Domains within Drosophila melanogaster protein CG445_DROME (P22978)

Rhodanese domain-containing protein CG4456

Alternative representations: 1 /

Protein length111 aa
Source databaseUniProt
Identifiers CG445_DROME, P22978, FBPP0100114, FBPP0100115, FBPP0292525, FBPP0292526, F0J880, Q0E8G7, Q9VSX0, M9MRT2_DROME, M9MRT2
Source gene FBgn0001228

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

CG445_DROME is shown as CG4456 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 CG4456

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.FBpp0100115 in eggNOG.

OGTaxonomic classDescription
EIAZZEndopterygota (cohort)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-]
LCOG0607All organisms (root)sulfur-carrier protein adenylyltransferase/sulfurtransferase [EC:2.7.7.80 2.7.7.- 2.8.1.11 2.8.1.-],hydroxyacylglutathione hydrolase [EC:3.1.2.6],phage shock protein E
FDXR0melanogaster subgroup (species subgroup)Rhodanese
FUXNImelanogaster group (species group)Rhodanese
KOG1530Eukaryota (superkingdom)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-],arsenate reductase [EC:1.20.4.1],thiosulfate/3-mercaptopyruvate sulfurtransferase [EC:2.8.1.1 2.8.1.2]
HTN0JMetazoa (kingdom)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-],thiosulfate/3-mercaptopyruvate sulfurtransferase [EC:2.8.1.1 2.8.1.2]
HID07Arthropoda (phylum)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-],thiosulfate/3-mercaptopyruvate sulfurtransferase [EC:2.8.1.1 2.8.1.2]
85KGAHexapoda (subphylum)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-],thiosulfate/3-mercaptopyruvate sulfurtransferase [EC:2.8.1.1 2.8.1.2]
AHS4MNeoptera (infraclass)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-]
ANKPPDiptera (order)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-]
7GNHGOpisthokonta (clade)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-],thiosulfate/3-mercaptopyruvate sulfurtransferase [EC:2.8.1.1 2.8.1.2]
H5DY6Bilateria (clade)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-],thiosulfate/3-mercaptopyruvate sulfurtransferase [EC:2.8.1.1 2.8.1.2]
EH5D5Drosophila (genus)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-]
50MWISophophora (subgenus)thiosulfate:glutathione sulfurtransferase [EC:2.8.1.-]

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: