
Cdd:cd05932 317 LNYP----------------GRDKIGTVGNAgPGVEVRISEDGEILVRSPALMMGYYKDPEATAEAF---TADG--FLRT 375
|
410
....*....|....*..
gi 535686385 374 GDRGRYFADGQVAFLGR 390
Cdd:cd05932 376 GDKGELDADGNLTITGR 392
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
135-394 |
3.68e-14 |
|
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: 72.75 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFgLSSLSFDLS-VYDAFAPFMVGAALVLPE---AGR 210
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGgLAILVRSLLAGAELVLLErnqALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 211 EKDPRHWQTvmahgHVSVwnaVPALMQMLCEYHsGDRMSYPTLRLALLSGDWIPLTLPEQMRERlneTMDIISLGGATEC 290
Cdd:cd17630 80 EDLAPPGVT-----HVSL---VPTQLQRLLDSG-QGPAALKSLRAVLLGGAPIPPELLERAADR---GIPLYTTYGMTET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 291 AiwsvyypiGEVeSTWTSIPYGRGLrnqpVYVLNAQLEECpVGVEGEICIGGMGLAQGYLNDAEKtaasfvwREASGERI 370
Cdd:cd17630 148 A--------SQV-ATKRPDGFGRGG----VGVLLPGRELR-IVEDGEIWVGGASLAMGYLRGQLV-------PEFNEDGW 206
|
250 260
....*....|....*....|....
gi 535686385 371 YRTGDRGRYFADGQVAFLGRNDTQ 394
Cdd:cd17630 207 FTTKDLGELHADGRLTVLGRADNM 230
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
16-405 |
3.96e-14 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 73.79 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 16 SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGavyLPVDPVLPpqrrqlllTVGEVRV 95
Cdd:cd17639 1 GEYKYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYA--------TLGEDAL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 96 QVtqpGLTQLEPSLpvlIIDDGMLDtpaaplpevagdvtDLAYIIFTSGSTGTPKGVMIDHR---AAMNTLED-INERfg 171
Cdd:cd17639 70 IH---SLNETECSA---IFTDGKPD--------------DLACIMYTSGSTGNPKGVMLTHGnlvAGIAGLGDrVPEL-- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 172 LNAQDRV-----------FGLSSLSF------------------------DLSVYDAFapFMVGAALVLP------EAGR 210
Cdd:cd17639 128 LGPDDRYlaylplahifeLAAENVCLyrggtigygsprtltdkskrgckgDLTEFKPT--LMVGVPAIWDtirkgvLAKL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 211 EKDPRHWQTVMAHGhvsvWNAVPALMQMLCEYHSGDRMSYPTLRLAL-------LSGDwIPLTLPEQmrERLNETMDIIS 283
Cdd:cd17639 206 NPMGGLKRTLFWTA----YQSKLKALKEGPGTPLLDELVFKKVRAALggrlrymLSGG-APLSADTQ--EFLNIVLCPVI 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 284 LG-GATE-CAIWSVyypigeveSTWTSIPYGR-GlrnQPVYVLNAQLEECPVG--------VEGEICIGGMGLAQGYLND 352
Cdd:cd17639 279 QGyGLTEtCAGGTV--------QDPGDLETGRvG---PPLPCCEIKLVDWEEGgystdkppPRGEILIRGPNVFKGYYKN 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 535686385 353 AEKTAASFvwreaSGERIYRTGDRGRYFADGQVAFLGRNDTQVKV-NGYRIELG 405
Cdd:cd17639 348 PEKTKEAF-----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEYIALE 396
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-390 |
6.21e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 74.05 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALI------SPIRELTYRQLSTAADHVARALLALGvQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLP 74
Cdd:PRK05691 15 LQRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 75 VDPvlPPQRRQ----------------LLLTVGEVRvqvtqPGLTQLE----PSLPVLIIDDGMLDTPAAPLPEVAGDVT 134
Cdd:PRK05691 94 AYP--PESARRhhqerllsiiadaeprLLLTVADLR-----DSLLQMEelaaANAPELLCVDTLDPALAEAWQEPALQPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFG--LNAQDRVFGLSSLSFDLSVYDA-FAPFMVGAALVL--PEAG 209
Cdd:PRK05691 167 DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGlLQPIFSGVPCVLmsPAYF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 210 REKdPRHWQTVMAH--GHVSvwnAVPALMQMLCEyhsgDRMSYPTLRLALLSGDWIPLTLPEQMRE-RLNETMDIISLGG 286
Cdd:PRK05691 247 LER-PLRWLEAISEygGTIS---GGPDFAYRLCS----ERVSESALERLDLSRWRVAYSGSEPIRQdSLERFAEKFAACG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 287 ATECAIWSVYypiGEVESTW--TSIPYGRGL---------------------------RNQP---VYVLNAQ-LEECPVG 333
Cdd:PRK05691 319 FDPDSFFASY---GLAEATLfvSGGRRGQGIpaleldaealarnraepgtgsvlmscgRSQPghaVLIVDPQsLEVLGDN 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 535686385 334 VEGEICIGGMGLAQGYLNDAEKTAASFVwrEASGERIYRTGDRGrYFADGQVAFLGR 390
Cdd:PRK05691 396 RVGEIWASGPSIAHGYWRNPEASAKTFV--EHDGRTWLRTGDLG-FLRDGELFVTGR 449
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
18-177 |
7.33e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 73.12 E-value: 7.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 18 IRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVD-PVLPPQR----RQL--LLTV 90
Cdd:PRK09192 47 EEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGResyiAQLrgMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 91 GEVRVQVTQPGLTQL-----EPSLPVLIIDDGMLDTPAAP---LPEVAGDvtDLAYIIFTSGSTGTPKGVMIDHRAAMNT 162
Cdd:PRK09192 127 AQPAAIITPDELLPWvneatHGNPLLHVLSHAWFKALPEAdvaLPRPTPD--DIAYLQYSSGSTRFPRGVIITHRALMAN 204
|
170
....*....|....*..
gi 535686385 163 LEDINeRFGLN--AQDR 177
Cdd:PRK09192 205 LRAIS-HDGLKvrPGDR 220
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
5-403 |
8.79e-14 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 72.87 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAvylpvDPVL----- 79
Cdd:PRK13382 53 AQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGA-----DILLlntsf 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 80 -PPQRRQLLLTVGEVRVQVTQ-------------PGLTQLE--PSLPVLIIDDGMLDTPAAPLPEVAGDVTDLayIIFTS 143
Cdd:PRK13382 128 aGPALAEVVTREGVDTVIYDEefsatvdraladcPQATRIVawTDEDHDLTVEVLIAAHAGQRPEPTGRKGRV--ILLTS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 144 GSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVF---------GLSSLSFDLSvydaFAPFMVGAALVLPEAGREKDP 214
Cdd:PRK13382 206 GTTGTPKGARRSGPGGIGTLKAILDRTPWRAEEPTVivapmfhawGFSQLVLAAS----LACTIVTRRRFDPEATLDLID 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 215 RHWQTVMAhghvsvwnAVPALMQMLCEY--HSGDRMSYPTLRLALLSGDWIPltlPEQMRERLNETMDIIslggatecai 292
Cdd:PRK13382 282 RHRATGLA--------VVPVMFDRIMDLpaEVRNRYSGRSLRFAAASGSRMR---PDVVIAFMDQFGDVI---------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 293 wsvYYPIGEVESTWTSIPYGRGLRNQP-----------VYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEK-TAASF 360
Cdd:PRK13382 341 ---YNNYNATEAGMIATATPADLRAAPdtagrpaegteIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKdFHDGF 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 535686385 361 VwreasgeriyRTGDRGRYFADGQVAFLGRNDTQVKVNG---YRIE 403
Cdd:PRK13382 418 M----------ASGDVGYLDENGRLFVVGRDDEMIVSGGenvYPIE 453
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
3-390 |
1.19e-13 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 72.20 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALISPIRELTYRQLSTAADHVARALL-ALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPP 81
Cdd:PRK06839 10 KRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 82 QRRQLLLTVGEVRVQVTQPGLTQLEPSL-------PVLIIDD--GMLDTPAAPLPEVAGDVTDLayIIFTSGSTGTPKGV 152
Cdd:PRK06839 90 NELIFQLKDSGTTVLFVEKTFQNMALSMqkvsyvqRVISITSlkEIEDRKIDNFVEKNESASFI--ICYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 153 MIDHR----AAMNTLEDINerfgLNAQDRVFGLSSLsFDLSVYDAFA--PFMVGAALVLPeagREKDPRHWQTVMAHGHV 226
Cdd:PRK06839 168 VLTQEnmfwNALNNTFAID----LTMHDRSIVLLPL-FHIGGIGLFAfpTLFAGGVIIVP---RKFEPTKALSMIEKHKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 227 SVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLnetmdiISLG---GATECAiwSVYYPIGEVE 303
Cdd:PRK06839 240 TVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRG------FLFGqgfGMTETS--PTVFMLSEED 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 304 STWTSIPYGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAasfvwrEASGERIYRTGDRGRYFADG 383
Cdd:PRK06839 312 ARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATE------ETIQDGWLCTGDLARVDEDG 385
|
....*..
gi 535686385 384 QVAFLGR 390
Cdd:PRK06839 386 FVYIVGR 392
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1-185 |
2.89e-13 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 71.19 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETAL--ISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPV 78
Cdd:PRK05857 20 VFEQARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 79 LPPQRRQLLLTVGEVRVQVTQPG-------LTQLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAY-------IIFTSG 144
Cdd:PRK05857 100 LPIAAIERFCQITDPAAALVAPGskmassaVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQgsedplaMIFTSG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 535686385 145 STGTPKGVMIDHRAAMnTLEDINERFGLNAQDRVFGLSSLS 185
Cdd:PRK05857 180 TTGEPKAVLLANRTFF-AVPDILQKEGLNWVTWVVGETTYS 219
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1-233 |
3.19e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 71.13 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAA-LTPQETALI--------SPIRE-LTYRQLSTAADHVARALLALGVqHGDRVAVVMEKGWQQIAAVHGILRLG- 69
Cdd:PRK05850 6 LLRERAsLQPDDAAFTfidyeqdpAGVAEtLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 70 -AVYLPVdpvlpPQRRQ---------------LLLT----VGEVRVQVTQPgltQLEPSLPVLIIDDGMLDTPAAPLPeV 129
Cdd:PRK05850 85 iAVPLSV-----PQGGAhdervsavlrdtspsVVLTtsavVDDVTEYVAPQ---PGQSAPPVIEVDLLDLDSPRGSDA-R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 130 AGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERF-----GLNAQDRVFgLSSLSF--DLS-VYDAFAPFMVG- 200
Cdd:PRK05850 156 PRDLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtgGVPPPDTTV-VSWLPFyhDMGlVLGVCAPILGGc 234
|
250 260 270
....*....|....*....|....*....|....
gi 535686385 201 -AALVLPEAGREKdPRHWQTVMAhGHVSVWNAVP 233
Cdd:PRK05850 235 pAVLTSPVAFLQR-PARWMQLLA-SNPHAFSAAP 266
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1-392 |
3.74e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 70.73 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALT-PQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAV-----------------------VMEKGW 56
Cdd:PRK07788 54 LVAHAARRaPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVlarnhrgfvlalyaagkvgariiLLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 57 --QQIAAVhgILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTQP-GLTQLEPSLPVL--IIDDGmlDTPAAPLPEVAG 131
Cdd:PRK07788 134 sgPQLAEV--AAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGNPdDDEPSGSTDETLddLIAGS--STAPLPKPPKPG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 132 dvtdlAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPeagRE 211
Cdd:PRK07788 210 -----GIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLR---RR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 212 KDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPT--LRLALLSGDWIPLTLPEQMRERLNETmdIISLGGATE 289
Cdd:PRK07788 282 FDPEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTssLKIIFVSGSALSPELATRALEAFGPV--LYNLYGSTE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 290 CAIWSVYYPIGEVESTWTSIPYGRGLRnqpVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKtaasfvwreasgER 369
Cdd:PRK07788 360 VAFATIATPEDLAEAPGTVGRPPKGVT---VKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDK------------QI 424
|
410 420
....*....|....*....|....*.
gi 535686385 370 I---YRTGDRGRYFADGQVAFLGRND 392
Cdd:PRK07788 425 IdglLSSGDVGYFDEDGLLFVDGRDD 450
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
20-302 |
5.14e-13 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 70.58 E-value: 5.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 20 ELTYRQLSTAADHVARALL-ALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVT 98
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 QPGLT-QLEPSLP-------VLIIDDGMLDTPAAPLPE----------VAG----------DVTDLAYIIFTSGSTGTPK 150
Cdd:PRK05620 118 DPRLAeQLGEILKecpcvraVVFIGPSDADSAAAHMPEgikvysyealLDGrstvydwpelDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 151 GVMIDHRAAMntLEDINerfgLNAQDRVFGLSSLSFDLSV--YDA------FAPFMVGAALVLPeaGREKDPRHWQTVMA 222
Cdd:PRK05620 198 GVVYSHRSLY--LQSLS----LRTTDSLAVTHGESFLCCVpiYHVlswgvpLAAFMSGTPLVFP--GPDLSAPTLAKIIA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 223 HGHVSVWNAVPAL-MQMLCEY--HSGDRMSyptLRLALLSGDWIPLTLPEQMRERLNetMDIISLGGATECAiwsvyyPI 299
Cdd:PRK05620 270 TAMPRVAHGVPTLwIQLMVHYlkNPPERMS---LQEIYVGGSAVPPILIKAWEERYG--VDVVHVWGMTETS------PV 338
|
...
gi 535686385 300 GEV 302
Cdd:PRK05620 339 GTV 341
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
135-402 |
5.79e-13 |
|
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: 69.60 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDI-NERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLpeAGREKD 213
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILqKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVT--GGENTT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 214 PRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIpltlpeqmrerLNETMDIISLGGATECAIw 293
Cdd:cd17635 80 YKSLFKILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRA-----------IAADVRFIEATGLTNTAQ- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 294 svYYPIGEVeSTWTSIPYGRGLRN----------QPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVwr 363
Cdd:cd17635 148 --VYGLSET-GTALCLPTDDDSIEinavgrpypgVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-- 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 535686385 364 easgERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd17635 223 ----DGWVNTGDLGERREDGFLFITGRSSESINCGGVKI 257
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
5-399 |
7.49e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 70.03 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRR 84
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 85 QLLLTVGEVRVQVTQPGLTQLEPSL--PVLIIDD---GMLDTPAAPLPEVAGDVtdlayIIFTSGSTGTPKGV--MIDHR 157
Cdd:PRK13383 125 AAALRAHHISTVVADNEFAERIAGAddAVAVIDPataGAEESGGRPAVAAPGRI-----VLLTSGTTGKPKGVprAPQLR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 158 AAMNTLEDINERFGLNAQDRVfglsSLSFDLSVYDAFAPFMVGAALvlpeAGREKDPRHWQTVMAHGHVSV-----WNAV 232
Cdd:PRK13383 200 SAVGVWVTILDRTRLRTGSRI----SVAMPMFHGLGLGMLMLTIAL----GGTVLTHRHFDAEAALAQASLhradaFTAV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 233 PALMQMLCEY--HSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETMdiISLGGATECAIWSVYYPIGEVESTWTsip 310
Cdd:PRK13383 272 PVVLARILELppRVRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDIL--YNGYGSTEVGIGALATPADLRDAPET--- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 311 YGRGLRNQPVYVLNAQLEecPVG--VEGEICIGGMGLAQGYLNDAEKtaasfvwreASGERIYRTGDRGRYFADGQVAFL 388
Cdd:PRK13383 347 VGKPVAGCPVRILDRNNR--PVGprVTGRIFVGGELAGTRYTDGGGK---------AVVDGMTSTGDMGYLDNAGRLFIV 415
|
410
....*....|.
gi 535686385 389 GRNDTQVKVNG 399
Cdd:PRK13383 416 GREDDMIISGG 426
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
5-383 |
1.35e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 68.95 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPI--RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ 82
Cdd:PRK13391 7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 83 RRQLLLTVGEVRVQVTQ-------PGLTQLEPSL-PVLIID-DGMLD-----------TPAAPLP-EVAGdvTDLAYiif 141
Cdd:PRK13391 87 EAAYIVDDSGARALITSaakldvaRALLKQCPGVrHRLVLDgDGELEgfvgyaeavagLPATPIAdESLG--TDMLY--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 142 TSGSTGTPKGVmidhRAAMNTLEdINERFGLNAQ-DRVFGLSSLSFDLS---VYDAfAPFM-------VGAALVLPEAgr 210
Cdd:PRK13391 162 SSGTTGRPKGI----KRPLPEQP-PDTPLPLTAFlQRLWGFRSDMVYLSpapLYHS-APQRavmlvirLGGTVIVMEH-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 211 eKDPRHW-QTVMAHGhVSVWNAVPALMQMLCEYHSGDRMSY--PTLRLALLSGDWIPLTLPEQMRERLNETMDiiSLGGA 287
Cdd:PRK13391 234 -FDAEQYlALIEEYG-VTHTQLVPTMFSRMLKLPEEVRDKYdlSSLEVAIHAAAPCPPQVKEQMIDWWGPIIH--EYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 288 TE----CAIWSvyypigeveSTWTSIP--YGRGLRNQPvYVLNAQLEECPVGVEGEICIGGmGLAQGYLNDAEKTAASfv 361
Cdd:PRK13391 310 TEglgfTACDS---------EEWLAHPgtVGRAMFGDL-HILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEA-- 376
|
410 420
....*....|....*....|..
gi 535686385 362 wREASGErIYRTGDRGRYFADG 383
Cdd:PRK13391 377 -RHPDGT-WSTVGDIGYVDEDG 396
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1-379 |
1.36e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 69.30 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTP------QETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQqiaavHGILRLGA--VY 72
Cdd:PRK12582 55 LAKWAAEAPdrpwlaQREPGHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIE-----HALMTLAAmqAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 73 LPVDPVLPP--------QRRQLLLTVGEVRVQVTQPG------LTQLEPSLPVLIIDDGMLD-TPAAPLPE-VAGDVTD- 135
Cdd:PRK12582 130 VPAAPVSPAyslmshdhAKLKHLFDLVKPRVVFAQSGapfaraLAALDLLDVTVVHVTGPGEgIASIAFADlAATPPTAa 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 136 ------------LAYIIFTSGSTGTPKGVMIDHR------AAMNTLEDI---------------NERFGLNAqdrvfgls 182
Cdd:PRK12582 210 vaaaiaaitpdtVAKYLFTSGSTGMPKAVINTQRmmcaniAMQEQLRPRepdppppvsldwmpwNHTMGGNA-------- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 183 slsfdlsvydAFAPFMVGAALVLPEAGREKDPRHWQTVMAHGHVS--VWNAVPALMQMLCEYHSGD----RMSYPTLRLA 256
Cdd:PRK12582 282 ----------NFNGLLWGGGTLYIDDGKPLPGMFEETIRNLREISptVYGNVPAGYAMLAEAMEKDdalrRSFFKNLRLM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 257 LLSGdwipLTLPEQMRERLN--------ETMDIISLGGATECA--IWSVYYPIGEVestwtsipygrGLRNQPVYVLnaQ 326
Cdd:PRK12582 352 AYGG----ATLSDDLYERMQalavrttgHRIPFYTGYGATETAptTTGTHWDTERV-----------GLIGLPLPGV--E 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 535686385 327 LEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSGERIYRTGDRGRY 379
Cdd:PRK12582 415 LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF-----DEEGFYRLGDAARF 462
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
17-403 |
1.86e-12 |
|
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: 68.54 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 17 PIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPvdpvlppqrRQLLLTVGEVRVQ 96
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVV---------RGSDSSVEELLYI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 97 vtqpgltqLEPSLPVLIIddgmldtpaaplpeVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQD 176
Cdd:cd17640 73 --------LNHSESVALV--------------VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 177 RVfgLSSL----SFDLSV-YDAFApfmVGAALVLPEAGREKD-------------PRHWQTVMAHGHVSVwNAVPALMQM 238
Cdd:cd17640 131 RF--LSILpiwhSYERSAeYFIFA---CGCSQAYTSIRTLKDdlkrvkphyivsvPRLWESLYSGIQKQV-SKSSPIKQF 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 239 LCEYH-SGDRmsyptLRLALLSGDWIPLTLpeqmrERLNETMDIISLG--GATECAiwsvyyPIGEVESTWTSIpygRGL 315
Cdd:cd17640 205 LFLFFlSGGI-----FKFGISGGGALPPHV-----DTFFEAIGIEVLNgyGLTETS------PVVSARRLKCNV---RGS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 316 RNQPVYVLNAQL------EECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSGERIYRTGDRGRYFADGQVAFLG 389
Cdd:cd17640 266 VGRPLPGTEIKIvdpegnVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVL-----DSDGWFNTGDLGWLTCGGELVLTG 340
|
410
....*....|....*
gi 535686385 390 R-NDTQVKVNGYRIE 403
Cdd:cd17640 341 RaKDTIVLSNGENVE 355
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
19-399 |
2.29e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 68.60 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVArALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV-DPVLPPQRRQL----------- 86
Cdd:PRK07769 54 RDLTWSQFGARNRAVG-ARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHVGRLhavlddctpsa 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 87 LLTVGEVRVQVTQPGLTQLEPSLPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDI 166
Cdd:PRK07769 133 ILTTTDSAEGVRKFFRARPAKERPRVIAVDAVPDEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 167 NERFGLNAQDRvfGLSSLSF--DLSVYDAFAPFMVGAALVL--PEAGREKdPRHWQTVMA---HGHVSVWNAVPALMQML 239
Cdd:PRK07769 213 IDALEGQEGDR--GVSWLPFfhDMGLITVLLPALLGHYITFmsPAAFVRR-PGRWIRELArkpGGTGGTFSAAPNFAFEH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 240 CEYHSGDRMSYPTLRL----ALLSGDWiPLTlPEQMReRLNETMdiiSLGGATECAIWSVYypiGEVESTW--TSIPygr 313
Cdd:PRK07769 290 AAARGLPKDGEPPLDLsnvkGLLNGSE-PVS-PASMR-KFNEAF---APYGLPPTAIKPSY---GMAEATLfvSTTP--- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 314 gLRNQP--VYV----LNAQ----------------------------------LEECPVGVEGEICIGGMGLAQGYLNDA 353
Cdd:PRK07769 358 -MDEEPtvIYVdrdeLNAGrfvevpadapnavaqvsagkvgvsewavivdpetASELPDGQIGEIWLHGNNIGTGYWGKP 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 354 EKTAASFvwREASGERI--------------YRTGDRGRYFaDGQVAFLGRNDTQVKVNG 399
Cdd:PRK07769 437 EETAATF--QNILKSRLseshaegapddalwVRTGDYGVYF-DGELYITGRVKDLVIIDG 493
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
21-402 |
3.75e-12 |
|
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: 67.59 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVdpvlppqrrQLLLTVGEVRVQVtQP 100
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA---------TTLLTPDDLRDRV-DR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 101 GLTQLEPSLPVLIIDDGMLdtpaaplpevagdvtdlayIIFTSGSTGTPKGVMIDHRA----AMNTLEDInerfGLNAQD 176
Cdd:cd05974 71 GGAVYAAVDENTHADDPML-------------------LYFTSGTTSKPKLVEHTHRSypvgHLSTMYWI----GLKPGD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 177 RVFGLSSLSFDLSVYDA-FAPFMVGAALVLPEAGReKDPRHWQTVMAHGHVSVWNAVPALMQMLCEyhsGDRMSYPT-LR 254
Cdd:cd05974 128 VHWNISSPGWAKHAWSCfFAPWNAGATVFLFNYAR-FDAKRVLAALVRYGVTTLCAPPTVWRMLIQ---QDLASFDVkLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 255 LALLSGDWIPLTLPEQMRERLNETmdIISLGGATECAIWSVYYPiGEVESTWTsipYGRGLRNQPVYVLNAQLEEcpvGV 334
Cdd:cd05974 204 EVVGAGEPLNPEVIEQVRRAWGLT--IRDGYGQTETTALVGNSP-GQPVKAGS---MGRPLPGYRVALLDPDGAP---AT 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535686385 335 EGEICIG-----GMGLAQGYLNDAEKTAasfvwrEASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05974 275 EGEVALDlgdtrPVGLMKGYAGDPDKTA------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRI 341
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
21-402 |
9.90e-12 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 66.44 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLA-LGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQ--RRQLLLTVGEVRVQV 97
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRelKHQLIDSGASVLVVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 98 TQPGLT--QLEPSLPV-LIIDDG---MLDTPAAPL-----------------------------------PEVAGDVTDL 136
Cdd:PRK08751 131 DNFGTTvqQVIADTPVkQVITTGlgdMLGFPKAALvnfvvkyvkklvpeyringairfrealalgrkhsmPTLQIEPDDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 137 AYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfGLSSLSFDLSVYDAFApfMVGAALVLPEAG------- 209
Cdd:PRK08751 211 AFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEE-GCEVVITALPLYHIFA--LTANGLVFMKIGgcnhlis 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 210 REKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEQMRERLNETMdiISLGGATE 289
Cdd:PRK08751 288 NPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIDFSSLKMTLGGGMAVQRSVAERWKQVTGLTL--VEAYGLTE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 290 CAIWSVYYPIGEVE---STWTSIPygrglrNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwrEAS 366
Cdd:PRK08751 366 TSPAACINPLTLKEyngSIGLPIP------STDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVM---DAD 436
|
410 420 430
....*....|....*....|....*....|....*.
gi 535686385 367 GerIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:PRK08751 437 G--WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNV 470
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
19-359 |
9.93e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 66.54 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVT 98
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 QPG----LTQL--EPSLPVLIIDDG---------MLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTL 163
Cdd:PLN02246 129 QSCyvdkLKGLaeDDGVTVVTIDDPpegclhfseLTQADENELPEVEISPDDVVALPYSSGTTGLPKGVMLTHKGLVTSV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 164 EDI----NERFGLNAQDRV------FGLSSLSfdlSVYdaFAPFMVGAALVLPEagREKDPRHWQTVMAHGhVSVWNAVP 233
Cdd:PLN02246 209 AQQvdgeNPNLYFHSDDVIlcvlpmFHIYSLN---SVL--LCGLRVGAAILIMP--KFEIGALLELIQRHK-VTIAPFVP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 234 ALMQMLCEYHSGDRMSYPTLRLaLLSGDwIPL--TLPEQMRERLNETmdIISLG-GATE-------C-AIWSVYYPI--- 299
Cdd:PLN02246 281 PIVLAIAKSPVVEKYDLSSIRM-VLSGA-APLgkELEDAFRAKLPNA--VLGQGyGMTEagpvlamClAFAKEPFPVksg 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535686385 300 --GEV----------ESTWTSIPygrglRNQPvyvlnaqleecpvgveGEICIGGMGLAQGYLNDAEKTAAS 359
Cdd:PLN02246 357 scGTVvrnaelkivdPETGASLP-----RNQP----------------GEICIRGPQIMKGYLNDPEATANT 407
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1-390 |
1.79e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 65.75 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALI--------SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVY 72
Cdd:PRK07529 31 LSRAAARHPDAPALSflldadplDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 73 lPVDPVLPPQRRQLLLTVGEVRVQVT-------------QPGLTQLEPSLPVLIIDDGMLDTPAAPLP------------ 127
Cdd:PRK07529 111 -PINPLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwqkvAEVLAALPELRTVVEVDLARYLPGPKRLAvplirrkahari 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 128 -----EVAGD------------VTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFglsslsFDLSV 190
Cdd:PRK07529 190 ldfdaELARQpgdrlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVF------CGLPL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 191 YDAFA-------PFMVGAALVLPEAGREKDP----RHWQTVmAHGHVSVWNAVP----ALMQMLCEYHSGDrmsypTLRL 255
Cdd:PRK07529 264 FHVNAllvtglaPLARGAHVVLATPQGYRGPgviaNFWKIV-ERYRINFLSGVPtvyaALLQVPVDGHDIS-----SLRY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 256 ALLSGDWIPLTLPEQMRERLNETmdIISLGGATECA-IWSVYYPIGEVESTWTSIPygrgLRNQPVYVL-----NAQLEE 329
Cdd:PRK07529 338 ALCGAAPLPVEVFRRFEAATGVR--IVEGYGLTEATcVSSVNPPDGERRIGSVGLR----LPYQRVRVVilddaGRYLRD 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 535686385 330 CPVGVEGEICIGGMGLAQGYLNdAEKTAASFVwreasGERIYRTGDRGRYFADGQVAFLGR 390
Cdd:PRK07529 412 CAVDEVGVLCIAGPNVFSGYLE-AAHNKGLWL-----EDGWLNTGDLGRIDADGYFWLTGR 466
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
22-402 |
2.25e-11 |
|
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: 65.18 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 22 TYRQLSTAADHVARALL-ALGVQHGDRVAVVMEK--GWQQIAAvhGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVT 98
Cdd:cd05928 43 SFRELGSLSRKAANVLSgACGLQRGDRVAVILPRvpEWWLVNV--ACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 QPGLTQLE-------PSLPV-LIID----DGMLDtpaapLPEVAGDVT-----------DLAYIIFTSGSTGTPKgvMID 155
Cdd:cd05928 121 SDELAPEVdsvasecPSLKTkLLVSeksrDGWLN-----FKELLNEAStehhcvetgsqEPMAIYFTSGTTGSPK--MAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 156 HRAAMNTLE-DINERF--GLNAQDRVFGLSSLSFDLSVYDA-FAPFMVGAALVLPEAGReKDPRHWQTVMAHGHVSVWNA 231
Cdd:cd05928 194 HSHSSLGLGlKVNGRYwlDLTASDIMWNTSDTGWIKSAWSSlFEPWIQGACVFVHHLPR-FDPLVILKTLSSYPITTFCG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 232 VPALMQMLCEyHSGDRMSYPTLRLALLSGDWIpltLPEQMRERLNET-MDIISLGGATECAIWSVYYPIGEVESTWtsip 310
Cdd:cd05928 273 APTVYRMLVQ-QDLSSYKFPSLQHCVTGGEPL---NPEVLEKWKAQTgLDIYEGYGQTETGLICANFKGMKIKPGS---- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 311 YGRGLRNQPVYVLNAQLEECPVGVEGEICI-----GGMGLAQGYLNDAEKTAASFvwreaSGErIYRTGDRGRYFADGQV 385
Cdd:cd05928 345 MGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATI-----RGD-FYLTGDRGIMDEDGYF 418
|
410
....*....|....*..
gi 535686385 386 AFLGRNDTQVKVNGYRI 402
Cdd:cd05928 419 WFMGRADDVINSSGYRI 435
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1-179 |
2.94e-11 |
|
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: 64.98 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAalTPQETALI-----SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV 75
Cdd:cd05943 76 LLRHA--DADDPAAIyaaedGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSC 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 76 DPVLPPQ----R-RQ----LLLTVGEVR-----------VQVTQPGLTQLEPSL-----------------PVLIIDDGM 118
Cdd:cd05943 154 SPDFGVPgvldRfGQiepkVLFAVDAYTyngkrhdvrekVAELVKGLPSLLAVVvvpytvaagqpdlskiaKALTLEDFL 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535686385 119 LDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMidHRAAMNTLEDINE---RFGLNAQDRVF 179
Cdd:cd05943 234 ATGAAGELEFEPLPFDHPLYILYSSGTTGLPKCIV--HGAGGTLLQHLKEhilHCDLRPGDRLF 295
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
22-399 |
1.14e-10 |
|
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: 62.89 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 22 TYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQvtqpg 101
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKLKLNKVWNTLKN----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 102 ltqlepslPVLIIDDGMLDTpaapLPEvagdvtDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGL 181
Cdd:cd05908 92 --------PYLITEEEVLCE----LAD------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 182 SSLSFDLSVYdAF--APFMVGA-ALVLPEAGREKDPRHWQTVMAHGHVSV----------------------W------- 229
Cdd:cd05908 154 MPLTHDMGLI-AFhlAPLIAGMnQYLMPTRLFIRRPILWLKKASEHKATIvsspnfgykyflktlkpekandWdlssirm 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 230 --NAVPALMQMLCEyHSGDRMS---------YPTLRLALLSgdwIPLTLPEQmrerlNETMDIISLGGATEcaiwSVYYP 298
Cdd:cd05908 233 ilNGAEPIDYELCH-EFLDHMSkyglkrnaiLPVYGLAEAS---VGASLPKA-----QSPFKTITLGRRHV----THGEP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 299 IGEVEST----WTSIPYGRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSGERIYRTG 374
Cdd:cd05908 300 EPEVDKKdsecLTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVF-----TDDGWLKTG 374
|
410 420
....*....|....*....|....*
gi 535686385 375 DRGRYFaDGQVAFLGRNDTQVKVNG 399
Cdd:cd05908 375 DLGFIR-NGRLVITGREKDIIFVNG 398
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
5-353 |
1.60e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 62.49 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 5 AALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHgDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRR 84
Cdd:PRK07638 11 ASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 85 QLLLTVGEVRVQVTQPGLTQ--LEPSLPVLIIDDGMLDTP-AAPLPEVAGDVTDLA-YIIFTSGSTGTPKGVMIDHRAAM 160
Cdd:PRK07638 90 KERLAISNADMIVTERYKLNdlPDEEGRVIEIDEWKRMIEkYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQSWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 161 NTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPeagREKDPRHWQTVMAHGHVSVWNAVPAlmqMLC 240
Cdd:PRK07638 170 HSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLM---RKFIPNQVLDKLETENISVMYTVPT---MLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 241 EYHSGDRMSYPTLRLALLSGDWipltlPEQMRERLNETMDIISL---GGATECAIWSVYYPigeVESTWTSIPYGRGLRN 317
Cdd:PRK07638 244 SLYKENRVIENKMKIISSGAKW-----EAEAKEKIKNIFPYAKLyefYGASELSFVTALVD---EESERRPNSVGRPFHN 315
|
330 340 350
....*....|....*....|....*....|....*.
gi 535686385 318 QPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDA 353
Cdd:PRK07638 316 VQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGG 351
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1-382 |
2.90e-10 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 62.06 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALIS-----PIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV 75
Cdd:cd05921 1 LAHWARQAPDRTWLAEregngGWRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 76 DPVLPPQRRQL--------LLTVGEVRVQVTQP---GLTQLEPSLPVLIID------------DGMLDTPA-APLPEVAG 131
Cdd:cd05921 81 SPAYSLMSQDLaklkhlfeLLKPGLVFAQDAAPfarALAAIFPLGTPLVVSrnavagrgaisfAELAATPPtAAVDAAFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 132 DVT--DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSL--SFDLSVYDAFAPFMVGAALVLPE 207
Cdd:cd05921 161 AVGpdTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFFGEEPPVLVDWLpwNHTFGGNHNFNLVLYNGGTLYID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 208 AGREKDPRHWQTVMAHGHVS--VWNAVPALMQMLCEYHSGD----RMSYPTLRLALLSGdwipLTLPEQMRERLN----- 276
Cdd:cd05921 241 DGKPMPGGFEETLRNLREISptVYFNVPAGWEMLVAALEKDealrRRFFKRLKLMFYAG----AGLSQDVWDRLQalava 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 277 ---ETMDIISLGGATECAiwsvyyPIgeveSTWTSIPYGR-GLRNQPVYVLNAQLeeCPVGVEGEICIGGMGLAQGYLND 352
Cdd:cd05921 317 tvgERIPMMAGLGATETA------PT----ATFTHWPTERsGLIGLPAPGTELKL--VPSGGKYEVRVKGPNVTPGYWRQ 384
|
410 420 430
....*....|....*....|....*....|
gi 535686385 353 AEKTAASFvwreaSGERIYRTGDRGRyFAD 382
Cdd:cd05921 385 PELTAQAF-----DEEGFYCLGDAAK-LAD 408
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
20-163 |
3.36e-10 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 61.68 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 20 ELTYRQLSTAADHVArALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV------------DPVLPPQRRQLL 87
Cdd:PRK12476 68 ELTWTQLGVRLRAVG-ARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfapelpghaerlDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 88 LTVGEVRVQVTQ-----PGLTQlepslPVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNT 162
Cdd:PRK12476 147 LTTTAAAEAVEGflrnlPRLRR-----PRVIAIDAIPDSAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTN 221
|
.
gi 535686385 163 L 163
Cdd:PRK12476 222 L 222
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
135-402 |
5.49e-10 |
|
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: 60.11 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMVGAALVLPeagREKDP 214
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQ---RKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 215 RHWQTVMAHGHVSVWNAVPALMQMLCeyhsgdRMSYP--TLRLALLSGDWIPLTLPEQMRERLNETmDIISLGGATECAI 292
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALA------RTLEPesKIKSIFSSGQKLFESTKKKLKNIFPKA-NLIEFYGTSELSF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 293 --WSVYYPIGEVESTwtsipyGRGLRNQPVYVLNAQleecpVGVEGEICIGGMGLAQGYLNDAEKTAASfvWreasgeri 370
Cdd:cd17633 151 itYNFNQESRPPNSV------GRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDG--W-------- 209
|
250 260 270
....*....|....*....|....*....|..
gi 535686385 371 YRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINI 241
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
20-161 |
5.82e-10 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 60.82 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 20 ELTYRQL-STAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQrrQLLLTVGEVRVQV- 97
Cdd:cd05905 14 TLTWGKLlSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQ--QLGFLLGTCKVRVa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 98 -----TQPGL-TQLEPSLPVLIIDDGML--------DTP---AAPLPEVAGD----VTDLAYIIFTSGSTGTPKGVMIDH 156
Cdd:cd05905 92 ltveaCLKGLpKKLLKSKTAAEIAKKKGwpkildfvKIPkskRSKLKKWGPHpptrDGDTAYIEYSFSSDGSLSGVAVSH 171
|
....*
gi 535686385 157 RAAMN 161
Cdd:cd05905 172 SSLLA 176
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
3-402 |
5.95e-10 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 61.12 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALI------SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEkgwqQIA-AVHGIL---RLGAVY 72
Cdd:PRK10524 61 RHLAKRPEQLALIavstetDEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMP----MIAeAAFAMLacaRIGAIH 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 73 LPV-------------DPVLPpqrrQLLLTV------GEV-----------RVQVTQPGltqlepslPVLIIDDGMldtp 122
Cdd:PRK10524 137 SVVfggfashslaariDDAKP----VLIVSAdagsrgGKVvpykplldeaiALAQHKPR--------HVLLVDRGL---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 123 aAPLPEVAG----------------------DVTDLAYIIFTSGSTGTPKGVMID---HRAAMNT-LEDInerFGLNAQD 176
Cdd:PRK10524 201 -APMARVAGrdvdyatlraqhlgarvpvewlESNEPSYILYTSGTTGKPKGVQRDtggYAVALATsMDTI---FGGKAGE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 177 RVFGLSSLSFDLS-VYDAFAPFMVGAALVL-------PEAGrekdpRHWQTVMAHGhVSVWNAVPALMQMLCEYHSG--D 246
Cdd:PRK10524 277 TFFCASDIGWVVGhSYIVYAPLLAGMATIMyeglptrPDAG-----IWWRIVEKYK-VNRMFSAPTAIRVLKKQDPAllR 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 247 RMSYPTLRLALLSGDwiPLTLPeqmrerlneTMDIISlgGATECAIWSVYYpigEVESTWTSIPYGRGLRNQ-------- 318
Cdd:PRK10524 351 KHDLSSLRALFLAGE--PLDEP---------TASWIS--EALGVPVIDNYW---QTETGWPILAIARGVEDRptrlgspg 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 319 -PVYVLNAQL------EECPVGVEGEICIGGmGLAQGYLNDAEKTAASFV---WReASGERIYRTGDRGRYFADGQVAFL 388
Cdd:PRK10524 415 vPMYGYNVKLlnevtgEPCGPNEKGVLVIEG-PLPPGCMQTVWGDDDRFVktyWS-LFGRQVYSTFDWGIRDADGYYFIL 492
|
490
....*....|....
gi 535686385 389 GRNDTQVKVNGYRI 402
Cdd:PRK10524 493 GRTDDVINVAGHRL 506
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
21-177 |
6.58e-10 |
|
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: 60.69 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGV--QHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVT 98
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 99 QPGLTqlepslpVLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTL----EDINERFGLNA 174
Cdd:cd05927 86 DAGVK-------VYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVagvfKILEILNKINP 158
|
...
gi 535686385 175 QDR 177
Cdd:cd05927 159 TDV 161
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1-166 |
6.82e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 60.73 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP 80
Cdd:PRK08162 24 LERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 PQRRQLLLTVGEVRV--------QVTQPGLTQLEPSLPVLIIDDGMLDTPAAPLPE------VAGDVTDLAYII------ 140
Cdd:PRK08162 104 AASIAFMLRHGEAKVlivdtefaEVAREALALLPGPKPLVIDVDDPEYPGGRFIGAldyeafLASGDPDFAWTLpadewd 183
|
170 180 190
....*....|....*....|....*....|..
gi 535686385 141 -----FTSGSTGTPKGVMIDHR-AAMNTLEDI 166
Cdd:PRK08162 184 aialnYTSGTTGNPKGVVYHHRgAYLNALSNI 215
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1-157 |
2.21e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 59.12 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALI-----SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGwqqIAavHGILRLGAVYL-- 73
Cdd:PRK08180 45 LVHWAQEAPDRVFLAergadGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNS---IE--HALLALAAMYAgv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 74 PVDPVLPP---------QRRQL--LLTVGEVRV---QVTQPGLTQLEPSLPVLIIDDG------------MLDTPAAPLP 127
Cdd:PRK08180 120 PYAPVSPAyslvsqdfgKLRHVleLLTPGLVFAddgAAFARALAAVVPADVEVVAVRGavpgraatpfaaLLATPPTAAV 199
|
170 180 190
....*....|....*....|....*....|...
gi 535686385 128 EVAGDVT---DLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:PRK08180 200 DAAHAAVgpdTIAKFLFTSGSTGLPKAVINTHR 232
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
139-390 |
3.19e-09 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 58.05 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 139 IIFTSGSTGTPKGVMIDHR----AAMNTlediNERFGLNAQDR------VFGLSSLSFdlsvydAFAPFMVGAALVLPEA 208
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGnliaANLQL----IHAMGLTEADVylnmlpLFHIAGLNL------ALATFHAGGANVVMEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 209 greKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLalLSGdwipLTLPEQMrERLNETmdiislGGAT 288
Cdd:cd17637 75 ---FDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRH--VLG----LDAPETI-QRFEET------TGAT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 289 ecaIWSVYypiGEVESTW--TSIPY-------GRGLRNQPVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAAS 359
Cdd:cd17637 139 ---FWSLY---GQTETSGlvTLSPYrerpgsaGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYT 212
|
250 260 270
....*....|....*....|....*....|...
gi 535686385 360 FV--WreasgeriYRTGDRGRYFADGQVAFLGR 390
Cdd:cd17637 213 FRngW--------HHTGDLGRFDEDGYLWYAGR 237
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
139-389 |
4.59e-09 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 57.31 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 139 IIFTSGSTGTPKGVMIDHRA--AMNT----LEDINERFGLNAQDRVFGLSSLSFDLSVYdafapFMVGAALVLPEAgrek 212
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQAllAQALvlavLQAIDEGTVFLNSGPLFHIGTLMFTLATF-----HAGGTNVFVRRV---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 213 DPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDWIPLTLPEqmrerlnETMDIISLGGatecai 292
Cdd:cd17636 76 DAEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWNDMATVD-------TSPWGRKPGG------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 293 wsvyYPIGEVESTWTSIPYGRGL-----RNQP---VYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAAsfvwRE 364
Cdd:cd17636 143 ----YGQTEVMGLATFAALGGGAiggagRPSPlvqVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNAR----RT 214
|
250 260
....*....|....*....|....*
gi 535686385 365 ASGerIYRTGDRGRYFADGQVAFLG 389
Cdd:cd17636 215 RGG--WHHTNDLGRREPDGSLSFVG 237
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
135-403 |
6.15e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 57.11 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPK------GVMIDHRAAMNTLEDINERFGLnaqdrVFGLSSLSFDLSVYDAFAPFMVGAALVLPEA 208
Cdd:cd05944 3 DVAAYFHTGGTTGTPKlaqhthSNEVYNAWMLALNSLFDPDDVL-----LCGLPLFHVNGSVVTLLTPLASGAHVVLAGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 209 GREKDP----RHWQTVmAHGHVSVWNAVPALMQMLCEYHSGDRMSypTLRLALLSGDWIPLTLPEQMRERLNetMDIISL 284
Cdd:cd05944 78 AGYRNPglfdNFWKLV-ERYRITSLSTVPTVYAALLQVPVNADIS--SLRFAMSGAAPLPVELRARFEDATG--LPVVEG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 285 GGATECA-IWSVYYPIGEVE--STWTSIPYGRglrnQPVYVLNAQ---LEECPVGVEGEICIGGMGLAQGYLNDAEKTAA 358
Cdd:cd05944 153 YGLTEATcLVAVNPPDGPKRpgSVGLRLPYAR----VRIKVLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLYTEGNKNA 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 535686385 359 SfvwreaSGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIE 403
Cdd:cd05944 229 F------VADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNID 267
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
135-404 |
6.67e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 57.52 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 135 DLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfglssLSFdLSVYDAFA-------PFMVGAALVLpe 207
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVM-----MSF-LPPFHAYGfnsctlfPLLSGVPVVF-- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 208 AGREKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGDRMSYPTLRLALLSGDwiplTLPEQMRERLNETMDIISLG-- 285
Cdd:PRK06334 256 AYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGD----AFKDSLYQEALKTFPHIQLRqg 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 286 -GATECaiwSVYYPIGEVESTWTSIPYGRGLRNQPVYVLNAQlEECPV--GVEGEICIGGMGLAQGYLndAEKTAASFVw 362
Cdd:PRK06334 332 yGTTEC---SPVITINTVNSPKHESCVGMPIRGMDVLIVSEE-TKVPVssGETGLVLTRGTSLFSGYL--GEDFGQGFV- 404
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 535686385 363 rEASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIEL 404
Cdd:PRK06334 405 -ELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSL 445
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1-289 |
1.46e-08 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 56.73 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVV-----------------------MEKGWQ 57
Cdd:PLN02860 13 LTRLATLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAalnsdlylewllavacaggivapLNYRWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 58 QIAAVHGILRLGAVYLPVDPV------------LPPQRRQLLLtvgEVRVQVTQPGLTQLepslpvLIIDDGMLDTPAAP 125
Cdd:PLN02860 93 FEEAKSAMLLVRPVMLVTDETcsswyeelqndrLPSLMWQVFL---ESPSSSVFIFLNSF------LTTEMLKQRALGTT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 126 LPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRA-AMNTLEDInERFGLNAQD---------RVFGLSSlsfdlsvydAFA 195
Cdd:PLN02860 164 ELDYAWAPDDAVLICFTSGTTGRPKGVTISHSAlIVQSLAKI-AIVGYGEDDvylhtaplcHIGGLSS---------ALA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 196 PFMVGAA-LVLP--EAGREKDprhwqtVMAHGHVSVWNAVPALMQMLCEY--HSGDRMSYPTLRLALLSGDWIPLTLPEQ 270
Cdd:PLN02860 234 MLMVGAChVLLPkfDAKAALQ------AIKQHNVTSMITVPAMMADLISLtrKSMTWKVFPSVRKILNGGGSLSSRLLPD 307
|
330
....*....|....*....
gi 535686385 271 MRErLNETMDIISLGGATE 289
Cdd:PLN02860 308 AKK-LFPNAKLFSAYGMTE 325
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
19-179 |
2.09e-08 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports 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 FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 55.89 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLppQRRQLL--LTVGEVRVQ 96
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNL--RLESLLhcITVSKAKAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 97 VT---QPGLTQLEPSLPVLIIddgmldtpaaplpevaGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLN 173
Cdd:cd05939 80 IFnllDPLLTQSSTEPPSQDD----------------VNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR 143
|
....*.
gi 535686385 174 AQDRVF 179
Cdd:cd05939 144 PEDVVY 149
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
19-157 |
4.35e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 55.00 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAvylPVDPVLPPQRRQLLLT--------- 89
Cdd:PRK07768 28 VRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGA---SLTMLHQPTPRTDLAVwaedtlrvi 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535686385 90 --VGEVRVQVTQPgLTQLEPSLP-----VLIIDDgMLDTPAAPLPEVAGDvtDLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:PRK07768 105 gmIGAKAVVVGEP-FLAAAPVLEekgirVLTVAD-LLAADPIDPVETGED--DLALMQLTSGSTGSPKAVQITHG 175
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
2-406 |
6.12e-08 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 54.46 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 2 LRQAALTPQETALISPIRE--LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVL 79
Cdd:cd17642 24 MKRYASVPGTIAFTDAHTGvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 80 ppQRRQLLLTVGEVR---VQVTQPGLTQL------EPSLPVLIIDDGMLD------------TPAAP-------LPEVAG 131
Cdd:cd17642 104 --NERELDHSLNISKptiVFCSKKGLQKVlnvqkkLKIIKTIIILDSKEDykgyqclytfitQNLPPgfneydfKPPSFD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 132 DVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLED-INERFGLNAQDRVFGLSSLSF--DLSVYDAFAPFMVGAALVLPEA 208
Cdd:cd17642 182 RDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHaRDPIFGNQIIPDTAILTVIPFhhGFGMFTTLGYLICGFRVVLMYK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 209 GREK-------DPRHWQTVMahghvsvwnaVPALMQMLCEYHSGDRMSYPTLrLALLSGDwIPLT--LPEQMRERLNetM 279
Cdd:cd17642 262 FEEElflrslqDYKVQSALL----------VPTLFAFFAKSTLVDKYDLSNL-HEIASGG-APLSkeVGEAVAKRFK--L 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 280 DIISLG-GATECAIWSVYYPIGEVEStwtsipygrGLRNQPVYVLNAQLEECPVGV------EGEICIGGMGLAQGYLND 352
Cdd:cd17642 328 PGIRQGyGLTETTSAILITPEGDDKP---------GAVGKVVPFFYAKVVDLDTGKtlgpneRGELCVKGPMIMKGYVNN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 535686385 353 AEKTAASFV---WreasgeriYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRIELGE 406
Cdd:cd17642 399 PEATKALIDkdgW--------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAE 447
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
19-171 |
9.02e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 54.21 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGI----LRLGAVY--LPVDPVLPPQRR---QLLLT 89
Cdd:PTZ00216 120 RYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVYanLGEDALAYALREtecKAIVC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 90 VGEvRVQVTQPGLTQLE-PSLPVLIIDD---------------------GMLDTPAAPLPeVAGDVTDLAYIIFTSGSTG 147
Cdd:PTZ00216 200 NGK-NVPNLLRLMKSGGmPNTTIIYLDSlpasvdtegcrlvawtdvvakGHSAGSHHPLN-IPENNDDLALIMYTSGTTG 277
|
170 180
....*....|....*....|....*...
gi 535686385 148 TPKGVMIDHR---AAMNTLED-INERFG 171
Cdd:PTZ00216 278 DPKGVMHTHGsltAGILALEDrLNDLIG 305
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
3-402 |
1.03e-07 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 54.10 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 3 RQAALTPQETALI------SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV- 75
Cdd:cd05966 61 RHLKERGDKVAIIwegdepDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVf 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 76 ---------DPVLPPQRRqLLLTVGEVR--------VQVTQPGLTQLEPSLPVLII-----------------DDGMLDT 121
Cdd:cd05966 141 agfsaeslaDRINDAQCK-LVITADGGYrggkviplKEIVDEALEKCPSVEKVLVVkrtggevpmtegrdlwwHDLMAKQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 122 PAAPLPEVAgDVTDLAYIIFTSGSTGTPKGVMidHR-------AAMnTLEDInerFGLNAQDRVF---------GLSsls 185
Cdd:cd05966 220 SPECEPEWM-DSEDPLFILYTSGSTGKPKGVV--HTtggyllyAAT-TFKYV---FDYHPDDIYWctadigwitGHS--- 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 186 fdlsvYDAFAPFMVGAALVL-------PEAGrekdpRHWQTVMAHGhVSVWNAVP----ALMQMLCEY-HSGDRMSyptL 253
Cdd:cd05966 290 -----YIVYGPLANGATTVMfegtptyPDPG-----RYWDIVEKHK-VTIFYTAPtairALMKFGDEWvKKHDLSS---L 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 254 RLallsgdwipltlpeqmrerlnetmdIISLGGATECAIWSVYYP-IGE----VESTW----------TSIPYGRGLRN- 317
Cdd:cd05966 356 RV-------------------------LGSVGEPINPEAWMWYYEvIGKercpIVDTWwqtetggimiTPLPGATPLKPg 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 318 ---------QPVyVLNAQLEECPVGVEGEICIG----GMglAQGYLNDAEKtaasFV---WREASGerIYRTGDRGRYFA 381
Cdd:cd05966 411 satrpffgiEPA-ILDEEGNEVEGEVEGYLVIKrpwpGM--ARTIYGDHER----YEdtyFSKFPG--YYFTGDGARRDE 481
|
490 500
....*....|....*....|.
gi 535686385 382 DGQVAFLGRNDTQVKVNGYRI 402
Cdd:cd05966 482 DGYYWITGRVDDVINVSGHRL 502
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1-179 |
1.15e-07 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 53.65 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAAltPQETALIS-----PIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV 75
Cdd:PRK03584 92 LLRHRR--DDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSC 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 76 DPVLPPQ----R-RQLlltvgEVRVQVTQPG-------------LTQLEPSLP----VLIIDDGMLDTPAAPLPEVA--G 131
Cdd:PRK03584 170 SPDFGVQgvldRfGQI-----EPKVLIAVDGyryggkafdrrakVAELRAALPslehVVVVPYLGPAAAAAALPGALlwE 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535686385 132 DVTDLA----------------YIIFTSGSTGTPKGvmIDHRAAMNTLEDINE---RFGLNAQDRVF 179
Cdd:PRK03584 245 DFLAPAeaaelefepvpfdhplWILYSSGTTGLPKC--IVHGHGGILLEHLKElglHCDLGPGDRFF 309
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1-206 |
1.94e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 53.11 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAAlTPQETALISPIRELTYRQLstAADHVARALLALGVQHGDR---VAVVMEKGWQQIAAVHGILRLGAVYLPVDP 77
Cdd:PRK13388 8 LLRDRA-GDDTIAVRYGDRTWTWREV--LAEAAARAAALIALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 78 VlppqRR-------------QLLLTVGEVRVQVTQPGLtqlePSLPVLIIDD----GMLDTPAAPLPEVAGDVTDLAYII 140
Cdd:PRK13388 85 T----RRgaalaadirradcQLLVTDAEHRPLLDGLDL----PGVRVLDVDTpayaELVAAAGALTPHREVDAMDPFMLI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535686385 141 FTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVFGLSSLSFDLSVYDAFAPFMV-GAALVLP 206
Cdd:PRK13388 157 FTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVAsGAAVALP 223
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
15-157 |
2.00e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 53.18 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 15 ISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPV-DPVLP------------- 80
Cdd:PLN02736 73 VGEYKWMTYGEAGTARTAIGSGLVQHGIPKGACVGLYFINRPEWLIVDHACSAYSYVSVPLyDTLGPdavkfivnhaeva 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 81 -----PQRRQLLLT----VGEVRVQVTQPGLTQLEPSLP------VLIIDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGS 145
Cdd:PLN02736 153 aifcvPQTLNTLLSclseIPSVRLIVVVGGADEPLPSLPsgtgveIVTYSKLLAQGRSSPQPFRPPKPEDVATICYTSGT 232
|
170
....*....|..
gi 535686385 146 TGTPKGVMIDHR 157
Cdd:PLN02736 233 TGTPKGVVLTHG 244
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
12-400 |
3.35e-07 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 52.33 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 12 TALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQR--RQL--- 86
Cdd:PRK07059 40 PAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPREleHQLkds 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 87 ------LL-----TVGEV-------RVQVTQPG----------------LTQLEP--SLP-------VLIIDDGMLDTPa 123
Cdd:PRK07059 120 gaeaivVLenfatTVQQVlaktavkHVVVASMGdllgfkghivnfvvrrVKKMVPawSLPghvrfndALAEGARQTFKP- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 124 aplPEVAGDvtDLAYIIFTSGSTGTPKGVMIDHRAAM-NTLEdiNERFGLNAQDRVFGLSSLSF--DLSVYDAFApFMVG 200
Cdd:PRK07059 199 ---VKLGPD--DVAFLQYTGGTTGVSKGATLLHRNIVaNVLQ--MEAWLQPAFEKKPRPDQLNFvcALPLYHIFA-LTVC 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 201 AALVLPEAGRE---KDPRHwqtvmahghvsvwnaVPALMQMLCEYhsgDRMSYP---TLRLALLSGdwipltlPEqmRER 274
Cdd:PRK07059 271 GLLGMRTGGRNiliPNPRD---------------IPGFIKELKKY---QVHIFPavnTLYNALLNN-------PD--FDK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 275 LNETMDIISLGGATecaiwSVYYPIGE--VESTWTSIPYGRGL-RNQPVYVLNA------------------------QL 327
Cdd:PRK07059 324 LDFSKLIVANGGGM-----AVQRPVAErwLEMTGCPITEGYGLsETSPVATCNPvdatefsgtiglplpstevsirddDG 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535686385 328 EECPVGVEGEICIGGMGLAQGYLNDAEKTAasfvwREASGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGY 400
Cdd:PRK07059 399 NDLPLGEPGEICIRGPQVMAGYWNRPDETA-----KVMTADGFFRTGDVGVMDERGYTKIVDRKKDMILVSGF 466
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
122-179 |
3.53e-07 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 52.66 E-value: 3.53e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 535686385 122 PAAPLPEVAGDvtDLAYIIFTSGSTGTPKGVMIDHRaamNTLEDINE---RFGLNAQDRVF 179
Cdd:PRK06814 783 PLVYFCNRDPD--DPAVILFTSGSEGTPKGVVLSHR---NLLANRAQvaaRIDFSPEDKVF 838
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
4-359 |
3.65e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALI--SPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPP 81
Cdd:PRK13390 6 HAQIAPDRPAVIvaETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 82 QRRQLLLTVGEVRVQVTQPGLTQLEPS----LPVLIIDDGMLDTPAAPLPEVAGDVTDL------AYIIFTSGSTGTPKG 151
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAKvgadLPLRLSFGGEIDGFGSFEAALAGAGPRLteqpcgAVMLYSSGTTGFPKG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 152 VMidhraamntlEDINERFGLNAQDRVFGLSSLSFDLS---VYDAFAPFMVGAAL-----VLPEAGREKDPRHWQTVMAH 223
Cdd:PRK13390 166 IQ----------PDLPGRDVDAPGDPIVAIARAFYDISesdIYYSSAPIYHAAPLrwcsmVHALGGTVVLAKRFDAQATL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 224 GHV-----SVWNAVPALMQMLCEYHSGDRMSY--PTLRLALLSGDWIPLTLPEQMRERLNETmdiislggatecaIWSvY 296
Cdd:PRK13390 236 GHVeryriTVTQMVPTMFVRLLKLDADVRTRYdvSSLRAVIHAAAPCPVDVKHAMIDWLGPI-------------VYE-Y 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 535686385 297 YPIGEVEST-------WTSIP--YGRGLRNQpVYVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAAS 359
Cdd:PRK13390 302 YSSTEAHGMtfidspdWLAHPgsVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAA 372
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
4-160 |
9.93e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 50.87 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 4 QAALTPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVylpvdPVLPPQR 83
Cdd:PRK07868 456 QARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAV-----AVLMPPD 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 84 RQL--LLTVGEVRVQVTQPglTQLEPSL----PVLI----------------------IDDGMLDTPA--APLPEVAGdv 133
Cdd:PRK07868 531 TDLaaAVRLGGVTEIITDP--TNLEAARqlpgRVLVlgggesrdldlpddadvidmekIDPDAVELPGwyRPNPGLAR-- 606
|
170 180
....*....|....*....|....*...
gi 535686385 134 tDLAYIIF-TSGSTGTPKGVMiDHRAAM 160
Cdd:PRK07868 607 -DLAFIAFsTAGGELVAKQIT-NYRWAL 632
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
134-205 |
1.28e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 50.48 E-value: 1.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535686385 134 TDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfgLSSL----SFDLSVyDAFAPFMVGAALVL 205
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRF--MSALplfhSFGLTV-GLFTPLLTGAEVFL 437
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
122-405 |
1.37e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 50.50 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 122 PAAPLPevagdvTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERF-GLNAQD---------RVFGLSSLSFDLSVY 191
Cdd:PLN02387 244 PDLPSP------NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVpKLGKNDvylaylplaHILELAAESVMAAVG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 192 DAFApfmVGAALVLPEA------GREKDPRHWQ-TVMAhghvsvwnAVPALMqmlceyhsgDRMSYPTL----------- 253
Cdd:PLN02387 318 AAIG---YGSPLTLTDTsnkikkGTKGDASALKpTLMT--------AVPAIL---------DRVRDGVRkkvdakgglak 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 254 ---------RLALLSGDWIPLTLPEQM----------RERLNETMDIISLGGA------------------------TE- 289
Cdd:PLN02387 378 klfdiaykrRLAAIEGSWFGAWGLEKLlwdalvfkkiRAVLGGRIRFMLSGGAplsgdtqrfiniclgapigqgyglTEt 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 290 CAiwsvyypiGEVESTWTSIPYGRglRNQPVYVLNAQLEECPVG---------VEGEICIGGMGLAQGYLNDAEKTAASF 360
Cdd:PLN02387 458 CA--------GATFSEWDDTSVGR--VGPPLPCCYVKLVSWEEGgylisdkpmPRGEIVIGGPSVTLGYFKNQEKTDEVY 527
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 535686385 361 VWREaSGERIYRTGDRGRYFADGQVAFLGRNDTQVKV-NGYRIELG 405
Cdd:PLN02387 528 KVDE-RGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLqHGEYVSLG 572
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
19-393 |
1.68e-06 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 49.74 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 19 RELTYRQLSTAADHVARALL-ALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAV------YLPVDPVLPpqrrqlLLTVG 91
Cdd:cd05937 4 KTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAApafinyNLSGDPLIH------CLKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 92 EVRVqvtqpgltqlepslpvLIIDDgmlDTPAAplpevagdvtdlayIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFG 171
Cdd:cd05937 78 GSRF----------------VIVDP---DDPAI--------------LIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 172 LNAQDRVFGLSSLSFDLSVYDAFAP-FMVGAALVLpeaGREKDPRH-WQTVMAHGHVSVwnavpALMQMLCEY------H 243
Cdd:cd05937 125 LKNGDRTYTCMPLYHGTAAFLGACNcLMSGGTLAL---SRKFSASQfWKDVRDSGATII-----QYVGELCRYllstppS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 244 SGDRMSypTLRLAL---LSGD-WipltlpEQMRERLNeTMDIISLGGATEcaiwsvyypigEVESTWT--SIPYGRG--- 314
Cdd:cd05937 197 PYDRDH--KVRVAWgngLRPDiW------ERFRERFN-VPEIGEFYAATE-----------GVFALTNhnVGDFGAGaig 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 315 ---------LRNQPVYV---LNAQ----------LEECPVGVEGEICI----GGMGLAQGYLNDAEKTAASF---VWREa 365
Cdd:cd05937 257 hhglirrwkFENQVVLVkmdPETDdpirdpktgfCVRAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLvrdVFRK- 335
|
410 420
....*....|....*....|....*....
gi 535686385 366 sGERIYRTGDRGRYFADGQVAFLGR-NDT 393
Cdd:cd05937 336 -GDIYFRTGDLLRQDADGRWYFLDRlGDT 363
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
21-402 |
1.79e-06 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 50.03 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLP------PQR---RQLLLTVG 91
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHrddhalAARntePALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 92 EVRVQVTQPGLTQlepslPVLIIDDGMLDTPAAPLPeVAGDVTdlAYIIFTSGSTGTPKGVMIDHRAAMNTLEDI-NERF 170
Cdd:PRK06060 111 ALRDRFQPSRVAE-----AAELMSEAARVAPGGYEP-MGGDAL--AYATYTSGTTGPPKAAIHRHADPLTFVDAMcRKAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 171 GLNAQDrvFGLSSlsfdLSVYDAFA-------PFMVGAALV---LPEAGREKdprhwQTVMAHGHVSVWNAVPALMQMLC 240
Cdd:PRK06060 183 RLTPED--TGLCS----ARMYFAYGlgnsvwfPLATGGSAVinsAPVTPEAA-----AILSARFGPSVLYGVPNFFARVI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 241 EYHSGDrmSYPTLRLALLSGDWIPLTLPEQMRERLNeTMDIISLGGATECAIWSVYYPIGEvestWTSIPYGRGLRNQPV 320
Cdd:PRK06060 252 DSCSPD--SFRSLRCVVSAGEALELGLAERLMEFFG-GIPILDGIGSTEVGQTFVSNRVDE----WRLGTLGRVLPPYEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 321 YVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFVWREasgeriyrTGDRGRYFADGQVAFLGRNDTQVKVNGY 400
Cdd:PRK06060 325 RVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDSPVANEGWLD--------TRDRVCIDSDGWVTYRCRADDTEVIGGV 396
|
..
gi 535686385 401 RI 402
Cdd:PRK06060 397 NV 398
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
10-152 |
2.03e-06 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 49.70 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 10 QETALISPIRELTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLT 89
Cdd:PRK12406 1 MYATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 90 VGEVRVQVTQPGL-----TQLEPSLPVLI------------IDDGMLDTPAAPL----------PEVAGDVTDLAYIIFT 142
Cdd:PRK12406 81 DSGARVLIAHADLlhglaSALPAGVTVLSvptppeiaaayrISPALLTPPAGAIdwegwlaqqePYDGPPVPQPQSMIYT 160
|
170
....*....|
gi 535686385 143 SGSTGTPKGV 152
Cdd:PRK12406 161 SGTTGHPKGV 170
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1-208 |
2.29e-06 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 49.60 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 1 LLRQAAltPQETALISPIRELTYRQLSTAADHVARALLALGVQHGDrVAVVmekgwqQIAAV-------HGILRLGAVyl 73
Cdd:PRK10946 31 LTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGD-TALV------QLGNVaefyitfFALLKLGVA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 74 PVDPVLPPQRRQLLLTVgevrvqvtqpglTQLEPSLPV------LIIDDGMLDTPAAPLPEV-----AGDVTDL------ 136
Cdd:PRK10946 100 PVNALFSHQRSELNAYA------------SQIEPALLIadrqhaLFSDDDFLNTLVAEHSSLrvvllLNDDGEHslddai 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 137 -----------------AYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNAQDRVfgLSSL----SFDLSVYDAFA 195
Cdd:PRK10946 168 nhpaedftatpspadevAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRY--LCALpaahNYPMSSPGALG 245
|
250
....*....|....*.
gi 535686385 196 PFMVGAALVL---PEA 208
Cdd:PRK10946 246 VFLAGGTVVLapdPSA 261
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
21-157 |
5.82e-06 |
|
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: 48.44 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLA-LGVQHGDRVAVVMEKGWQQIAAVHGILRLGavyLPVDPVLPPQRRQLLL---TVGEVRVQ 96
Cdd:cd05938 6 YTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLG---CPVAFLNTNIRSKSLLhcfRCCGAKVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 97 VTQPGLTQ-LEPSLPVL------------------IID--DGMLDTPAAPLPEVAGDV---TDLAYIIFTSGSTGTPKGV 152
Cdd:cd05938 83 VVAPELQEaVEEVLPALradgvsvwylshtsntegVISllDKVDAASDEPVPASLRAHvtiKSPALYIYTSGTTGLPKAA 162
|
....*
gi 535686385 153 MIDHR 157
Cdd:cd05938 163 RISHL 167
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
114-157 |
8.67e-06 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 47.84 E-value: 8.67e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 535686385 114 IDDGMLDTPAAPLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:cd17632 203 IAVRGRDLPPAPLFRPEPDDDPLALLIYTSGSTGTPKGAMYTER 246
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
21-157 |
8.91e-06 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 47.74 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLstaaDHVARALLA-----LGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPqrRQL---LLTVGE 92
Cdd:PRK08974 49 MTFRKL----EERSRAFAAylqngLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTP--RELehqLNDSGA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 93 VRVQVTQPGLTQLE------PSLPVLIIDDG-MLDTPAAPL-------------------------------------PE 128
Cdd:PRK08974 123 KAIVIVSNFAHTLEkvvfktPVKHVILTRMGdQLSTAKGTLvnfvvkyikrlvpkyhlpdaisfrsalhkgrrmqyvkPE 202
|
170 180
....*....|....*....|....*....
gi 535686385 129 VAGDvtDLAYIIFTSGSTGTPKGVMIDHR 157
Cdd:PRK08974 203 LVPE--DLAFLQYTGGTTGVAKGAMLTHR 229
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
100-399 |
6.16e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 45.06 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 100 PGLTQLEPSLPVLIID----DGMLDTPA-APLPEVAGDVTDLAYIIFTSGSTGTPKGVMIDHRAAMNTLEDINERFGLNA 174
Cdd:PRK07867 113 ELLDGLDPGVRVINVDspawADELAAHRdAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGP 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 175 QDRVFglssLSFDL----SVYDAFAPFM-VGAALVLPEagREKDPRHWQTVMAHGhVSVWNAVpalmqmlceyhsGDRMS 249
Cdd:PRK07867 193 DDVCY----VSMPLfhsnAVMAGWAVALaAGASIALRR--KFSASGFLPDVRRYG-ATYANYV------------GKPLS 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 250 YptlrlallsgdwiPLTLPEQMRERLNE----------TMDIISLGGATECAIWSVYYPI-GEVESTWT-SIPYGR-GLR 316
Cdd:PRK07867 254 Y-------------VLATPERPDDADNPlrivygnegaPGDIARFARRFGCVVVDGFGSTeGGVAITRTpDTPPGAlGPL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 317 NQPVYVLNAQ-LEECPVGVE------------GEIC-IGGMGLAQGYLNDAEKTAAsfvwREASGerIYRTGDRGRYFAD 382
Cdd:PRK07867 321 PPGVAIVDPDtGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAE----RMRGG--VYWSGDLAYRDAD 394
|
330
....*....|....*..
gi 535686385 383 GQVAFLGRNDTQVKVNG 399
Cdd:PRK07867 395 GYAYFAGRLGDWMRVDG 411
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
9-402 |
2.85e-04 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 42.91 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 9 PQETALI--SPIRELTYRQLSTAADHVARALL-ALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPvlppqrrq 85
Cdd:PLN02574 53 NGDTALIdsSTGFSISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP-------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 86 lLLTVGEVRVQV--TQPGLTQLEPS---------LPVLII------DDGMLDTPA-----------APLPEVAGDvtDLA 137
Cdd:PLN02574 125 -SSSLGEIKKRVvdCSVGLAFTSPEnveklsplgVPVIGVpenydfDSKRIEFPKfyelikedfdfVPKPVIKQD--DVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 138 YIIFTSGSTGTPKGVMIDHRAAMNTLEDI----NERFGLNAQDRVFgLSSLS----FDLSVYdAFAPFMVGAALVLPeag 209
Cdd:PLN02574 202 AIMYSSGTTGASKGVVLTHRNLIAMVELFvrfeASQYEYPGSDNVY-LAALPmfhiYGLSLF-VVGLLSLGSTIVVM--- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 210 REKDPRHWQTVMAHGHVSVWNAVPALMQMLCEYHSGD-RMSYPTLRL-----ALLSGDWIP---LTLPEqmrerlnetMD 280
Cdd:PLN02574 277 RRFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVcGEVLKSLKQvscgaAPLSGKFIQdfvQTLPH---------VD 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 281 IISLGGATECAIWSVYYPIGEVESTWTSIpyGRGLRNQPVYVLNAQLEEC-PVGVEGEICIGGMGLAQGYLNDAEKTAAS 359
Cdd:PLN02574 348 FIQGYGMTESTAVGTRGFNTEKLSKYSSV--GLLAPNMQAKVVDWSTGCLlPPGNCGELWIQGPGVMKGYLNNPKATQST 425
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 535686385 360 FVwreasGERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:PLN02574 426 ID-----KDGWLRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQI 463
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
297-402 |
1.26e-03 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 40.96 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 297 YPIGEVESTWTSIPYGR----GLRNQPV-----YVLNAQLEECPVGVEGEICIGGMGLAQGYLNDAEKTAASFvwreaSG 367
Cdd:PRK12492 365 YGLTETSPVASTNPYGElarlGTVGIPVpgtalKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL-----DA 439
|
90 100 110
....*....|....*....|....*....|....*
gi 535686385 368 ERIYRTGDRGRYFADGQVAFLGRNDTQVKVNGYRI 402
Cdd:PRK12492 440 EGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNV 474
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
130-291 |
2.36e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 39.75 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 130 AGDVTDLAYIIFTSGSTGTPKGVMIDHraamNTLEDINERF-------GLNAQDRVfgLSSLSFDLSVydAFAPFMVGA- 201
Cdd:COG1541 79 AVPLEEIVRIHASSGTTGKPTVVGYTR----KDLDRWAELFarslraaGVRPGDRV--QNAFGYGLFT--GGLGLHYGAe 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 202 ---ALVLPEAGREKDpRHWQtVMAHGHVSVWNAVPALMQMLCEY--HSGDRMSYPTLRLALLSGDwiplTLPEQMRERLN 276
Cdd:COG1541 151 rlgATVIPAGGGNTE-RQLR-LMQDFGPTVLVGTPSYLLYLAEVaeEEGIDPRDLSLKKGIFGGE----PWSEEMRKEIE 224
|
170 180
....*....|....*....|....*
gi 535686385 277 ETMDI----------ISLGGATECA 291
Cdd:COG1541 225 ERWGIkaydiyglteVGPGVAYECE 249
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
19-52 |
4.39e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 39.35 E-value: 4.39e-03
10 20 30
....*....|....*....|....*....|....
gi 535686385 19 RELTYRQLSTAADHVARALLALGVQHGDRVAVVM 52
Cdd:PRK00174 97 RKITYRELHREVCRFANALKSLGVKKGDRVAIYM 130
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
139-156 |
8.89e-03 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341256 [Multi-domain] Cd Length: 596 Bit Score: 38.11 E-value: 8.89e-03
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
21-160 |
9.87e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 38.28 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 21 LTYRQLSTAADHVARALLALGVQHGDRVAVVMEKGWQQIAAVHGILRLGAVYLPVDPVLPPQRRQLLLTVGEVRVQVTQP 100
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535686385 101 glTQLEPSLPVL---------IIDDG------------------------MLDTPAAPLPevAGDVTDLAYIIFTSGSTG 147
Cdd:PLN02861 158 --SKISSILSCLpkcssnlktIVSFGdvsseqkeeaeelgvscfsweefsLMGSLDCELP--PKQKTDICTIMYTSGTTG 233
|
170
....*....|...
gi 535686385 148 TPKGVMIDHRAAM 160
Cdd:PLN02861 234 EPKGVILTNRAII 246
|
|
| |
