Domains within Drosophila melanogaster protein Q9VHI7_DROME (Q9VHI7)

LD47007p

Alternative representations: 1 /

Protein length380 aa
Source databaseUniProt
Identifiers Q9VHI7_DROME, Q9VHI7, FBPP0081445
Source gene FBgn0037653

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

Q9VHI7_DROME is shown as Iru 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 Iru

Protein Q9VHI7_DROME is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04310Wnt signaling pathway
map00310Lysine degradation iPath3
Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

KONameDescription
K11982RNF115_126E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]

Post-translational modifications

PTM annotation is taken from PTMcode, a resource of known and predicted functional associations between protein post-translational modifications (PTMs). There are 1 PTMs annotated in this protein:

PTMCount
Phosphorylation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein CG11982.

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 7227.FBpp0081445 in eggNOG.

OGTaxonomic classDescription
EIGKGEndopterygota (cohort)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]
FV3XRmelanogaster group (species group)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]
FDUX4melanogaster subgroup (species subgroup)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]
LKOG0800All organisms (root)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27],E3 ubiquitin-protein ligase ATL6/9/15/31/42/55 [EC:2.3.2.27],E3 ubiquitin-protein ligase RNF38/44 [EC:2.3.2.27]
KOG0800Eukaryota (superkingdom)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27],E3 ubiquitin-protein ligase ATL6/9/15/31/42/55 [EC:2.3.2.27],E3 ubiquitin-protein ligase RNF38/44 [EC:2.3.2.27]
HTX8TMetazoa (kingdom)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27],[histone H3]-lysine4 N-trimethyltransferase ASH1L [EC:2.1.1.354]
HI3TAArthropoda (phylum)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]
85HP2Hexapoda (subphylum)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]
AH0V0Neoptera (infraclass)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]
ANI97Diptera (order)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]
H6E1FBilateria (clade)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27],[histone H3]-lysine4 N-trimethyltransferase ASH1L [EC:2.1.1.354]
7I45IOpisthokonta (clade)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27],E3 ubiquitin-protein ligase RNF43 [EC:2.3.2.27],E3 ubiquitin-protein ligase Praja2 [EC:2.3.2.27]
EGX5VDrosophila (genus)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]
50F60Sophophora (subgenus)E3 ubiquitin-protein ligase RNF115/126 [EC:2.3.2.27]

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: