Domain of unknown function (DUF4135); This presumed domain is functionally uncharacterized. ...
119-468
1.90e-70
Domain of unknown function (DUF4135); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and archaea, and is approximately 380 amino acids in length. The family is found in association with pfam05147. This domain may be involved in synthesis of a lantibiotic compound.
:
Pssm-ID: 433321 Cd Length: 374 Bit Score: 229.85 E-value: 1.90e-70
Domain of unknown function (DUF4135); This presumed domain is functionally uncharacterized. ...
119-468
1.90e-70
Domain of unknown function (DUF4135); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and archaea, and is approximately 380 amino acids in length. The family is found in association with pfam05147. This domain may be involved in synthesis of a lantibiotic compound.
Pssm-ID: 433321 Cd Length: 374 Bit Score: 229.85 E-value: 1.90e-70
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
135-514
4.17e-64
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
Pssm-ID: 271200 [Multi-domain] Cd Length: 836 Bit Score: 223.73 E-value: 4.17e-64
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
30-497
4.19e-63
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis. This catalysis by LanM distinguishes the type 2 lantibiotics, such as mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin. The N-terminal domain contains regions associated with Ser and Thr dehydration. The C-terminal region contains a pfam05147 domain, which catalyzes the formation of the lanthionine bridge. [Cellular processes, Toxin production and resistance]
Pssm-ID: 274840 [Multi-domain] Cd Length: 931 Bit Score: 221.75 E-value: 4.19e-63
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442859 [Multi-domain] Cd Length: 159 Bit Score: 43.02 E-value: 8.09e-05
Domain of unknown function (DUF4135); This presumed domain is functionally uncharacterized. ...
119-468
1.90e-70
Domain of unknown function (DUF4135); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and archaea, and is approximately 380 amino acids in length. The family is found in association with pfam05147. This domain may be involved in synthesis of a lantibiotic compound.
Pssm-ID: 433321 Cd Length: 374 Bit Score: 229.85 E-value: 1.90e-70
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
135-514
4.17e-64
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
Pssm-ID: 271200 [Multi-domain] Cd Length: 836 Bit Score: 223.73 E-value: 4.17e-64
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as ...
30-497
4.19e-63
type 2 lantibiotic biosynthesis protein LanM; Members of this family are known generally as LanM, a multifunctional enzyme of lantibiotic biosynthesis. This catalysis by LanM distinguishes the type 2 lantibiotics, such as mersacidin, cinnamycin, and lichenicidin, from LanBC-produced type 1 lantibiotics such as nisin and subtilin. The N-terminal domain contains regions associated with Ser and Thr dehydration. The C-terminal region contains a pfam05147 domain, which catalyzes the formation of the lanthionine bridge. [Cellular processes, Toxin production and resistance]
Pssm-ID: 274840 [Multi-domain] Cd Length: 931 Bit Score: 221.75 E-value: 4.19e-63
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442859 [Multi-domain] Cd Length: 159 Bit Score: 43.02 E-value: 8.09e-05
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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