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Conserved domains on  [gi|308051803|gb|ADO00329|]
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non-ribosomal peptide synthetase, partial [Planktothrix rubescens No65]

Protein Classification

condensation domain-containing protein( domain architecture ID 1562932)

condensation (C) domain-containing protein catalyzes peptide bond formation; the C domain is found in non-ribosomal peptide synthetases (NRPSs), modular multidomain enzymes that catalyze the biosynthesis of diverse peptides with a wide variety of activities

CATH:  3.30.559.30
Gene Ontology:  GO:0019184|GO:1904091
PubMed:  9712910|17506888

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C_NRPS-like super family cl40425
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 2-114 9.41e-41

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


The actual alignment was detected with superfamily member cd19534:

Pssm-ID: 394795 [Multi-domain]  Cd Length: 428  Bit Score: 139.31  E-value: 9.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQEQWQQYHSDD-WESFGFEVMDLSllsSGEQLTTMAEISEVQQRSLNLEKGPLISVVFFQL-GD 79
Cdd:cd19534   45 ALVEHHDALRMRFRREDGGWQQRIRGDvEELFRLEVVDLS---SLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGtDG 121

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051803  80 AGRLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19534  122 GDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG 156
 
Name Accession Description Interval E-value
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2-114 9.41e-41

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 139.31  E-value: 9.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQEQWQQYHSDD-WESFGFEVMDLSllsSGEQLTTMAEISEVQQRSLNLEKGPLISVVFFQL-GD 79
Cdd:cd19534   45 ALVEHHDALRMRFRREDGGWQQRIRGDvEELFRLEVVDLS---SLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGtDG 121

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051803  80 AGRLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19534  122 GDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG 156
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 2-114 3.63e-28

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 102.42  E-value: 3.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQEQWQQYHSDDWEsFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDA 80
Cdd:COG4908   41 ELVRRHPALRTRFVEEDGEPVQRIDPDAD-LPLEVVDLSALPEPEREAELEElVAEEASRPFDLARGPLLRAALIRLGED 119

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051803  81 G-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:COG4908  120 EhVLLLTIHHIISDGWSLGILLRELAALYAALLEG 154
PRK12467 PRK12467
peptide synthase; Provisional
 3-114 1.09e-27

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 105.63  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    3 LLYRHDALRLRFLHKQEQWQQYHSDDwESFGFEVMDLSLLSSGEQLTTMAEISevqQRSLNLEKGPLISVVFFQLGDAG- 81
Cdd:PRK12467 2225 LLVHHDALRLGFVQEDGGWSAMHRAP-EQERRPLLWQVVVADKEELEALCEQA---QRSLDLEEGPLLRAVLATLPDGSq 2300

                          90       100       110
                  ....*....|....*....|....*....|...
gi 308051803   82 RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12467 2301 RLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGG 2333
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 2-114 7.65e-20

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 82.77  E-value: 7.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    2 KLLYRHDALRLRFLHKQ--EQWQQYHSDDweSFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLG 78
Cdd:pfam00668  50 ELINRHDALRTVFIRQEngEPVQVILEER--PFELEIIDISDLSESEEEEAIEAfIQRDLQSPFDLEKGPLFRAGLFRIA 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 308051803   79 DAG-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:pfam00668 128 ENRhHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164
 
Name Accession Description Interval E-value
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2-114 9.41e-41

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 139.31  E-value: 9.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQEQWQQYHSDD-WESFGFEVMDLSllsSGEQLTTMAEISEVQQRSLNLEKGPLISVVFFQL-GD 79
Cdd:cd19534   45 ALVEHHDALRMRFRREDGGWQQRIRGDvEELFRLEVVDLS---SLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGtDG 121

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051803  80 AGRLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19534  122 GDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG 156
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 2-114 3.63e-28

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 102.42  E-value: 3.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQEQWQQYHSDDWEsFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDA 80
Cdd:COG4908   41 ELVRRHPALRTRFVEEDGEPVQRIDPDAD-LPLEVVDLSALPEPEREAELEElVAEEASRPFDLARGPLLRAALIRLGED 119

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051803  81 G-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:COG4908  120 EhVLLLTIHHIISDGWSLGILLRELAALYAALLEG 154
PRK12467 PRK12467
peptide synthase; Provisional
 3-114 1.09e-27

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 105.63  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    3 LLYRHDALRLRFLHKQEQWQQYHSDDwESFGFEVMDLSLLSSGEQLTTMAEISevqQRSLNLEKGPLISVVFFQLGDAG- 81
Cdd:PRK12467 2225 LLVHHDALRLGFVQEDGGWSAMHRAP-EQERRPLLWQVVVADKEELEALCEQA---QRSLDLEEGPLLRAVLATLPDGSq 2300

                          90       100       110
                  ....*....|....*....|....*....|...
gi 308051803   82 RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12467 2301 RLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGG 2333
PRK12316 PRK12316
peptide synthase; Provisional
 2-111 1.29e-26

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 102.73  E-value: 1.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    2 KLLYRHDALRLRFLHKQEQWQQYHSDDWESfgfEVMDLSLLSSGEQLttmAEISEVQQRSLNLEKGPLISVVFFQLGDAG 81
Cdd:PRK12316 1144 RLVAHHDALRLRFREEDGGWQQAYAAPQAG---EVLWQRQAASEEEL---LALCEEAQRSLDLEQGPLLRALLVDMADGS 1217

                          90       100       110
                  ....*....|....*....|....*....|.
gi 308051803   82 -RLLIIIHHLVVDGVSWRIFLEDLLTSYHQL 111
Cdd:PRK12316 1218 qRLLLVIHHLVVDGVSWRILLEDLQRAYADL 1248
PRK12316 PRK12316
peptide synthase; Provisional
 3-114 1.26e-24

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 96.95  E-value: 1.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    3 LLYRHDALRLRFLHKQEQWQQYHSDdwESFGFEVMDLSLLSSGEQLTtmaEISEVQQRSLNLEKGPLISVVFFQLGDAG- 81
Cdd:PRK12316 3683 LVEHHDALRLRFVEDAGGWTAEHLP--VELGGALLWRAELDDAEELE---RLGEEAQRSLDLADGPLLRALLATLADGSq 3757

                          90       100       110
                  ....*....|....*....|....*....|...
gi 308051803   82 RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12316 3758 RLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQG 3790
PRK05691 PRK05691
peptide synthase; Validated
 1-114 1.35e-22

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 91.00  E-value: 1.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    1 AKLLYRHDALRLRFLHKQEQWQQYHSddwesfgfEVMDLSLLSSGeQLTTMAEISEV---QQRSLNLEKGPLISVVFFQL 77
Cdd:PRK05691 2834 QALVEHHDALRLRFSQADGRWQAEYR--------AVTAQELLWQV-TVADFAECAALfadAQRSLDLQQGPLLRALLVDG 2904

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 308051803   78 GDAG-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK05691 2905 PQGQqRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAG 2942
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 2-114 7.65e-20

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 82.77  E-value: 7.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    2 KLLYRHDALRLRFLHKQ--EQWQQYHSDDweSFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLG 78
Cdd:pfam00668  50 ELINRHDALRTVFIRQEngEPVQVILEER--PFELEIIDISDLSESEEEEAIEAfIQRDLQSPFDLEKGPLFRAGLFRIA 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 308051803   79 DAG-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:pfam00668 128 ENRhHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 2-114 3.62e-17

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 75.52  E-value: 3.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQEQWQQYHSDDWESFGFEVMDLSLLSSGEQlTTMAEISEVQQRSLNLEKGPLISVVFFQLGDAG 81
Cdd:cd19066   47 AVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEIIDLRNLADPEA-RLLELIDQIQQTIYDLERGPLVRVALFRLADER 125

                         90       100       110
                 ....*....|....*....|....*....|....
gi 308051803  82 -RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19066  126 dVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQ 159
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 6-114 2.91e-14

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 66.99  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   6 RHDALRLRF-LHKQEQWQQYHSDDweSFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDAG-R 82
Cdd:cd19531   51 RHEALRTTFvEVDGEPVQVILPPL--PLPLPVVDLSGLPEAEREAEAQRlAREEARRPFDLARGPLLRATLLRLGEDEhV 128

                         90       100       110
                 ....*....|....*....|....*....|..
gi 308051803  83 LLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19531  129 LLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2-110 2.40e-13

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 64.43  E-value: 2.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQEQWQQyhsDDWESFGFEVMDLSLLSSGEQLTTMAEI-SEVQQRSLNLEKGPLISVVFFQL-GD 79
Cdd:cd19535   48 KLIARHPMLRAVFLDDGTQQIL---PEVPWYGITVHDLRGLSEEEAEAALEELrERLSHRVLDVERGPLFDIRLSLLpEG 124

                         90       100       110
                 ....*....|....*....|....*....|.
gi 308051803  80 AGRLLIIIHHLVVDGVSWRIFLEDLLTSYHQ 110
Cdd:cd19535  125 RTRLHLSIDLLVADALSLQILLRELAALYED 155
PRK12316 PRK12316
peptide synthase; Provisional
 3-114 4.14e-12

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 61.13  E-value: 4.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    3 LLYRHDALRLRFLHKQEQWQQYHSDDwesfGFEVMDLSLLSSGEQLTTMAEISEVQQRSLNLEKGPLISVVFFQL-GDAG 81
Cdd:PRK12316 2649 LVLRHETLRTRFVEVGEQTRQVILPN----MSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALdGQEH 2724

                          90       100       110
                  ....*....|....*....|....*....|...
gi 308051803   82 RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12316 2725 VLVITQHHIVSDGWSMQVMVDELVQAYAGARRG 2757
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 2-114 4.32e-12

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 61.06  E-value: 4.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQ-EQWQQYHSDDWEsFGFEVMDLSLLSSGEQLTTMAEI-SEVQQRSLNLEKGPLISVVFFQLGD 79
Cdd:cd19543   47 AVVDRHPILRTSFVWEGlGEPLQVVLKDRK-LPWRELDLSHLSEAEQEAELEALaEEDRERGFDLARAPLMRLTLIRLGD 125

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 308051803  80 AG-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19543  126 DRyRLVWSFHHILLDGWSLPILLKELFAIYAALGEG 161
PRK05691 PRK05691
peptide synthase; Validated
 1-108 2.50e-11

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 59.03  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    1 AKLLYRHDALRLRFLHKQEQWQQyHSDDWESFGFEVMDLSLLSSGEQLTTMAEISEVQQRS-LNLEKGPLISVVFFQLGD 79
Cdd:PRK05691  720 QRLVERHESLRTRFYERDGVALQ-RIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQpFDLEKGPLLRVTLVRLDD 798

                          90       100       110
                  ....*....|....*....|....*....|
gi 308051803   80 AG-RLLIIIHHLVVDGVSWRIFLEDLLTSY 108
Cdd:PRK05691  799 EEhQLLVTLHHIVADGWSLNILLDEFSRLY 828
PRK12316 PRK12316
peptide synthase; Provisional
 1-114 5.07e-10

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 55.35  E-value: 5.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    1 AKLLYRHDALRLRFLHK-QEQWQQYHSDdwESFGFEVMDLSLLSSGEQLTTMAEisEVQQRSL---NLEKGPLISVVFFQ 76
Cdd:PRK12316   94 ASLVQRHETLRTVFPRGaDDSLAQVPLD--RPLEVEFEDCSGLPEAEQEARLRD--EAQRESLqpfDLCEGPLLRVRLLR 169

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 308051803   77 LGDAGR-LLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12316  170 LGEEEHvLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATG 208
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 2-108 1.55e-08

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 50.92  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLHKQE--QWQQYhsddwesfgfeVMDLSLLssgeQLTTM---------AEISEVQQRSLNLEKGPLI 70
Cdd:cd19532   47 AVGQRHEALRTCFFTDPEdgEPMQG-----------VLASSPL----RLEHVqisdeaeveEEFERLKNHVYDLESGETM 111

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 308051803  71 SVVFFQLGDAGRLLII-IHHLVVDGVSWRIFLEDLLTSY 108
Cdd:cd19532  112 RIVLLSLSPTEHYLIFgYHHIAMDGVSFQIFLRDLERAY 150
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 30-114 1.41e-07

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 48.08  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803  30 ESFGFEVMDLSLLSSGEqltTMAEISEVQQRSLNLEKGPLISVVFFQLGDAGR-LLIIIHHLVVDGVSWRIFLEDLLTSY 108
Cdd:cd20484   74 KPLSFQEEDISSLKESE---IIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAY 150


                 ....*.
gi 308051803 109 HQLETG 114
Cdd:cd20484  151 QALLQG 156
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 6-114 5.54e-07

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 46.49  E-value: 5.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   6 RHDALRLRF-LHKQEQWQQYHSDDWESFGFEVMDLSllssGEQLTTmaEISEVQQRSLNLEKGPLISVVFFQLGDAGR-L 83
Cdd:cd19538   51 RHESLRTVFpEEDGVPYQLILEEDEATPKLEIKEVD----EEELES--EINEAVRYPFDLSEEPPFRATLFELGENEHvL 124

                         90       100       110
                 ....*....|....*....|....*....|.
gi 308051803  84 LIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19538  125 LLLLHHIAADGWSLAPLTRDLSKAYRARCKG 155
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 3-108 7.65e-07

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 46.10  E-value: 7.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   3 LLYRHDALRLRFLHKQEQWQQYHSDDwESFGFEVMDLSLLSSGEQLTTmAEISEVQQRSLNLEKGPLISVVFFQLGDAG- 81
Cdd:cd20483   48 LVRRHEVLRTAYFEGDDFGEQQVLDD-PSFHLIVIDLSEAADPEAALD-QLVRNLRRQELDIEEGEVIRGWLVKLPDEEf 125

                         90       100
                 ....*....|....*....|....*..
gi 308051803  82 RLLIIIHHLVVDGVSWRIFLEDLLTSY 108
Cdd:cd20483  126 ALVLASHHIAWDRGSSKSIFEQFTALY 152
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 3-114 3.23e-06

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 44.29  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   3 LLYRHDALRLRFL-HKQEQWQQYHSDDwESFGFEVMDLSllSSGEQLTTMAEI--SEVQQRSLNLEKGPLISVVFFQLG- 78
Cdd:cd19539   48 VVARHEALRTLLVrDDGGVPRQEILPP-GPAPLEVRDLS--DPDSDRERRLEEllRERESRGFDLDEEPPIRAVLGRFDp 124

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 308051803  79 DAGRLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19539  125 DDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 6-108 1.97e-05

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 42.02  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   6 RHDALRLRF-LHKQEQWQQYHSDDWESFGFEVMDLSllssGEQLTtmAEISEVQQRSLNLEKGPLISVVFFQLGDAGR-L 83
Cdd:cd19540   51 RHESLRTVFpEDDGGPYQVVLPAAEARPDLTVVDVT----EDELA--ARLAEAARRGFDLTAELPLRARLFRLGPDEHvL 124

                         90       100
                 ....*....|....*....|....*
gi 308051803  84 LIIIHHLVVDGVSWRIFLEDLLTSY 108
Cdd:cd19540  125 VLVVHHIAADGWSMAPLARDLATAY 149
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 6-111 2.88e-05

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 41.28  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   6 RHDALRLRFLHKQE----QWQQYHSDdwesfgFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDA 80
Cdd:cd19536   51 RHDILRTSFIEDGLgqpvQVVHRQAQ------VPVTELDLTPLEEQLDPLRAyKEETKIRRFDLGRAPLVRAALVRKDER 124

                         90       100       110
                 ....*....|....*....|....*....|...
gi 308051803  81 GR--LLIIIHHLVVDGVSWRIFLEDLLTSYHQL 111
Cdd:cd19536  125 ERflLVISDHHSILDGWSLYLLVKEILAVYNQL 157
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 2-110 4.92e-05

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 40.75  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRFLH--KQEQWQQ--YHSDDWEsfgfevmdLSLLSSGEQLTTMAEISEVQQRSLNleKGPLISVVFFQL 77
Cdd:cd19542   45 QLVQRHDILRTVFVEssAEGTFLQvvLKSLDPP--------IEEVETDEDSLDALTRDLLDDPTLF--GQPPHRLTLLET 114

                         90       100       110
                 ....*....|....*....|....*....|....
gi 308051803  78 GDAG-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQ 110
Cdd:cd19542  115 SSGEvYLVLRISHALYDGVSLPIILRDLAAAYNG 148
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
8-96 1.66e-03

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 36.56  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    8 DALRLRFLHK-QEQWQQYHSDDWESFgFEVMDLSLlSSGEQLTTMAEISEVQQRSLNLEKG-PLISVVFFQLGDAGRLLI 85
Cdd:PRK10252   59 DTLRMRFTEDnGEVWQWVDPALTFPL-PEIIDLRT-QPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWY 136

                          90
                  ....*....|..
gi 308051803   86 I-IHHLVVDGVS 96
Cdd:PRK10252  137 QrYHHLLVDGFS 148
PRK05691 PRK05691
peptide synthase; Validated
 3-104 1.93e-03

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 36.30  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803    3 LLYRHDALRLRFLH-KQEQWQQYHSD-----DWEsfgfevmDLSLLSSGEQLTTMAEISEVQ-QRSLNLEKGPLISVVFF 75
Cdd:PRK05691 1775 LILRHETLRTTFPSvDGVPVQQVAEDsglrmDWQ-------DFSALPADARQQRLQQLADSEaHQPFDLERGPLLRACLV 1847

                          90       100       110
                  ....*....|....*....|....*....|
gi 308051803   76 QLGDAGRLLII-IHHLVVDGVSWRIFLEDL 104
Cdd:PRK05691 1848 KAAEREHYFVLtLHHIVTEGWAMDIFAREL 1877
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 2-114 2.03e-03

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 36.19  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051803   2 KLLYRHDALRLRF-LHKQEQWQqyHSDDWESFGFEVMDLSllssgeqlTTMAEISEVQQ-------RSLNLEKGPLISVV 73
Cdd:cd19533   47 QVIAEAETLRLRFtEEEGEPYQ--WIDPYTPVPIRHIDLS--------GDPDPEGAAQQwmqedlrKPLPLDNDPLFRHA 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 308051803  74 FFQLGDaGRLLII--IHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19533  117 LFTLGD-NRHFWYqrVHHIVMDGFSFALFGQRVAEIYTALLKG 158
 
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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