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Conserved domains on  [gi|308051801|gb|ADO00328|]
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non-ribosomal peptide synthetase, partial [Planktothrix agardhii SAG 6.89]

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 5.41e-42

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: 142.39  E-value: 5.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFLHKQGQWQQYHSDD-WESFGFEVMDLSllsSGEQLTTMAEISEVQQRSLNLEKGPLISVVFFQL-GD 79
Cdd:cd19534   45 ALVEHHDALRMRFRREDGGWQQRIRGDvEELFRLEVVDLS---SLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGtDG 121

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051801  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 5.41e-42

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: 142.39  E-value: 5.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFLHKQGQWQQYHSDD-WESFGFEVMDLSllsSGEQLTTMAEISEVQQRSLNLEKGPLISVVFFQL-GD 79
Cdd:cd19534   45 ALVEHHDALRMRFRREDGGWQQRIRGDvEELFRLEVVDLS---SLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGtDG 121

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051801  80 AGRLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19534  122 GDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG 156
PRK12467 PRK12467
peptide synthase; Provisional
 3-114 5.89e-30

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 112.18  E-value: 5.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    3 LLYHHDALRLRFLHKQGQWQQYHSDDwESFGFEVMDLSLLSSGEQLTTMAEISevqQRSLNLEKGPLISVVFFQLGDAG- 81
Cdd:PRK12467 2225 LLVHHDALRLGFVQEDGGWSAMHRAP-EQERRPLLWQVVVADKEELEALCEQA---QRSLDLEEGPLLRAVLATLPDGSq 2300

                          90       100       110
                  ....*....|....*....|....*....|...
gi 308051801   82 RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12467 2301 RLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGG 2333
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 2-114 9.92e-29

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 103.97  E-value: 9.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFLHKQGQWQQYHSDDWEsFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDA 80
Cdd:COG4908   41 ELVRRHPALRTRFVEEDGEPVQRIDPDAD-LPLEVVDLSALPEPEREAELEElVAEEASRPFDLARGPLLRAALIRLGED 119

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051801  81 G-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:COG4908  120 EhVLLLTIHHIISDGWSLGILLRELAALYAALLEG 154
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 2-114 5.64e-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: 83.15  E-value: 5.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    2 KLLYHHDALRLRFLHKQGQWQQYHSDDWESFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDA 80
Cdd:pfam00668  50 ELINRHDALRTVFIRQENGEPVQVILEERPFELEIIDISDLSESEEEEAIEAfIQRDLQSPFDLEKGPLFRAGLFRIAEN 129

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 308051801   81 G-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:pfam00668 130 RhHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164
 
Name Accession Description Interval E-value
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2-114 5.41e-42

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: 142.39  E-value: 5.41e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFLHKQGQWQQYHSDD-WESFGFEVMDLSllsSGEQLTTMAEISEVQQRSLNLEKGPLISVVFFQL-GD 79
Cdd:cd19534   45 ALVEHHDALRMRFRREDGGWQQRIRGDvEELFRLEVVDLS---SLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGtDG 121

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051801  80 AGRLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19534  122 GDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG 156
PRK12467 PRK12467
peptide synthase; Provisional
 3-114 5.89e-30

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 112.18  E-value: 5.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    3 LLYHHDALRLRFLHKQGQWQQYHSDDwESFGFEVMDLSLLSSGEQLTTMAEISevqQRSLNLEKGPLISVVFFQLGDAG- 81
Cdd:PRK12467 2225 LLVHHDALRLGFVQEDGGWSAMHRAP-EQERRPLLWQVVVADKEELEALCEQA---QRSLDLEEGPLLRAVLATLPDGSq 2300

                          90       100       110
                  ....*....|....*....|....*....|...
gi 308051801   82 RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12467 2301 RLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGG 2333
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 2-114 9.92e-29

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 103.97  E-value: 9.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFLHKQGQWQQYHSDDWEsFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDA 80
Cdd:COG4908   41 ELVRRHPALRTRFVEEDGEPVQRIDPDAD-LPLEVVDLSALPEPEREAELEElVAEEASRPFDLARGPLLRAALIRLGED 119

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 308051801  81 G-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:COG4908  120 EhVLLLTIHHIISDGWSLGILLRELAALYAALLEG 154
PRK12316 PRK12316
peptide synthase; Provisional
 2-111 9.57e-28

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 105.81  E-value: 9.57e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    2 KLLYHHDALRLRFLHKQGQWQQYHSDDWESfgfEVMDLSLLSSGEQLttmAEISEVQQRSLNLEKGPLISVVFFQLGDAG 81
Cdd:PRK12316 1144 RLVAHHDALRLRFREEDGGWQQAYAAPQAG---EVLWQRQAASEEEL---LALCEEAQRSLDLEQGPLLRALLVDMADGS 1217

                          90       100       110
                  ....*....|....*....|....*....|.
gi 308051801   82 -RLLIIIHHLVVDGVSWRIFLEDLLTSYHQL 111
Cdd:PRK12316 1218 qRLLLVIHHLVVDGVSWRILLEDLQRAYADL 1248
PRK12316 PRK12316
peptide synthase; Provisional
 3-114 2.62e-26

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 101.57  E-value: 2.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    3 LLYHHDALRLRFLHKQGQWQQYHSDdwESFGFEVMDLSLLSSGEQLTtmaEISEVQQRSLNLEKGPLISVVFFQLGDAG- 81
Cdd:PRK12316 3683 LVEHHDALRLRFVEDAGGWTAEHLP--VELGGALLWRAELDDAEELE---RLGEEAQRSLDLADGPLLRALLATLADGSq 3757

                          90       100       110
                  ....*....|....*....|....*....|...
gi 308051801   82 RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12316 3758 RLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQG 3790
PRK05691 PRK05691
peptide synthase; Validated
 1-114 5.49e-25

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 97.93  E-value: 5.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    1 AKLLYHHDALRLRFLHKQGQWQQYHSddwesfgfEVMDLSLLSSGeQLTTMAEISEV---QQRSLNLEKGPLISVVFFQL 77
Cdd:PRK05691 2834 QALVEHHDALRLRFSQADGRWQAEYR--------AVTAQELLWQV-TVADFAECAALfadAQRSLDLQQGPLLRALLVDG 2904

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 308051801   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 5.64e-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: 83.15  E-value: 5.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    2 KLLYHHDALRLRFLHKQGQWQQYHSDDWESFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDA 80
Cdd:pfam00668  50 ELINRHDALRTVFIRQENGEPVQVILEERPFELEIIDISDLSESEEEEAIEAfIQRDLQSPFDLEKGPLFRAGLFRIAEN 129

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 308051801   81 G-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:pfam00668 130 RhHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKG 164
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 2-114 2.11e-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: 75.91  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFLHKQGQWQQYHSDDWESFGFEVMDLSLLSSGEQlTTMAEISEVQQRSLNLEKGPLISVVFFQLGDAG 81
Cdd:cd19066   47 AVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEIIDLRNLADPEA-RLLELIDQIQQTIYDLERGPLVRVALFRLADER 125

                         90       100       110
                 ....*....|....*....|....*....|....
gi 308051801  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 ...
 7-114 5.23e-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: 66.22  E-value: 5.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   7 HDALRLRFLHKQGQ-WQQYHSDDweSFGFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDAG-RL 83
Cdd:cd19531   52 HEALRTTFVEVDGEpVQVILPPL--PLPLPVVDLSGLPEAEREAEAQRlAREEARRPFDLARGPLLRATLLRLGEDEhVL 129

                         90       100       110
                 ....*....|....*....|....*....|.
gi 308051801  84 LIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19531  130 LLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 2-110 3.44e-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: 64.05  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFLHkQGQwQQYHsDDWESFGFEVMDLSLLSSGEQLTTMAEI-SEVQQRSLNLEKGPLISVVFFQL-GD 79
Cdd:cd19535   48 KLIARHPMLRAVFLD-DGT-QQIL-PEVPWYGITVHDLRGLSEEEAEAALEELrERLSHRVLDVERGPLFDIRLSLLpEG 124

                         90       100       110
                 ....*....|....*....|....*....|.
gi 308051801  80 AGRLLIIIHHLVVDGVSWRIFLEDLLTSYHQ 110
Cdd:cd19535  125 RTRLHLSIDLLVADALSLQILLRELAALYED 155
PRK12316 PRK12316
peptide synthase; Provisional
 3-114 7.87e-12

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 60.36  E-value: 7.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    3 LLYHHDALRLRFLHKQGQWQQYHSDDwesfGFEVMDLSLLSSGEQLTTMAEISEVQQRSLNLEKGPLISVVFFQL-GDAG 81
Cdd:PRK12316 2649 LVLRHETLRTRFVEVGEQTRQVILPN----MSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALdGQEH 2724

                          90       100       110
                  ....*....|....*....|....*....|...
gi 308051801   82 RLLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12316 2725 VLVITQHHIVSDGWSMQVMVDELVQAYAGARRG 2757
PRK05691 PRK05691
peptide synthase; Validated
 1-108 1.33e-11

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 59.80  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    1 AKLLYHHDALRLRFLHKQGQWQQyHSDDWESFGFEVMDLSLLSSGEQLTTMAEISEVQQRS-LNLEKGPLISVVFFQLGD 79
Cdd:PRK05691  720 QRLVERHESLRTRFYERDGVALQ-RIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQpFDLEKGPLLRVTLVRLDD 798

                          90       100       110
                  ....*....|....*....|....*....|
gi 308051801   80 AG-RLLIIIHHLVVDGVSWRIFLEDLLTSY 108
Cdd:PRK05691  799 EEhQLLVTLHHIVADGWSLNILLDEFSRLY 828
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 7-114 9.60e-11

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: 57.21  E-value: 9.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   7 HDALRLRFLHKQ-GQWQQYHSDDWEsFGFEVMDLSLLSSGEQLTTMAEI-SEVQQRSLNLEKGPLISVVFFQLGDAG-RL 83
Cdd:cd19543   52 HPILRTSFVWEGlGEPLQVVLKDRK-LPWRELDLSHLSEAEQEAELEALaEEDRERGFDLARAPLMRLTLIRLGDDRyRL 130

                         90       100       110
                 ....*....|....*....|....*....|.
gi 308051801  84 LIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19543  131 VWSFHHILLDGWSLPILLKELFAIYAALGEG 161
PRK12316 PRK12316
peptide synthase; Provisional
 1-114 5.86e-09

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 52.27  E-value: 5.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    1 AKLLYHHDALRLRFLHKQGQWQQYHSDDwESFGFEVMDLSLLSSGEQLTTMAEisEVQQRSL---NLEKGPLISVVFFQL 77
Cdd:PRK12316   94 ASLVQRHETLRTVFPRGADDSLAQVPLD-RPLEVEFEDCSGLPEAEQEARLRD--EAQRESLqpfDLCEGPLLRVRLLRL 170

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 308051801   78 GDAGR-LLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:PRK12316  171 GEEEHvLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATG 208
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 2-108 8.65e-09

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: 51.30  E-value: 8.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFL--HKQGQWQQYhsddwesfgfeVMDLSLLssgeQLTTM---------AEISEVQQRSLNLEKGPLI 70
Cdd:cd19532   47 AVGQRHEALRTCFFtdPEDGEPMQG-----------VLASSPL----RLEHVqisdeaeveEEFERLKNHVYDLESGETM 111

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 308051801  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 1.30e-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: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801  30 ESFGFEVMDLSLLSSGEqltTMAEISEVQQRSLNLEKGPLISVVFFQLGDAGR-LLIIIHHLVVDGVSWRIFLEDLLTSY 108
Cdd:cd20484   74 KPLSFQEEDISSLKESE---IIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHfVLITIHHIIFDGSSSLTLIHSLLDAY 150


                 ....*.
gi 308051801 109 HQLETG 114
Cdd:cd20484  151 QALLQG 156
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 7-114 1.39e-06

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: 45.33  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   7 HDALRLRFLHKQGQ-WQQYHSDDWESFGFEVMDLSllssGEQLTTmaEISEVQQRSLNLEKGPLISVVFFQLGDAGR-LL 84
Cdd:cd19538   52 HESLRTVFPEEDGVpYQLILEEDEATPKLEIKEVD----EEELES--EINEAVRYPFDLSEEPPFRATLFELGENEHvLL 125

                         90       100       110
                 ....*....|....*....|....*....|
gi 308051801  85 IIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19538  126 LLLHHIAADGWSLAPLTRDLSKAYRARCKG 155
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 7-114 3.88e-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: 43.91  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   7 HDALRLRFL-HKQGQWQQYHSDDwESFGFEVMDLSllSSGEQLTTMAEI--SEVQQRSLNLEKGPLISVVFFQLG-DAGR 82
Cdd:cd19539   52 HEALRTLLVrDDGGVPRQEILPP-GPAPLEVRDLS--DPDSDRERRLEEllRERESRGFDLDEEPPIRAVLGRFDpDDHV 128

                         90       100       110
                 ....*....|....*....|....*....|..
gi 308051801  83 LLIIIHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19539  129 LVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 2-110 5.98e-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: 40.37  E-value: 5.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   2 KLLYHHDALRLRFLH--KQGQWQQ--YHSDDWEsfgfevmdLSLLSSGEQLTTMAEISEVQQRSLNleKGPLISVVFFQL 77
Cdd:cd19542   45 QLVQRHDILRTVFVEssAEGTFLQvvLKSLDPP--------IEEVETDEDSLDALTRDLLDDPTLF--GQPPHRLTLLET 114

                         90       100       110
                 ....*....|....*....|....*....|....
gi 308051801  78 GDAG-RLLIIIHHLVVDGVSWRIFLEDLLTSYHQ 110
Cdd:cd19542  115 SSGEvYLVLRISHALYDGVSLPIILRDLAAAYNG 148
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 7-108 7.95e-05

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: 40.32  E-value: 7.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   7 HDALRLRFLHKQGQWQQYHSDDwESFGFEVMDLSLLSSGEQLTTmAEISEVQQRSLNLEKGPLISVVFFQLGDAG-RLLI 85
Cdd:cd20483   52 HEVLRTAYFEGDDFGEQQVLDD-PSFHLIVIDLSEAADPEAALD-QLVRNLRRQELDIEEGEVIRGWLVKLPDEEfALVL 129

                         90       100
                 ....*....|....*....|...
gi 308051801  86 IIHHLVVDGVSWRIFLEDLLTSY 108
Cdd:cd20483  130 ASHHIAWDRGSSKSIFEQFTALY 152
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 7-108 1.69e-04

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: 39.33  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   7 HDALRLRF-LHKQGQWQQYHSDDWESFGFEVMDLSllssGEQLTtmAEISEVQQRSLNLEKGPLISVVFFQLGDAGR-LL 84
Cdd:cd19540   52 HESLRTVFpEDDGGPYQVVLPAAEARPDLTVVDVT----EDELA--ARLAEAARRGFDLTAELPLRARLFRLGPDEHvLV 125

                         90       100
                 ....*....|....*....|....
gi 308051801  85 IIIHHLVVDGVSWRIFLEDLLTSY 108
Cdd:cd19540  126 LVVHHIAADGWSMAPLARDLATAY 149
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 7-111 2.20e-04

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: 38.97  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   7 HDALRLRFLHKQG----QWQQYHSDdwesfgFEVMDLSLLSSGEQLTTMAE-ISEVQQRSLNLEKGPLISVVFFQLGDAG 81
Cdd:cd19536   52 HDILRTSFIEDGLgqpvQVVHRQAQ------VPVTELDLTPLEEQLDPLRAyKEETKIRRFDLGRAPLVRAALVRKDERE 125

                         90       100       110
                 ....*....|....*....|....*....|..
gi 308051801  82 R--LLIIIHHLVVDGVSWRIFLEDLLTSYHQL 111
Cdd:cd19536  126 RflLVISDHHSILDGWSLYLLVKEILAVYNQL 157
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
8-96 3.37e-04

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 38.49  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    8 DALRLRFLHKQGQ-WQQYHSDDWESFgFEVMDLSLlSSGEQLTTMAEISEVQQRSLNLEKG-PLISVVFFQLGDAGRLLI 85
Cdd:PRK10252   59 DTLRMRFTEDNGEvWQWVDPALTFPL-PEIIDLRT-QPDPHAAAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWY 136

                          90
                  ....*....|..
gi 308051801   86 I-IHHLVVDGVS 96
Cdd:PRK10252  137 QrYHHLLVDGFS 148
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 8-114 1.18e-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: 36.96  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801   8 DALRLRFLHKQGQWQQYHSDDWEsFGFEVMDLSllssgeqlTTMAEISEVQQ-------RSLNLEKGPLISVVFFQLGDa 80
Cdd:cd19533   53 ETLRLRFTEEEGEPYQWIDPYTP-VPIRHIDLS--------GDPDPEGAAQQwmqedlrKPLPLDNDPLFRHALFTLGD- 122

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 308051801  81 GRLLII--IHHLVVDGVSWRIFLEDLLTSYHQLETG 114
Cdd:cd19533  123 NRHFWYqrVHHIVMDGFSFALFGQRVAEIYTALLKG 158
PRK05691 PRK05691
peptide synthase; Validated
 3-104 1.35e-03

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 36.68  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308051801    3 LLYHHDALRLRFLHKQG-QWQQYHSD-----DWEsfgfevmDLSLLSSGEQLTTMAEISEVQ-QRSLNLEKGPLISVVFF 75
Cdd:PRK05691 1775 LILRHETLRTTFPSVDGvPVQQVAEDsglrmDWQ-------DFSALPADARQQRLQQLADSEaHQPFDLERGPLLRACLV 1847

                          90       100       110
                  ....*....|....*....|....*....|
gi 308051801   76 QLGDAGRLLII-IHHLVVDGVSWRIFLEDL 104
Cdd:PRK05691 1848 KAAEREHYFVLtLHHIVTEGWAMDIFAREL 1877
 
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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