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Conserved domains on  [gi|1681255617|ref|WP_139125009|]
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AMP-binding protein, partial [Bacillus subtilis]

Protein Classification

acyl-CoA synthetase family protein( domain architecture ID 102275)

acyl-CoA synthetase family protein functions in fatty acid synthesis, and may catalyze the ATP-dependent activation of fatty acids in a two-step reaction to form acyl-CoA esters; belongs to the class I adenylate-forming enzyme superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
 1-113 3.94e-69

Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


The actual alignment was detected with superfamily member cd17645:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 440  Bit Score: 213.18  E-value: 3.94e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPYTLVNNYGPT 80
Cdd:cd17645   165 PHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYKLVNNYGPT 244

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1681255617  81 ENTVVATSAEIHPEEGSLSIGRAIANTRVYILG 113
Cdd:cd17645   245 ENTVVATSFEIDKPYANIPIGKPIDNTRVYILD 277
 
Name Accession Description Interval E-value
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1-113 3.94e-69

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: 213.18  E-value: 3.94e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPYTLVNNYGPT 80
Cdd:cd17645   165 PHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYKLVNNYGPT 244

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1681255617  81 ENTVVATSAEIHPEEGSLSIGRAIANTRVYILG 113
Cdd:cd17645   245 ENTVVATSFEIDKPYANIPIGKPIDNTRVYILD 277
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-112 3.59e-28

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: 106.86  E-value: 3.59e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELEN---TSLRVLLTGGDKLK-------RAVKKP 70
Cdd:COG1020    678 GALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPealPSLRLVLVGGEALPpelvrrwRARLPG 757

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1681255617   71 YTLVNNYGPTENTVVATSAEIHPEE---GSLSIGRAIANTRVYIL 112
Cdd:COG1020    758 ARLVNLYGPTETTVDSTYYEVTPPDadgGSVPIGRPIANTRVYVL 802
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1-112 2.31e-19

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: 81.54  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYF-ETNGITITFLPTQLAEQFMELENT---SLRVLLTGGDKLK-------RAVKK 69
Cdd:TIGR01733 181 GALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAALPPalaSLRLVILGGEALTpalvdrwRARGP 260

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1681255617  70 PYTLVNNYGPTENTVVATSAEIHP----EEGSLSIGRAIANTRVYIL 112
Cdd:TIGR01733 261 GARLINLYGPTETTVWSTATLVDPddapRESPVPIGRPLANTRLYVL 307
AMP-binding pfam00501
AMP-binding enzyme;
1-112 1.63e-18

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 78.89  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELEN------TSLRVLLTGGDKLKRAVKKPY--- 71
Cdd:pfam00501 221 GPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGApkrallSSLRLVLSGGAPLPPELARRFrel 300

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1681255617  72 ---TLVNNYGPTENTVVATSAEIHPEEGSL--SIGRAIANTRVYIL 112
Cdd:pfam00501 301 fggALVNGYGLTETTGVVTTPLPLDEDLRSlgSVGRPLPGTEVKIV 346
PRK12316 PRK12316
peptide synthase; Provisional
 6-112 6.69e-12

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 60.74  E-value: 6.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    6 GAELHVIDEAIRLDIVRLNDYFETNGI-TITFLPTQLaEQFMELEN----TSLRVLLTGGDKLKRAV------KKPYT-L 73
Cdd:PRK12316   721 GARLVVAAPGDHRDPAKLVELINREGVdTLHFVPSML-QAFLQDEDvascTSLRRIVCSGEALPADAqeqvfaKLPQAgL 799

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1681255617   74 VNNYGPTENTVVATSAEIHPEEG-SLSIGRAIANTRVYIL 112
Cdd:PRK12316   800 YNLYGPTEAAIDVTHWTCVEEGGdSVPIGRPIANLACYIL 839
 
Name Accession Description Interval E-value
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1-113 3.94e-69

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: 213.18  E-value: 3.94e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPYTLVNNYGPT 80
Cdd:cd17645   165 PHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYKLVNNYGPT 244

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1681255617  81 ENTVVATSAEIHPEEGSLSIGRAIANTRVYILG 113
Cdd:cd17645   245 ENTVVATSFEIDKPYANIPIGKPIDNTRVYILD 277
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1-112 3.47e-30

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: 111.47  E-value: 3.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFME----LENTSLRVLLTGGDKLK-------RAVKK 69
Cdd:cd05930   154 GALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQelelAALPSLRLVLVGGEALPpdlvrrwRELLP 233

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1681255617  70 PYTLVNNYGPTENTVVATSAEIHPEE---GSLSIGRAIANTRVYIL 112
Cdd:cd05930   234 GARLVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRVYVL 279
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1-112 3.59e-28

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: 106.86  E-value: 3.59e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELEN---TSLRVLLTGGDKLK-------RAVKKP 70
Cdd:COG1020    678 GALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPealPSLRLVLVGGEALPpelvrrwRARLPG 757

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1681255617   71 YTLVNNYGPTENTVVATSAEIHPEE---GSLSIGRAIANTRVYIL 112
Cdd:COG1020    758 ARLVNLYGPTETTVDSTYYEVTPPDadgGSVPIGRPIANTRVYVL 802
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1-112 1.14e-23

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: 93.56  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMEL------ENTSLRVLLTGGDKLKRAVKKPY--- 71
Cdd:cd17651   197 STLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHgrplgvRLAALRYLLTGGEQLVLTEDLREfca 276

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1681255617  72 -----TLVNNYGPTENTVVatSAEIHPEEGS-----LSIGRAIANTRVYIL 112
Cdd:cd17651   277 glpglRLHNHYGPTETHVV--TALSLPGDPAawpapPPIGRPIDNTRVYVL 325
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 6-112 3.50e-23

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: 92.26  E-value: 3.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   6 GAELHVIDEAIRLDIVRLNDYFETNGITITFLPT----QLAEQFMELEnTSLRVLLTGGDKLK-RAVKK------PYTLV 74
Cdd:cd12117   201 GARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAalfnQLADEDPECF-AGLRELLTGGEVVSpPHVRRvlaacpGLRLV 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1681255617  75 NNYGPTENTVVATSAEIHP---EEGSLSIGRAIANTRVYIL 112
Cdd:cd12117   280 NGYGPTENTTFTTSHVVTEldeVAGSIPIGRPIANTRVYVL 320
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 1-112 2.31e-19

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: 81.54  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYF-ETNGITITFLPTQLAEQFMELENT---SLRVLLTGGDKLK-------RAVKK 69
Cdd:TIGR01733 181 GALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAALPPalaSLRLVILGGEALTpalvdrwRARGP 260

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1681255617  70 PYTLVNNYGPTENTVVATSAEIHP----EEGSLSIGRAIANTRVYIL 112
Cdd:TIGR01733 261 GARLINLYGPTETTVWSTATLVDPddapRESPVPIGRPLANTRLYVL 307
AMP-binding pfam00501
AMP-binding enzyme;
1-112 1.63e-18

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 78.89  E-value: 1.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELEN------TSLRVLLTGGDKLKRAVKKPY--- 71
Cdd:pfam00501 221 GPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGApkrallSSLRLVLSGGAPLPPELARRFrel 300

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1681255617  72 ---TLVNNYGPTENTVVATSAEIHPEEGSL--SIGRAIANTRVYIL 112
Cdd:pfam00501 301 fggALVNGYGLTETTGVVTTPLPLDEDLRSlgSVGRPLPGTEVKIV 346
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 6-112 4.70e-16

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: 72.36  E-value: 4.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   6 GAELHVIDEAIRLDIVRLNDYFETNGITITFLP---TQLAEQFMELENTSLRVLLTGGDKLK-RAVKKPY-------TLV 74
Cdd:cd17655   203 GNTLYIVRKETVLDGQALTQYIRQNRITIIDLTpahLKLLDAADDSEGLSLKHLIVGGEALStELAKKIIelfgtnpTIT 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1681255617  75 NNYGPTENTVVATSAEIHPE---EGSLSIGRAIANTRVYIL 112
Cdd:cd17655   283 NAYGPTETTVDASIYQYEPEtdqQVSVPIGKPLGNTRIYIL 323
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 1-113 3.18e-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: 67.01  E-value: 3.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPT----QLAEQFMELENT---SLRVLLTGGDK-----LKRAVK 68
Cdd:cd17649   155 PPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPaylqQLAEEADRTGDGrppSLRLYIFGGEAlspelLRRWLK 234

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1681255617  69 KPYTLVNNYGPTENTVVATSAEIHPEEG----SLSIGRAIANTRVYILG 113
Cdd:cd17649   235 APVRLFNAYGPTEATVTPLVWKCEAGAAragaSMPIGRPLGGRSAYILD 283
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 2-112 3.24e-14

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: 67.11  E-value: 3.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   2 TWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELEN------TSLRVLLTGGDKL-------KRAVK 68
Cdd:cd17656   190 TLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREfinrfpTCVKHIITAGEQLvitnefkEMLHE 269

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1681255617  69 KPYTLVNNYGPTENTVVaTSAEIHPE-EGSL--SIGRAIANTRVYIL 112
Cdd:cd17656   270 HNVHLHNHYGPSETHVV-TTYTINPEaEIPElpPIGKPISNTWIYIL 315
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 2-112 5.66e-14

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: 66.12  E-value: 5.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   2 TWTIGAELHVIDEAIRLDIVRLNDYFETNGITITFLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPY----TLVNNY 77
Cdd:cd17652   155 ALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPDLRTLVVAGEACPAELVDRWapgrRMINAY 234

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1681255617  78 GPTENTVVATSAEIHPEEGSLSIGRAIANTRVYIL 112
Cdd:cd17652   235 GPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVL 269
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 2-107 7.60e-13

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: 62.95  E-value: 7.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   2 TWTIGAELHVIDEAIRLDivRLNDYFETNGITITFLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPY----TLVNNY 77
Cdd:cd05918   168 TLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWadrvRLINAY 245

                          90       100       110
                  ....*....|....*....|....*....|
gi 1681255617  78 GPTENTVVATSAEIHPEEGSLSIGRAIANT 107
Cdd:cd05918   246 GPAECTIAATVSPVVPSTDPRNIGRPLGAT 275
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1-112 3.62e-12

similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341299 [Multi-domain]  Cd Length: 465  Bit Score: 61.30  E-value: 3.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITI-TFLPTQLAEQFMELENT------SLRVLLTGGDK--------LKR 65
Cdd:cd17644   167 VTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVlSLPPAYWHLLVLELLLStidlpsSLRLVIVGGEAvqpelvrqWQK 246

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1681255617  66 AVKKPYTLVNNYGPTENTVVATSAEI----HPEEGSLSIGRAIANTRVYIL 112
Cdd:cd17644   247 NVGNFIQLINVYGPTEATIAATVCRLtqltERNITSVPIGRPIANTQVYIL 297
PRK12316 PRK12316
peptide synthase; Provisional
 6-112 6.69e-12

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 60.74  E-value: 6.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    6 GAELHVIDEAIRLDIVRLNDYFETNGI-TITFLPTQLaEQFMELEN----TSLRVLLTGGDKLKRAV------KKPYT-L 73
Cdd:PRK12316   721 GARLVVAAPGDHRDPAKLVELINREGVdTLHFVPSML-QAFLQDEDvascTSLRRIVCSGEALPADAqeqvfaKLPQAgL 799

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1681255617   74 VNNYGPTENTVVATSAEIHPEEG-SLSIGRAIANTRVYIL 112
Cdd:PRK12316   800 YNLYGPTEAAIDVTHWTCVEEGGdSVPIGRPIANLACYIL 839
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 1-112 4.33e-11

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: 58.07  E-value: 4.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTiGAELHVIDEAIRLDIVRLNDYFETNGITI---TflPT--QLAEQFMELENTSLRvLLTGGDKL-----KRAVKKP 70
Cdd:cd12116   188 PLLA-GARVVIAPRETQRDPEALARLIEAHSITVmqaT--PAtwRMLLDAGWQGRAGLT-ALCGGEALppdlaARLLSRV 263

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1681255617  71 YTLVNNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYIL 112
Cdd:cd12116   264 GSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVL 305
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 19-112 7.97e-11

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: 57.29  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617  19 DIVRLNDYFETNGITIT-FLPTQLaEQFMEL----ENTSLRVLLTGGDKL-----KRAVKKPY-TLVNNYGPTENTVVAT 87
Cdd:cd17646   217 DPAYLAALIREHGVTTChFVPSML-RVFLAEpaagSCASLRRVFCSGEALppelaARFLALPGaELHNLYGPTEAAIDVT 295

                          90       100
                  ....*....|....*....|....*..
gi 1681255617  88 SAEIHP--EEGSLSIGRAIANTRVYIL 112
Cdd:cd17646   296 HWPVRGpaETPSVPIGRPVPNTRLYVL 322
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 6-113 8.12e-10

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: 54.33  E-value: 8.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   6 GAELHVIDEAIRLDIVRLNDYFETNGIT-ITFLPTQLaeQFMELEN-TSLRVLLTGGDKLKRAVKK------PYTLVNNY 77
Cdd:cd17648   162 GQKLVVPPDEMRFDPDRFYAYINREKVTyLSGTPSVL--QQYDLARlPHLKRVDAAGEEFTAPVFEklrsrfAGLIINAY 239

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1681255617  78 GPTENTVVATsaeIHPEEGS----LSIGRAIANTRVYILG 113
Cdd:cd17648   240 GPTETTVTNH---KRFFPGDqrfdKSLGRPVRNTKCYVLN 276
PRK12316 PRK12316
peptide synthase; Provisional
 4-113 1.28e-09

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 54.19  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    4 TIGAELHVIDEAIRlDIVRLNDYFETNGITITFLPTQLAEQFMELEN-----TSLRVLLTGGD--------KLKRAVKKP 70
Cdd:PRK12316  2210 LNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEHAErdgrpPAVRVYCFGGEavpaaslrLAWEALRPV 2288

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1681255617   71 YtLVNNYGPTENTVVATSAEIHPEEGS----LSIGRAIANTRVYILG 113
Cdd:PRK12316  2289 Y-LFNGYGPTEAVVTPLLWKCRPQDPCgaayVPIGRALGNRRAYILD 2334
PRK12467 PRK12467
peptide synthase; Provisional
 3-112 2.94e-09

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 52.86  E-value: 2.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    3 WTI--GAELHVIDEAIRlDIVRLNDYFETNGITITFLPTQLAEQFMELEN----TSLRVLLTGGDKLK-------RAVKK 69
Cdd:PRK12467  3298 WTLicGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDAGgadcASLDIYVFGGEAVPpaafeqvKRKLK 3376

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1681255617   70 PYTLVNNYGPTENTVV----ATSAEIHPEEGSLSIGRAIANTRVYIL 112
Cdd:PRK12467  3377 PRGLTNGYGPTEAVVTvtlwKCGGDAVCEAPYAPIGRPVAGRSIYVL 3423
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 9-113 3.22e-09

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: 52.70  E-value: 3.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   9 LHVIDEAIRLDIVRLNdyfetngiTItflPTqLAEQFMELEN--TSLRVLLTGGDKLKRA-VKKPYT------LVNNYGP 79
Cdd:cd12115   181 LALPDLPAAAEVTLIN--------TV---PS-AAAELLRHDAlpASVRVVNLAGEPLPRDlVQRLYArlqverVVNLYGP 248

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1681255617  80 TENTVVATSAEIHPE-EGSLSIGRAIANTRVYILG 113
Cdd:cd12115   249 SEDTTYSTVAPVPPGaSGEVSIGRPLANTQAYVLD 283
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1-112 6.25e-09

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: 51.73  E-value: 6.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDeaiRLDIVRLNDYFETNGITITFL-PTQL-----AEQFMELENTSLRVLLTGGDKLKRAVKKPY--- 71
Cdd:COG0318   162 APLLAGATLVLLP---RFDPERVLELIERERVTVLFGvPTMLarllrHPEFARYDLSSLRLVVSGGAPLPPELLERFeer 238

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1681255617  72 ---TLVNNYGPTENTVVAT-SAEIHPEEGSLSIGRAIANTRVYIL 112
Cdd:COG0318   239 fgvRIVEGYGLTETSPVVTvNPEDPGERRPGSVGRPLPGVEVRIV 283
PRK05691 PRK05691
peptide synthase; Validated
 39-112 1.70e-08

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 50.94  E-value: 1.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   39 TQLAeQFMELENTSL--RVLLTGGDKLK-------RAVKKPYTLVNNYGPTEnTVVATSAEIHPE-----EGSLSIGRAI 104
Cdd:PRK05691  2435 SQLA-QWLAGQGEQLpvRMCITGGEALTgehlqriRQAFAPQLFFNAYGPTE-TVVMPLACLAPEqleegAASVPIGRVV 2512


                   ....*...
gi 1681255617  105 ANTRVYIL 112
Cdd:PRK05691  2513 GARVAYIL 2520
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1-112 1.87e-08

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: 50.32  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITI-----TFLPTQLAEQ-FMELENTSLR-VLLTGGDKLKRAVKK---- 69
Cdd:cd05945   158 PALASGATLVPVPRDATADPKQLFRFLAEHGITVwvstpSFAAMCLLSPtFTPESLPSLRhFLFCGEVLPHKTARAlqqr 237

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1681255617  70 --PYTLVNNYGPTENTVVATSAEIHPE----EGSLSIGRAIANTRVYIL 112
Cdd:cd05945   238 fpDARIYNTYGPTEATVAVTYIEVTPEvldgYDRLPIGYAKPGAKLVIL 286
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 6-112 1.92e-08

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: 50.38  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   6 GAELHVIDEAIRLDIVRLNDYFETNGITI------TFLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPY-------- 71
Cdd:cd17643   159 GGRLVVVPYEVARSPEDFARLLRDEGVTVlnqtpsAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWagrfgldr 238

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1681255617  72 -TLVNNYGPTENTVVATSAEIHPEEGSLS----IGRAIANTRVYIL 112
Cdd:cd17643   239 pQLVNMYGITETTVHVTFRPLDAADLPAAaaspIGRPLPGLRVYVL 284
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 32-112 2.08e-08

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: 50.39  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617  32 ITITFLPTQLAEQFmelenTSLRVLLTGGD----KLKRAVKKPYTLVNNYGPTENTVVATSAEIHPEEgSLSIGRAIANT 107
Cdd:cd17653   195 STPSILSTLSPQDF-----PNLKTIFLGGEavppSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQ-PVTIGKPIPNS 268


                  ....*
gi 1681255617 108 RVYIL 112
Cdd:cd17653   269 TCYIL 273
PRK12316 PRK12316
peptide synthase; Provisional
 6-112 3.82e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 46.87  E-value: 3.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    6 GAELHVIDEAIRlDIVRLNDYFETNGITITFLPT----QLAEQFMELEN-TSLRVLLTGGDKLKRAVK-------KPYTL 73
Cdd:PRK12316  4760 GASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPvylqQLAEHAERDGEpPSLRVYCFGGEAVAQASYdlawralKPVYL 4838

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1681255617   74 VNNYGPTENTVV----ATSAEIHPEEGSLSIGRAIANTRVYIL 112
Cdd:PRK12316  4839 FNGYGPTETTVTvllwKARDGDACGAAYMPIGTPLGNRSGYVL 4881
PRK12316 PRK12316
peptide synthase; Provisional
 1-112 7.32e-07

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 46.10  E-value: 7.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGI-TITFLPTQLAEQFMEL---ENTSLRVLLTGGDKLK----RAVKKPYT 72
Cdd:PRK12316  3257 WPLMSGARVVLAGPEDWRDPALLVELINSEGVdVLHAYPSMLQAFLEEEdahRCTSLKRIVCGGEALPadlqQQVFAGLP 3336

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1681255617   73 LVNNYGPTENTVVATSAEIHPE-EGSLSIGRAIANTRVYIL 112
Cdd:PRK12316  3337 LYNLYGPTEATITVTHWQCVEEgKDAVPIGRPIANRACYIL 3377
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 6-111 2.13e-06

acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341309 [Multi-domain]  Cd Length: 449  Bit Score: 44.77  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   6 GAELHVIDEAIRLDIVRLND-YFETNGITITFLPTQLAEQF----MELEN----TSLRVLLTGGDKL-------KRAVKK 69
Cdd:cd17654   184 GATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFgsqsIKSTVlsatSSLRVLALGGEPFpslvilsSWRGKG 263

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1681255617  70 PYTLV-NNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYI 111
Cdd:cd17654   264 NRTRIfNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEV 306
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 6-112 5.57e-06

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 43.61  E-value: 5.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   6 GAELHVIDEAIRLDIVRLNDYFETNGITI-TFLPTqLAEQFME------LENTSLRVLLTGGDKLKRAVKKPYT------ 72
Cdd:cd17650   160 GGTLVICPDEVKLDPAALYDLILKSRITLmESTPA-LIRPVMAyvyrngLDLSAMRLLIVGSDGCKAQDFKTLAarfgqg 238

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1681255617  73 --LVNNYGPTENTVVAT----SAEIHPEEGSLSIGRAIANTRVYIL 112
Cdd:cd17650   239 mrIINSYGVTEATIDSTyyeeGRDPLGDSANVPIGRPLPNTAMYVL 284
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1-112 2.75e-05

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 41.42  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   1 PTWTIGAELHVIDEAIRLDIVRLNDYFETNGITI-TFLPT-----QLAEQFMELENTSLRVLLTGGDKL-KRAVKKPY-- 71
Cdd:PRK04813  204 PTLASGGTLVALPKDMTANFKQLFETLPQLPINVwVSTPSfadmcLLDPSFNEEHLPNLTHFLFCGEELpHKTAKKLLer 283

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1681255617  72 ----TLVNNYGPTENTVVATSAEIHPE----EGSLSIGRAIANTRVYIL 112
Cdd:PRK04813  284 fpsaTIYNTYGPTEATVAVTSIEITDEmldqYKRLPIGYAKPDSPLLII 332
PRK05691 PRK05691
peptide synthase; Validated
 33-107 5.02e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 40.92  E-value: 5.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617   33 TITFLPTqLAEQFME----LENTSLRVLLTGGDKLKRAVKK-------PYTLVNNYGPTENTVVATSAEIHPEEGSLS-I 100
Cdd:PRK05691  1367 TLHFVPP-LLQLFIDeplaAACTSLRRLFSGGEALPAELRNrvlqrlpQVQLHNRYGPTETAINVTHWQCQAEDGERSpI 1445


                   ....*..
gi 1681255617  101 GRAIANT 107
Cdd:PRK05691  1446 GRPLGNV 1452
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
6-112 4.05e-04

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 38.10  E-value: 4.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1681255617    6 GAELHVIDEAIRLDIVRLNDYFETNGITIT-FLPTQLAEQFMELEN-------TSLRVLLTGGDKL--------KRAVKK 69
Cdd:PRK10252   664 GAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPSMLAAFVASLTPegarqscASLRQVFCSGEALpadlcrewQQLTGA 743

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1681255617   70 PytLVNNYGPTENTV-----VATSAEIHPEEG-SLSIGRAIANTRVYIL 112
Cdd:PRK10252   744 P--LHNLYGPTEAAVdvswyPAFGEELAAVRGsSVPIGYPVWNTGLRIL 790
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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