|
Name |
Accession |
Description |
Interval |
E-value |
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
7-451 |
2.86e-29 |
|
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: 119.14 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 7 LAQWL---CAPRPDDVPVAWqEEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKTPVip 80
Cdd:COG0318 1 LADLLrraAARHPDRPALVF-GGRRLTYAELDARARRLAAALRALgvgPGDRVALLLPNSPEFVVAFLAALRAGAVVV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 81 ghcrvsLLN----EQHLLFdgVLSDkamdwqgtlrvvSSAMTSVAhditfpairsdAFVeLFTSGSTGQPKRVIKPIARL 156
Cdd:COG0318 78 ------PLNprltAEELAY--ILED------------SGARALVT-----------ALI-LYTSGTTGRPKGVMLTHRNL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 157 DSEAALLATRFadRLAGCRVVASVVPQ-HLYGLTFRIFLPMALGLPLHAAMLWYAEQLAALSAEHRYAFIS-SPAFLKRL 234
Cdd:COG0318 126 LANAAAIAAAL--GLTPGDVVLVALPLfHVFGLTVGLLAPLLAGATLVLLPRFDPERVLELIERERVTVLFgVPTMLARL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 235 -----DHNLTPPPVELILSAGGMLPWQDVTQAADWLNVWPDEIYGSTETGILAWRYRHQDDVAWL-----PFPGVRFQPE 304
Cdd:COG0318 204 lrhpeFARYDLSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRPgsvgrPLPGVEVRIV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 305 DDAFR-----------VFSPLI-----NADDGLLLDDVLQFI---------ENGQFRLMGRRGRVVKIEEKRISLSEVEQ 359
Cdd:COG0318 284 DEDGRelppgevgeivVRGPNVmkgywNDPEATAEAFRDGWLrtgdlgrldEDGYLYIVGRKKDMIISGGENVYPAEVEE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 360 RLLALDGICEVA--ALPVSRGGrQGVGVLLVLNDEARqrwlecgGKPQELtwRRSLLPWLEPVAVPRYWRVIDEIPVNSM 437
Cdd:COG0318 364 VLAAHPGVAEAAvvGVPDEKWG-ERVVAFVVLRPGAE-------LDAEEL--RAFLRERLARYKVPRRVEFVDELPRTAS 433
|
490
....*....|....
gi 1736059155 438 NKRVYAQLQELFHE 451
Cdd:COG0318 434 GKIDRRALRERYAA 447
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
137-439 |
2.90e-18 |
|
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: 85.41 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 137 LFTSGSTGQPKRVIKPIARLDSEAALLATRFADRlAGCRVVaSVVPQHLYGLTFRIFLPMALGLPLHAAMLWYAEQLAAL 216
Cdd:cd04433 6 LYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLT-EGDVFL-STLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAALEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 217 SAEHR-YAFISSPAFLKRLDHNLTPPPVEL-----ILSAGGMLPWQDVTQAADWLNVWPDEIYGSTETG-----ILAWRY 285
Cdd:cd04433 84 IEREKvTILLGVPTLLARLLKAPESAGYDLsslraLVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGgtvatGPPDDD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 286 RHQDDVAWLPFPGVRFQPEDDAFR-----------VFSPLINADDGLLLDDVLQFI--------------ENGQFRLMGR 340
Cdd:cd04433 164 ARKPGSVGRPVPGVEVRIVDPDGGelppgeigelvVRGPSVMKGYWNNPEATAAVDedgwyrtgdlgrldEDGYLYIVGR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 341 RGRVVKIEEKRISLSEVEQRLLALDGICEVAALPV---SRGGRqgVGVLLVLNDEARQrwlecggKPQELtwRRSLLPWL 417
Cdd:cd04433 244 LKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVpdpEWGER--VVAVVVLRPGADL-------DAEEL--RAHVRERL 312
|
330 340
....*....|....*....|..
gi 1736059155 418 EPVAVPRYWRVIDEIPVNSMNK 439
Cdd:cd04433 313 APYKVPRRVVFVDALPRTASGK 334
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
16-435 |
1.10e-16 |
|
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: 81.81 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 16 PDDVPVAWqEEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT--PVIPGHcrvsllNE 90
Cdd:cd05930 1 PDAVAVVD-GDQSLTYAELDARANRLARYLRERgvgPGDLVAVLLERSLEMVVAILAVLKAGAAyvPLDPSY------PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 91 QHLLFdgVLSDkamdwqgtlrvvSSAMTSVAHDitfpaiRSDAFVeLFTSGSTGQPKRVIKP----IARLDSEAALLATR 166
Cdd:cd05930 74 ERLAY--ILED------------SGAKLVLTDP------DDLAYV-IYTSGSTGKPKGVMVEhrglVNLLLWMQEAYPLT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 167 FADRLAgcrvvasvvpqHLYGLTF-----RIFLPMALGLPLHAA---MLWYAEQLAALSAEHRYAFISS-PAFLKRLDHN 237
Cdd:cd05930 133 PGDRVL-----------QFTSFSFdvsvwEIFGALLAGATLVVLpeeVRKDPEALADLLAEEGITVLHLtPSLLRLLLQE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 238 LTP---PPVELILSAGGMLPWQDVTQaadWLNVWPDE----IYGSTETGILAWRYRHQDDVAWL-------PFPGVRF-- 301
Cdd:cd05930 202 LELaalPSLRLVLVGGEALPPDLVRR---WRELLPGArlvnLYGPTEATVDATYYRVPPDDEEDgrvpigrPIPNTRVyv 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 302 -----------------------------QPEDDAFRvfsplinaddglllddvlqFIEN-------------------- 332
Cdd:cd05930 279 ldenlrpvppgvpgelyiggaglargylnRPELTAER-------------------FVPNpfgpgermyrtgdlvrwlpd 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 333 GQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAAlpVSRGGRQGVGVL---LVLNDearqrwlecGGKPQELTW 409
Cdd:cd05930 340 GNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAV--VAREDGDGEKRLvayVVPDE---------GGELDEEEL 408
|
490 500
....*....|....*....|....*.
gi 1736059155 410 RRSLLPWLEPVAVPRYWRVIDEIPVN 435
Cdd:cd05930 409 RAHLAERLPDYMVPSAFVVLDALPLT 434
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
30-372 |
5.97e-16 |
|
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: 79.23 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 30 TLGHLRHDVAQLLAYLRQ----QEGERWALCFENSYLFIVALLATLHAGKT--PVIPGH-----------CRVSLL--NE 90
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaggvGPGDRVAVLLERSAELVVAILAVLKAGAAyvPLDPAYpaerlafiledAGARLLltDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 91 QHLLFDGVLSDKAMDWQGTLRVVSSAMTSVAHDITFPAIRSDAFVeLFTSGSTGQPKRVIKP----IARLDSEAALLATR 166
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYV-IYTSGSTGRPKGVVVThrslVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 167 FADRlagcrvVASVVPQHLYGLTFRIFLPMALG----LPLHAAMLWYAEQLAALSAEHRYAFISS-PAFLKRLD--HNLT 239
Cdd:TIGR01733 160 PDDR------VLQFASLSFDASVEEIFGALLAGatlvVPPEDEERDDAALLAALIAEHPVTVLNLtPSLLALLAaaLPPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 240 PPPVELILSAGGMLP------WQDVTQAADWLNVwpdeiYGSTETGILAWRYRHQDDVAWL--------PFPGVRFQPED 305
Cdd:TIGR01733 234 LASLRLVILGGEALTpalvdrWRARGPGARLINL-----YGPTETTVWSTATLVDPDDAPRespvpigrPLANTRLYVLD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 306 DAFR----------------VFS-----PLINAddglllddvLQFIEN-----GQFRL-----------------MGRRG 342
Cdd:TIGR01733 309 DDLRpvpvgvvgelyiggpgVARgylnrPELTA---------ERFVPDpfaggDGARLyrtgdlvrylpdgnlefLGRID 379
|
410 420 430
....*....|....*....|....*....|
gi 1736059155 343 RVVKIEEKRISLSEVEQRLLALDGICEVAA 372
Cdd:TIGR01733 380 DQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
18-439 |
7.08e-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: 79.21 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 18 DVPVAWQEEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT--PVIPGHCrvsllNEQh 92
Cdd:cd05945 6 DRPAVVEGGRTLTYRELKERADALAAALASLgldAGDPVVVYGHKSPDAIAAFLAALKAGHAyvPLDASSP-----AER- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 93 llfdgvlsdkamdWQGTLRVVSSAMTSVAHDitfpairsDAFVELFTSGSTGQPKRVikPIAR--LDSEAALLATRFAdr 170
Cdd:cd05945 80 -------------IREILDAAKPALLIADGD--------DNAYIIFTSGSTGRPKGV--QISHdnLVSFTNWMLSDFP-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 171 LAGCRVVASVVPQHLYGLTFRIFLPMALGLPLHA---AMLWYAEQLAALSAEHRYA-FISSPAFLK--RLDHNLTP---P 241
Cdd:cd05945 135 LGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPvprDATADPKQLFRFLAEHGITvWVSTPSFAAmcLLSPTFTPeslP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 242 PVELILSAGGMLPwqdVTQAADWLNVWPD----EIYGSTETGILAWRYRHQDDVAW--------LPFPGVRFQPEDDAFR 309
Cdd:cd05945 215 SLRHFLFCGEVLP---HKTARALQQRFPDariyNTYGPTEATVAVTYIEVTPEVLDgydrlpigYAKPGAKLVILDEDGR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 310 VFSP-----------------LINADDGLLLDDVLQ-----------FIEN-GQFRLMGRRGRVVKIEEKRISLSEVEQR 360
Cdd:cd05945 292 PVPPgekgelvisgpsvskgyLNNPEKTAAAFFPDEgqrayrtgdlvRLEAdGLLFYRGRLDFQVKLNGYRIELEEIEAA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 361 LLALDGICEVAALPV-SRGGRQGVGVLLVLNDEARQrwlecggkPQELTWRRSLLPWLEPVAVPRYWRVIDEIPVNSMNK 439
Cdd:cd05945 372 LRQVPGVKEAVVVPKyKGEKVTELIAFVVPKPGAEA--------GLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGK 443
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
16-435 |
1.51e-14 |
|
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: 75.48 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 16 PDDVPVAwQEEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT--PVIPGHCRVSLlne 90
Cdd:cd17649 1 PDAVALV-FGDQSLSYAELDARANRLAHRLRALgvgPEVRVGIALERSLEMVVALLAILKAGGAyvPLDPEYPAERL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 91 QHLLFDgvlsdkamdwqgtlrvvSSAMTSVAHDItfpaiRSDAFVeLFTSGSTGQPKRVIKpiarldSEAALlaTRFADR 170
Cdd:cd17649 77 RYMLED-----------------SGAGLLLTHHP-----RQLAYV-IYTSGSTGTPKGVAV------SHGPL--AAHCQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 171 LAGC-RVVASVVPQHLYGLTF-----RIFLPMALG--LPLHAAMLWYAEQlaALSAEHRYAFIS----SPAFLKRL---- 234
Cdd:cd17649 126 TAERyGLTPGDRELQFASFNFdgaheQLLPPLICGacVVLRPDELWASAD--ELAEMVRELGVTvldlPPAYLQQLaeea 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 235 --DHNLTPPPVELILSAGGMLP----WQDVTQAADWLNVwpdeiYGSTETGI--LAWRYRHQDDVAWL------PFPGVR 300
Cdd:cd17649 204 drTGDGRPPSLRLYIFGGEALSpellRRWLKAPVRLFNA-----YGPTEATVtpLVWKCEAGAARAGAsmpigrPLGGRS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 301 FQPEDDAFRVFSP------------LINADDGLLLDDVLQFIEN---------------------GQFRLMGRRGRVVKI 347
Cdd:cd17649 279 AYILDADLNPVPVgvtgelyiggegLARGYLGRPELTAERFVPDpfgapgsrlyrtgdlarwrddGVIEYLGRVDHQVKI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 348 EEKRISLSEVEQRLLALDGICEVAALPVS-RGGRQGVGVLLVLNDEARQRWLEcggkpQELTWRRSLLPwlePVAVPRYW 426
Cdd:cd17649 359 RGFRIELGEIEAALLEHPGVREAAVVALDgAGGKQLVAYVVLRAAAAQPELRA-----QLRTALRASLP---DYMVPAHL 430
|
....*....
gi 1736059155 427 RVIDEIPVN 435
Cdd:cd17649 431 VFLARLPLT 439
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
9-300 |
1.93e-13 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 71.57 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 9 QWLCAPRPDDVPVAWQEEHTWTLGHLRHDVAQLLAYLRQ---QEGERWALCFENSYLFIVALLATLHAGKT--PVIPG-- 81
Cdd:pfam00501 2 ERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRAlgvGKGDRVAILLPNSPEWVVAFLACLKAGAVyvPLNPRlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 82 ---------HCRVS-LLNEQHLLFDGVLSDKAMDWQGTLRVVS-------------SAMTSVAHDITFPAIRSD--AFVe 136
Cdd:pfam00501 82 aeelayileDSGAKvLITDDALKLEELLEALGKLEVVKLVLVLdrdpvlkeeplpeEAKPADVPPPPPPPPDPDdlAYI- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 137 LFTSGSTGQPKRVIKpiarldSEAALLATRFA--------DRLAGCRVVASVVPQ-HLYGLTFRIFLPMALGLPLHAAML 207
Cdd:pfam00501 161 IYTSGTTGKPKGVML------THRNLVANVLSikrvrprgFGLGPDDRVLSTLPLfHDFGLSLGLLGPLLAGATVVLPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 208 WYAEQLAALSAE-HRY---AFISSPAFLKRLDHNLTPPP-----VELILSAGGMLPwqdVTQAADWLNVWPDEI---YGS 275
Cdd:pfam00501 235 FPALDPAALLELiERYkvtVLYGVPTLLNMLLEAGAPKRallssLRLVLSGGAPLP---PELARRFRELFGGALvngYGL 311
|
330 340 350
....*....|....*....|....*....|..
gi 1736059155 276 TETGILAWrYRHQDDVAW-------LPFPGVR 300
Cdd:pfam00501 312 TETTGVVT-TPLPLDEDLrslgsvgRPLPGTE 342
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
12-445 |
4.88e-12 |
|
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: 67.69 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 12 CAPRPDDVPVAWqEEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT--PVIPGH---- 82
Cdd:cd17646 8 AARTPDAPAVVD-EGRTLTYRELDERANRLAHLLRARgvgPEDRVAVLLPRSADLVVALLAVLKAGAAylPLDPGYpadr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 83 -------CRVSLLneqhlLFDGVLSDKAMDWQGTLRVVSSAMTSVAHDITFPAIRSD--AFVeLFTSGSTGQPKRVIKPI 153
Cdd:cd17646 87 laymladAGPAVV-----LTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDnlAYV-IYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 154 ARLdseaallatrfADRLAGCrvvasvvpQHLYGLT-----------------FRIFLPMALGlplhaAMLWYAEQ---- 212
Cdd:cd17646 161 AGI-----------VNRLLWM--------QDEYPLGpgdrvlqktplsfdvsvWELFWPLVAG-----ARLVVARPgghr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 213 ----LAALSAEHRYA---FISS--PAFLKRLDHNLTpPPVELILSAGGMLPWQDVTQAADWLNVWPDEIYGSTETGI--L 281
Cdd:cd17646 217 dpayLAALIREHGVTtchFVPSmlRVFLAEPAAGSC-ASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIdvT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 282 AWRYRHQDDVAWL----PFPGVRFQPEDDAFR--------------------------------VFSPLINADDGLLLDD 325
Cdd:cd17646 296 HWPVRGPAETPSVpigrPVPNTRLYVLDDALRpvpvgvpgelylggvqlargylgrpaltaerfVPDPFGPGSRMYRTGD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 326 VLQFIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPV--SRGGRQGVGVLLVLNDEArqrwlecGGK 403
Cdd:cd17646 376 LARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARaaPAGAARLVGYVVPAAGAA-------GPD 448
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1736059155 404 PQELtwRRSLLPWLEPVAVPRYWRVIDEIPVNSMNKRVYAQL 445
Cdd:cd17646 449 TAAL--RAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
25-435 |
5.98e-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: 67.32 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 25 EEHTWTLGHLRHDVAQLLAYLRQQE---GERWALCFENSYLFIVALLATLHAGKT--PVIPGHCRVSLlneQHLLFDG-- 97
Cdd:cd12116 9 DDRSLSYAELDERANRLAARLRARGvgpGDRVAVYLPRSARLVAAMLAVLKAGAAyvPLDPDYPADRL---RYILEDAep 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 98 --VLSDKAMDWQGTLRVVSSAMTSVAHDITFPAIR------SDAFVeLFTSGSTGQPKRVIKPIARLDSEAALLATRFAD 169
Cdd:cd12116 86 alVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRtpvspdDLAYV-IYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 170 RlAGCRVVASVVPqhlyglTFRIFLPMALgLPlhaamLWYAEQLAALSAEHryafISSPAFLKRL--DHNL-----TPPP 242
Cdd:cd12116 165 G-PGDRLLAVTTY------AFDISLLELL-LP-----LLAGARVVIAPRET----QRDPEALARLieAHSItvmqaTPAT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 243 VELILSAGgmlpWQD-------------VTQAADWL-----NVWpdEIYGSTETGILAWRYRHQDDVAWL----PFPGVR 300
Cdd:cd12116 228 WRMLLDAG----WQGragltalcggealPPDLAARLlsrvgSLW--NLYGPTETTIWSTAARVTAAAGPIpigrPLANTQ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 301 FQPEDDAFRVFSP------------LINADDGLLLDDVLQFIEN---------------------GQFRLMGRRGRVVKI 347
Cdd:cd12116 302 VYVLDAALRPVPPgvpgelyiggdgVAQGYLGRPALTAERFVPDpfagpgsrlyrtgdlvrrradGRLEYLGRADGQVKI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 348 EEKRISLSEVEQRLLALDGICEVAALPV-SRGGRQGVGVLlvlndearqrWLECGGKPQELTWRRSLLPWLEPVAVPRYW 426
Cdd:cd12116 382 RGHRIELGEIEAALAAHPGVAQAAVVVReDGGDRRLVAYV----------VLKAGAAPDAAALRAHLRATLPAYMVPSAF 451
|
....*....
gi 1736059155 427 RVIDEIPVN 435
Cdd:cd12116 452 VRLDALPLT 460
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
137-449 |
6.48e-12 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 66.20 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 137 LFTSGSTGQPKRVIKPIARLDSEAALLATRFADRLAGCRVVAsvVPQHLYGLTFRIFLPMALGLPLHAAMLWYAEQLAAL 216
Cdd:cd17630 6 ILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLS--LPLYHVGGLAILVRSLLAGAELVLLERNQALAEDLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 217 SAEHRYAFISSPAFLKRLDHNLTPPP---VELILSAGGMLPWQDVTQAADW-LNVWPdeIYGSTETG--ILAWRY-RHQD 289
Cdd:cd17630 84 PPGVTHVSLVPTQLQRLLDSGQGPAAlksLRAVLLGGAPIPPELLERAADRgIPLYT--TYGMTETAsqVATKRPdGFGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 290 DVAWLPFPGVRFQPEDD------AFRVFSPLINADDGLLLDDVL--------QFIENGQFRLMGRRGRVVKIEEKRISLS 355
Cdd:cd17630 162 GGVGVLLPGRELRIVEDgeiwvgGASLAMGYLRGQLVPEFNEDGwfttkdlgELHADGRLTVLGRADNMIISGGENIQPE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 356 EVEQRLLALDGICEVAALPV--SRGGRQGVgVLLVLNDEARqrwlecggkPQEL-TWRRSLLPWLEpvaVPRYWRVIDEI 432
Cdd:cd17630 242 EIEAALAAHPAVRDAFVVGVpdEELGQRPV-AVIVGRGPAD---------PAELrAWLKDKLARFK---LPKRIYPVPEL 308
|
330
....*....|....*..
gi 1736059155 433 PVNSMNKRVYAQLQELF 449
Cdd:cd17630 309 PRTGGGKVDRRALRAWL 325
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
15-439 |
9.61e-12 |
|
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: 66.84 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 15 RPDDVPVAWQEEhTWTLGHLRHDVAQLLAYLRQ---QEGERWALCFENSYLFIVALLATLHAGKTpVIPGHCRVSLLNEQ 91
Cdd:cd12117 10 TPDAVAVVYGDR-SLTYAELNERANRLARRLRAagvGPGDVVGVLAERSPELVVALLAVLKAGAA-YVPLDPELPAERLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 92 HLLFDG----VLSDKAM--DWQGTLRVVSSAMTSVAHDITFPAIRSD----AFVeLFTSGSTGQPKRVIKP---IARLds 158
Cdd:cd12117 88 FMLADAgakvLLTDRSLagRAGGLEVAVVIDEALDAGPAGNPAVPVSpddlAYV-MYTSGSTGRPKGVAVThrgVVRL-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 159 eaaLLATRFADrLAGCRVVASVVPQHLYGLTFRIFLPMALGLPLHAA---MLWYAEQLAALSAEHRY--AFISSPAFLKR 233
Cdd:cd12117 165 ---VKNTNYVT-LGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLApkgTLLDPDALGALIAEEGVtvLWLTAALFNQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 234 LDHNltppP-----VELILSAGGMLPwqdVTQAADWLNVWPD----EIYGSTETGILAWRYRHQDDVAW-------LPFP 297
Cdd:cd12117 241 ADED----PecfagLRELLTGGEVVS---PPHVRRVLAACPGlrlvNGYGPTENTTFTTSHVVTELDEVagsipigRPIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 298 GVRFQPEDDAFRVFSP------------LINADDGLLLDDVLQFIEN--------------------GQFRLMGRRGRVV 345
Cdd:cd12117 314 NTRVYVLDEDGRPVPPgvpgelyvggdgLALGYLNRPALTAERFVADpfgpgerlyrtgdlarwlpdGRLEFLGRIDDQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 346 KIEEKRISLSEVEQRLLALDGICEVAALPVSRGGRQGVGVLLVLNDEARQrwlecggkPQELtwRRSLLPWLEPVAVPRY 425
Cdd:cd12117 394 KIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALD--------AAEL--RAFLRERLPAYMVPAA 463
|
490
....*....|....
gi 1736059155 426 WRVIDEIPVNSMNK 439
Cdd:cd12117 464 FVVLDELPLTANGK 477
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
15-233 |
2.50e-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: 65.72 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 15 RPDDVPVAW-----QEEHTWTLGHLRHDVAQLLAYLRQ--QEGERWALCFENSYLFIVALLATLHAGKTPVI------PG 81
Cdd:cd05931 6 RPDRPAYTFlddegGREETLTYAELDRRARAIAARLQAvgKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPlppptpGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 82 H----------CRVSLL---NEQHLLFDGVLSDKAMDWQGTLRVVSSAMTSVAHDITFPAIRSDAFVEL-FTSGSTGQPK 147
Cdd:cd05931 86 HaerlaailadAGPRVVlttAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLqYTSGSTGTPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 148 RVikpiarLDSEAALLAT-RFADRLAGCR---VVASVVPQ-HLYGLTFRIFLPMALGLPLHaamlwyaeqlaalsaehry 222
Cdd:cd05931 166 GV------VVTHRNLLANvRQIRRAYGLDpgdVVVSWLPLyHDMGLIGGLLTPLYSGGPSV------------------- 220
|
250
....*....|.
gi 1736059155 223 aFISSPAFLKR 233
Cdd:cd05931 221 -LMSPAAFLRR 230
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
13-445 |
7.94e-11 |
|
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: 63.90 E-value: 7.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 13 APRPDDVPVAWqEEHTWTLGHLRHDVAQLLAYLRQ---QEGERWALCFENSYLFIVALLATLHAGKT--PVIPGH----- 82
Cdd:cd17651 6 ARTPDAPALVA-EGRRLTYAELDRRANRLAHRLRArgvGPGDLVALCARRSAELVVALLAILKAGAAyvPLDPAYpaerl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 83 -------CRVSLLNEQHLLFDgvLSDKAMDWQGTLRVVSSAMTSVAHDITfPAIRSDAFVeLFTSGSTGQPKRVIKPIAR 155
Cdd:cd17651 85 afmladaGPVLVLTHPALAGE--LAVELVAVTLLDQPGAAAGADAEPDPA-LDADDLAYV-IYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 156 LdseAALLA--TRFADRLAGCRVVAsvvpqhLYGLTF-----RIFLPMALGLPLH---AAMLWYAEQLAALSAEHRYAFI 225
Cdd:cd17651 161 L---ANLVAwqARASSLGPGARTLQ------FAGLGFdvsvqEIFSTLCAGATLVlppEEVRTDPPALAAWLDEQRISRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 226 SSP-AFLKRLDHNLTPPPVEL-----ILSAGGMLPWQDVTQA-------ADWLNVwpdeiYGSTETGILAWRYRHQDDVA 292
Cdd:cd17651 232 FLPtVALRALAEHGRPLGVRLaalryLLTGGEQLVLTEDLREfcaglpgLRLHNH-----YGPTETHVVTALSLPGDPAA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 293 W-------LPFPGVRFQPEDDAFR--------------------------------VFSPLINADDGLLLDDVLQFIENG 333
Cdd:cd17651 307 WpapppigRPIDNTRVYVLDAALRpvppgvpgelyiggaglargylnrpeltaerfVPDPFVPGARMYRTGDLARWLPDG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 334 QFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICE--VAALPVSRGGRQGVGvLLVLNDEARqrwlecggkPQELTWRR 411
Cdd:cd17651 387 ELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREavVLAREDRPGEKRLVA-YVVGDPEAP---------VDAAELRA 456
|
490 500 510
....*....|....*....|....*....|....
gi 1736059155 412 SLLPWLEPVAVPRYWRVIDEIPVNSMNKRVYAQL 445
Cdd:cd17651 457 ALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
18-439 |
1.72e-10 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 63.64 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 18 DVPVAWQEEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT--PVIPGHCRVSLlneQH 92
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAHVLIAAgvgPDVLVGIAVERSIEMVVGLLAVLKAGGAyvPLDPEYPQDRL---AY 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 93 LLFDG----VLSD----KAMDWQGTLRVV------------SSAMTSVAHDitfPaiRSDAFVeLFTSGSTGQPKRVIKP 152
Cdd:PRK12467 604 MLDDSgvrlLLTQshllAQLPVPAGLRSLcldepadllcgySGHNPEVALD---P--DNLAYV-IYTSGSTGQPKGVAIS 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 153 IARLDSEAALLATRFadRLAGCRVVASVVPQHLYGLTFRIFLPMALGLPLHAA---MLWYAEQLAALSAEHRYAFIS-SP 228
Cdd:PRK12467 678 HGALANYVCVIAERL--QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLppdCARDAEAFAALMADQGVTVLKiVP 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 229 AFLKRL--DHNLTPP-PVELILSAGGMLPW---QDVTQAADWLNVWpdEIYGSTET--GILAWRYRHQD----------- 289
Cdd:PRK12467 756 SHLQALlqASRVALPrPQRALVCGGEALQVdllARVRALGPGARLI--NHYGPTETtvGVSTYELSDEErdfgnvpigqp 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 290 --DVAWL-------PFP----------------GVRFQPEDDAFR-VFSPL-INADDGLLLDDVLQFIENGQFRLMGRRG 342
Cdd:PRK12467 834 laNLGLYildhylnPVPvgvvgelyiggaglarGYHRRPALTAERfVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMD 913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 343 RVVKIEEKRISLSEVEQRLLALDGICEVAALPVS-RGGRQGVGvLLVLNDEARqrwlecGGKPQEL--TWRRSLLPWLEP 419
Cdd:PRK12467 914 HQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPgDAGLQLVA-YLVPAAVAD------GAEHQATrdELKAQLRQVLPD 986
|
490 500
....*....|....*....|
gi 1736059155 420 VAVPRYWRVIDEIPVNSMNK 439
Cdd:PRK12467 987 YMVPAHLLLLDSLPLTPNGK 1006
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
31-394 |
4.44e-10 |
|
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: 61.24 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 31 LGHLRHDVAQLLAYLRQQEGERWALCFENSYLFIVALLATLHAGKT--PVIPghcrvsLLNEQHLLFdgVLSDKAMdwqg 108
Cdd:cd05903 7 LDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVtnPILP------FFREHELAF--ILRRAKA---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 109 tlRVVssAMTSVAHDITFPAIRSDAFVELFTSGSTGQPKRVIKPIARLDSEAALLATRFADRLAGCRVVASVVpQHLYGL 188
Cdd:cd05903 75 --KVF--VVPERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVFLVASPM-AHQTGF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 189 TFRIFLPMALGLPLHAAMLWYAEQLAALSAEHRYAFI-SSPAFLKRL-DHNLT----PPPVELILSAGGMLPWQDVTQAA 262
Cdd:cd05903 150 VYGFTLPLLLGAPVVLQDIWDPDKALALMREHGVTFMmGATPFLTDLlNAVEEagepLSRLRTFVCGGATVPRSLARRAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 263 DWLNVWPDEIYGSTET-GILAWRYRHQDDVAWL----PFPGVRFQPEDDAFRVFSP-----------------LINADDG 320
Cdd:cd05903 230 ELLGAKVCSAYGSTECpGAVTSITPAPEDRRLYtdgrPLPGVEIKVVDDTGATLAPgvegellsrgpsvflgyLDRPDLT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 321 LLLDDVLQF--------IENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVA--ALPVSRGGRQGVGVlLVLN 390
Cdd:cd05903 310 ADAAPEGWFrtgdlarlDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAvvALPDERLGERACAV-VVTK 388
|
....
gi 1736059155 391 DEAR 394
Cdd:cd05903 389 SGAL 392
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
138-439 |
1.35e-09 |
|
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: 59.34 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 138 FTSGSTGQPKRVIKP----IARLDSEAALLATRFADRLAgcrVVASVVPQH-LYGLTFRIFLpmalGLPLHA-AMLWYAE 211
Cdd:cd17633 7 FTSGTTGLPKAYYRSerswIESFVCNEDLFNISGEDAIL---APGPLSHSLfLYGAISALYL----GGTFIGqRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 212 QLAALSAEHRYAFISSPAFLKRL-DHNLTPPPVELILSAGGMLPwqdVTQAADWLNVWPD----EIYGSTETGILAWRYR 286
Cdd:cd17633 80 WIRKINQYNATVIYLVPTMLQALaRTLEPESKIKSIFSSGQKLF---ESTKKKLKNIFPKanliEFYGTSELSFITYNFN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 287 HQDD---VAWLPFPGVRFQPEDDAFRVFSPL-INADDGLLLDDVLQFI---------------ENGQFRLMGRRGRVVKI 347
Cdd:cd17633 157 QESRppnSVGRPFPNVEIEIRNADGGEIGKIfVKSEMVFSGYVRGGFSnpdgwmsvgdigyvdEEGYLYLVGRESDMIII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 348 EEKRISLSEVEQRLLALDGICEVAALPVSRGGRQGVGVLLVLNDEARQRWLecggkpqeltwRRSLLPWLEPVAVPRYWR 427
Cdd:cd17633 237 GGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQL-----------KRFLKQKLSRYEIPKKII 305
|
330
....*....|..
gi 1736059155 428 VIDEIPVNSMNK 439
Cdd:cd17633 306 FVDSLPYTSSGK 317
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
13-439 |
1.44e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.74 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 13 APRPDDVPVAWQEEHtWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT-----PVIPGH-- 82
Cdd:PRK12316 2014 ARAPEAIAVVFGDQH-LSYAELDSRANRLAHRLRARgvgPEVRVAIAAERSFELVVALLAVLKAGGAyvpldPNYPAErl 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 83 ------CRVSLL-NEQHLLFD-----GVLS---DKAMDWQGtlrvvssamtsvaHDITFPAIRSD----AFVeLFTSGST 143
Cdd:PRK12316 2093 aymledSGAALLlTQRHLLERlplpaGVARlplDRDAEWAD-------------YPDTAPAVQLAgenlAYV-IYTSGST 2158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 144 GQPKRVIKPIARLDSEAALLATRFADRLAGCrvVASVVPQHLYGLTFRIFLPMALG--LPLHAAMLWYAEQLAALSAEHR 221
Cdd:PRK12316 2159 GLPKGVAVSHGALVAHCQAAGERYELSPADC--ELQFMSFSFDGAHEQWFHPLLNGarVLIRDDELWDPEQLYDEMERHG 2236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 222 YAFISSPA-----FLKRLDHNLTPPPVELILSAGGMLPWQDVTQAadWLNVWPDEI---YGSTETGI--LAWRYRHQD-- 289
Cdd:PRK12316 2237 VTILDFPPvylqqLAEHAERDGRPPAVRVYCFGGEAVPAASLRLA--WEALRPVYLfngYGPTEAVVtpLLWKCRPQDpc 2314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 290 DVAWLP----FPGVRFQPEDDAFRVFSP------------LINADDGLLLDDVLQFI---------------------EN 332
Cdd:PRK12316 2315 GAAYVPigraLGNRRAYILDADLNLLAPgmagelylggegLARGYLNRPGLTAERFVpdpfsasgerlyrtgdlaryrAD 2394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 333 GQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPVS-RGGRQGVGvlLVLNDEARQrwlecgGKPQEL-TWR 410
Cdd:PRK12316 2395 GVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDgASGKQLVA--YVVPDDAAE------DLLAELrAWL 2466
|
490 500
....*....|....*....|....*....
gi 1736059155 411 RSLLPwlePVAVPRYWRVIDEIPVNSMNK 439
Cdd:PRK12316 2467 AARLP---AYMVPAHWVVLERLPLNPNGK 2492
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
31-447 |
2.27e-09 |
|
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: 59.25 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 31 LGHLRHDVAQLLAYLRQQEGERWALCFENSYLFIVALLATLHAGKtpvipghCRVSLlneqhllfDGVLSDKAMdwQGTL 110
Cdd:cd17653 28 LDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGA-------AYVPL--------DAKLPSARI--QAIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 111 RVVSSAMTsvahdITFPAIRSDAFVeLFTSGSTGQPKRVIKP---IARLDSEA-ALLATRFADRLAgcrvvasvvpqHLY 186
Cdd:cd17653 91 RTSGATLL-----LTTDSPDDLAYI-IFTSGSTGIPKGVMVPhrgVLNYVSQPpARLDVGPGSRVA-----------QVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 187 GLTFRIFLPMALGLPLHAAMLWYAEQLAALSAEHRY--AFISSPAFLKRLDHNlTPPPVELILSAGGMLPwQDVtqAADW 264
Cdd:cd17653 154 SIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVARTvdALMSTPSILSTLSPQ-DFPNLKTIFLGGEAVP-PSL--LDRW 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 265 L-NVWPDEIYGSTETGILAWRYRHQDDVA------------------------------WLPFPGVR----FQPEDDAFR 309
Cdd:cd17653 230 SpGRRLYNAYGPTECTISSTMTELLPGQPvtigkpipnstcyildadlqpvpegvvgeiCISGVQVArgylGNPALTASK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 310 -VFSPLINADDGLLLDDVLQFIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPVSrggrQGVGVLLV 388
Cdd:cd17653 310 fVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEVVLQSQPEVTQAAAIVV----NGRLVAFV 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1736059155 389 LNDEARQRWLecggkpqeltwRRSLLPWLEPVAVPRYWRVIDEIPVNSMNKRVYAQLQE 447
Cdd:cd17653 386 TPETVDVDGL-----------RSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
126-445 |
3.43e-09 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 58.61 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 126 FPAIRSDAFVELFTSGSTGQPKRVIKPIARLDSEAALLATRFADRlaGCRVVASVVPQHL-YGLTFriflpmalglpLHA 204
Cdd:cd05922 112 HEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGIT--ADDRALTVLPLSYdYGLSV-----------LNT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 205 AMLWYAEQLAALSAEHRYAFISS------------P---AFLKRLDHNLTP-PPVELILSAGGMLPWQDVTQAADWLNVW 268
Cdd:cd05922 179 HLLRGATLVLTNDGVLDDAFWEDlrehgatglagvPstyAMLTRLGFDPAKlPSLRYLTQAGGRLPQETIARLRELLPGA 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 269 PDEI-YGSTE-----TGILAWRYRHQDDVAWLPFPGVRFQPEDDAFRVFSPLI-------NADDGLLLDDVLQFI----- 330
Cdd:cd05922 259 QVYVmYGQTEatrrmTYLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEpgeivhrGPNVMKGYWNDPPYRrkegr 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 331 --------------ENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLA--LDGICEVAALPVSRGGRQGVGVLLVLNDEar 394
Cdd:cd05922 339 gggvlhtgdlarrdEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSigLIIEAAAVGLPDPLGEKLALFVTAPDKID-- 416
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1736059155 395 qrwlecggkPQELtwRRSLLPWLEPVAVPRYWRVIDEIPVNSMNKRVYAQL 445
Cdd:cd05922 417 ---------PKDV--LRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
26-446 |
6.85e-09 |
|
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: 57.47 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 26 EHTWTLGHLRHDVAQLLAYLRQ---QEGERWALCFENSYLFIVALLATLHAGKTPVIPGhcrvSLLNEQHLLfdgvlsDK 102
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNlgvSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVIN----PLLHPDDYA------YI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 103 AMDWQGTLRVVSsamtsvAHDITFpairsdafvELFTSGSTGQPKRVIKPIARLDSEAALLATRFADRLAGCRVVASVVP 182
Cdd:cd05919 78 ARDCEARLVVTS------ADDIAY---------LLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLTPGDRVFSSAKM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 183 QHLYGLTFRIFLPMALGLPLHAAMLW-YAEQLAALSAEHR-YAFISSPAFLKRLDHNLTPPP-----VELILSAGGMLPw 255
Cdd:cd05919 143 FFGYGLGNSLWFPLAVGASAVLNPGWpTAERVLATLARFRpTVLYGVPTFYANLLDSCAGSPdalrsLRLCVSAGEALP- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 256 qdVTQAADWLNVWPDEI---YGSTETGIL-------AWRYrhqdDVAWLPFPGVRFQPEDDAFRVFSP------LI---- 315
Cdd:cd05919 222 --RGLGERWMEHFGGPIldgIGATEVGHIflsnrpgAWRL----GSTGRPVPGYEIRLVDEEGHTIPPgeegdlLVrgps 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 316 ------NADDGLLLDDVLQFI---------ENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPVSRG-G 379
Cdd:cd05919 296 aavgywNNPEKSRATFNGGWYrtgdkfcrdADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVVAVPEStG 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 380 RQGVGVLLVLNDEArqrwlecggKPQEL---TWRRSLLPWLEPVAVPRYWRVIDEIPVNSMNKRVYAQLQ 446
Cdd:cd05919 376 LSRLTAFVVLKSPA---------APQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKLR 436
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
39-439 |
1.03e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.04 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 39 AQLLAYLRQQEG----ERWALCFENSYLFIVALLATLHAGKT--PVIPGHC--RVSLLNE----QHLLFDGVLSDKAMDW 106
Cdd:PRK12316 546 ANRLAHALIERGvgpdVLVGVAMERSIEMVVALLAILKAGGAyvPLDPEYPaeRLAYMLEdsgvQLLLSQSHLGRKLPLA 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 107 QGTLRVVSSAMTS--VAHDITFPAIRSD----AFVeLFTSGSTGQPKRVIkpIARLDSEAALLATRFADRLAGCRVVASV 180
Cdd:PRK12316 626 AGVQVLDLDRPAAwlEGYSEENPGTELNpenlAYV-IYTSGSTGKPKGAG--NRHRALSNRLCWMQQAYGLGVGDTVLQK 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 181 VPQHLYGLTFRIFLPMALGLPLHAAMLWYA---EQLAALSAEHRYAFISS-PAFLKRLDHNLTPP---PVELILSAGGML 253
Cdd:PRK12316 703 TPFSFDVSVWEFFWPLMSGARLVVAAPGDHrdpAKLVELINREGVDTLHFvPSMLQAFLQDEDVAsctSLRRIVCSGEAL 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 254 PWQDVTQAADWLnvWPDEI---YGSTETGI----LAWRYRHQD----------------DVAWLPFP------------- 297
Cdd:PRK12316 783 PADAQEQVFAKL--PQAGLynlYGPTEAAIdvthWTCVEEGGDsvpigrpianlacyilDANLEPVPvgvlgelylagrg 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 298 ---GVRFQPEDDAFR-VFSPLINADDGLLLDDVLQFIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAAL 373
Cdd:PRK12316 861 larGYHGRPGLTAERfVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVL 940
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1736059155 374 PVsrGGRQGVGvLLVLNDEArqrwlecGGKPQEL-TWRRSLLPwlePVAVPRYWRVIDEIPVNSMNK 439
Cdd:PRK12316 941 AV--DGKQLVG-YVVLESEG-------GDWREALkAHLAASLP---EYMVPAQWLALERLPLTPNGK 994
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
15-439 |
1.89e-08 |
|
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: 56.17 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 15 RPDDVPVAWQEEHTwTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT--PVIPGHCRVSLln 89
Cdd:cd12115 12 TPDAIALVCGDESL-TYAELNRRANRLAARLRAAgvgPESRVGVCLERTPDLVVALLAVLKAGAAyvPLDPAYPPERL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 90 eqhllfDGVLSDKAMdwqgtlrvvssamtsvAHDITFPAirSDAFVeLFTSGSTGQPKRVIKPiarLDSEAALL---ATR 166
Cdd:cd12115 89 ------RFILEDAQA----------------RLVLTDPD--DLAYV-IYTSGSTGRPKGVAIE---HRNAAAFLqwaAAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 167 F-ADRLAGCRVVASVVpqhlYGLT-FRIFLPMALGLPLHaaMLWYAEQLAALSAEHRYAFISS-PAFLKRL-DHNLTPPP 242
Cdd:cd12115 141 FsAEELAGVLASTSIC----FDLSvFELFGPLATGGKVV--LADNVLALPDLPAAAEVTLINTvPSAAAELlRHDALPAS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 243 VELILSAGGMLPWQDVTQAADWLNVwpDEI---YGSTE-----TGILAWRYRHQDDVAWLPFPGVRFQPEDDAFR----- 309
Cdd:cd12115 215 VRVVNLAGEPLPRDLVQRLYARLQV--ERVvnlYGPSEdttysTVAPVPPGASGEVSIGRPLANTQAYVLDRALQpvplg 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 310 ---------------------------VFSPLINADDGLLLDDVLQFIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLL 362
Cdd:cd12115 293 vpgelyiggagvargylgrpgltaerfLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1736059155 363 ALDGICE-VAALPVSRGGRQGVGVLLVLNDEArqrwlecGGKPQELtwRRSLLPWLEPVAVPRYWRVIDEIPVNSMNK 439
Cdd:cd12115 373 SIPGVREaVVVAIGDAAGERRLVAYIVAEPGA-------AGLVEDL--RRHLGTRLPAYMVPSRFVRLDALPLTPNGK 441
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
3-440 |
8.34e-08 |
|
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: 54.86 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 3 QPLTLAQWL---CAPRPDDVPVAWqEEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT 76
Cdd:COG1020 474 ADATLHELFeaqAARTPDAVAVVF-GDQSLTYAELNARANRLAHHLRALgvgPGDLVGVCLERSLEMVVALLAVLKAGAA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 77 --PVIPGH-----------CRVSLLneqhlLFDGVLSDKAMDWQGTLRVVSSAMTSvAHDITFPAIRSD----AFVeLFT 139
Cdd:COG1020 553 yvPLDPAYpaerlaymledAGARLV-----LTQSALAARLPELGVPVLALDALALA-AEPATNPPVPVTpddlAYV-IYT 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 140 SGSTGQPKRVIKP----IARLDSEAALLATRFADRLAGcrvVASvvpqhlygLTF-----RIFLPMALGLPLH---AAML 207
Cdd:COG1020 626 SGSTGRPKGVMVEhralVNLLAWMQRRYGLGPGDRVLQ---FAS--------LSFdasvwEIFGALLSGATLVlapPEAR 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 208 WYAEQLAALSAEHRYAFISS-PAFLKRLDHNL--TPPPVELILSAGGMLPWQDVTQaadWLNVWPDEI----YGSTETGI 280
Cdd:COG1020 695 RDPAALAELLARHRVTVLNLtPSLLRALLDAApeALPSLRLVLVGGEALPPELVRR---WRARLPGARlvnlYGPTETTV 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 281 LAWRYRHQDDVAWL-------PFPGVRF-------------------------------QPEDDAFRvfsplinaddgll 322
Cdd:COG1020 772 DSTYYEVTPPDADGgsvpigrPIANTRVyvldahlqpvpvgvpgelyiggaglargylnRPELTAER------------- 838
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 323 lddvlqFIEN---------------------GQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPVS-RGGR 380
Cdd:COG1020 839 ------FVADpfgfpgarlyrtgdlarwlpdGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREdAPGD 912
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 381 QGVGVLLVLNDEARqrwlecggkPQELTWRRSLLPWLEPVAVPRYWRVIDEIPVNSMNKR 440
Cdd:COG1020 913 KRLVAYVVPEAGAA---------AAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKL 963
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
15-439 |
1.45e-07 |
|
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: 53.49 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 15 RPDDVPVAWqEEHTWTLGHLRHDVAQLLAYLRQ---QEGERWALCFENSYLFIVALLATLHAGKT--PVIPGHC--RVsl 87
Cdd:cd17655 10 TPDHTAVVF-EDQTLTYRELNERANQLARTLREkgvGPDTIVGIMAERSLEMIVGILGILKAGGAylPIDPDYPeeRI-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 88 lneQHLLFDG----VLSDKAMD----WQGTLRVVSSAMTSVAHDITF-PAIRSD--AFVeLFTSGSTGQPKRVIkpiarL 156
Cdd:cd17655 87 ---QYILEDSgadiLLTQSHLQppiaFIGLIDLLDEDTIYHEESENLePVSKSDdlAYV-IYTSGSTGKPKGVM-----I 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 157 DSEAALLATRFADR---LAGCRVVASVVPQHLYGLTFRIFLPMALGLPLH---AAMLWYAEQLAALSAEHRYAFIS-SPA 229
Cdd:cd17655 158 EHRGVVNLVEWANKviyQGEHLRVALFASISFDASVTEIFASLLSGNTLYivrKETVLDGQALTQYIRQNRITIIDlTPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 230 FLKRLDHN--LTPPPVELILSAGGMLPWQDVTQAADWLNVWPDEI--YGSTETGILA--WRYRHQDDVAWLPFPGV---- 299
Cdd:cd17655 238 HLKLLDAAddSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITnaYGPTETTVDAsiYQYEPETDQQVSVPIGKplgn 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 300 ----------RFQPE------------------------DDAFrVFSPLINADDGLLLDDVLQFIENGQFRLMGRRGRVV 345
Cdd:cd17655 318 triyildqygRPQPVgvagelyiggegvargylnrpeltAEKF-VDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 346 KIEEKRISLSEVEQRLLALDGICEVAALpvSRGGRQGVGVL---LVLNDEArqrwlecggKPQELtwRRSLLPWLEPVAV 422
Cdd:cd17655 397 KIRGYRIELGEIEARLLQHPDIKEAVVI--ARKDEQGQNYLcayIVSEKEL---------PVAQL--REFLARELPDYMI 463
|
490
....*....|....*..
gi 1736059155 423 PRYWRVIDEIPVNSMNK 439
Cdd:cd17655 464 PSYFIKLDEIPLTPNGK 480
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
131-448 |
1.52e-07 |
|
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: 53.49 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 131 SDAFVELFTSGSTGQPKRVIKPIARLDSEAALLATRFadRLAGCRVVASVVPQ-HLYGLTFRIFLPMALGLP--LHAAML 207
Cdd:cd05909 147 DDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIF--DPNPEDVVFGALPFfHSFGLTGCLWLPLLSGIKvvFHPNPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 208 wYAEQLAALSAEHRYA-FISSPAFLK---RLDHNLTPPPVELILSAGGMLPWQDVTQAADWLNVWPDEIYGSTETGIL-- 281
Cdd:cd05909 225 -DYKKIPELIYDKKATiLLGTPTFLRgyaRAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTECSPVis 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 282 ---AWRYRHQDDVAwLPFPG--VRFQPEDDAFRVFSP---LI------------NADDGLLLDDVLQ---------FIEN 332
Cdd:cd05909 304 vntPQSPNKEGTVG-RPLPGmeVKIVSVETHEEVPIGeggLLlvrgpnvmlgylNEPELTSFAFGDGwydtgdigkIDGE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 333 GQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPVSRGGRQGVGVLLVLNDEArqrwlecgGKPQELT--WR 410
Cdd:cd05909 383 GFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKGEKIVLLTTTTD--------TDPSSLNdiLK 454
|
330 340 350
....*....|....*....|....*....|....*...
gi 1736059155 411 RSLLPWLepvAVPRYWRVIDEIPVNSMNKRVYAQLQEL 448
Cdd:cd05909 455 NAGISNL---AKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
16-435 |
4.66e-07 |
|
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: 51.92 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 16 PDDVPVAWqEEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT--PVIPGH--CRVSLl 88
Cdd:cd17643 1 PEAVAVVD-EDRRLTYGELDARANRLARTLRAEgvgPGDRVALALPRSAELIVALLAILKAGGAyvPIDPAYpvERIAF- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 89 neqhllfdgVLSDKAmdwqgtLRVVssamtsvahdITFPAirSDAFVeLFTSGSTGQPKRVIKPIARLdseAALLAtrfa 168
Cdd:cd17643 79 ---------ILADSG------PSLL----------LTDPD--DLAYV-IYTSGSTGRPKGVVVSHANV---LALFA---- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 169 drlaGCRVVASVVPQ------HLYGLTF---RIFLPMALG-----LPLHAAMlwYAEQLAALSAEHRYAFIS-SP----A 229
Cdd:cd17643 124 ----ATQRWFGFNEDdvwtlfHSYAFDFsvwEIWGALLHGgrlvvVPYEVAR--SPEDFARLLRDEGVTVLNqTPsafyQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 230 FLKRLDHNLT-PPPVELILSAG-----GML-PWQD--VTQAADWLNvwpdeIYGSTETGILA-WRYRHQDDVAWL----- 294
Cdd:cd17643 198 LVEAADRDGRdPLALRYVIFGGealeaAMLrPWAGrfGLDRPQLVN-----MYGITETTVHVtFRPLDAADLPAAaaspi 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 295 --PFPGVRFQPEDDAFRVFSP------------LINADDGLLLDDVLQFIEN---------------------GQFRLMG 339
Cdd:cd17643 273 grPLPGLRVYVLDADGRPVPPgvvgelyvsgagVARGYLGRPELTAERFVANpfggpgsrmyrtgdlarrlpdGELEYLG 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 340 RRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPvsRGGRQGVGVL---LVLNDEARQRwlecggkPQEL-TWRRSLLP 415
Cdd:cd17643 353 RADEQVKIRGFRIELGEIEAALATHPSVRDAAVIV--REDEPGDTRLvayVVADDGAAAD-------IAELrALLKELLP 423
|
490 500
....*....|....*....|
gi 1736059155 416 wlePVAVPRYWRVIDEIPVN 435
Cdd:cd17643 424 ---DYMVPARYVPLDALPLT 440
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
52-399 |
1.40e-06 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.94 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 52 RWALCFENSYLFIVALLATLHAGKT--PVIPGH-----------CRVSLLNEQHLLFD--GVLSDKAMDW--QGTLRVVS 114
Cdd:PRK05691 2240 RVGLALERSLEMVVGLLAILKAGGAyvPLDPEYplerlhymiedSGIGLLLSDRALFEalGELPAGVARWclEDDAAALA 2319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 115 SAMTSVAHDITFPaiRSDAFVeLFTSGSTGQPKRVIKPIARLDSEAALLATRFADRLAGCRVvasvvpqHLYGLTF---- 190
Cdd:PRK05691 2320 AYSDAPLPFLSLP--QHQAYL-IYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCEL-------HFYSINFdaas 2389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 191 -RIFLPMALG--LPLHAAMLWYAEQLAALSAEHRYAFIS-SPAFLKRLDHNLTPP----PVELILSAGGMLP---WQDVT 259
Cdd:PRK05691 2390 eRLLVPLLCGarVVLRAQGQWGAEEICQLIREQQVSILGfTPSYGSQLAQWLAGQgeqlPVRMCITGGEALTgehLQRIR 2469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 260 QA---ADWLNVwpdeiYGSTETGI--LAWR-----------------------YRHQDDVAWLP--------------FP 297
Cdd:PRK05691 2470 QAfapQLFFNA-----YGPTETVVmpLACLapeqleegaasvpigrvvgarvaYILDADLALVPqgatgelyvggaglAQ 2544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 298 GVRFQPEDDAFR-VFSPL-INADDGLLLDDVLQFIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPV 375
Cdd:PRK05691 2545 GYHDRPGLTAERfVADPFaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL 2624
|
410 420
....*....|....*....|....*....
gi 1736059155 376 -SRGGRQGVGVL----LVLNDEARQRWLE 399
Cdd:PRK05691 2625 dTPSGKQLAGYLvsavAGQDDEAQAALRE 2653
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
15-164 |
1.94e-06 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 49.87 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 15 RPDDVPVAWQEEhTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGktpvipghCRVSLLNEQ 91
Cdd:PRK09029 16 RPQAIALRLNDE-VLTWQQLCARIDQLAAGFAQQgvvEGSGVALRGKNSPETLLAYLALLQCG--------ARVLPLNPQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 92 -----------HLLFDGVLSDKAMDWQGTLRVVSSAMTSVAHDITFPAIRSDAFVelFTSGSTGQPKRVIKPI-ARLDSE 159
Cdd:PRK09029 87 lpqplleellpSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMT--LTSGSTGLPKAAVHTAqAHLASA 164
|
....*
gi 1736059155 160 AALLA 164
Cdd:PRK09029 165 EGVLS 169
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
129-313 |
1.95e-06 |
|
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: 49.82 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 129 IRSDAFVELFTSGSTGQPKRVIKPIARLDSEAALLatRFA-DRLAGCRVVASVVPQHLYGLTFRIFLPMALGLPlhaaML 207
Cdd:cd05973 86 LDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYL--RDAvDLRPEDSFWNAADPGWAYGLYYAITGPLALGHP----TI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 208 WYAeqlAALSAEHRY---------AFISSPAFLKRLDHNLTPPPVELIL------SAGGMLPWQDVTQAADWLNVWPDEI 272
Cdd:cd05973 160 LLE---GGFSVESTWrvierlgvtNLAGSPTAYRLLMAAGAEVPARPKGrlrrvsSAGEPLTPEVIRWFDAALGVPIHDH 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1736059155 273 YGSTETGILAWRYRHQDDV-----AWLPFPGVRFQPEDDAFRVFSP 313
Cdd:cd05973 237 YGQTELGMVLANHHALEHPvhagsAGRAMPGWRVAVLDDDGDELGP 282
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
26-444 |
4.80e-06 |
|
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: 48.83 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 26 EHTWTLGHLRHDVAQ----LLAYLRQQEGERWALCFENSYLFIVALLATLHAGKT--PVIPGHCRVSLlneQHLLFDgvl 99
Cdd:cd05941 9 GDSITYADLVARAARlanrLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVavPLNPSYPLAEL---EYVITD--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 100 SDKAMdwqgtlrVVSSAMTsvahditfpairsdafveLFTSGSTGQPKRVIKPIARLDSEAALLAT--RFADRlagcRVV 177
Cdd:cd05941 83 SEPSL-------VLDPALI------------------LYTSGTTGRPKGVVLTHANLAANVRALVDawRWTED----DVL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 178 ASVVP-QHLYGLTFRIFLPMALGlplhAAMLWYAEQLAALSAEHRY-----AFISSPAFLKRL----DHNLTPPPVELIL 247
Cdd:cd05941 134 LHVLPlHHVHGLVNALLCPLFAG----ASVEFLPKFDPKEVAISRLmpsitVFMGVPTIYTRLlqyyEAHFTDPQFARAA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 248 SAGGM---------LP------WQDVTQAAdwlnvwPDEIYGSTETGI-LAWRY---RHQDDVAWlPFPGV--RFQPEDD 306
Cdd:cd05941 210 AAERLrlmvsgsaaLPvptleeWEAITGHT------LLERYGMTEIGMaLSNPLdgeRRPGTVGM-PLPGVqaRIVDEET 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 307 A----------FRVFSP-LINADDGLLLDDVLQFIENGQFRL--MGRR---------GR----VVKIEEKRISLSEVEQR 360
Cdd:cd05941 283 GeplprgevgeIQVRGPsVFKEYWNKPEATKEEFTDDGWFKTgdLGVVdedgyywilGRssvdIIKSGGYKVSALEIERV 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 361 LLALDGICEVA--ALPVSRGGrQGVGVLLVLNDEARQRWLEcggkpQELTWRRSLLPwlePVAVPRYWRVIDEIPVNSM- 437
Cdd:cd05941 363 LLAHPGVSECAviGVPDPDWG-ERVVAVVVLRAGAAALSLE-----ELKEWAKQRLA---PYKRPRRLILVDELPRNAMg 433
|
....*....
gi 1736059155 438 --NKRVYAQ 444
Cdd:cd05941 434 kvNKKELRK 442
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
331-448 |
6.22e-06 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 48.60 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 331 ENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPV-SRGGRQGVGVLLVLNDEARqrwLEcggkPQELTw 409
Cdd:PRK06155 412 ADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVpSELGEDEVMAAVVLRDGTA---LE----PVALV- 483
|
90 100 110
....*....|....*....|....*....|....*....
gi 1736059155 410 rRSLLPWLEPVAVPRYWRVIDEIPVNSMNKRVYAQLQEL 448
Cdd:PRK06155 484 -RHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQ 521
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
16-396 |
1.06e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.41 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 16 PDDVPVAWQEEHTwTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT-----PVIPGHCRVSL 87
Cdd:PRK12316 3071 PDAVALAFGEQRL-SYAELNRRANRLAHRLIERgvgPDVLVGVAVERSLEMVVGLLAILKAGGAyvpldPEYPEERLAYM 3149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 88 LNE---QHLLFDGVLSDKAMDWQGTLRVVSSAMTSVAHDITFPAIRSDAFVELFTSGSTGQPKRVIKPIARLDSEAALLA 164
Cdd:PRK12316 3150 LEDsgaQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQ 3229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 165 TRFADRLAGCrvVASVVPQHLYGLTFRIFLPMALG--LPLHAAMLWYAEQLAAlSAEHRYAFISSPAFLKRLDHNLTPPP 242
Cdd:PRK12316 3230 QAYGLGVGDR--VLQFTTFSFDVFVEELFWPLMSGarVVLAGPEDWRDPALLV-ELINSEGVDVLHAYPSMLQAFLEEED 3306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 243 ------VELILSAGGMLPWQDVTQAADWLNVWpdEIYGSTETGILAWRYRHQD--------------------DVAWLPF 296
Cdd:PRK12316 3307 ahrctsLKRIVCGGEALPADLQQQVFAGLPLY--NLYGPTEATITVTHWQCVEegkdavpigrpianracyilDGSLEPV 3384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 297 P----------------GVRFQPEDDAFR-VFSPLINADDGLLLDDVLQFIENGQFRLMGRRGRVVKIEEKRISLSEVEQ 359
Cdd:PRK12316 3385 PvgalgelylggeglarGYHNRPGLTAERfVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEA 3464
|
410 420 430
....*....|....*....|....*....|....*..
gi 1736059155 360 RLLALDGICEVAALPVSrgGRQGVGVLLVLNDEARQR 396
Cdd:PRK12316 3465 RLLEHPWVREAVVLAVD--GRQLVAYVVPEDEAGDLR 3499
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
12-439 |
2.19e-05 |
|
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: 46.77 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 12 CAPRPDDVPV-AWQEEhtWT---LGHLRHDVAQLLAYLRQQEGERWALCFENSYLFIVALLATLHAGKT--PVIPGHcrv 85
Cdd:cd05918 9 ARSQPDAPAVcAWDGS--LTyaeLDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAfvPLDPSH--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 86 sllNEQHLlfdgvlsdkamdwQGTLRVVSS--AMTSVAHDItfpairsdAFVeLFTSGSTGQPKrvikpiarldseaall 163
Cdd:cd05918 84 ---PLQRL-------------QEILQDTGAkvVLTSSPSDA--------AYV-IFTSGSTGKPK---------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 164 atrfadrlaGCRV----VASVVPQHLYgltfriflpmALGLPLHAAMLWYA---------EQLAALSAeHRYAFISS--- 227
Cdd:cd05918 123 ---------GVVIehraLSTSALAHGR----------ALGLTSESRVLQFAsytfdvsilEIFTTLAA-GGCLCIPSeed 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 228 -----PAFLKRLDHN---LTP-----------PPVELILSAGGMLPWQDVTQAADWLNVWpdEIYGSTETGILAwrYRHQ 288
Cdd:cd05918 183 rlndlAGFINRLRVTwafLTPsvarlldpedvPSLRTLVLGGEALTQSDVDTWADRVRLI--NAYGPAECTIAA--TVSP 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 289 DDVAW------LPFPGVRF--------------------------------QPEDDAFRVFSPLINADDGLLLDDVL--- 327
Cdd:cd05918 259 VVPSTdprnigRPLGATCWvvdpdnhdrlvpigavgelliegpilargylnDPEKTAAAFIEDPAWLKQEGSGRGRRlyr 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 328 -----QFIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLA-LDGICEVAALPVSRGGRQGVGVL---LVLNDEARQR-- 396
Cdd:cd05918 339 tgdlvRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVEVVKPKDGSSSPQLvafVVLDGSSSGSgd 418
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1736059155 397 --WLECGGKPQELTWRRSLLPWLE---PVA-VPRYWRVIDEIPVNSMNK 439
Cdd:cd05918 419 gdSLFLEPSDEFRALVAELRSKLRqrlPSYmVPSVFLPLSHLPLTASGK 467
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
39-435 |
4.68e-05 |
|
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: 45.71 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 39 AQLLAYLRQQEGERWALCFENSYLFIVALLATLHAGKT--PVIPGHC--RVSLLneqhllfdgvLSDKAmdwqgtlrvVS 114
Cdd:cd17652 26 ARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAylPLDPAYPaeRIAYM----------LADAR---------PA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 115 SAMTSVAHDitfpairsdAFVeLFTSGSTGQPKRVIKPIARLDSEAALLATRFADRlAGCRVVAsvvpqhLYGLTFRIFL 194
Cdd:cd17652 87 LLLTTPDNL---------AYV-IYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG-PGSRVLQ------FASPSFDASV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 195 P---MAL--GLPLH---AAMLWYAEQLAALSAEHRyafisspaflkrLDHNLTPPPVELILSAGGMLPWQDVTQAAD--- 263
Cdd:cd17652 150 WellMALlaGATLVlapAEELLPGEPLADLLREHR------------ITHVTLPPAALAALPPDDLPDLRTLVVAGEacp 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 264 ------W------LNvwpdeIYGSTETGILAWRYRHQDDVAWLPF----PGVRFQPEDDAFRVFSP------------LI 315
Cdd:cd17652 218 aelvdrWapgrrmIN-----AYGPTETTVCATMAGPLPGGGVPPIgrpvPGTRVYVLDARLRPVPPgvpgelyiagagLA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 316 NADDGLLLDDVLQFIEN---------------------GQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGIceVAALP 374
Cdd:cd17652 293 RGYLNRPGLTAERFVADpfgapgsrmyrtgdlarwradGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGV--AEAVV 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1736059155 375 VSRGGRQGVGVL---LVLNDEARQrwlecggKPQELtwRRSLLPWLEPVAVPRYWRVIDEIPVN 435
Cdd:cd17652 371 VVRDDRPGDKRLvayVVPAPGAAP-------TAAEL--RAHLAERLPGYMVPAAFVVLDALPLT 425
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
25-150 |
6.15e-05 |
|
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: 45.35 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 25 EEHTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKTPVI---PGHCRVSLLNEQHL----- 93
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLglrPGDSVILQFDDNEDFIPAFWACVLAGFVPAPltvPPTYDEPNARLRKLrhiwq 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1736059155 94 LFDG--VLSDKAM-----------DWQGTLRVVSSAMTSVAHDITFPAIRS-DAFVELFTSGSTGQPKRVI 150
Cdd:cd05906 116 LLGSpvVLTDAELvaefagletlsGLPGIRVLSIEELLDTAADHDLPQSRPdDLALLMLTSGSTGFPKAVP 186
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
331-446 |
8.38e-05 |
|
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: 44.59 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 331 ENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPV-SRGGRQGVGVLLVLNDEARQrwlecggKPQEL-T 408
Cdd:cd05934 315 ADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVpDEVGEDEVKAVVVLRPGETL-------DPEELfA 387
|
90 100 110
....*....|....*....|....*....|....*...
gi 1736059155 409 WRRSLLPwlePVAVPRYWRVIDEIPVNSMNKRVYAQLQ 446
Cdd:cd05934 388 FCEGQLA---YFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
16-149 |
1.21e-04 |
|
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: 44.18 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 16 PDDVPVAWQEEhTWTLGHLRHDVAQLLAYLRQ---QEGERWALCFENSYLFIVALLATLHAGKT--PVIPGHCRVSLlne 90
Cdd:cd12114 1 PDATAVICGDG-TLTYGELAERARRVAGALKAagvRPGDLVAVTLPKGPEQVVAVLGILAAGAAyvPVDIDQPAARR--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 91 QHLLFDG----VLSDKAmDWQG---TLRVVSSAMTSVAHDITFPAIRSD----AFVeLFTSGSTGQPKRV 149
Cdd:cd12114 77 EAILADAgarlVLTDGP-DAQLdvaVFDVLILDLDALAAPAPPPPVDVApddlAYV-IFTSGSTGTPKGV 144
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
127-282 |
1.47e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 44.22 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 127 PAIRSDAFVELFTSGSTGQPKRVikPIARLDSEAALLATRFADRL---AGCRVvaSVVPQHLYGLTF-RIFLPMALGLPL 202
Cdd:PRK13383 170 PAVAAPGRIVLLTSGTTGKPKGV--PRAPQLRSAVGVWVTILDRTrlrTGSRI--SVAMPMFHGLGLgMLMLTIALGGTV 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 203 HAAMLWYAEQLAALSAEHRY-AFISSPAFLKRLdHNLTP--------PPVELILSAGGMLpwqDVTQAADWLNVWPD--- 270
Cdd:PRK13383 246 LTHRHFDAEAALAQASLHRAdAFTAVPVVLARI-LELPPrvrarnplPQLRVVMSSGDRL---DPTLGQRFMDTYGDily 321
|
170
....*....|..
gi 1736059155 271 EIYGSTETGILA 282
Cdd:PRK13383 322 NGYGSTEVGIGA 333
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
16-439 |
2.91e-04 |
|
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: 43.23 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 16 PDDVPVAWQEEhTWTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT-----PVIPGHCRVSL 87
Cdd:cd17656 2 PDAVAVVFENQ-KLTYRELNERSNQLARFLREKgvkKDSIVAIMMERSAEMIVGILGILKAGGAfvpidPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 88 LNE---QHLLFDGVLSDKAMDWQGTLRVVSSAMTSV-AHDITFPAIRSDAFVELFTSGSTGQPKRVIKPIARLdseAALL 163
Cdd:cd17656 81 MLDsgvRVVLTQRHLKSKLSFNKSTILLEDPSISQEdTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNM---VNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 164 ATRF--ADRLAGCRVVASVVPQhlYGLTFR-IFLPMALGLPLH---AAMLWYAEQLAALSAEHRYAFISSP-AFLKRLDH 236
Cdd:cd17656 158 HFERekTNINFSDKVLQFATCS--FDVCYQeIFSTLLSGGTLYiirEETKRDVEQLFDLVKRHNIEVVFLPvAFLKFIFS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 237 -----NLTPPPVELILSAGGML----PWQDVTQAAdwlNVWPDEIYGSTETGIL-AWRYRHQDDVAWLPFPGV------- 299
Cdd:cd17656 236 erefiNRFPTCVKHIITAGEQLvitnEFKEMLHEH---NVHLHNHYGPSETHVVtTYTINPEAEIPELPPIGKpisntwi 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 300 -----RFQPE--------------------------DDAFrVFSPLINADDGLLLDDVLQFIENGQFRLMGRRGRVVKIE 348
Cdd:cd17656 313 yildqEQQLQpqgivgelyisgasvargylnrqeltAEKF-FPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 349 EKRISLSEVEQRLLALDGICEvaalpvsrggrqgvGVLLVLNDEARQRWLECGGKP-QELT---WRRSLLPWLEPVAVPR 424
Cdd:cd17656 392 GYRIELGEIEAQLLNHPGVSE--------------AVVLDKADDKGEKYLCAYFVMeQELNisqLREYLAKQLPEYMIPS 457
|
490
....*....|....*
gi 1736059155 425 YWRVIDEIPVNSMNK 439
Cdd:cd17656 458 FFVPLDQLPLTPNGK 472
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
332-433 |
3.19e-04 |
|
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: 42.84 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 332 NGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICE-VAALPVSRGGRQGVGVLLVLNDEARQRWLecggkpqeltwR 410
Cdd:cd17650 344 DGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEaVVAVREDKGGEARLCAYVVAAATLNTAEL-----------R 412
|
90 100
....*....|....*....|...
gi 1736059155 411 RSLLPWLEPVAVPRYWRVIDEIP 433
Cdd:cd17650 413 AFLAKELPSYMIPSYYVQLDALP 435
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1-167 |
3.87e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 42.75 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 1 MKQPLTLAQWLCAPRPDDVPVAWQEEHTWTLGHLRHDVAQLLAYLRQQ-EGERWA---LCFENSYLFIVALLATLHAGKT 76
Cdd:PRK07867 1 TSSAPTVAELLLPLAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPhvgVLLDNTPEFSLLLGAAALSGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 77 PV---------------IPGHCRVSLLNEQHL-LFDGVLSDKAMdwqgtLRVVSSAMTSV--AH-DITFPAIR---SDAF 134
Cdd:PRK07867 81 PVglnptrrgaalardiAHADCQLVLTESAHAeLLDGLDPGVRV-----INVDSPAWADElaAHrDAEPPFRVadpDDLF 155
|
170 180 190
....*....|....*....|....*....|...
gi 1736059155 135 VELFTSGSTGQPKRVIKPIARLDSEAALLATRF 167
Cdd:PRK07867 156 MLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRF 188
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
52-289 |
4.08e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 43.02 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 52 RWALCFENSYLFIVALLATLHAGKT--PVIPGHCRVSL------------LNEQHLL-----FDGVLS---DKAMDWQGt 109
Cdd:PRK12316 4603 LVGIAMERSAEMMVGLLAVLKAGGAyvPLDPEYPRERLaymmedsgaallLTQSHLLqrlpiPDGLASlalDRDEDWEG- 4681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 110 lrvvssamtSVAHDitfPAIRSD----AFVeLFTSGSTGQPKRVIKPIARLDSEAALLATRFADRLAGCRVvasvvpqHL 185
Cdd:PRK12316 4682 ---------FPAHD---PAVRLHpdnlAYV-IYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVL-------QF 4741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 186 YGLTFRI-----FLPMALGLPLH--AAMLWYAEQLAALSAEHRYAFISSP-----AFLKRLDHNLTPPPVELILSAGGML 253
Cdd:PRK12316 4742 MSFSFDGsheglYHPLINGASVVirDDSLWDPERLYAEIHEHRVTVLVFPpvylqQLAEHAERDGEPPSLRVYCFGGEAV 4821
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1736059155 254 PWQDVTQAadWLNVWPDEI---YGSTETGI--LAWRYRHQD 289
Cdd:PRK12316 4822 AQASYDLA--WRALKPVYLfngYGPTETTVtvLLWKARDGD 4860
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
329-435 |
5.07e-04 |
|
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: 42.39 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 329 FIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGIceVAALPVSRGGRQGvgvllvlNDEARQRWL------ECGG 402
Cdd:cd17648 340 WLPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGV--RECAVVAKEDASQ-------AQSRIQKYLvgyylpEPGH 410
|
90 100 110
....*....|....*....|....*....|....*
gi 1736059155 403 KPQE--LTWRRSLLPwlePVAVPRYWRVIDEIPVN 435
Cdd:cd17648 411 VPESdlLSFLRAKLP---RYMVPARLVRLEGIPVT 442
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
28-278 |
5.44e-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: 41.95 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 28 TWTLGHLRHDVAQL---LAYLRQQEGERWALCFENSYLFIVALLATLHAGKTPVipghcrvsLLNEQhllfdgvLSDKAM 104
Cdd:cd05912 1 SYTFAELFEEVSRLaehLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAV--------LLNTR-------LTPNEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 105 DWQgtlrvvssaMTSVAhditfpAIRSDAFVELFTSGSTGQPKRVIKPI----ARLDSEAALLATRFADR-LAgcrvvas 179
Cdd:cd05912 66 AFQ---------LKDSD------VKLDDIATIMYTSGTTGKPKGVQQTFgnhwWSAIGSALNLGLTEDDNwLC------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 180 VVPQ-HLYGLTFrIFLPMALGLPLHAAMLWYAEQLAALSAEHRYAFISS-PAFLKRL---DHNLTPPPVELILSAGGMLP 254
Cdd:cd05912 124 ALPLfHISGLSI-LMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVvPTMLQRLleiLGEGYPNNLRCILLGGGPAP 202
|
250 260
....*....|....*....|....
gi 1736059155 255 wQDVTQAADWLNVWPDEIYGSTET 278
Cdd:cd05912 203 -KPLLEQCKEKGIPVYQSYGMTET 225
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
13-439 |
6.24e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 42.46 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 13 APRPDDVPVAWQEEHTwTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKT--PVIPGHCRVSL 87
Cdd:PRK12467 1585 AATPEAVALVFGEQEL-TYGELNRRANRLAHRLIALgvgPEVLVGIAVERSLEMVVGLLAILKAGGAyvPLDPEYPRERL 1663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 88 ------------LNEQHL-----LFDGVLS---DKAMDWQGTlrvvssamtsvaHDITFPAIRSD----AFVeLFTSGST 143
Cdd:PRK12467 1664 aymiedsgiellLTQSHLqarlpLPDGLRSlvlDQEDDWLEG------------YSDSNPAVNLApqnlAYV-IYTSGST 1730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 144 GQPKRVIKP----IARLDseaallATRFADRLAGCRVVASVVPQHLYGLTFRIFLPMALGLPLHAAMLWYA---EQLAAL 216
Cdd:PRK12467 1731 GRPKGAGNRhgalVNRLC------ATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHrdpEQLIQL 1804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 217 SAEHRYAFISSP-----AFLKRLDHNLTPPPVELILSAGGMLPWQDVTQaadWLNVWPD----EIYGSTETGI--LAWRY 285
Cdd:PRK12467 1805 IERQQVTTLHFVpsmlqQLLQMDEQVEHPLSLRRVVCGGEALEVEALRP---WLERLPDtglfNLYGPTETAVdvTHWTC 1881
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 286 RHQD--------------DVAWL-------PFP----------------GVRFQPEDDAFR-VFSPL-INADDGLLLDDV 326
Cdd:PRK12467 1882 RRKDlegrdsvpigqpiaNLSTYildaslnPVPigvagelylggvglarGYLNRPALTAERfVADPFgTVGSRLYRTGDL 1961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 327 LQFIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPV-SRGGRQGVGVL------LVLNDEARQRWLE 399
Cdd:PRK12467 1962 ARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQdGANGKQLVAYVvptdpgLVDDDEAQVALRA 2041
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1736059155 400 cggkpqelTWRRSLLPWLEPVAVPRYWRVIDEIPVNSMNK 439
Cdd:PRK12467 2042 --------ILKNHLKASLPEYMVPAHLVFLARMPLTPNGK 2073
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
29-150 |
7.91e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 41.72 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 29 WTLGHLRHDVAQLLAYLRQQ---EGERWALCFENSYLFIVALLATLHAGKTPViPGHCRVSLLNEQHLLFDG----VLSD 101
Cdd:PRK09088 23 WTYAELDALVGRLAAVLRRRgcvDGERLAVLARNSVWLVALHFACARVGAIYV-PLNWRLSASELDALLQDAeprlLLGD 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1736059155 102 KAMDwQGTLRVVSSAMTSVAHDITFPAIRSDAFVE-----LFTSGSTGQPKRVI 150
Cdd:PRK09088 102 DAVA-AGRTDVEDLAAFIASADALEPADTPSIPPErvsliLFTSGTSGQPKGVM 154
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
328-439 |
9.75e-04 |
|
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: 41.39 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 328 QFIENGQFRLMGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPVS-RGGRQGVGVLLVLNDEArqrwlecggKPQE 406
Cdd:cd17645 332 KFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEdADGRKYLVAYVTAPEEI---------PHEE 402
|
90 100 110
....*....|....*....|....*....|....
gi 1736059155 407 L-TWRRSLLPwlePVAVPRYWRVIDEIPVNSMNK 439
Cdd:cd17645 403 LrEWLKNDLP---DYMIPTYFVHLKALPLTANGK 433
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
137-231 |
1.11e-03 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 41.45 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 137 LFTSGSTGQPKRVI---KPI-ARLDSEAALLATRFADRLAGcrvvaSVVPQHLYGLTFRIFLPMALGLPL--HAAMLwYA 210
Cdd:PRK08633 788 IFSSGSEGEPKGVMlshHNIlSNIEQISDVFNLRNDDVILS-----SLPFFHSFGLTVTLWLPLLEGIKVvyHPDPT-DA 861
|
90 100
....*....|....*....|..
gi 1736059155 211 EQLAALSAEHRYAF-ISSPAFL 231
Cdd:PRK08633 862 LGIAKLVAKHRATIlLGTPTFL 883
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
338-439 |
1.15e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 41.69 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 338 MGRRGRVVKIEEKRISLSEVEQRLLALDGICEVAALPV-SRGGRQGVGvLLVLNDEaRQRWLEcggkpqelTWRRSLLPW 416
Cdd:PRK12467 3490 LGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARdGAGGKQLVA-YVVPADP-QGDWRE--------TLRDHLAAS 3559
|
90 100
....*....|....*....|...
gi 1736059155 417 LEPVAVPRYWRVIDEIPVNSMNK 439
Cdd:PRK12467 3560 LPDYMVPAQLLVLAAMPLGPNGK 3582
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
15-150 |
2.22e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 40.33 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 15 RPDDVPVAwQEEHTWTLGHLRHDVAQL---LAYLRQQEGERWALCFENSYLFIVALLATLHAGKTPV-IPGHCRVSLLNE 90
Cdd:PRK03640 15 TPDRTAIE-FEEKKVTFMELHEAVVSVagkLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVlLNTRLSREELLW 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 91 Q-------HLLFDGVLSDKAmdwQGTLRV-VSSAMTSVAHDITFPAIRSDAFVE--LFTSGSTGQPKRVI 150
Cdd:PRK03640 94 QlddaevkCLITDDDFEAKL---IPGISVkFAELMNGPKEEAEIQEEFDLDEVAtiMYTSGTTGKPKGVI 160
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
137-277 |
2.74e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 40.14 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 137 LFTSGSTGQPKRVIKPIARLDSEAALLATRFADRlAGCRVVASVVPqhlygltFRIFLPmALGL--------PLHAAMLW 208
Cdd:cd05910 91 LFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIR-PGEVDLATFPL-------FALFGP-ALGLtsvipdmdPTRPARAD 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 209 YAEQLAALsAEHRYAFI-SSPAFLKRL-----DHNLTPPPVELILSAGGMLPWQDVTQAADWLnvwPDEI-----YGSTE 277
Cdd:cd05910 162 PQKLVGAI-RQYGVSIVfGSPALLERVarycaQHGITLPSLRRVLSAGAPVPIALAARLRKML---SDEAeiltpYGATE 237
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
137-306 |
3.88e-03 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 39.65 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 137 LFTSGSTGQPKRVIKPIARLDSEAALLATRFadRLAGCRVVASVVP-QHLYGLTFRIFLPMALGLPLHAAMLWYAEQLAA 215
Cdd:PRK13295 203 IYTSGTTGEPKGVMHTANTLMANIVPYAERL--GLGADDVILMASPmAHQTGFMYGLMMPVMLGATAVLQDIWDPARAAE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 216 LSAEHRYAF-ISSPAFLKRLDH--NLTPPPV---ELILSAGGMLPWQDVTQAADWLNVWPDEIYGSTETGILAW-RYRHQ 288
Cdd:PRK13295 281 LIRTEGVTFtMASTPFLTDLTRavKESGRPVsslRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLtKLDDP 360
|
170 180
....*....|....*....|..
gi 1736059155 289 DDVAW----LPFPGVRFQPEDD 306
Cdd:PRK13295 361 DERASttdgCPLPGVEVRVVDA 382
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
132-203 |
4.93e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 39.31 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 132 DAFVELFTSGSTGQPKRVIKpiarldSEAALLAT-----RFADRLAGCRVVASVVPQHLYGLTFRIFLPMALGL------ 200
Cdd:PRK08043 366 DAALILFTSGSEGHPKGVVH------SHKSLLANveqikTIADFTPNDRFMSALPLFHSFGLTVGLFTPLLTGAevflyp 439
|
....
gi 1736059155 201 -PLH 203
Cdd:PRK08043 440 sPLH 443
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
30-204 |
4.97e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 39.10 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 30 TLGHLRHDVAQLLAYLRQQEGERWALCFENSYLFIVALLATLHAG--------KTPVIPGHCRVSLLNEQHLLFDGV-LS 100
Cdd:PRK05852 48 DLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADlvvvpldpALPIAEQRVRSQAAGARVVLIDADgPH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 101 DKAMD----WQGTLRVVSSAMTSVA-------------HDITFP-AIRSDAFVELFTSGSTGQPKRVikPIARLDSEAAL 162
Cdd:PRK05852 128 DRAEPttrwWPLTVNVGGDSGPSGGtlsvhldaateptPATSTPeGLRPDDAMIMFTGGTTGLPKMV--PWTHANIASSV 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1736059155 163 LATRFADRLAGCRVVASVVP-QHLYGLTFRIFLPMALG----LPLHA 204
Cdd:PRK05852 206 RAIITGYRLSPRDATVAVMPlYHGHGLIAALLATLASGgavlLPARG 252
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
124-278 |
7.24e-03 |
|
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: 38.64 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 124 ITFPAIR--SDAFVeLFTSGSTGQPKRVIKPIARLDSEAALLATRFADRLAGCRVVASVVP-QHLYGltFRIFLPMALGL 200
Cdd:cd05923 142 IEDPPREpeQPAFV-FYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPlYHVIG--FFAVLVAALAL 218
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736059155 201 -----------PLHAAMLWYAEQLAALSA--EHRYAFISSPAF----LKRLDHnltpppvelILSAGGMLP---WQDVTQ 260
Cdd:cd05923 219 dgtyvvveefdPADALKLIEQERVTSLFAtpTHLDALAAAAEFaglkLSSLRH---------VTFAGATMPdavLERVNQ 289
|
170
....*....|....*...
gi 1736059155 261 AADWLNVwpdEIYGSTET 278
Cdd:cd05923 290 HLPGEKV---NIYGTTEA 304
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