P9WNV3 ligD, Rv0938, MTCY08D9.01c, MTCY10D7.36c
Source: Uniprot proteome:up000001584
| Title | id | ORF names | Protein names | PubMed ID | Short | Synonyms | EnsemblBacteria |
|---|---|---|---|---|---|---|---|
| P9WNV3 LIGD_MYCTU | MTCY08D9.01c, MTCY10D7.36c | Multifunctional non-homologous end joining DNA repair protein LigD (NHEJ DNA repair protein D) (Mt-Lig) (NHEJ DNA polymerase) [Includes: DNA repair polymerase (Pol) (Polymerase | 9634230, 12215643, 14985346, 15499016, 16023671, 15778718, 16949369, 21637345, 16476729, 17174332, 17947582, 21255731, 24239356 | ligD | ligD, Rv0938, MTCY08D9.01c, MTCY10D7.36c |
| Binding Site |
|---|
| 52 52 Substrate, for polymerase activity., 111 111 Substrate, for polymerase activity., 230 230 Substrate, for polymerase activity., 236 236 Substrate, for polymerase activity., 244 244 Substrate, for polymerase activity. |
| Domain | InterPro | Pfam | ProDom | Region | Similarity | SUPFAM |
|---|---|---|---|---|---|---|
| The N-terminal Mn(2+)-dependent polymerase/primase domain (Pol) functions as an independent domain, binds DNA, is sufficient for DNA-directed and non-DNA-directed DNA synthesis (PubMed:15778718) and interacts with Ku (PubMed:16023671).; The central 3'-phosphoesterase domain (PE) has exonuclease activity probably constituted of 3'-ribonuclease and 3'-phosphatase activity (PubMed:15499016). It does not function as an independent domain (PubMed:16023671).; The C-terminal ligase domain (Lig) binds dsDNA and functions as an independent domain (PubMed:14985346, PubMed:16023671). | PF04679, PF01068, PF01896, PF13298 | In the N-terminal section, belongs to the LigD polymerase family., In the central section, belongs to the LigD 3'-phosphoesterase family., In the C-terminal section, belongs to the ATP-dependent DNA ligase family. | SSF50249 |
| SSGCID ID |
|---|
| PDB | Protein Model Portal |
|---|---|
| EC number | KEGG KO | UniPathway |
|---|---|---|
| 6.5.1.1 |
| HOGENOM | KEGG KO | OMA | OrthoDB |
|---|---|---|---|