O05956 (END3_RICPR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 79.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 | Rickettsia prowazekii (strain Madrid E) | ||||
| Taxonomic identifier | 272947 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group |
Protein attributes
| Sequence length | 212 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 Reference 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 metal 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 – 212 | 212 | Endonuclease III | PRO_0000102221 | |||||
Sites | |||||||||
| Metal binding | 187 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 194 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 197 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
| Metal binding | 203 | 1 | Iron-sulfur (4Fe-4S) By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genomic rearrangements during evolution of the obligate intracellular parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp nucleotide sequence." Andersson J.O., Andersson S.G.E. Microbiology 143:2783-2795(1997) [PubMed: 9274032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Madrid E. |
| [2] | "The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed: 9823893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y11778 Genomic DNA. Translation: CAA72458.1. AJ235273 Genomic DNA. Translation: CAA15174.1. |
| PIR | F71634. |
| RefSeq | NP_221098.1. NC_000963.1. |
3D structure databases | |
| ProteinModelPortal | O05956. |
| SMR | O05956. Positions 7-208. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 883968. |
| GenomeReviews | Gene locus RP746 in contig AJ235269_GR. |
| KEGG | rpr:RP746. |
| PATRIC | 17902351. VBIRicPro72556_0779. |
Phylogenomic databases | |
| HOGENOM | HBG464473. |
| OMA | EVPQTRE. |
| ProtClustDB | CLSK871058. |
Enzyme and pathway databases | |
| BioCyc | RPRO272947:RP746-MONOMER. |
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. IPR000445. HhH_motif. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. IPR023170. HTH_base_excis_C. [Graphical view] |
| Gene3D | G3DSA:1.10.340.30. DNA_glycosylase. 1 hit. G3DSA:1.10.1670.10. HTH_base_excis_C. 1 hit. |
| KO | K10773. |
| Pfam | PF10576. EndIII_4Fe-2S. 1 hit. PF00633. HHH. 1 hit. PF00730. HhH-GPD. 1 hit. [Graphical view] |
| SMART | SM00478. ENDO3c. 1 hit. SM00525. FES. 1 hit. SM00278. HhH1. 1 hit. [Graphical view] |
| SUPFAM | SSF48150. DNA_glycsylse. 1 hit. |
| 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_RICPR | ||||||||
| Accession | Primary (citable) accession number: O05956 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Rickettsia prowazekii Rickettsia prowazekii (strain Madrid E): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with