thiopeptide-type bacteriocin biosynthesis domain; This domain occurs within longer proteins ...
189-445
4.78e-77
thiopeptide-type bacteriocin biosynthesis domain; This domain occurs within longer proteins that contain lantibiotic dehydratase domains (see pfam04737 and pfam04738), and as single-domain proteins in bacteriocin biosynthesis genomic contexts. Three named genes in this family, SioK in Streptomyces sioyaensis, TsrD in Streptomyces laurentii, and NosD in Streptomyces actuosus, all occur in regions associated with thiopeptide biosynthesis. [Cellular processes, Toxin production and resistance]
:
Pssm-ID: 274836 Cd Length: 263 Bit Score: 241.12 E-value: 4.78e-77
Lantibiotic dehydratase, N terminus; Lantibiotics are ribosomally synthesized antimicrobial ...
5-118
1.74e-15
Lantibiotic dehydratase, N terminus; Lantibiotics are ribosomally synthesized antimicrobial agents derived from ribosomally synthesized peptides. They are produced by bacteria of the Firmicutes phylum, and include mutacin, subtilin, and nisin. Lantibiotic peptides contain thioether bridges termed lanthionines that are thought to be generated by dehydration of serine and threonine residues followed by addition of cysteine residues. This family constitutes the N-terminus of the enzyme proposed to catalyze the dehydration step via glutamylation of the substrate during lantibiotic biosynthesis. The enzyme dehydrates Ser/Thr residues in the precursor by glutamylation.
The actual alignment was detected with superfamily member pfam04738:
Pssm-ID: 428098 Cd Length: 648 Bit Score: 78.87 E-value: 1.74e-15
thiopeptide-type bacteriocin biosynthesis domain; This domain occurs within longer proteins ...
189-445
4.78e-77
thiopeptide-type bacteriocin biosynthesis domain; This domain occurs within longer proteins that contain lantibiotic dehydratase domains (see pfam04737 and pfam04738), and as single-domain proteins in bacteriocin biosynthesis genomic contexts. Three named genes in this family, SioK in Streptomyces sioyaensis, TsrD in Streptomyces laurentii, and NosD in Streptomyces actuosus, all occur in regions associated with thiopeptide biosynthesis. [Cellular processes, Toxin production and resistance]
Pssm-ID: 274836 Cd Length: 263 Bit Score: 241.12 E-value: 4.78e-77
Lantibiotic biosynthesis dehydratase C-term; Lant_dehydr_C is the C-terminal domain of a ...
189-448
1.23e-23
Lantibiotic biosynthesis dehydratase C-term; Lant_dehydr_C is the C-terminal domain of a family of dehydratases that are involved in the biosynthesis of lantibiotics. While the extensive N-terminal domain, pfam04738, is involved in the serine-threonine glutamylation step of the synthetic process, this C-terminal domain, once thought to be a separate domain from the dehydratase enzymic activity, is necessary for the final glutamate-elimination step in the generation of the lantibiotic. Lantibiotics are a class of peptide antibiotic that contains one or more thioether bonds.
Pssm-ID: 433656 [Multi-domain] Cd Length: 278 Bit Score: 100.14 E-value: 1.23e-23
Lantibiotic dehydratase, N terminus; Lantibiotics are ribosomally synthesized antimicrobial ...
5-118
1.74e-15
Lantibiotic dehydratase, N terminus; Lantibiotics are ribosomally synthesized antimicrobial agents derived from ribosomally synthesized peptides. They are produced by bacteria of the Firmicutes phylum, and include mutacin, subtilin, and nisin. Lantibiotic peptides contain thioether bridges termed lanthionines that are thought to be generated by dehydration of serine and threonine residues followed by addition of cysteine residues. This family constitutes the N-terminus of the enzyme proposed to catalyze the dehydration step via glutamylation of the substrate during lantibiotic biosynthesis. The enzyme dehydrates Ser/Thr residues in the precursor by glutamylation.
Pssm-ID: 428098 Cd Length: 648 Bit Score: 78.87 E-value: 1.74e-15
thiopeptide-type bacteriocin biosynthesis domain; This domain occurs within longer proteins ...
189-445
4.78e-77
thiopeptide-type bacteriocin biosynthesis domain; This domain occurs within longer proteins that contain lantibiotic dehydratase domains (see pfam04737 and pfam04738), and as single-domain proteins in bacteriocin biosynthesis genomic contexts. Three named genes in this family, SioK in Streptomyces sioyaensis, TsrD in Streptomyces laurentii, and NosD in Streptomyces actuosus, all occur in regions associated with thiopeptide biosynthesis. [Cellular processes, Toxin production and resistance]
Pssm-ID: 274836 Cd Length: 263 Bit Score: 241.12 E-value: 4.78e-77
Lantibiotic biosynthesis dehydratase C-term; Lant_dehydr_C is the C-terminal domain of a ...
189-448
1.23e-23
Lantibiotic biosynthesis dehydratase C-term; Lant_dehydr_C is the C-terminal domain of a family of dehydratases that are involved in the biosynthesis of lantibiotics. While the extensive N-terminal domain, pfam04738, is involved in the serine-threonine glutamylation step of the synthetic process, this C-terminal domain, once thought to be a separate domain from the dehydratase enzymic activity, is necessary for the final glutamate-elimination step in the generation of the lantibiotic. Lantibiotics are a class of peptide antibiotic that contains one or more thioether bonds.
Pssm-ID: 433656 [Multi-domain] Cd Length: 278 Bit Score: 100.14 E-value: 1.23e-23
Lantibiotic dehydratase, N terminus; Lantibiotics are ribosomally synthesized antimicrobial ...
5-118
1.74e-15
Lantibiotic dehydratase, N terminus; Lantibiotics are ribosomally synthesized antimicrobial agents derived from ribosomally synthesized peptides. They are produced by bacteria of the Firmicutes phylum, and include mutacin, subtilin, and nisin. Lantibiotic peptides contain thioether bridges termed lanthionines that are thought to be generated by dehydration of serine and threonine residues followed by addition of cysteine residues. This family constitutes the N-terminus of the enzyme proposed to catalyze the dehydration step via glutamylation of the substrate during lantibiotic biosynthesis. The enzyme dehydrates Ser/Thr residues in the precursor by glutamylation.
Pssm-ID: 428098 Cd Length: 648 Bit Score: 78.87 E-value: 1.74e-15
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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