Alternative representations: 1 /
| Protein length | 965 aa |
|---|---|
| Source database | UniProt |
| Identifiers | A7TGW3_VANPO, A7TGW3 |
| Domain organisation | Proteins having all the domains as the query in the same order. Additional domains are allowed. |
|---|---|
| Domain composition | Proteins 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 Eukaryota
A7TGW3_VANPO is shown as
Kpol_1032p7 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.
Protein A7TGW3_VANPO is possibly involved in these pathways, based on its similarity to the listed KEGG 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 436907.A7TGW3 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| FT6BV | Dikarya (subkingdom) | DNA ligase 4 [EC:6.5.1.1] |
| LCOG1793 | All organisms (root) | DNA ligase 1 [EC:6.5.1.1 6.5.1.6 6.5.1.7],bifunctional non-homologous end joining protein LigD [EC:6.5.1.1],DNA ligase 4 [EC:6.5.1.1] |
| KOG0966 | Eukaryota (superkingdom) | DNA ligase 4 [EC:6.5.1.1],DNA ligase 1 [EC:6.5.1.1 6.5.1.6 6.5.1.7],DNA ligase 3 [EC:6.5.1.1] |
| BNIW0 | Fungi (kingdom) | DNA ligase 4 [EC:6.5.1.1] |
| 9UF6M | Ascomycota (phylum) | DNA ligase 4 [EC:6.5.1.1] |
| 91J27 | Saccharomycetales (order) | DNA ligase 4 [EC:6.5.1.1] |
| 7JWT3 | Opisthokonta (clade) | DNA ligase 4 [EC:6.5.1.1],vacuolar fusion protein MON1,general transcription factor 3C polypeptide 3 (transcription factor C subunit 4) |
| AT4HQ | Saccharomycetaceae (family) | DNA ligase 4 [EC:6.5.1.1] |
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.