Domains within Paramecium tetraurelia protein A0EHS3_PARTE (A0EHS3)

Uncharacterized protein

Alternative representations: 1 /

Protein length2950 aa
Source databaseUniProt
Identifiers A0EHS3_PARTE, A0EHS3

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.

Predicted functional partners

A0EHS3_PARTE is shown as A0EHS3_PARTE 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 A0EHS3_PARTE

Protein A0EHS3_PARTE is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04931Insulin resistance

KEGG orthologous groups

KONameDescription
K09667OGTprotein O-GlcNAc transferase [EC:2.4.1.255]

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 5888.A0EHS3 in eggNOG.

OGTaxonomic classDescription
LCOG3914All organisms (root)protein O-GlcNAc transferase [EC:2.4.1.255],tetratricopeptide repeat protein 6,CRISPR-associated protein Csy1
KOG4626Eukaryota (superkingdom)protein O-GlcNAc transferase [EC:2.4.1.255],tetratricopeptide repeat protein 6,tetratricopeptide repeat protein 17
CKTTHOligohymenophorea (class)trichohyalin

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: