|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
7-453 |
5.11e-37 |
|
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: 140.72 E-value: 5.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 7 LARWLTApRPDDTPIAWLNEsTWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKTPVLpghn 83
Cdd:COG0318 5 LRRAAAR-HPDRPALVFGGR-RLTYAELDARARRLAAALRAlgvGPGDRVALLLPNSPEFVVAFLAALRAGAVVVP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 84 rviqLN---EQRELfDGVLSDSELnwqgSLLLVAsspqiatqsftfaaiapeaFIeLFTSGSTGQPKRAIKPVHLLDREA 160
Cdd:COG0318 79 ----LNprlTAEEL-AYILEDSGA----RALVTA-------------------LI-LYTSGTTGRPKGVMLTHRNLLANA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 161 ELLAERLGARlAGCRVVgSVLPQ-HLYGLTFRVFLPMALGLPLHAAMLWYVEQFAALSHQHR-YIFISSPAFLKRL---- 234
Cdd:COG0318 130 AAIAAALGLT-PGDVVL-VALPLfHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERvTVLFGVPTMLARLlrhp 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 235 -DTQLSPPPVQVLLSAGGELPWQDVQHTASWLRVWPDEIYGSTETG-VIAWRYREQEQRRW----LPLPGMQFQ------ 302
Cdd:COG0318 208 eFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSpVVTVNPEDPGERRPgsvgRPLPGVEVRivdedg 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 303 ---AEGDAFRLF--SPLIAE-------------DNGMLL-DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLA 363
Cdd:COG0318 288 relPPGEVGEIVvrGPNVMKgywndpeataeafRDGWLRtGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 364 LDGIREAAAVPVT--RGGrQSIGVLLVLDDEAHLQwqnggghSQEMtwRRLLRPTLEPVAIPRYWRVIDEMPVNSMNKRV 441
Cdd:COG0318 368 HPGVAEAAVVGVPdeKWG-ERVVAFVVLRPGAELD-------AEEL--RAFLRERLARYKVPRRVEFVDELPRTASGKID 437
|
490
....*....|..
gi 15833585 442 YAQLQELFHEAP 453
Cdd:COG0318 438 RRALRERYAAGA 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
25-435 |
1.30e-23 |
|
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: 102.61 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 25 NESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGH--NRViqlneqrelfDG 97
Cdd:cd05930 9 GDQSLTYAELDARANRLARYLRERgvgPGDLVAVLLERSLEMVVAILAVLKAGAAyvPLDPSYpaERL----------AY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 98 VLSDSelnwQGSLLLVASSpqiatqsfTFAAIapeafieLFTSGSTGQPK------RAIkpVHLLDREAELLAERLGARL 171
Cdd:cd05930 79 ILEDS----GAKLVLTDPD--------DLAYV-------IYTSGSTGKPKgvmvehRGL--VNLLLWMQEAYPLTPGDRV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 172 AgcrvvgsvlpqHLYGLTF-----RVFLPMALGLPLHAA---MLWYVEQFAALSHQHRYIFISS-PAFLKRLDTQLSP-- 240
Cdd:cd05930 138 L-----------QFTSFSFdvsvwEIFGALLAGATLVVLpeeVRKDPEALADLLAEEGITVLHLtPSLLRLLLQELELaa 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 241 -PPVQVLLSAGGELPWQDVQhtaSWLRVWPDE----IYGSTETGVIAWRYREQEQRRWL-------PLPGMQFQAEGDAF 308
Cdd:cd05930 207 lPSLRLVLVGGEALPPDLVR---RWRELLPGArlvnLYGPTEATVDATYYRVPPDDEEDgrvpigrPIPNTRVYVLDENL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 309 RL------------------------------FSPLIAEDNGMLLD--DILQFSEDGQFHLMGRRGRIVKIEEKRISLQE 356
Cdd:cd05930 284 RPvppgvpgelyiggaglargylnrpeltaerFVPNPFGPGERMYRtgDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 357 VEQRLLALDGIREAAAVPVTRG-GRQSIGVLLVLDDEAHLqwqnggghsQEMTWRRLLRPTLEPVAIPRYWRVIDEMPVN 435
Cdd:cd05930 364 IEAALLAHPGVREAAVVAREDGdGEKRLVAYVVPDEGGEL---------DEEELRAHLAERLPDYMVPSAFVVLDALPLT 434
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
133-439 |
1.65e-22 |
|
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: 97.74 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 133 AFIeLFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGcrVVGSVLPQHLYGLTFRVFLPMALGlplhaAMLWYVEQ 212
Cdd:cd04433 3 ALI-LYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGD--VFLSTLPLFHIGGLFGLLGALLAG-----GTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 213 F---AALSHQHRY---IFISSPAFLKRLDTQLSPPP-----VQVLLSAGGELPWQDVQHTASWLRVWPDEIYGSTETG-- 279
Cdd:cd04433 75 FdpeAALELIEREkvtILLGVPTLLARLLKAPESAGydlssLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgt 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 280 VIAWRYREQEQRR---WLPLPGMQFQ---AEGD------------------AFRLFSPLIAE---DNGMLL-DDILQFSE 331
Cdd:cd04433 155 VATGPPDDDARKPgsvGRPVPGVEVRivdPDGGelppgeigelvvrgpsvmKGYWNNPEATAavdEDGWYRtGDLGRLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 332 DGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAA--AVPVTRGGrQSIGVLLVLDDEAHLQwqnggghSQEMtw 409
Cdd:cd04433 235 DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAvvGVPDPEWG-ERVVAVVVLRPGADLD-------AEEL-- 304
|
330 340 350
....*....|....*....|....*....|
gi 15833585 410 RRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:cd04433 305 RAHVRERLAPYKVPRRVVFVDALPRTASGK 334
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
16-435 |
1.34e-17 |
|
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: 84.73 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 16 PDDTPIAwLNESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGHnrviqlne 90
Cdd:cd17649 1 PDAVALV-FGDQSLSYAELDARANRLAHRLRALgvgPEVRVGIALERSLEMVVALLAILKAGGAyvPLDPEY-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 91 QRELFDGVLSDSELNWqgsllLVASSPQIAtqsftfaaiapeAFIeLFTSGSTGQPKRAIKPVHLLDREAELLAERLGAR 170
Cdd:cd17649 72 PAERLRYMLEDSGAGL-----LLTHHPRQL------------AYV-IYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 171 lAGCRVVgsvlpqHLYGLTF-----RVFLPMALG--LPLHAAMLWYVEQFaaLSHQHRYIFIS----SPAFLKRL----- 234
Cdd:cd17649 134 -PGDREL------QFASFNFdgaheQLLPPLICGacVVLRPDELWASADE--LAEMVRELGVTvldlPPAYLQQLaeead 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 235 -DTQLSPPPVQvLLSAGGELpwQDVQHTASWL--RVWPDEIYGSTETGV--IAWRYREQEQRRWL------PLPGMQFQA 303
Cdd:cd17649 205 rTGDGRPPSLR-LYIFGGEA--LSPELLRRWLkaPVRLFNAYGPTEATVtpLVWKCEAGAARAGAsmpigrPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 304 EGDAFRLFSP----------------------LIAE--------DNGMLL---DDILQFSEDGQFHLMGRRGRIVKIEEK 350
Cdd:cd17649 282 LDADLNPVPVgvtgelyiggeglargylgrpeLTAErfvpdpfgAPGSRLyrtGDLARWRDDGVIEYLGRVDHQVKIRGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 351 RISLQEVEQRLLALDGIREAAAVPV-TRGGRQSIGVLLVLDDEAHLQWQNggghsqemTWRRLLRPTLEPVAIPRYWRVI 429
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVALdGAGGKQLVAYVVLRAAAAQPELRA--------QLRTALRASLPDYMVPAHLVFL 433
|
....*.
gi 15833585 430 DEMPVN 435
Cdd:cd17649 434 ARLPLT 439
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
30-372 |
6.17e-17 |
|
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: 82.31 E-value: 6.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 30 TLGDLRHDVAQLICRLQQ----QPGERWALCFENSYLFIVALLATLHAGKT--PVLPGH--------------NRVIQLN 89
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaggvGPGDRVAVLLERSAELVVAILAVLKAGAAyvPLDPAYpaerlafiledagaRLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 90 EQRELFDG-VLSDSELNWQGSLLLVASSPQIATQSFTfaaiAPE--AFIeLFTSGSTGQPK------RAIkpVHLLDREA 160
Cdd:TIGR01733 81 ALASRLAGlVLPVILLDPLELAALDDAPAPPPPDAPS----GPDdlAYV-IYTSGSTGRPKgvvvthRSL--VNLLAWLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 161 ELLAERLGARLAgcrvvgSVLPQHLYGLTFRVFLPMALG----LPLHAAMLWYVEQFAALSHQHRY-IFISSPAFLKRLD 235
Cdd:TIGR01733 154 RRYGLDPDDRVL------QFASLSFDASVEEIFGALLAGatlvVPPEDEERDDAALLAALIAEHPVtVLNLTPSLLALLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 236 TQL--SPPPVQVLLSAGGELPWQDVQhtaSWLRVWPDE----IYGSTET--GVIAWRYREQEQRRWLPLP---------- 297
Cdd:TIGR01733 228 AALppALASLRLVILGGEALTPALVD---RWRARGPGArlinLYGPTETtvWSTATLVDPDDAPRESPVPigrplantrl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 298 -----GMQFQAEG----------------------DAFRLFSPLIAEDNGMLL---DDILQFSEDGQFHLMGRRGRIVKI 347
Cdd:TIGR01733 305 yvlddDLRPVPVGvvgelyiggpgvargylnrpelTAERFVPDPFAGGDGARLyrtGDLVRYLPDGNLEFLGRIDDQVKI 384
|
410 420
....*....|....*....|....*
gi 15833585 348 EEKRISLQEVEQRLLALDGIREAAA 372
Cdd:TIGR01733 385 RGYRIELGEIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
18-439 |
1.26e-16 |
|
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: 81.52 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 18 DTPIAWLNESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGHN--RVIQLNE 90
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLgldAGDPVVVYGHKSPDAIAAFLAALKAGHAyvPLDASSPaeRIREILD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 91 qrelfdgvlsdselnwqgslllvASSPQIAtqsftFAAIAPEAFIeLFTSGSTGQPK------RAIkpVHLLDREAELLA 164
Cdd:cd05945 86 -----------------------AAKPALL-----IADGDDNAYI-IFTSGSTGRPKgvqishDNL--VSFTNWMLSDFP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 165 erLGARLagcrVVGSVLPQHLYGLTFRVFLPMALG-----LPlHAAMLWYVEQFAALSHQHRYIFISSPAFLKRL----- 234
Cdd:cd05945 135 --LGPGD----VFLNQAPFSFDLSVMDLYPALASGatlvpVP-RDATADPKQLFRFLAEHGITVWVSTPSFAAMCllspt 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 235 DTQLSPPPVQVLLSAGGELPwqdVQHTASWLRVWPD----EIYGSTETGVIAWRYR------EQEQRrwLP----LPGMQ 300
Cdd:cd05945 208 FTPESLPSLRHFLFCGEVLP---HKTARALQQRFPDariyNTYGPTEATVAVTYIEvtpevlDGYDR--LPigyaKPGAK 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 301 FQAEGDAFRLFSP-----LI-------------AEDNGMLLD-----------DILQFSEDGQFHLMGRRGRIVKIEEKR 351
Cdd:cd05945 283 LVILDEDGRPVPPgekgeLVisgpsvskgylnnPEKTAAAFFpdegqrayrtgDLVRLEADGLLFYRGRLDFQVKLNGYR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 352 ISLQEVEQRLLALDGIREAAAVPV-TRGGRQSIGVLLVLDDEAHLQwqnggghsQEMTWRRLLRPTLEPVAIPRYWRVID 430
Cdd:cd05945 363 IELEEIEAALRQVPGVKEAVVVPKyKGEKVTELIAFVVPKPGAEAG--------LTKAIKAELAERLPPYMIPRRFVYLD 434
|
....*....
gi 15833585 431 EMPVNSMNK 439
Cdd:cd05945 435 ELPLNANGK 443
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
137-445 |
1.54e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 81.33 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 137 LFTSGSTGQPKRAIKPVHLLDREAELLAERLGARlaGCRVVGSVLPQHL-YGL---------------TFRVFLPMAL-- 198
Cdd:cd05922 123 LYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT--ADDRALTVLPLSYdYGLsvlnthllrgatlvlTNDGVLDDAFwe 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 199 -----------GLPLHAAMLwyveqfaalshqhryifisspAFLKRLDTQLspPPVQVLLSAGGELPWQDVQHTASWLRV 267
Cdd:cd05922 201 dlrehgatglaGVPSTYAML---------------------TRLGFDPAKL--PSLRYLTQAGGRLPQETIARLRELLPG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 268 WPDEI-YGSTE-TGVIAWRYREQEQRR----WLPLPGMQFQAEGDAFRLFSP-----------------------LIAED 318
Cdd:cd05922 258 AQVYVmYGQTEaTRRMTYLPPERILEKpgsiGLAIPGGEFEILDDDGTPTPPgepgeivhrgpnvmkgywndppyRRKEG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 319 NGMLL---DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAV--PVTRGGRQSIGVLLVLDDEA 393
Cdd:cd05922 338 RGGGVlhtGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVglPDPLGEKLALFVTAPDKIDP 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15833585 394 HlqwqnggghsqemTWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNKRVYAQL 445
Cdd:cd05922 418 K-------------DVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
18-439 |
1.80e-16 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 82.52 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 18 DTPIAWLNESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKTpVLPGHNRVIQLNEQREL 94
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAHVLIAAgvgPDVLVGIAVERSIEMVVGLLAVLKAGGA-YVPLDPEYPQDRLAYML 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 95 FDG----VLSDSELNWQ-------GSLLLVASSPQIATQS--FTFAAIAPE--AFIeLFTSGSTGQPKRAIKPVHLLDRE 159
Cdd:PRK12467 606 DDSgvrlLLTQSHLLAQlpvpaglRSLCLDEPADLLCGYSghNPEVALDPDnlAYV-IYTSGSTGQPKGVAISHGALANY 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 160 AELLAERLgaRLAGCRVVGSVLPQHLYGLTFRVFLPMALGLPLHAA---MLWYVEQFAALSHQHRY-IFISSPAFLKRL- 234
Cdd:PRK12467 685 VCVIAERL--QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLppdCARDAEAFAALMADQGVtVLKIVPSHLQALl 762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 235 -DTQLSPPPVQVLLSAGGE-LPW---QDVQHTASWLRVWpdEIYGSTET--GVIAWRYREQEQRRWL-----PLPGMQFQ 302
Cdd:PRK12467 763 qASRVALPRPQRALVCGGEaLQVdllARVRALGPGARLI--NHYGPTETtvGVSTYELSDEERDFGNvpigqPLANLGLY 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 303 ------------------------AEG-------DAFRLFSPLIAEDNGMLL--DDILQFSEDGQFHLMGRRGRIVKIEE 349
Cdd:PRK12467 841 ildhylnpvpvgvvgelyiggaglARGyhrrpalTAERFVPDPFGADGGRLYrtGDLARYRADGVIEYLGRMDHQVKIRG 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 350 KRISLQEVEQRLLALDGIREAAAVPVTRGGRQSIGVLLVLDDEAhlqwQNGGGHSQEMTWRRLLRPTLEPVAIPRYWRVI 429
Cdd:PRK12467 921 FRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVA----DGAEHQATRDELKAQLRQVLPDYMVPAHLLLL 996
|
490
....*....|
gi 15833585 430 DEMPVNSMNK 439
Cdd:PRK12467 997 DSLPLTPNGK 1006
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
26-436 |
2.37e-14 |
|
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: 74.93 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 26 ESTWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGK--TPVLPghnrviQLNEQRELF---DG 97
Cdd:cd12117 20 DRSLTYAELNERANRLARRLRAagvGPGDVVGVLAERSPELVVALLAVLKAGAayVPLDP------ELPAERLAFmlaDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 98 ----VLSDSELnwQGSLLLVASSPQIATQSFTFAAIAPE--------AFIeLFTSGSTGQPKRAIKPVHLLDReaeLLAE 165
Cdd:cd12117 94 gakvLLTDRSL--AGRAGGLEVAVVIDEALDAGPAGNPAvpvspddlAYV-MYTSGSTGRPKGVAVTHRGVVR---LVKN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 166 RLGARLAGCRVVGSVLPQHLYGLTFRVFLPMALGLPLHAA---MLWYVEQFAALSHQHRY--IFISSPAFlkRLDTQLSP 240
Cdd:cd12117 168 TNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLApkgTLLDPDALGALIAEEGVtvLWLTAALF--NQLADEDP 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 241 ppvQVL-----LSAGGELpwQDVQHTASWLRVWPD----EIYGSTETGVIAWRYREQEQRRW-------LPLPGM----- 299
Cdd:cd12117 246 ---ECFaglreLLTGGEV--VSPPHVRRVLAACPGlrlvNGYGPTENTTFTTSHVVTELDEVagsipigRPIANTrvyvl 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 300 ----QFQAEGDAFRL---------------------FSPLIAEDNGMLL--DDILQFSEDGQFHLMGRRGRIVKIEEKRI 352
Cdd:cd12117 321 dedgRPVPPGVPGELyvggdglalgylnrpaltaerFVADPFGPGERLYrtGDLARWLPDGRLEFLGRIDDQVKIRGFRI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 353 SLQEVEQRLLALDGIREAAAVPVT-RGGRQSIGVLLVLDdeahlqwqnGGGHSQEMtwRRLLRPTLEPVAIPRYWRVIDE 431
Cdd:cd12117 401 ELGEIEAALRAHPGVREAVVVVREdAGGDKRLVAYVVAE---------GALDAAEL--RAFLRERLPAYMVPAAFVVLDE 469
|
....*
gi 15833585 432 MPVNS 436
Cdd:cd12117 470 LPLTA 474
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
138-439 |
5.54e-14 |
|
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: 72.44 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 138 FTSGSTGQPK---RAIKP-VHLLDREAELLAERLGARLAgcrVVGSVLPQH-LYGLTFRVFLPMALGLP--LHAAMLWYV 210
Cdd:cd17633 7 FTSGTTGLPKayyRSERSwIESFVCNEDLFNISGEDAIL---APGPLSHSLfLYGAISALYLGGTFIGQrkFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 211 eqfaaLSHQHRYIFISSPAFLKRLDTQLSP-PPVQVLLSAGGELPwqdvQHTASWLR-VWPD----EIYGSTETGVIAWR 284
Cdd:cd17633 84 -----INQYNATVIYLVPTMLQALARTLEPeSKIKSIFSSGQKLF----ESTKKKLKnIFPKanliEFYGTSELSFITYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 285 YREQEQRR---WLPLPGMQF----QAEGDAFRLF--SPLI----------AEDNGMLLDDILQFSEDGQFHLMGRRGRIV 345
Cdd:cd17633 155 FNQESRPPnsvGRPFPNVEIeirnADGGEIGKIFvkSEMVfsgyvrggfsNPDGWMSVGDIGYVDEEGYLYLVGRESDMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 346 KIEEKRISLQEVEQRLLALDGIREAAAVPVTRGGRQSIGVLLVLDDEAHLQwqnggghsqemTWRRLLRPTLEPVAIPRY 425
Cdd:cd17633 235 IIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYK-----------QLKRFLKQKLSRYEIPKK 303
|
330
....*....|....
gi 15833585 426 WRVIDEMPVNSMNK 439
Cdd:cd17633 304 IIFVDSLPYTSSGK 317
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
137-449 |
1.60e-13 |
|
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: 71.21 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 137 LFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVVgsVLPQHLYGLTFRVFLPMALGLPLHAAMlwyVEQFAAL 216
Cdd:cd17630 6 ILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLL--SLPLYHVGGLAILVRSLLAGAELVLLE---RNQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 217 SHQH-RYIFIS-SPAFLKRLDTQLSPPP----VQVLLSAGGELPWQDVQH-TASWLRVWPdeIYGSTETG--VIAWRYRE 287
Cdd:cd17630 81 DLAPpGVTHVSlVPTQLQRLLDSGQGPAalksLRAVLLGGAPIPPELLERaADRGIPLYT--TYGMTETAsqVATKRPDG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 288 QEQRR-WLPLPGMQFQ--------------AEGDAFRLFSPLIAEDNGMLLDDILQFSEDGQFHLMGRRGRIVKIEEKRI 352
Cdd:cd17630 159 FGRGGvGVLLPGRELRivedgeiwvggaslAMGYLRGQLVPEFNEDGWFTTKDLGELHADGRLTVLGRADNMIISGGENI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 353 SLQEVEQRLLALDGIREAAAVPV--TRGGRQSIGVLlvlddeahlqwQNGGGHSQEmTWRRLLRPTLEPVAIPRYWRVID 430
Cdd:cd17630 239 QPEEIEAALAAHPAVRDAFVVGVpdEELGQRPVAVI-----------VGRGPADPA-ELRAWLKDKLARFKLPKRIYPVP 306
|
330
....*....|....*....
gi 15833585 431 EMPVNSMNKRVYAQLQELF 449
Cdd:cd17630 307 ELPRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
30-447 |
2.93e-13 |
|
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: 71.19 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 30 TLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGhnrviqLNEQRelFDGVLSDSel 104
Cdd:cd17653 24 TYGELDAASNALANRLLQLgvvPGDVVPLLSDRSLEMLVAILAILKAGAAyvPLDAK------LPSAR--IQAILRTS-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 105 nwQGSLLLVASSPQiatqsfTFAAIapeafieLFTSGSTGQPK------RAIkpVHLLDREAELLAERLGARLAgcrvvg 178
Cdd:cd17653 94 --GATLLLTTDSPD------DLAYI-------IFTSGSTGIPKgvmvphRGV--LNYVSQPPARLDVGPGSRVA------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 179 svlpqHLYGLTFRVFLPMALGLPLHAAMLWYVEQFAALSHQHRY--IFISSPAFLKRLDTQlSPPPVQVLLsAGGELPWQ 256
Cdd:cd17653 151 -----QVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVARTvdALMSTPSILSTLSPQ-DFPNLKTIF-LGGEAVPP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 257 DVqhTASWL---RVWpdEIYGSTETGVIAwRYREQEQRRWL----PLPG------------------------------- 298
Cdd:cd17653 224 SL--LDRWSpgrRLY--NAYGPTECTISS-TMTELLPGQPVtigkPIPNstcyildadlqpvpegvvgeicisgvqvarg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 299 -MQFQAEGDAFRLFSPLiaeDNGMLL---DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVP 374
Cdd:cd17653 299 yLGNPALTASKFVPDPF---WPGSRMyrtGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAI 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833585 375 VTRGgrQSIGVLLVLD-DEAHLqwqnggghsqemtwRRLLRPTLEPVAIPRYWRVIDEMPVNSMNKRVYAQLQE 447
Cdd:cd17653 376 VVNG--RLVAFVTPETvDVDGL--------------RSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
28-300 |
3.34e-13 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 70.80 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 28 TWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKTPV-----LPGHNRVIQLNE--------- 90
Cdd:pfam00501 21 RLTYRELDERANRLAAGLRAlgvGKGDRVAILLPNSPEWVVAFLACLKAGAVYVplnprLPAEELAYILEDsgakvlitd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 91 -------------QRELFDGVLSDSELNWQGSLLLVASSPQIATQSFTFAAIAPE--AFIeLFTSGSTGQPK------RA 149
Cdd:pfam00501 101 dalkleellealgKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDdlAYI-IYTSGTTGKPKgvmlthRN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 150 IkpVHLLdrEAELLAERLGARLAGCRVVGSVLPQ-HLYGLTFRVFLPMALGLPLHaamlwYVEQFAALS--HQHRYI--- 223
Cdd:pfam00501 180 L--VANV--LSIKRVRPRGFGLGPDDRVLSTLPLfHDFGLSLGLLGPLLAGATVV-----LPPGFPALDpaALLELIery 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 224 ----FISSPAFLKRL-----DTQLSPPPVQVLLSAGGELPwqdVQHTASWLRVWPDEI---YGSTETGVIAWRYREQEQR 291
Cdd:pfam00501 251 kvtvLYGVPTLLNMLleagaPKRALLSSLRLVLSGGAPLP---PELARRFRELFGGALvngYGLTETTGVVTTPLPLDED 327
|
330
....*....|....*
gi 15833585 292 RWL------PLPGMQ 300
Cdd:pfam00501 328 LRSlgsvgrPLPGTE 342
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
48-448 |
5.26e-13 |
|
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: 70.82 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 48 QPGERWALCFENSYLFIVALLATLHAGKTPV----------------LPGHNRVI---QLNEQRELFDGVLSDSELNW-- 106
Cdd:cd05909 29 KEGENVGVMLPPSAGGALANFALALSGKVPVmlnytaglrelracikLAGIKTVLtskQFIEKLKLHHLFDVEYDARIvy 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 107 --------------QGSLLLVASSPQIATQSFTFAAIAPEAFIELFTSGSTGQPKrAIKPVH---LLDREAELLAERLGA 169
Cdd:cd05909 109 ledlrakiskadkcKAFLAGKFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLPK-GVVLSHknlLANVEQITAIFDPNP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 170 RlagcRVVGSVLPQ-HLYGLTFRVFLPMALGLP--LHAAMLWYvEQFAALSHQHR-YIFISSPAFLKRLDTQLSPPPVQV 245
Cdd:cd05909 188 E----DVVFGALPFfHSFGLTGCLWLPLLSGIKvvFHPNPLDY-KKIPELIYDKKaTILLGTPTFLRGYARAAHPEDFSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 246 L--LSAGGE-LP------WQDVQHtaswlrVWPDEIYGSTETGVIAWRYREQEQRR----WLPLPGMQFqaegdafRLFS 312
Cdd:cd05909 263 LrlVVAGAEkLKdtlrqeFQEKFG------IRILEGYGTTECSPVISVNTPQSPNKegtvGRPLPGMEV-------KIVS 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 313 -----PLIAEDNGMLL----------------------------DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQ 359
Cdd:cd05909 330 vetheEVPIGEGGLLLvrgpnvmlgylnepeltsfafgdgwydtGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIED 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 360 RLLALDGIREAAAVPVTRGGR--QSIGVLLVLDDEAHLQWQNGGGHSQemtwrrllrptLEPVAIPRYWRVIDEMPVNSM 437
Cdd:cd05909 410 ILSEILPEDNEVAVVSVPDGRkgEKIVLLTTTTDTDPSSLNDILKNAG-----------ISNLAKPSYIHQVEEIPLLGT 478
|
490
....*....|.
gi 15833585 438 NKRVYAQLQEL 448
Cdd:cd05909 479 GKPDYVTLKAL 489
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
26-446 |
2.09e-12 |
|
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: 68.64 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 26 ESTWTLGDLRHDVAQL---ICRLQQQPGERWALCFENSYLFIVALLATLHAGKTPVlpghnrVIQLNEQRELFDGVLSDS 102
Cdd:cd05919 8 DRSVTYGQLHDGANRLgsaLRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAV------VINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 103 ElnwqgSLLLVASSPQIAtqsftFAaiapeafieLFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVVGSVLP 182
Cdd:cd05919 82 E-----ARLVVTSADDIA-----YL---------LYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 183 QHLYGLTFRVFLPMALGLPLHAAMLWYV-EQFAALSHQHR-YIFISSPAFLKRLDTQLSPPP-----VQVLLSAGGELPW 255
Cdd:cd05919 143 FFGYGLGNSLWFPLAVGASAVLNPGWPTaERVLATLARFRpTVLYGVPTFYANLLDSCAGSPdalrsLRLCVSAGEALPR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 256 QDVQhtaSWLRVWPDEI---YGSTETGVI-------AWRYREQEqrrwLPLPGMQFQ------------AEGDA------ 307
Cdd:cd05919 223 GLGE---RWMEHFGGPIldgIGATEVGHIflsnrpgAWRLGSTG----RPVPGYEIRlvdeeghtippgEEGDLlvrgps 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 308 -----FRLFSPLIAEDNGMLLD--DILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVTRGGR 380
Cdd:cd05919 296 aavgyWNNPEKSRATFNGGWYRtgDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTG 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833585 381 QS-IGVLLVLDDEAHLQwqngGGHSQEmtWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNKRVYAQLQ 446
Cdd:cd05919 376 LSrLTAFVVLKSPAAPQ----ESLARD--IHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
13-445 |
3.89e-12 |
|
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: 68.14 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 13 APRPDDTPIAWlNESTWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKT--PVLPGHNR--- 84
Cdd:cd17651 6 ARTPDAPALVA-EGRRLTYAELDRRANRLAHRLRArgvGPGDLVALCARRSAELVVALLAILKAGAAyvPLDPAYPAerl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 85 ---------VIQLNEQRELFDgvlSDSELNWqGSLLLVASSPQIATQSfTFAAIAPE--AFIeLFTSGSTGQPKraikPV 153
Cdd:cd17651 85 afmladagpVLVLTHPALAGE---LAVELVA-VTLLDQPGAAAGADAE-PDPALDADdlAYV-IYTSGSTGRPK----GV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 154 HLLDRE-AELLA--ERLGARLAGCRVvgsvlpQHLYGLTFRVFLPMALGLPLHAAMLWYV--------EQFAALSHQHRY 222
Cdd:cd17651 155 VMPHRSlANLVAwqARASSLGPGART------LQFAGLGFDVSVQEIFSTLCAGATLVLPpeevrtdpPALAAWLDEQRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 223 IFISSP-AFLKRLDTQLSPPPVQVL----LSAGGElpwQDVQHTAswLRVWPDEI--------YGSTETGVIAWRYREQE 289
Cdd:cd17651 229 SRVFLPtVALRALAEHGRPLGVRLAalryLLTGGE---QLVLTED--LREFCAGLpglrlhnhYGPTETHVVTALSLPGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 290 QRRW-------LPLPGMQFQAEGDAFRLFSP----------------------LIAEDngMLLD------------DILQ 328
Cdd:cd17651 304 PAAWpapppigRPIDNTRVYVLDAALRPVPPgvpgelyiggaglargylnrpeLTAER--FVPDpfvpgarmyrtgDLAR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 329 FSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAA--AVPVTRGGRQSIGvLLVLDDEAHLQWQNggghsqe 406
Cdd:cd17651 382 WLPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVvlAREDRPGEKRLVA-YVVGDPEAPVDAAE------- 453
|
490 500 510
....*....|....*....|....*....|....*....
gi 15833585 407 mtWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNKRVYAQL 445
Cdd:cd17651 454 --LRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
25-435 |
7.60e-12 |
|
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: 66.93 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 25 NESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGH--NRVIQLNEQRELFdG 97
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARgvgPGDRVAVYLPRSARLVAAMLAVLKAGAAyvPLDPDYpaDRLRYILEDAEPA-L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 98 VLSDSELNWQGSLLLVASSPQIATQSFTFAAIAPE------AFIeLFTSGSTGQPK------RAIkpVHLLDREAELLAE 165
Cdd:cd12116 88 VLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPvspddlAYV-IYTSGSTGRPKgvvvshRNL--VNFLHSMRERLGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 166 RLGARLAGCRVVG---SVLpqhlygltfRVFLPMALGLPLHAAMLWYVEQFAALSHQHRYIFIS----SPAFLKRL-DTQ 237
Cdd:cd12116 165 GPGDRLLAVTTYAfdiSLL---------ELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITvmqaTPATWRMLlDAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 238 LSPPPVQVLLsAGGE-LPWQDVQHTASWLR-VWpdEIYGSTETGVIAWRYREQEQRRWL----PLPGMQF---------- 301
Cdd:cd12116 236 WQGRAGLTAL-CGGEaLPPDLAARLLSRVGsLW--NLYGPTETTIWSTAARVTAAAGPIpigrPLANTQVyvldaalrpv 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 302 --------------------QAEGDAFRLFSPLIAEDNGMLL---DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVE 358
Cdd:cd12116 313 ppgvpgelyiggdgvaqgylGRPALTAERFVPDPFAGPGSRLyrtGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833585 359 QRLLALDGIREAAAVPVTRGGRQSIGVLLVLDDEAHLqwqnggghsQEMTWRRLLRPTLEPVAIPRYWRVIDEMPVN 435
Cdd:cd12116 393 AALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAP---------DAAALRAHLRATLPAYMVPSAFVRLDALPLT 460
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-439 |
2.09e-11 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 66.52 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 49 PGERWALCFENSYLFIVALLATLHAGKT-----PVLPGHNRVIQLNEQRelFDGVLSDSELNWQ----GSLLLVASSPQI 119
Cdd:PRK12316 2052 PEVRVAIAAERSFELVVALLAVLKAGGAyvpldPNYPAERLAYMLEDSG--AALLLTQRHLLERlplpAGVARLPLDRDA 2129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 120 ATQSFTFAAIAPEAFIE-----LFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVvgSVLPQHLYGLTFRVFL 194
Cdd:PRK12316 2130 EWADYPDTAPAVQLAGEnlayvIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCEL--QFMSFSFDGAHEQWFH 2207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 195 PMALG--LPLHAAMLWYVEQFAALSHQHRY-IFISSPAFLKRLDTQLS----PPPVQVLLSAGGELPWQdvQHTASWLRV 267
Cdd:PRK12316 2208 PLLNGarVLIRDDELWDPEQLYDEMERHGVtILDFPPVYLQQLAEHAErdgrPPAVRVYCFGGEAVPAA--SLRLAWEAL 2285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 268 WPDEI---YGSTETGV--IAWRYREQEQ-------------RRWLPLPGMQFQ-------------AEGDAFRLFS--PL 314
Cdd:PRK12316 2286 RPVYLfngYGPTEAVVtpLLWKCRPQDPcgaayvpigralgNRRAYILDADLNllapgmagelylgGEGLARGYLNrpGL 2365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 315 IAE--------DNGMLL---DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVTRGGRQSI 383
Cdd:PRK12316 2366 TAErfvpdpfsASGERLyrtGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQL 2445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 15833585 384 GVLLVLDDEAHLQWQNggghsqemtWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:PRK12316 2446 VAYVVPDDAAEDLLAE---------LRAWLAARLPAYMVPAHWVVLERLPLNPNGK 2492
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
38-439 |
5.15e-11 |
|
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: 64.32 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 38 VAQLICRLQQQPGERWALCFENSYLFIVALLATLHAGKT--PVLPGHNrviqlneQRELfDGVLSDSelnwQGSLLLVAS 115
Cdd:cd05903 14 LAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVtnPILPFFR-------EHEL-AFILRRA----KAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 116 SpqiaTQSFTFAAIAPEAFIELFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVVGSVLpQHLYGLTFRVFLP 195
Cdd:cd05903 82 R----FRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPM-AHQTGFVYGFTLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 196 MALGLPLHAAMLWYVEQFAALSHQHRY-IFISSPAFLKRLDTQLS-----PPPVQVLLSAGGELPWQDVQHTASWLRVWP 269
Cdd:cd05903 157 LLLGAPVVLQDIWDPDKALALMREHGVtFMMGATPFLTDLLNAVEeagepLSRLRTFVCGGATVPRSLARRAAELLGAKV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 270 DEIYGSTETGVIAWRYRE-QEQRRWL----PLPGMQFQAEGDAFRLFSP-----LIAEDNGMLL---------------- 323
Cdd:cd05903 237 CSAYGSTECPGAVTSITPaPEDRRLYtdgrPLPGVEIKVVDDTGATLAPgvegeLLSRGPSVFLgyldrpdltadaapeg 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 324 ----DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAV--PVTRGGRQSIGVlLVLDDEAHLQW 397
Cdd:cd05903 317 wfrtGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVValPDERLGERACAV-VVTKSGALLTF 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 15833585 398 QNGGGHsqemtwrrLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:cd05903 396 DELVAY--------LDRQGVAKQYWPERLVHVDDLPRTPSGK 429
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
15-439 |
6.16e-11 |
|
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: 64.10 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 15 RPDDTPI-AWlnESTWT---LGDLRHDVAQLICRLQQQPGERWALCFENSYLFIVALLATLHAGKTPVL--PGH--NRVi 86
Cdd:cd05918 12 QPDAPAVcAW--DGSLTyaeLDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPldPSHplQRL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 87 qlneqRELFDGVlsdselnwqGSLLLVASSPQIAtqsftfaaiapeAFIeLFTSGSTGQPK------RAIKPVhlldreA 160
Cdd:cd05918 89 -----QEILQDT---------GAKVVLTSSPSDA------------AYV-IFTSGSTGKPKgvviehRALSTS------A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 161 ELLAERLGARLAGcRVVgsvlpqHLYGLTFRVFLpmalglplhaamlwyVEQFAALSHqHRYIFISS--------PAFLK 232
Cdd:cd05918 136 LAHGRALGLTSES-RVL------QFASYTFDVSI---------------LEIFTTLAA-GGCLCIPSeedrlndlAGFIN 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 233 RLD-----------TQLSP---PPVQVLLSAGGELPWQDVQHTASWLRVWpdEIYGSTET-------------------- 278
Cdd:cd05918 193 RLRvtwafltpsvaRLLDPedvPSLRTLVLGGEALTQSDVDTWADRVRLI--NAYGPAECtiaatvspvvpstdprnigr 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 279 --GVIAWRYREQEQRRWLPL----------PGMqfqAEG---------DAFrLFSPLIAEDNGMLLD-------DILQFS 330
Cdd:cd05918 271 plGATCWVVDPDNHDRLVPIgavgelliegPIL---ARGylndpektaAAF-IEDPAWLKQEGSGRGrrlyrtgDLVRYN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 331 EDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLA-LDGIREAAAVPVTRGGRQSIGVL--LVLDDEAHLQWQNGGGHSQEM 407
Cdd:cd05918 347 PDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVKPKDGSSSPQLvaFVVLDGSSSGSGDGDSLFLEP 426
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 15833585 408 T--WRRL-------LRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:cd05918 427 SdeFRALvaelrskLRQRLPSYMVPSVFLPLSHLPLTASGK 467
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
15-233 |
9.61e-11 |
|
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: 63.80 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 15 RPDDTPIAWLN-----ESTWTLGDLRHDVAQLICRLQQ--QPGERWALCFENSYLFIVALLATLHAGKTPV---LPGHNR 84
Cdd:cd05931 6 RPDRPAYTFLDdeggrEETLTYAELDRRARAIAARLQAvgKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVplpPPTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 85 ----------------VIQLNEQRELFDGVLSDSELNWQGSLLLVASSPQIATQSFTFAAIAPE--AFIElFTSGSTGQP 146
Cdd:cd05931 86 haerlaailadagprvVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDdiAYLQ-YTSGSTGTP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 147 kraiKPVHLldREAELLA-ERLGARLAGCR---VVGSVLPQ-HLYGLTFRVFLPMALGLPLhaamlwyveqfaalshqhr 221
Cdd:cd05931 165 ----KGVVV--THRNLLAnVRQIRRAYGLDpgdVVVSWLPLyHDMGLIGGLLTPLYSGGPS------------------- 219
|
250
....*....|..
gi 15833585 222 yIFISSPAFLKR 233
Cdd:cd05931 220 -VLMSPAAFLRR 230
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-445 |
1.63e-10 |
|
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: 63.06 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 12 TAPRPDDTPIAWlNESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGH--NR 84
Cdd:cd17646 8 AARTPDAPAVVD-EGRTLTYRELDERANRLAHLLRARgvgPEDRVAVLLPRSADLVVALLAVLKAGAAylPLDPGYpaDR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 85 VIQLneqreLFDG----VLSDSELNWQGSLLLVASSPQiATQSFTFAAIAPEAFIE-------LFTSGSTGQPKRAikpv 153
Cdd:cd17646 87 LAYM-----LADAgpavVLTTADLAARLPAGGDVALLG-DEALAAPPATPPLVPPRpdnlayvIYTSGSTGRPKGV---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 154 hLLDREAelLAERLGARlagcrvvgsvlpQHLYGLT------------FRV-----FLPMALGLPL-------HAAmlwy 209
Cdd:cd17646 157 -MVTHAG--IVNRLLWM------------QDEYPLGpgdrvlqktplsFDVsvwelFWPLVAGARLvvarpggHRD---- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 210 VEQFAALSHQHRYI---FISS--PAFLKRLDTQlSPPPVQVLLSAGGELPWQDVQHtasWLRVWPDEI---YGSTET--G 279
Cdd:cd17646 218 PAYLAALIREHGVTtchFVPSmlRVFLAEPAAG-SCASLRRVFCSGEALPPELAAR---FLALPGAELhnlYGPTEAaiD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 280 VIAWRYREQEQRRWLPL----PGMQFQAEGDAFRLFSP----------------------LIAE-------DNGMLL--- 323
Cdd:cd17646 294 VTHWPVRGPAETPSVPIgrpvPNTRLYVLDDALRPVPVgvpgelylggvqlargylgrpaLTAErfvpdpfGPGSRMyrt 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 324 DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVT--RGGRQSIGVLLVLDDEAHLqwqngg 401
Cdd:cd17646 374 GDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAapAGAARLVGYVVPAAGAAGP------ 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 15833585 402 ghsQEMTWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNKRVYAQL 445
Cdd:cd17646 448 ---DTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
15-439 |
3.95e-10 |
|
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: 61.56 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 15 RPDDTPIAWLNESTwTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGHnrviqln 89
Cdd:cd12115 12 TPDAIALVCGDESL-TYAELNRRANRLAARLRAAgvgPESRVGVCLERTPDLVVALLAVLKAGAAyvPLDPAY------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 90 eQRELFDGVLSDSelnwQGSLLLvasspqiaTQSFTFAAIapeafieLFTSGSTGQPKR-AIK---PVHLLDREAELL-A 164
Cdd:cd12115 84 -PPERLRFILEDA----QARLVL--------TDPDDLAYV-------IYTSGSTGRPKGvAIEhrnAAAFLQWAAAAFsA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 165 ERLGARLAGCRVVG--SVlpqhlygltFRVFLPMALGLPLHAAmlwyvEQFAALSHQHRYIFI-------SSPAFLKRLD 235
Cdd:cd12115 144 EELAGVLASTSICFdlSV---------FELFGPLATGGKVVLA-----DNVLALPDLPAAAEVtlintvpSAAAELLRHD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 236 TqlSPPPVQVLLSAGGELP---WQDVQHTASWLRVWpdEIYGSTE-----TGVIAWRYREQEQRRWLPLPGMQFQAEGDA 307
Cdd:cd12115 210 A--LPASVRVVNLAGEPLPrdlVQRLYARLQVERVV--NLYGPSEdttysTVAPVPPGASGEVSIGRPLANTQAYVLDRA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 308 FRL------------------------------FSPLIAEDNGMLLD--DILQFSEDGQFHLMGRRGRIVKIEEKRISLQ 355
Cdd:cd12115 286 LQPvplgvpgelyiggagvargylgrpgltaerFLPDPFGPGARLYRtgDLVRWRPDGLLEFLGRADNQVKVRGFRIELG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 356 EVEQRLLALDGIREAAAV-PVTRGGRQSIGVLLVLDDEAHLQWQNggghsqemtWRRLLRPTLEPVAIPRYWRVIDEMPV 434
Cdd:cd12115 366 EIEAALRSIPGVREAVVVaIGDAAGERRLVAYIVAEPGAAGLVED---------LRRHLGTRLPAYMVPSRFVRLDALPL 436
|
....*
gi 15833585 435 NSMNK 439
Cdd:cd12115 437 TPNGK 441
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
26-440 |
9.97e-10 |
|
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: 61.03 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 26 ESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGH--NRViqlneqrelfDGV 98
Cdd:COG1020 499 DQSLTYAELNARANRLAHHLRALgvgPGDLVGVCLERSLEMVVALLAVLKAGAAyvPLDPAYpaERL----------AYM 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 99 LSDS-------------ELNWQGSLLLVASSPQIATQSFTF--AAIAPE--AFIeLFTSGSTGQPK------RAIkpVHL 155
Cdd:COG1020 569 LEDAgarlvltqsalaaRLPELGVPVLALDALALAAEPATNppVPVTPDdlAYV-IYTSGSTGRPKgvmvehRAL--VNL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 156 LDREAELLAERLGARLAgcrvvgsvlpqHLYGLTF-----RVFLPMALGLPLH---AAMLWYVEQFAALSHQHRY-IFIS 226
Cdd:COG1020 646 LAWMQRRYGLGPGDRVL-----------QFASLSFdasvwEIFGALLSGATLVlapPEARRDPAALAELLARHRVtVLNL 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 227 SPAFLKRLDTQL--SPPPVQVLLSAGGELPWQDVQHtasWLRVWPDEI----YGSTET--GVIAWRYREQEQRRWL---- 294
Cdd:COG1020 715 TPSLLRALLDAApeALPSLRLVLVGGEALPPELVRR---WRARLPGARlvnlYGPTETtvDSTYYEVTPPDADGGSvpig 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 295 -PLPGMQF-------------------------------QAEGDAFRlFSPLIAEDNGMLL---DDILQFSEDGQFHLMG 339
Cdd:COG1020 792 rPIANTRVyvldahlqpvpvgvpgelyiggaglargylnRPELTAER-FVADPFGFPGARLyrtGDLARWLPDGNLEFLG 870
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 340 RRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVT-RGGRQSIGVLLVLDDEAHLqwqnggghsQEMTWRRLLRPTLE 418
Cdd:COG1020 871 RADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREdAPGDKRLVAYVVPEAGAAA---------AAALLRLALALLLP 941
|
490 500
....*....|....*....|..
gi 15833585 419 PVAIPRYWRVIDEMPVNSMNKR 440
Cdd:COG1020 942 PYMVPAAVVLLLPLPLTGNGKL 963
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
48-439 |
2.18e-09 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 60.18 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 48 QPGERWALCFENSYLFIVALLATLHAGKT--PVLPGH-----------NRVIQLNEQRELFD--GVLSDSELNWqgslLL 112
Cdd:PRK05691 2236 GPQVRVGLALERSLEMVVGLLAILKAGGAyvPLDPEYplerlhymiedSGIGLLLSDRALFEalGELPAGVARW----CL 2311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 113 VASSPQIATQSftfaaIAPEAFIEL--------FTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVvgsvlpqH 184
Cdd:PRK05691 2312 EDDAAALAAYS-----DAPLPFLSLpqhqayliYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCEL-------H 2379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 185 LYGLTF-----RVFLPMALG--LPLHAAMLWYVEQFAALSHQHRY-IFISSPAF----LKRLDTQLSPPPVQVLLSAGGE 252
Cdd:PRK05691 2380 FYSINFdaaseRLLVPLLCGarVVLRAQGQWGAEEICQLIREQQVsILGFTPSYgsqlAQWLAGQGEQLPVRMCITGGEA 2459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 253 LPWQDVQHTASWLRvwPDEI---YGSTETGVIAWRYREQEQRR-----------------------WLPLP--------- 297
Cdd:PRK05691 2460 LTGEHLQRIRQAFA--PQLFfnaYGPTETVVMPLACLAPEQLEegaasvpigrvvgarvayildadLALVPqgatgelyv 2537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 298 GMQFQAEG-------DAFRLFSPLIAEDNGMLL--DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIR 368
Cdd:PRK05691 2538 GGAGLAQGyhdrpglTAERFVADPFAADGGRLYrtGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVR 2617
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833585 369 EAAAVPV-TRGGRQSIGVL----LVLDDEAHLQWQNggghsqemTWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:PRK05691 2618 EAVVLALdTPSGKQLAGYLvsavAGQDDEAQAALRE--------ALKAHLKQQLPDYMVPAHLILLDSLPLTANGK 2685
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
15-439 |
2.92e-09 |
|
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: 58.88 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 15 RPDDTPIAWLNEsTWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKT--PVLPGHNrviqln 89
Cdd:cd17655 10 TPDHTAVVFEDQ-TLTYRELNERANQLARTLREkgvGPDTIVGIMAERSLEMIVGILGILKAGGAylPIDPDYP------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 90 EQRELFdgVLSDSELNWqgsllLVASSPQI---------------ATQSFTFAAIAPE------AFIeLFTSGSTGQPK- 147
Cdd:cd17655 83 EERIQY--ILEDSGADI-----LLTQSHLQppiafiglidlldedTIYHEESENLEPVsksddlAYV-IYTSGSTGKPKg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 148 -----RAIkpVHLLDreaelLAERLGARLAGCRVvGSVLPQHLYGLTFRVFLPMALGLPLH---AAMLWYVEQFAALSHQ 219
Cdd:cd17655 155 vmiehRGV--VNLVE-----WANKVIYQGEHLRV-ALFASISFDASVTEIFASLLSGNTLYivrKETVLDGQALTQYIRQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 220 HRYIFIS-SPAFLKRLD-TQLSP-PPVQVLLSAGGELPWQDVQhtaSWLRVWPDEI-----YGSTETGVIA--WRYrEQE 289
Cdd:cd17655 227 NRITIIDlTPAHLKLLDaADDSEgLSLKHLIVGGEALSTELAK---KIIELFGTNPtitnaYGPTETTVDAsiYQY-EPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 290 QRRWLPLP---------------GMQFQAEGDAFRLFsplIAEDN---GML----------LDDILQFSE---------- 331
Cdd:cd17655 303 TDQQVSVPigkplgntriyildqYGRPQPVGVAGELY---IGGEGvarGYLnrpeltaekfVDDPFVPGErmyrtgdlar 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 332 ---DGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVT-RGGRQSIGVLLVLDDEAHLqwqnggghSQem 407
Cdd:cd17655 380 wlpDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKdEQGQNYLCAYIVSEKELPV--------AQ-- 449
|
490 500 510
....*....|....*....|....*....|..
gi 15833585 408 tWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:cd17655 450 -LREFLARELPDYMIPSYFIKLDEIPLTPNGK 480
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
16-435 |
4.51e-09 |
|
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: 58.09 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 16 PDDTPIAWlNESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGH--NRVIql 88
Cdd:cd17643 1 PEAVAVVD-EDRRLTYGELDARANRLARTLRAEgvgPGDRVALALPRSAELIVALLAILKAGGAyvPIDPAYpvERIA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 89 neqrelfdGVLSDSELnwqgSLLLV-ASSPqiatqsftfaaiapeAFIeLFTSGSTGQPKRAIKPvHlldreAELLaeRL 167
Cdd:cd17643 78 --------FILADSGP----SLLLTdPDDL---------------AYV-IYTSGSTGRPKGVVVS-H-----ANVL--AL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 168 garLAGCRVVGSVLPQ------HLYGLTFRV---FLPMalglpLHAAMLWYV--------EQFAALSHQHRYIFIS-SP- 228
Cdd:cd17643 122 ---FAATQRWFGFNEDdvwtlfHSYAFDFSVweiWGAL-----LHGGRLVVVpyevarspEDFARLLRDEGVTVLNqTPs 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 229 AFLKRLDTQLSPPPVQ-----VLLsaGGElpwqdvQHTASWLRVW--------PDEI--YGSTETGVIAWRYREQEQRRW 293
Cdd:cd17643 194 AFYQLVEAADRDGRDPlalryVIF--GGE------ALEAAMLRPWagrfgldrPQLVnmYGITETTVHVTFRPLDAADLP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 294 L--------PLPGMQFQAEGDAFRLFSP----------------------LIAE---DNGMLLD--------DILQFSED 332
Cdd:cd17643 266 AaaaspigrPLPGLRVYVLDADGRPVPPgvvgelyvsgagvargylgrpeLTAErfvANPFGGPgsrmyrtgDLARRLPD 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 333 GQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVT-RGGRQSIGVLLVLDDEAhlqwqnggghSQEMTW-R 410
Cdd:cd17643 346 GELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREdEPGDTRLVAYVVADDGA----------AADIAElR 415
|
490 500
....*....|....*....|....*
gi 15833585 411 RLLRPTLEPVAIPRYWRVIDEMPVN 435
Cdd:cd17643 416 ALLKELLPDYMVPARYVPLDALPLT 440
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
12-439 |
5.34e-09 |
|
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: 57.95 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 12 TAPRPDDTPIAWLNESTWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKT--PVLPGHNrvi 86
Cdd:cd17645 7 QVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGkgvKPDDQVGIMLDKSLDMIAAILGVLKAGGAyvPIDPDYP--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 87 qlnEQRELFdgVLSDSELnwqgSLLLvasspqiaTQSFTFAAIapeafieLFTSGSTGQPKRAIKPVHLL------DREA 160
Cdd:cd17645 84 ---GERIAY--MLADSSA----KILL--------TNPDDLAYV-------IYTSGSTGLPKGVMIEHHNLvnlcewHRPY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 161 -ELLAERLGARLAGCRVVGSVLpqhlygltfRVFLPMALGLPLH---AAMLWYVEQFAALSHQHRYIFISSPAFLKRLDT 236
Cdd:cd17645 140 fGVTPADKSLVYASFSFDASAW---------EIFPHLTAGAALHvvpSERRLDLDALNDYFNQEGITISFLPTGAAEQFM 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 237 QLSPPPVQVLLSAGGEL------PWQDVQHtaswlrvwpdeiYGSTETGVIAWRYREQEQRRWLPL-------------P 297
Cdd:cd17645 211 QLDNQSLRVLLTGGDKLkkierkGYKLVNN------------YGPTENTVVATSFEIDKPYANIPIgkpidntrvyildE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 298 GMQFQAEGDAFRLF-----------------------SPLIAEDNGMLLDDILQFSEDGQFHLMGRRGRIVKIEEKRISL 354
Cdd:cd17645 279 ALQLQPIGVAGELCiageglargylnrpeltaekfivHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEP 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 355 QEVEQRLLALDGIREAAAVPVT-RGGRQSIGVLLVLDDEAHLQwqnggghsqemTWRRLLRPTLEPVAIPRYWRVIDEMP 433
Cdd:cd17645 359 GEIEPFLMNHPLIELAAVLAKEdADGRKYLVAYVTAPEEIPHE-----------ELREWLKNDLPDYMIPTYFVHLKALP 427
|
....*.
gi 15833585 434 VNSMNK 439
Cdd:cd17645 428 LTANGK 433
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
27-433 |
6.50e-09 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 57.76 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 27 STWTLGDLRHDVAQL---ICRLQQQPGERWALCFENSYLFIVALLATLHAGKTPVL---------------PGHNRVI-- 86
Cdd:cd05959 28 GSLTYAELEAEARRVagaLRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPvntlltpddyayyleDSRARVVvv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 87 ------QLNEQRELFDG-----VLSDSELNWQGSLLLVASSPQIATQsFTFAAIAPE--AFIeLFTSGSTGQPKRAikpV 153
Cdd:cd05959 108 sgelapVLAAALTKSEHtlvvlIVSGGAGPEAGALLLAELVAAEAEQ-LKPAATHADdpAFW-LYSSGSTGRPKGV---V 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 154 HL---LDREAELLAERLGARLAGCRVVGSVLPQHLYGLTFRVFLPMALGlplhAAMLWYVEQ-----FAALSHQHR-YIF 224
Cdd:cd05959 183 HLhadIYWTAELYARNVLGIREDDVCFSAAKLFFAYGLGNSLTFPLSVG----ATTVLMPERptpaaVFKRIRRYRpTVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 225 ISSPAFLKRL-----DTQLSPPPVQVLLSAGGELPWQDVQhtaSWLRVWPDEIY---GSTETGVIAWRYREQEQR---RW 293
Cdd:cd05959 259 FGVPTLYAAMlaapnLPSRDLSSLRLCVSAGEALPAEVGE---RWKARFGLDILdgiGSTEMLHIFLSNRPGRVRygtTG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 294 LPLPGMQFQAEGDAFrlfSPLIAEDNGMLL----------------------------DDILQFSEDGQFHLMGRRGRIV 345
Cdd:cd05959 336 KPVPGYEVELRDEDG---GDVADGEPGELYvrgpssatmywnnrdktrdtfqgewtrtGDKYVRDDDGFYTYAGRADDML 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 346 KIEEKRISLQEVEQRLLALDGIREAAAVPV-TRGGRQSIGVLLVLDDeahlqwqngGGHSQEMTWRRL---LRPTLEPVA 421
Cdd:cd05959 413 KVSGIWVSPFEVESALVQHPAVLEAAVVGVeDEDGLTKPKAFVVLRP---------GYEDSEALEEELkefVKDRLAPYK 483
|
490
....*....|..
gi 15833585 422 IPRYWRVIDEMP 433
Cdd:cd05959 484 YPRWIVFVDELP 495
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-439 |
6.99e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 58.63 E-value: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 30 TLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGHNR-----VIQLNEQRELfdgvL 99
Cdd:PRK12467 1601 TYGELNRRANRLAHRLIALgvgPEVLVGIAVERSLEMVVGLLAILKAGGAyvPLDPEYPRerlayMIEDSGIELL----L 1676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 100 SDSEL-------NWQGSLLLVASSPQIATQSFTFAAIAPE----AFIeLFTSGSTGQPKRAIKPVHLLDREAELLAERLG 168
Cdd:PRK12467 1677 TQSHLqarlplpDGLRSLVLDQEDDWLEGYSDSNPAVNLApqnlAYV-IYTSGSTGRPKGAGNRHGALVNRLCATQEAYQ 1755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 169 ARLAGCrvvgsVLPQHLYGLTFRV---FLPMALGLPLHAAMLWY---VEQFAALSHQHRYIFISSP-----AFLKRLDTQ 237
Cdd:PRK12467 1756 LSAADV-----VLQFTSFAFDVSVwelFWPLINGARLVIAPPGAhrdPEQLIQLIERQQVTTLHFVpsmlqQLLQMDEQV 1830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 238 LSPPPVQVLLSAGGELPwqdVQHTASWLRVWPD----EIYGSTETG--VIAW--RYREQEQRRWLPL------------- 296
Cdd:PRK12467 1831 EHPLSLRRVVCGGEALE---VEALRPWLERLPDtglfNLYGPTETAvdVTHWtcRRKDLEGRDSVPIgqpianlstyild 1907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 297 PGMQFQAEGDAFRLF-------------SPLIAE--------DNGMLL---DDILQFSEDGQFHLMGRRGRIVKIEEKRI 352
Cdd:PRK12467 1908 ASLNPVPIGVAGELYlggvglargylnrPALTAErfvadpfgTVGSRLyrtGDLARYRADGVIEYLGRIDHQVKIRGFRI 1987
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 353 SLQEVEQRLLALDGIREAAAVPVT-RGGRQSIGvLLVLDDEAHLQWQNGGGHSQEmTWRRLLRPTLEPVAIPRYWRVIDE 431
Cdd:PRK12467 1988 ELGEIEARLREQGGVREAVVIAQDgANGKQLVA-YVVPTDPGLVDDDEAQVALRA-ILKNHLKASLPEYMVPAHLVFLAR 2065
|
....*...
gi 15833585 432 MPVNSMNK 439
Cdd:PRK12467 2066 MPLTPNGK 2073
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
49-373 |
7.45e-09 |
|
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: 57.65 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 49 PGERWALCFENSYLFIVALLATLHAGKT--PVLPGHNrviqlnEQRELFdgVLSDSELnwqGSLLLVASSPqiatqsftf 126
Cdd:cd17652 36 PERLVALALPRSAELVVAILAVLKAGAAylPLDPAYP------AERIAY--MLADARP---ALLLTTPDNL--------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 127 aaiapeAFIeLFTSGSTGQPKRAIKPVHLLDREAELLAERLGARlAGCRVVgsvlpqHLYGLTFRVFLP---MAL--GLP 201
Cdd:cd17652 96 ------AYV-IYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG-PGSRVL------QFASPSFDASVWellMALlaGAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 202 LH---AAMLWYVEQFAALSHQHRYIFIS-SPAFLKRLDTQlSPPPVQVLLSAGGELPWQDVQHTASWLRVWpdEIYGSTE 277
Cdd:cd17652 162 LVlapAEELLPGEPLADLLREHRITHVTlPPAALAALPPD-DLPDLRTLVVAGEACPAELVDRWAPGRRMI--NAYGPTE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 278 TGVIAWRYREQEQRRWLPL----PGMQFQAEGDAFRLFSP----------------------LIAE--------DNGMLL 323
Cdd:cd17652 239 TTVCATMAGPLPGGGVPPIgrpvPGTRVYVLDARLRPVPPgvpgelyiagaglargylnrpgLTAErfvadpfgAPGSRM 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 15833585 324 ---DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAV 373
Cdd:cd17652 319 yrtGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVV 371
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
26-439 |
8.24e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.43 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 26 ESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT--PVLPGH--NRVIQLNE-------- 90
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIERgvgPDVLVGVAMERSIEMVVALLAILKAGGAyvPLDPEYpaERLAYMLEdsgvqlll 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 91 -QRELFDGVLSDSELNwqgSLLLVASSPQIATQSFTFAAIA--PE--AFIeLFTSGSTGQPKRAIKPVHLLDREAELLAE 165
Cdd:PRK12316 614 sQSHLGRKLPLAAGVQ---VLDLDRPAAWLEGYSEENPGTElnPEnlAYV-IYTSGSTGKPKGAGNRHRALSNRLCWMQQ 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 166 RLGarLAGCRVVGSVLPQHLYGLTFRVFLPMALGLPLHAA---MLWYVEQFAALSHQHRYIFISSP-----AFLKRLDTQ 237
Cdd:PRK12316 690 AYG--LGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAapgDHRDPAKLVELINREGVDTLHFVpsmlqAFLQDEDVA 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 238 lSPPPVQVLLSAGGELPWQDVQHTASwlRVWPDEI---YGSTET--GVIAWRYREQEQ---------------------- 290
Cdd:PRK12316 768 -SCTSLRRIVCSGEALPADAQEQVFA--KLPQAGLynlYGPTEAaiDVTHWTCVEEGGdsvpigrpianlacyildanle 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 291 ------------------RRWLPLPGMQfqaegdAFRLF-SPLIAEDNGMLLDDILQFSEDGQFHLMGRRGRIVKIEEKR 351
Cdd:PRK12316 845 pvpvgvlgelylagrglaRGYHGRPGLT------AERFVpSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLR 918
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 352 ISLQEVEQRLLALDGIREAAAVPVtrGGRQSIGvLLVLDDEahlqwqngGGHSQEmTWRRLLRPTLEPVAIPRYWRVIDE 431
Cdd:PRK12316 919 IELGEIEARLLEHPWVREAAVLAV--DGKQLVG-YVVLESE--------GGDWRE-ALKAHLAASLPEYMVPAQWLALER 986
|
....*...
gi 15833585 432 MPVNSMNK 439
Cdd:PRK12316 987 LPLTPNGK 994
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-453 |
2.81e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.50 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 13 APRPDDTPIAWLNESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT-----PVLPGHNR 84
Cdd:PRK12316 3067 VERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERgvgPDVLVGVAVERSLEMVVGLLAILKAGGAyvpldPEYPEERL 3146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 85 VIQLNEQRelFDGVLSDSELNWQGS-----LLLVASSPQIATQSFTFAAIAPEAFIELFTSGSTGQPKRAIKPVHLLDRE 159
Cdd:PRK12316 3147 AYMLEDSG--AQLLLSQSHLRLPLAqgvqvLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNH 3224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 160 AELLAERLGARLAGCRVVGSVLPQHLYGLTFRVFLPMALGLPLHAAMLWYVEQfAALSHQHRYIFISSPAFLKRLDTQLS 239
Cdd:PRK12316 3225 LCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPA-LLVELINSEGVDVLHAYPSMLQAFLE 3303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 240 PPPVQVLLS-----AGGE-LPWQDVQHTASWLRVWpdEIYGSTETGVIAWRYREQEQRRWLP------------------ 295
Cdd:PRK12316 3304 EEDAHRCTSlkrivCGGEaLPADLQQQVFAGLPLY--NLYGPTEATITVTHWQCVEEGKDAVpigrpianracyildgsl 3381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 296 -----------LPGMQFQAEGDAFR--------LFSPLIAEDNGMLLDDILQFSEDGQFHLMGRRGRIVKIEEKRISLQE 356
Cdd:PRK12316 3382 epvpvgalgelYLGGEGLARGYHNRpgltaerfVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGE 3461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 357 VEQRLLALDGIREAAAVPVTrgGRQSIGVLLVLDDEAHLQwqnggghsqeMTWRRLLRPTLEPVAIPRYWRVIDEMPVNS 436
Cdd:PRK12316 3462 IEARLLEHPWVREAVVLAVD--GRQLVAYVVPEDEAGDLR----------EALKAHLKASLPEYMVPAHLLFLERMPLTP 3529
|
490 500
....*....|....*....|....
gi 15833585 437 MNK-------RVYAQLQELFHEAP 453
Cdd:PRK12316 3530 NGKldrkalpRPDAALLQQDYVAP 3553
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
41-435 |
2.93e-08 |
|
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: 55.87 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 41 LICRLQQQPGERWALCFENSYLFIVALLATLHAGKT--PVLPGHNrviqlnEQRELFdgVLSDSelnwqGSLLLVASSPQ 118
Cdd:cd17648 29 LLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAyvPIDPSYP------DERIQF--ILEDT-----GARVVITNSTD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 119 IAtqsftfaaiapeaFIeLFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVVGS----VLPQHLYGLTFRVFL 194
Cdd:cd17648 96 LA-------------YA-IYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFGRDNGDEAVLFfsnyVFDFFVEQMTLALLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 195 PMALGLPlHAAMLWYVEQFAALSHQHRYIFIS-SPAFLKRLDTQlSPPPVQVLLSAGGELpwqdvqHTASWLRV---WPD 270
Cdd:cd17648 162 GQKLVVP-PDEMRFDPDRFYAYINREKVTYLSgTPSVLQQYDLA-RLPHLKRVDAAGEEF------TAPVFEKLrsrFAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 271 EI---YGSTETGVIAWRYREQEQRRW-----LPLPG---------MQ--------------------------------- 300
Cdd:cd17648 234 LIinaYGPTETTVTNHKRFFPGDQRFdkslgRPVRNtkcyvlndaMKrvpvgavgelylggdgvargylnrpeltaerfl 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 301 ---FQAEGDAFRlfspliaEDNGMLLD--DILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVP- 374
Cdd:cd17648 314 pnpFQTEQERAR-------GRNARLYKtgDLVRWLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAk 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833585 375 ----VTRGGRQSIGVLLVLDDEahlqwqnggGHSQEMTWRRLLRPTLEPVAIPRYWRVIDEMPVN 435
Cdd:cd17648 387 edasQAQSRIQKYLVGYYLPEP---------GHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVT 442
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
26-444 |
4.03e-08 |
|
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: 55.37 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 26 ESTWTLGDLRHDVAQLICRLQQQ----PGERWALCFENSYLFIVALLATLHAGKT--PVLPGHnrviqlnEQRELfDGVL 99
Cdd:cd05941 9 GDSITYADLVARAARLANRLLALgkdlRGDRVAFLAPPSAEYVVAQLAIWRAGGVavPLNPSY-------PLAEL-EYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 100 SDSElnwqgSLLLVASspqiatqsftfAAIapeafieLFTSGSTGQPKRAIKPVHLLDREAELLAERLgaRLAGCRVVGS 179
Cdd:cd05941 81 TDSE-----PSLVLDP-----------ALI-------LYTSGTTGRPKGVVLTHANLAANVRALVDAW--RWTEDDVLLH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 180 VLP-QHLYGLTFRVFLPMALG-----LPLHAAMLWyveqFAALSHQHRYIFISSPAFLKRL--DTQLSPPPVQVLLSAGG 251
Cdd:cd05941 136 VLPlHHVHGLVNALLCPLFAGasvefLPKFDPKEV----AISRLMPSITVFMGVPTIYTRLlqYYEAHFTDPQFARAAAA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 252 E-----------LP------WQDVQ-HTaswlrvwPDEIYGSTETGvIAWRYREQEQRR----WLPLPGMQ--FQAEGDA 307
Cdd:cd05941 212 ErlrlmvsgsaaLPvptleeWEAITgHT-------LLERYGMTEIG-MALSNPLDGERRpgtvGMPLPGVQarIVDEETG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 308 frlfSPLIAEDNGMLL-----------------------------DDILQFSEDGQFHLMGR-RGRIVKIEEKRISLQEV 357
Cdd:cd05941 284 ----EPLPRGEVGEIQvrgpsvfkeywnkpeatkeeftddgwfktGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 358 EQRLLALDGIREAAAVPV---TRGgrQSIGVLLVLDDEAHlQWqnggghsQEMTWRRLLRPTLEPVAIPRYWRVIDEMPV 434
Cdd:cd05941 360 ERVLLAHPGVSECAVIGVpdpDWG--ERVVAVVVLRAGAA-AL-------SLEELKEWAKQRLAPYKRPRRLILVDELPR 429
|
490
....*....|...
gi 15833585 435 NSM---NKRVYAQ 444
Cdd:cd05941 430 NAMgkvNKKELRK 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
29-446 |
4.41e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 54.99 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 29 WTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKTPVlPghnrvIQLNEQRELFDGVLSDSELN 105
Cdd:cd05934 4 WTYAELLRESARIAAALAAlgiRPGDRVALMLDNCPEFLFAWFALAKLGAVLV-P-----INTALRGDELAYIIDHSGAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 106 WqgslllvasspqiatqsftfaAIAPEAFIeLFTSGSTGQPKRAIKPVHLLDREAELLAERLGARlagcrvvgsvlPQHL 185
Cdd:cd05934 78 L---------------------VVVDPASI-LYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG-----------EDDV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 186 YGLTfrvflpmalgLPL-HA-AMLWYVeqFAALSHQHRYIFI---SSPAFLKRLD------TQLSPPPVQVLLSAGgELP 254
Cdd:cd05934 125 YLTV----------LPLfHInAQAVSV--LAALSVGATLVLLprfSASRFWSDVRrygatvTNYLGAMLSYLLAQP-PSP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 255 wQDVQHTaswLRVW-----PDEI---------------YGSTETGVIAWRYREqEQRRWLP--LPGMQFQAE-------- 304
Cdd:cd05934 192 -DDRAHR---LRAAygapnPPELheefeerfgvrllegYGMTETIVGVIGPRD-EPRRPGSigRPAPGYEVRivdddgqe 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 305 ---------------GDAF------RLFSPLIAEDNGMLLD-DILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLL 362
Cdd:cd05934 267 lpagepgelvirglrGWGFfkgyynMPEATAEAMRNGWFHTgDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 363 ALDGIREAAAVPV-TRGGRQSIGVLLVLDDeahlqwqngGGHSQEMTWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNKRV 441
Cdd:cd05934 347 RHPAVREAAVVAVpDEVGEDEVKAVVVLRP---------GETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVA 417
|
....*
gi 15833585 442 YAQLQ 446
Cdd:cd05934 418 KAQLR 422
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
128-433 |
7.88e-08 |
|
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: 54.27 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 128 AIAPEAFIELFTSGSTGQPKRAIKPVHLLdreaellaerLGARLAGCRVVGsVLPQHL----------YGLTFRVFLPMA 197
Cdd:cd05972 78 TDAEDPALIYFTSGTTGLPKGVLHTHSYP----------LGHIPTAAYWLG-LRPDDIhwniadpgwaKGAWSSFFGPWL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 198 LGLPLhaaMLWYVEQFAA---LSHQHRY---IFISSPAFLKRLDTQLS----PPPVQVLLSAGGELP------WQDvqHT 261
Cdd:cd05972 147 LGATV---FVYEGPRFDAeriLELLERYgvtSFCGPPTAYRMLIKQDLssykFSHLRLVVSAGEPLNpeviewWRA--AT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 262 ASWLRvwpdEIYGSTETGVIAWRYREQEQRRW---LPLPGMQFQAEGDAFRLFSP----LIA---EDNGMLLD------- 324
Cdd:cd05972 222 GLPIR----DGYGQTETGLTVGNFPDMPVKPGsmgRPTPGYDVAIIDDDGRELPPgeegDIAiklPPPGLFLGyvgdpek 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 325 -------------DILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPV---TRGgrQSIGVLLV 388
Cdd:cd05972 298 teasirgdyyltgDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPAVAEAAVVGSpdpVRG--EVVKAFVV 375
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15833585 389 LddeahlqwQNGGGHSQEMT--WRRLLRPTLEPVAIPRYWRVIDEMP 433
Cdd:cd05972 376 L--------TSGYEPSEELAeeLQGHVKKVLAPYKYPREIEFVEELP 414
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
30-439 |
2.72e-07 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 52.52 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 30 TLGDLR---HDVAQLICRLQQQPGERWALCFENSYLFIVALLATLHAGK------TPVLPghnrviQLNEQRelfdgvls 100
Cdd:cd05973 2 TFGELRalsARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAvyqplfTAFGP------KAIEHR-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 101 dseLNWQGSLLLVASSPQIATqsftfaaIAPEAFIELFTSGSTGQPKRAIKPVHLLDREAELLAERLGARlAGCRVVGSV 180
Cdd:cd05973 68 ---LRTSGARLVVTDAANRHK-------LDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLR-PEDSFWNAA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 181 LPQHLYGLTFRVFLPMALGLP---LHAAM----LWY------VEQFAALSHQHRYIFISSPAFLKRLDTQLspppvQVLL 247
Cdd:cd05973 137 DPGWAYGLYYAITGPLALGHPtilLEGGFsvesTWRvierlgVTNLAGSPTAYRLLMAAGAEVPARPKGRL-----RRVS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 248 SAGGELPWQDVQHTASWLRVWPDEIYGSTETG-VIAWRYREQEQRR----WLPLPGMQFQ---------AEGDAFRLF-- 311
Cdd:cd05973 212 SAGEPLTPEVIRWFDAALGVPIHDHYGQTELGmVLANHHALEHPVHagsaGRAMPGWRVAvldddgdelGPGEPGRLAid 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 312 ---SPLI-----------AEDNGMLLD-DILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVT 376
Cdd:cd05973 292 ianSPLMwfrgyqlpdtpAIDGGYYLTgDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVP 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833585 377 RGGRQSIgvllvldDEAHLQWQNGGGHSQEMT--WRRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:cd05973 372 DPERTEV-------VKAFVVLRGGHEGTPALAdeLQLHVKKRLSAHAYPRTIHFVDELPKTPSGK 429
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
58-439 |
7.47e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 52.09 E-value: 7.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 58 ENSYLFIVALLATLHAGKT--PVLPGHnrviqlneQRELFDGVLSDSELNwqgsLLLVASS-----PQIAT-QSFTFAAI 129
Cdd:PRK12467 3153 ERSVEMIVALLAVLKAGGAyvPLDPEY--------PRERLAYMIEDSGVK----LLLTQAHlleqlPAPAGdTALTLDRL 3220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 130 APEAFIE---------------LFTSGSTGQPKRAikpvhlldreaellAERLGARLAGCRVVgsvlpQHLYGLT----- 189
Cdd:PRK12467 3221 DLNGYSEnnpstrvmgenlayvIYTSGSTGKPKGV--------------GVRHGALANHLCWI-----AEAYELDandrv 3281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 190 ------------FRVFLPMALGLPLHAA--MLWYVEQFAALSHQHRY-IFISSPAFLKRLDTQLSP---PPVQVLLSAGG 251
Cdd:PRK12467 3282 llfmsfsfdgaqERFLWTLICGGCLVVRdnDLWDPEELWQAIHAHRIsIACFPPAYLQQFAEDAGGadcASLDIYVFGGE 3361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 252 ELPWQDVQHTASWL-RVWPDEIYGSTETGV--IAWRYREQEQRRWLPLP------------------------------G 298
Cdd:PRK12467 3362 AVPPAAFEQVKRKLkPRGLTNGYGPTEAVVtvTLWKCGGDAVCEAPYAPigrpvagrsiyvldgqlnpvpvgvagelyiG 3441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 299 MQFQAEG-------DAFRlFSPLIAEDNGMLL---DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIR 368
Cdd:PRK12467 3442 GVGLARGyhqrpslTAER-FVADPFSGSGGRLyrtGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR 3520
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833585 369 EAAAVPV-TRGGRQSIGvLLVLDDEahlqwqnGGGHSQEMtwRRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:PRK12467 3521 EAVVLARdGAGGKQLVA-YVVPADP-------QGDWRETL--RDHLAASLPDYMVPAQLLVLAAMPLGPNGK 3582
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
7-433 |
1.40e-06 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 50.50 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 7 LARWLtAPRPDDTPIAWLNES----TWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKTPVL 79
Cdd:COG0365 15 LDRHA-EGRGDKVALIWEGEDgeerTLTYAELRREVNRFANALRAlgvKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 80 -------------------------PGHNRVIQLNEQRELFDGVLSDS--------------ELNWQGSLL---LVASsp 117
Cdd:COG0365 94 vfpgfgaealadriedaeakvlitaDGGLRGGKVIDLKEKVDEALEELpslehvivvgrtgaDVPMEGDLDwdeLLAA-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 118 qiATQSFTFAAIAPE--AFIeLFTSGSTGQPKRAikpVHlldreaellaerlgarlagcrVVGSVLPQHL---------- 185
Cdd:COG0365 172 --ASAEFEPEPTDADdpLFI-LYTSGTTGKPKGV---VH---------------------THGGYLVHAAttakyvldlk 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 186 --------------YGLTFRVFLPMALGlplhAAMLWY--------VEQFAALSHQHRY-IFISSPAFLKRL-------- 234
Cdd:COG0365 225 pgdvfwctadigwaTGHSYIVYGPLLNG----ATVVLYegrpdfpdPGRLWELIEKYGVtVFFTAPTAIRALmkagdepl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 235 -DTQLSPppVQVLLSAGGELP---WQDV-QHTASWLRvwpdEIYGSTETG-VIAWRYREQEQRR---WLPLPGMQ---FQ 302
Cdd:COG0365 301 kKYDLSS--LRLLGSAGEPLNpevWEWWyEAVGVPIV----DGWGQTETGgIFISNLPGLPVKPgsmGKPVPGYDvavVD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 303 AEGDafrlfsPLIAEDNGMLL--------------D-------------------DILQFSEDGQFHLMGRRGRIVKIEE 349
Cdd:COG0365 375 EDGN------PVPPGEEGELVikgpwpgmfrgywnDperyretyfgrfpgwyrtgDGARRDEDGYFWILGRSDDVINVSG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 350 KRISLQEVEQRLLALDGIREAAAVPV---TRGgrQSIGVLLVLDDEAHLqwqnggghSQEMT--WRRLLRPTLEPVAIPR 424
Cdd:COG0365 449 HRIGTAEIESALVSHPAVAEAAVVGVpdeIRG--QVVKAFVVLKPGVEP--------SDELAkeLQAHVREELGPYAYPR 518
|
....*....
gi 15833585 425 YWRVIDEMP 433
Cdd:COG0365 519 EIEFVDELP 527
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
287-433 |
1.89e-06 |
|
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: 50.16 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 287 EQEQRRWLPLPgmqFQAEGDAFRLfspliaedngmllDDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDG 366
Cdd:cd17650 315 ELTAERFVENP---FAPGERMYRT-------------GDLARWRADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPA 378
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833585 367 IREAA-AVPVTRGGRQSIGVLLVLDDEAHLQwqnggghsqemTWRRLLRPTLEPVAIPRYWRVIDEMP 433
Cdd:cd17650 379 IDEAVvAVREDKGGEARLCAYVVAAATLNTA-----------ELRAFLAKELPSYMIPSYYVQLDALP 435
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
49-434 |
2.44e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.34 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 49 PGERWALCFENSYLFIVALLATLHAGKT--PVLP-----------GHNRVIQLNEQRELF------DGVLS---DSELNW 106
Cdd:PRK12316 4600 PEVLVGIAMERSAEMMVGLLAVLKAGGAyvPLDPeyprerlaymmEDSGAALLLTQSHLLqrlpipDGLASlalDRDEDW 4679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 107 QGsllLVASSPQIATQSFTFAAIapeafieLFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVVGSVLPQHLY 186
Cdd:PRK12316 4680 EG---FPAHDPAVRLHPDNLAYV-------IYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGS 4749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 187 GLTFrvFLPMALGLPLH--AAMLWYVEQFAALSHQHRYIFISSP-----AFLKRLDTQLSPPPVQVLLsAGGELPWQDVQ 259
Cdd:PRK12316 4750 HEGL--YHPLINGASVVirDDSLWDPERLYAEIHEHRVTVLVFPpvylqQLAEHAERDGEPPSLRVYC-FGGEAVAQASY 4826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 260 HTAsWLRVWPDEI---YGSTETGV--IAWRYR--EQEQRRWLP----LPG---------MQFQAEGDAFRL--------- 310
Cdd:PRK12316 4827 DLA-WRALKPVYLfngYGPTETTVtvLLWKARdgDACGAAYMPigtpLGNrsgyvldgqLNPLPVGVAGELylggegvar 4905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 311 ------------FSPLIAEDNGMLL---DDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPV 375
Cdd:PRK12316 4906 gylerpaltaerFVPDPFGAPGGRLyrtGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQ 4985
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15833585 376 T-RGGRQSIGVL------LVLDDEAHLQWQNggghsqemTWRRLLRPTLEPVAIPRYWRVIDEMPV 434
Cdd:PRK12316 4986 EgAVGKQLVGYVvpqdpaLADADEAQAELRD--------ELKAALRERLPEYMVPAHLVFLARMPL 5043
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
317-439 |
5.59e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 48.62 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 317 EDNGMLLDDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVTRGGRQSIGVLLVLddeahlq 396
Cdd:PRK07638 359 ADGWMTVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIK------- 431
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 15833585 397 wqnggGHSQEMTWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:PRK07638 432 -----GSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGK 469
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
26-445 |
1.55e-05 |
|
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: 47.27 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 26 ESTWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKT--PVLPGhnrviQLNEQRELF----- 95
Cdd:cd12114 10 DGTLTYGELAERARRVAGALKAagvRPGDLVAVTLPKGPEQVVAVLGILAAGAAyvPVDID-----QPAARREAIladag 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 96 -DGVLSDSE----LNWQGSLLLVASSPQIATQSFTFAAIAPE--AFIeLFTSGSTGQPK-------------RAIKPVHL 155
Cdd:cd12114 85 aRLVLTDGPdaqlDVAVFDVLILDLDALAAPAPPPPVDVAPDdlAYV-IFTSGSTGTPKgvmishraalntiLDINRRFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 156 LDREAELLAerlgarLAGCRVVGSVlpqhlygltFRVFLPMALG----LPLHA----AMLWyveqfAALSHQHRY-IFIS 226
Cdd:cd12114 164 VGPDDRVLA------LSSLSFDLSV---------YDIFGALSAGatlvLPDEArrrdPAHW-----AELIERHGVtLWNS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 227 SPAFLKRL------DTQLSPPPVQVLLSaggeLPWQDVQHTASWLRVWPD----EIYGSTETGV--IAWRYREQEqRRW- 293
Cdd:cd12114 224 VPALLEMLldvleaAQALLPSLRLVLLS----GDWIPLDLPARLRALAPDarliSLGGATEASIwsIYHPIDEVP-PDWr 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 294 -----LPLPGMQFQAEGDAFRLFSPLIAED---------NGMLLD---------------------DILQFSEDGQFHLM 338
Cdd:cd12114 299 sipygRPLANQRYRVLDPRGRDCPDWVPGElwiggrgvaLGYLGDpeltaarfvthpdgerlyrtgDLGRYRPDGTLEFL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 339 GRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVTRGGRQSIGVLLVLDdeahlqwqNGGGHSQEMTWRRLLRPTLE 418
Cdd:cd12114 379 GRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPD--------NDGTPIAPDALRAFLAQTLP 450
|
490 500
....*....|....*....|....*..
gi 15833585 419 PVAIPRYWRVIDEMPVNSMNKRVYAQL 445
Cdd:cd12114 451 AYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
137-439 |
2.32e-05 |
|
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: 46.70 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 137 LFTSGSTGQPK------RAIKP--VH---LLDREAE---LLA----------ERLGARLAGCRVVGS-----VLPQHLYG 187
Cdd:cd17654 124 IHTSGTTGTPKivavphKCILPniQHfrsLFNITSEdilFLTspltfdpsvvEIFLSLSSGATLLIVptsvkVLPSKLAD 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 188 LTFRVFLPMALGLPlhAAMLwyvEQFAALSHQHRyiFISSPAFLKRLDTQLSPPPVQVLLSAggelpWQdvqHTASWLRV 267
Cdd:cd17654 204 ILFKRHRITVLQAT--PTLF---RRFGSQSIKST--VLSATSSLRVLALGGEPFPSLVILSS-----WR---GKGNRTRI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 268 WpdEIYGSTETGVIAWRYREQEQRRWLPL------------PGMQFQAEGDAF----RLFSPLIAEDNGMLLD-----DI 326
Cdd:cd17654 269 F--NIYGITEVSCWALAYKVPEEDSPVQLgspllgtvievrDQNGSEGTGQVFlgglNRVCILDDEVTVPKGTmratgDF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 327 LQfSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIreaaavpvtrggrQSIGVLLvLDDEAHLQWQNGGGHSQE 406
Cdd:cd17654 347 VT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGV-------------ESCAVTL-SDQQRLIAFIVGESSSSR 411
|
330 340 350
....*....|....*....|....*....|...
gi 15833585 407 mTWRRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:cd17654 412 -IHKELQLTLLSSHAIPDTFVQIDKLPLTSHGK 443
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
15-154 |
5.25e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 45.25 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 15 RPDDTPIAwLNESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKtpvlpghnRVIQLNEQ 91
Cdd:PRK09029 16 RPQAIALR-LNDEVLTWQQLCARIDQLAAGFAQQgvvEGSGVALRGKNSPETLLAYLALLQCGA--------RVLPLNPQ 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833585 92 ----------REL-FDGVLSDSELNWQGSLLLVASSPQIATQSFTFAAIAPEAFIelFTSGSTGQPKRAikpVH 154
Cdd:PRK09029 87 lpqplleellPSLtLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMT--LTSGSTGLPKAA---VH 155
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
16-439 |
5.36e-05 |
|
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: 45.54 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 16 PDDTPIAWLNEsTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKT-----PVLPGHNRVIQ 87
Cdd:cd17656 2 PDAVAVVFENQ-KLTYRELNERSNQLARFLREKgvkKDSIVAIMMERSAEMIVGILGILKAGGAfvpidPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 88 LNE--------QRELFDGVlsdsELNWQGSLLLVASSPQIATQSFTFAAIAPEAFIELFTSGSTGQPKRAIKP----VHL 155
Cdd:cd17656 81 MLDsgvrvvltQRHLKSKL----SFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEhknmVNL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 156 LDREAELLAERLGARlagcrvvgsVLpqHLYGLTFRV-----FLPMALGLPLH---AAMLWYVEQFAALSHQHRYIFISS 227
Cdd:cd17656 157 LHFEREKTNINFSDK---------VL--QFATCSFDVcyqeiFSTLLSGGTLYiirEETKRDVEQLFDLVKRHNIEVVFL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 228 P-AFLKRL--DTQLSPP---PVQVLLSAGGEL----PWQDVQHTASwlrVWPDEIYGSTETGVIAwRYREQEQRRWLPLP 297
Cdd:cd17656 226 PvAFLKFIfsEREFINRfptCVKHIITAGEQLvitnEFKEMLHEHN---VHLHNHYGPSETHVVT-TYTINPEAEIPELP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 298 GM----------------QFQAEGDAFRL---------------------FSPLIAEDNGMLLD--DILQFSEDGQFHLM 338
Cdd:cd17656 302 PIgkpisntwiyildqeqQLQPQGIVGELyisgasvargylnrqeltaekFFPDPFDPNERMYRtgDLARYLPDGNIEFL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 339 GRRGRIVKIEEKRISLQEVEQRLLALDGIREAAavpvtrggrqsigvllVLDdeahlqWQNGGGHS---------QEMT- 408
Cdd:cd17656 382 GRADHQVKIRGYRIELGEIEAQLLNHPGVSEAV----------------VLD------KADDKGEKylcayfvmeQELNi 439
|
490 500 510
....*....|....*....|....*....|...
gi 15833585 409 --WRRLLRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:cd17656 440 sqLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
332-439 |
7.57e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 45.54 E-value: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 332 DGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREaAAVPVTRG--GRQSIGVLLVLDdeahlqwqngGGHSQEMTW 409
Cdd:PRK05691 4115 DGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVRE-AAVAVQEGvnGKHLVGYLVPHQ----------TVLAQGALL 4183
|
90 100 110
....*....|....*....|....*....|...
gi 15833585 410 RRL---LRPTLEPVAIPRYWRVIDEMPVNSMNK 439
Cdd:PRK05691 4184 ERIkqrLRAELPDYMVPLHWLWLDRLPLNANGK 4216
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
112-434 |
7.83e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 45.12 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 112 LVASSPQIATQSFTFAAIAPEAFIELFT-SGSTGQPKRAIKPVHLLDREAELLAERLGarLAGCRVVGSVLP-QHLYGLT 189
Cdd:PRK06164 161 LFALPDPAPPAAAGERAADPDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYG--YDPGAVLLAALPfCGVFGFS 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 190 fRVFLPMALGLPLHAAMLWYVEQFAALSHQHR--YIFISSPAFLKRLDTQLSPPPVQVL--------LSAGGELpwqdvq 259
Cdd:PRK06164 239 -TLLGALAGGAPLVCEPVFDAARTARALRRHRvtHTFGNDEMLRRILDTAGERADFPSArlfgfasfAPALGEL------ 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 260 htASWLRVWPDEI---YGSTETG--VIAWRYREQEQRRWLP----------------------LPGMQFQAEGDAFRLFS 312
Cdd:PRK06164 312 --AALARARGVPLtglYGSSEVQalVALQPATDPVSVRIEGggrpaspearvrardpqdgallPDGESGEIEIRAPSLMR 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 313 PL----------IAEDNGMLLDDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPVTRGGRQS 382
Cdd:PRK06164 390 GYldnpdataraLTDDGYFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTV 469
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15833585 383 IGVLLVLDDeahlqwqngGGHSQEMTWRRLLRPTLEPVAIPRYWRVIDEMPV 434
Cdd:PRK06164 470 PVAFVIPTD---------GASPDEAGLMAACREALAGFKVPARVQVVEAFPV 512
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
26-147 |
1.03e-04 |
|
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: 44.58 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 26 ESTWTLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKTPVL--PGHN------RVIQLNEQREL 94
Cdd:cd05906 37 EEFQSYQDLLEDARRLAAGLRQLglrPGDSVILQFDDNEDFIPAFWACVLAGFVPAPltVPPTydepnaRLRKLRHIWQL 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833585 95 FDG--VLSDSEL-----------NWQGSLLLVASS-PQIATQSFTFAAIAPEAFIELFTSGSTGQPK 147
Cdd:cd05906 117 LGSpvVLTDAELvaefagletlsGLPGIRVLSIEElLDTAADHDLPQSRPDDLALLMLTSGSTGFPK 183
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
28-373 |
2.01e-04 |
|
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: 43.49 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 28 TWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKTPVLpghnrviqLNEQrelfdgvLSDSEL 104
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAAlgvRKGDRVALLSKNSIEMILLIHALWLLGAEAVL--------LNTR-------LTPNEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 105 NWQgslllVASSpqiatqsftfAAIAPEAFIELFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVVgsVLPQ- 183
Cdd:cd05912 66 AFQ-----LKDS----------DVKLDDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWLC--ALPLf 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 184 HLYGLTFrVFLPMALGLPLHAAMLWYVEQFAALSHQHRYIFISS-PAFLKRLDTQLS---PPPVQVLLSAGGELPwQDVQ 259
Cdd:cd05912 129 HISGLSI-LMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVvPTMLQRLLEILGegyPNNLRCILLGGGPAP-KPLL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 260 HTASWLRVWPDEIYGSTETG--VIAWRYREQEQR---RWLPLPGMQFQAEGDAFRLF--------SPLIA---------- 316
Cdd:cd05912 207 EQCKEKGIPVYQSYGMTETCsqIVTLSPEDALNKigsAGKPLFPVELKIEDDGQPPYevgeillkGPNVTkgylnrpdat 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833585 317 ----EDNGMLLDDILQFSEDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAV 373
Cdd:cd05912 287 eesfENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGVV 347
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
331-447 |
2.24e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 43.48 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 331 EDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAA--AVPVTRGGRQSIGVLLVLDD--------EAHLQWQng 400
Cdd:PRK13388 392 ADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAvyAVPDERVGDQVMAALVLRDGatfdpdafAAFLAAQ-- 469
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15833585 401 gghsqemtwrrllrPTLEPVAIPRYWRVIDEMPVNSMNKRVYAQLQE 447
Cdd:PRK13388 470 --------------PDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
331-448 |
2.74e-04 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 43.21 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 331 EDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAAAVPV-TRGGRQSIGVLLVLDDEAHLQWQNGGGHSQemtw 409
Cdd:PRK06155 412 ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVpSELGEDEVMAAVVLRDGTALEPVALVRHCE---- 487
|
90 100 110
....*....|....*....|....*....|....*....
gi 15833585 410 rrllrPTLEPVAIPRYWRVIDEMPVNSMNKRVYAQLQEL 448
Cdd:PRK06155 488 -----PRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
26-419 |
2.94e-04 |
|
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: 43.23 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 26 ESTWtlGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAG--KTPVLPGHN-----RVIQLNEQRELF 95
Cdd:cd05932 6 EFTW--GEVADKARRLAAALRALglePGSKIALISKNCAEWFITDLAIWMAGhiSVPLYPTLNpdtirYVLEHSESKALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 96 DGVLSDselnWQ-------GSLLLVASSPQIATQSF-TFAAI-------------APEAFIEL-FTSGSTGQPKRAIKPV 153
Cdd:cd05932 84 VGKLDD----WKamapgvpEGLISISLPPPSAANCQyQWDDLiaqhppleerptrFPEQLATLiYTSGTTGQPKGVMLTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 154 HLLDREAELLAERLGARlAGCRVVgSVLPqhLYGLTFRVFLPMAlglPLHAAMLWY----VEQFAALSHQHR-YIFISSP 228
Cdd:cd05932 160 GSFAWAAQAGIEHIGTE-ENDRML-SYLP--LAHVTERVFVEGG---SLYGGVLVAfaesLDTFVEDVQRARpTLFFSVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 229 AF-------------LKRLDTQLSPPPV---------------QVLLSAGGELPWQDVqhTASWLR---VWPDEIYGSTE 277
Cdd:cd05932 233 RLwtkfqqgvqdkipQQKLNLLLKIPVVnslvkrkvlkglgldQCRLAGCGSAPVPPA--LLEWYRslgLNILEAYGMTE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 278 T---GVIAWRYREQEQRRWLPLPGMQF-QAEGDAFRLFSP---------------LIAEDNGMLLDDILQFSEDGQFHLM 338
Cdd:cd05932 311 NfaySHLNYPGRDKIGTVGNAGPGVEVrISEDGEILVRSPalmmgyykdpeataeAFTADGFLRTGDKGELDADGNLTIT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 339 GRRGRIVKIEE-KRISLQEVEQRLLALDGIReaaAVPVTRGGRQSIGVLLVLDDEAHLQWQNGGGHSQEMTWRRLLR--- 414
Cdd:cd05932 391 GRVKDIFKTSKgKYVAPAPIENKLAEHDRVE---MVCVIGSGLPAPLALVVLSEEARLRADAFARAELEASLRAHLArvn 467
|
....*
gi 15833585 415 PTLEP 419
Cdd:cd05932 468 STLDS 472
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
30-278 |
4.31e-04 |
|
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: 42.47 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 30 TLGDLRHDVAQLICRLQQQ---PGERWALCFENSYLFIVALLATLHAGKTPVlPghnrVIQLNEQRELfDGVLSDSelnw 106
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKgvrKGDRVGICLQNSPQYVIAYFAIWRANAVVV-P----INPMLKEREL-EYILNDS---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 107 qGSLLLVASSpqiatqSFTFAAIAPeafielFTSGSTGQPKrAIKPVHlLDREAELLAERLGARLAGCRVVGSVLPQ-HL 185
Cdd:cd05935 73 -GAKVAVVGS------ELDDLALIP------YTSGTTGLPK-GCMHTH-FSAAANALQSAVWTGLTPSDVILACLPLfHV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 186 YGLTFRVFLPMALGLPLHAAMLWYVEQFAALSHQHRYIF-----------ISSPAFLKRLDTQLspppvQVLLSAGGELP 254
Cdd:cd05935 138 TGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFwtniptmlvdlLATPEFKTRDLSSL-----KVLTGGGAPMP 212
|
250 260
....*....|....*....|....
gi 15833585 255 WQDVQHTASWLRVWPDEIYGSTET 278
Cdd:cd05935 213 PAVAEKLLKLTGLRFVEGYGLTET 236
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
38-200 |
4.97e-04 |
|
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: 42.50 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 38 VAQLICRLQQQPGERWALCFENSYLFIVALLATLHAGKTPVLPG----HNRVIQLNEQRELFDGVLSDSELNWQGSLLLV 113
Cdd:cd05923 41 VAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINprlkAAELAELIERGEMTAAVIAVDAQVMDAIFQSG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 114 A-----------SSPQIATQSFTFAAIAPE--AFIeLFTSGSTGQPKRAIKPVHLLDREAELLAERLGARLAGCRVVGSV 180
Cdd:cd05923 121 VrvlalsdlvglGEPESAGPLIEDPPREPEqpAFV-FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGL 199
|
170 180
....*....|....*....|.
gi 15833585 181 LP-QHLYGltFRVFLPMALGL 200
Cdd:cd05923 200 MPlYHVIG--FFAVLVAALAL 218
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
126-277 |
7.55e-04 |
|
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: 41.68 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 126 FAAIAPEAFIE----------LFTSGSTGQPKRAIKPVHLLDREAELLAERLGARlAGCRVVGSVLPqhlygltFRVFLP 195
Cdd:cd05910 70 LQEAEPDAFIGipkadepaaiLFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR-PGEVDLATFPL-------FALFGP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 196 mALGL--------PLHAAMLWYVEQFAALSHQHRYIFISSPAFLKRL-----DTQLSPPPVQVLLSAGGELPwqdVQHTA 262
Cdd:cd05910 142 -ALGLtsvipdmdPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVarycaQHGITLPSLRRVLSAGAPVP---IALAA 217
|
170 180
....*....|....*....|
gi 15833585 263 SWLRVWPDEI-----YGSTE 277
Cdd:cd05910 218 RLRKMLSDEAeiltpYGATE 237
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
139-433 |
1.13e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 41.18 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 139 TSGSTGQPKRAIKPVHLLDREAELLAERLGARlagcrvvGSVL----PQHLYGLtfRVFL--------PMALGLP----- 201
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDRLGGP-------GQWLlalpAHHIAGL--QVLVrsviagsePVELDVSagfdp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 202 --LHAAMlwyveqfAALSHQHRYIFISSPAFLKRLDtqlSPPPVQVL------LSAGGELPwQDVQHTASWLRVWPDEIY 273
Cdd:PRK07824 114 taLPRAV-------AELGGGRRYTSLVPMQLAKALD---DPAATAALaeldavLVGGGPAP-APVLDAAAAAGINVVRTY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 274 GSTET-------GViawryreqeqrrwlPLPGMQFQAEGDAFRLFSPLIAED--NGMLLDDilqFSEDGQFH-------- 336
Cdd:PRK07824 183 GMSETsggcvydGV--------------PLDGVRVRVEDGRIALGGPTLAKGyrNPVDPDP---FAEPGWFRtddlgald 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 337 -----LMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAA--AVPVTRGGRQSIGVLLvlddeahlqwqnGGGHSQEM-- 407
Cdd:PRK07824 246 dgvltVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAvfGLPDDRLGQRVVAAVV------------GDGGPAPTle 313
|
330 340
....*....|....*....|....*.
gi 15833585 408 TWRRLLRPTLEPVAIPRYWRVIDEMP 433
Cdd:PRK07824 314 ALRAHVARTLDRTAAPRELHVVDELP 339
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
137-323 |
1.91e-03 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 40.42 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 137 LFTSGSTGQPKRAIKPVHLLDREAELLAERLGarLAGCRVVGSVLP-QHLYGLTFRVFLPMALGLPLHAAMLWYVEQFAA 215
Cdd:PRK13295 203 IYTSGTTGEPKGVMHTANTLMANIVPYAERLG--LGADDVILMASPmAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 216 LSHQHRYIF-ISSPAFLKRLDT--QLSPPPV---QVLLSAGGELPWQDVQHT-----ASWLRVWpdeiyGSTETGVIAWR 284
Cdd:PRK13295 281 LIRTEGVTFtMASTPFLTDLTRavKESGRPVsslRTFLCAGAPIPGALVERAraalgAKIVSAW-----GMTENGAVTLT 355
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15833585 285 YREQEQRRW-----LPLPGMQFQ---AEGdafrlfSPLIAEDNGMLL 323
Cdd:PRK13295 356 KLDDPDERAsttdgCPLPGVEVRvvdADG------APLPAGQIGRLQ 396
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
34-147 |
2.10e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 40.80 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 34 LRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKT--PVLPGH--NR------------VIQLNEQREL 94
Cdd:PRK10252 489 MREQVVALANLLRErgvKPGDSVAVALPRSVFLTLALHAIVEAGAAwlPLDTGYpdDRlkmmledarpslLITTADQLPR 568
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 15833585 95 FDGVlsdselnwQGSLLLVASSPQIATQSFTFAAIAPE--AFIeLFTSGSTGQPK 147
Cdd:PRK10252 569 FADV--------PDLTSLCYNAPLAPQGAAPLQLSQPHhtAYI-IFTSGSTGRPK 614
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
331-380 |
2.60e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 40.26 E-value: 2.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15833585 331 EDGQFHLmgrRGRI---VKIEEKRISLQEVEQRLLALDGIREAAAVPVTRGGR 380
Cdd:PRK04813 387 EDGLLFY---QGRIdfqIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHK 436
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
25-147 |
3.86e-03 |
|
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: 39.65 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 25 NESTWTLGDLRHDVAQLICRLQQ---QPGERWALCFENSYLFIVALLATLHAGKTPVLPGHNRVIQlneqrELFDgVLSD 101
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSlgvKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVE-----ELLY-ILNH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 15833585 102 SElnwqGSLLLVASSPQ-IATQsftfaaiapeafieLFTSGSTGQPK 147
Cdd:cd17640 76 SE----SVALVVENDSDdLATI--------------IYTSGTTGNPK 104
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
356-433 |
4.44e-03 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 35.98 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 356 EVEQRLLALDGIREAAAVPV---TRGgrQSIGVLLVLDDEAHLQwqnggghSQEMtwRRLLRPTLEPVAIPRYWRVIDEM 432
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVpdeLKG--EAPVAFVVLKPGVELL-------EEEL--VAHVREELGPYAVPKEVVFVDEL 69
|
.
gi 15833585 433 P 433
Cdd:pfam13193 70 P 70
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
331-445 |
5.92e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 38.89 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833585 331 EDGQFHLMGRRGRIVKIEEKRISLQEVEQRLLALDGIREAA--AVPVTRGGRQsIGVLLVLDDEAHLQwqnggghsqEMT 408
Cdd:PRK07867 393 ADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAvyAVPDPVVGDQ-VMAALVLAPGAKFD---------PDA 462
|
90 100 110
....*....|....*....|....*....|....*....
gi 15833585 409 WRRLL--RPTLEPVAIPRYWRVIDEMPVNSMNKRVYAQL 445
Cdd:PRK07867 463 FAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| |
