LysM peptidoglycan-binding domain-containing protein may bind N-acetylglucosamine in carbohydrates such as chitin, chitio-oligosaccharides and peptidoglycan
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
3-45
1.81e-09
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
:
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 53.55 E-value: 1.81e-09
TLD; This domain is predicted to be an enzyme and is often found associated with pfam01476. It ...
674-819
2.86e-39
TLD; This domain is predicted to be an enzyme and is often found associated with pfam01476. It's structure consists of a beta-sandwich surrounded by two helices and two one-turn helices.
Pssm-ID: 429519 Cd Length: 139 Bit Score: 141.98 E-value: 2.86e-39
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
3-45
1.81e-09
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 53.55 E-value: 1.81e-09
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
3-44
1.44e-05
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 42.86 E-value: 1.44e-05
TLD; This domain is predicted to be an enzyme and is often found associated with pfam01476. It ...
674-819
2.86e-39
TLD; This domain is predicted to be an enzyme and is often found associated with pfam01476. It's structure consists of a beta-sandwich surrounded by two helices and two one-turn helices.
Pssm-ID: 429519 Cd Length: 139 Bit Score: 141.98 E-value: 2.86e-39
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
3-45
1.81e-09
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.
Pssm-ID: 396179 [Multi-domain] Cd Length: 43 Bit Score: 53.55 E-value: 1.81e-09
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
3-44
1.44e-05
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
Pssm-ID: 212030 [Multi-domain] Cd Length: 45 Bit Score: 42.86 E-value: 1.44e-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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Functional characterization of the conserved domain architecture found on the query.
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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.
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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.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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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
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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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