Reviewed,
UniProtKB/Swiss-Prot Q9WYK0 (END3_THEMA)
Last modified
February 9, 2010.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Endonuclease III EC=4.2.99.18 Alternative name(s): DNA-(apurinic or apyrimidinic site) lyase | ||||
| Gene names |
| ||||
| Organism | Thermotoga maritima [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2336 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga |
Protein attributes
| Sequence length | 213 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Has both an apurinic and/or apyrimidinic endonuclease activity and a DNA N-glycosylase activity. Incises damaged DNA at cytosines, thymines and guanines. Acts on a damaged strand, 5' from the damaged site By similarity. |
| Catalytic activity | The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate. |
| Cofactor | Binds 1 4Fe-4S cluster. The cluster is not important for the catalytic activity, but which is probably involved in the proper positioning of the enzyme along the DNA strand By similarity. |
| Sequence similarities | Belongs to the nth/mutY family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA repair |
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding |
| Molecular function | Glycosidase Hydrolase Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | base-excision repair Inferred from electronic annotation. Source: InterPro |
| Cellular component | intracellular Inferred from electronic annotation. Source: InterPro |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW DNA bindingInferred from electronic annotation. Source: InterPro DNA-(apurinic or apyrimidinic site) lyase activityInferred from electronic annotation. Source: EC endonuclease activityInferred from electronic annotation. Source: InterPro hydrolase activity, acting on glycosyl bondsInferred from electronic annotation. Source: UniProtKB-KW iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 213 | 213 | Endonuclease III | PRO_0000102224 | |||||
Sites | |||||||||
| Metal binding | 180 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 187 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 190 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 196 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| [1] | "Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M.Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000512 Genomic DNA. Translation: AAD35453.1. |
| PIR | F72387. |
| RefSeq | NP_228177.1. |
3D structure databases | |
| SMR | Q9WYK0. Positions 3-203. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 897325. |
| GenomeReviews | Gene locus TM_0366 in contig AE000512_GR. |
| KEGG | tma:TM0366. |
| NMPDR | fig|243274.1.peg.361. |
| TIGR | TM_0366. |
Phylogenomic databases | |
| HOGENOM | HBG464473. |
| OMA | ANCVLVY. |
Enzyme and pathway databases | |
| BioCyc | TMAR243274:TM_0366-MONOMER. |
| BRENDA | 4.2.99.18. 16699. |
Family and domain databases | |
| InterPro | IPR011257. DNA_glycosylase. IPR004036. Endonuclease-III_CS2. IPR005759. Endonuclease-III_Nth. IPR004035. Endouclease-III_FeS-bd_BS. IPR003651. Endouclease3_FeS-loop_motif. IPR003265. HhH-GPD_domain. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. [Graphical view] |
| Pfam | PF10576. EndIII_4Fe-2S. 1 hit. PF00730. HhH-GPD. 1 hit. [Graphical view] |
| SMART | SM00478. ENDO3c. 1 hit. SM00525. FES. 1 hit. SM00278. HhH1. 2 hits. [Graphical view] |
| TIGRFAMs | TIGR01083. nth. 1 hit. |
| PROSITE | PS00764. ENDONUCLEASE_III_1. 1 hit. PS01155. ENDONUCLEASE_III_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | END3_THEMA | ||||||||
| Accession | Primary (citable) accession number: Q9WYK0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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