Domains within Streptomyces hygroscopicus subsp. limoneus protein A0A0S2P7R8_STRHL (A0A0S2P7R8)

Beta-xylanase

Alternative representations: 1 /

Protein length477 aa
Source databaseUniProt
Identifiers H2K2E3_STRHJ, H2K2E3, Q7SI98_STROI, Q7SI98, Q7SID1, A0A0S2P7R8_STRHL, A0A0S2P7R8

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

This domain architecture was probably invented with the emergence of cellular organisms

Predicted functional partners

A0A0S2P7R8_STRHL is shown as SHJG_6984 in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for SHJG_6984

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 1133850.SHJG_6984 in eggNOG.

OGTaxonomic classDescription
LCOG3693All organisms (root)endo-1,4-beta-xylanase [EC:3.2.1.8],polysaccharide biosynthesis protein PslG,cytochrome o ubiquinol oxidase subunit IV
COG3693Bacteria (superkingdom)endo-1,4-beta-xylanase [EC:3.2.1.8],polysaccharide biosynthesis protein PslG,cytochrome o ubiquinol oxidase subunit IV
6AHCUActinobacteria (phylum)endo-1,4-beta-xylanase [EC:3.2.1.8]
FC2RPActinomycetia (class)endo-1,4-beta-xylanase [EC:3.2.1.8]
BBECMStreptomycetaceae (family)endo-1,4-beta-xylanase [EC:3.2.1.8]
CIFH4Streptomyces (genus)endo-1,4-beta-xylanase [EC:3.2.1.8]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: