condensation domain-containing protein, partial [Bacillus atrophaeus]
Protein Classification
non-ribosomal peptide synthetase( domain architecture ID 10019828)
non-ribosomal peptide synthetase is a modular multidomain enzyme that acts as an assembly line to catalyze the biosynthesis of complex natural products
List of domain hits
| Name | Accession | Description | Interval | E-value | |||
| NRPS-para261 | TIGR01720 | non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
19-158 | 1.46e-67 | |||
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant. : Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 202.50 E-value: 1.46e-67
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| Name | Accession | Description | Interval | E-value | ||||
| NRPS-para261 | TIGR01720 | non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
19-158 | 1.46e-67 | ||||
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant. Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 202.50 E-value: 1.46e-67
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| E_NRPS | cd19534 | Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1-147 | 1.65e-60 | ||||
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: 193.62 E-value: 1.65e-60
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| Condensation | pfam00668 | Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1-158 | 1.29e-42 | ||||
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: 147.48 E-value: 1.29e-42
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| PRK12467 | PRK12467 | peptide synthase; Provisional |
1-158 | 5.24e-39 | ||||
peptide synthase; Provisional Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 141.07 E-value: 5.24e-39
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| Name | Accession | Description | Interval | E-value | ||||
| NRPS-para261 | TIGR01720 | non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
19-158 | 1.46e-67 | ||||
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant. Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 202.50 E-value: 1.46e-67
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| E_NRPS | cd19534 | Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1-147 | 1.65e-60 | ||||
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: 193.62 E-value: 1.65e-60
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| Condensation | pfam00668 | Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1-158 | 1.29e-42 | ||||
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: 147.48 E-value: 1.29e-42
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| PRK12467 | PRK12467 | peptide synthase; Provisional |
1-158 | 5.24e-39 | ||||
peptide synthase; Provisional Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 141.07 E-value: 5.24e-39
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| PRK12316 | PRK12316 | peptide synthase; Provisional |
1-158 | 2.55e-38 | ||||
peptide synthase; Provisional Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 138.94 E-value: 2.55e-38
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| PRK12316 | PRK12316 | peptide synthase; Provisional |
1-158 | 4.31e-34 | ||||
peptide synthase; Provisional Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 127.00 E-value: 4.31e-34
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| PRK05691 | PRK05691 | peptide synthase; Validated |
1-158 | 2.43e-33 | ||||
peptide synthase; Validated Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 124.90 E-value: 2.43e-33
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| C_NRPS-like | cd19066 | Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1-147 | 8.62e-16 | ||||
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: 73.98 E-value: 8.62e-16
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| Blast search parameters | ||||
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