A0A1D1VU85 · SODC_RAMVA
- ProteinSuperoxide dismutase [Cu-Zn]
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids194 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic activity
- 2 H+ + 2 superoxide = H2O2 + O2
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 copper ion per subunit.
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 85 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 104 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 104 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 112 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 121 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: H | ||||||
Binding site | 124 | Zn2+ (UniProtKB | ChEBI); structural | ||||
Sequence: D | ||||||
Binding site | 162 | Cu cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | copper ion binding | |
Molecular Function | identical protein binding | |
Molecular Function | protein homodimerization activity | |
Molecular Function | superoxide dismutase activity | |
Molecular Function | zinc ion binding | |
Biological Process | removal of superoxide radicals |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuperoxide dismutase [Cu-Zn]
- EC number
- Short namesCuZnSOD
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Tardigrada > Eutardigrada > Parachela > Hypsibioidea > Ramazzottiidae > Ramazzottius
Accessions
- Primary accessionA0A1D1VU85
Proteomes
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MTRPLALIIFLVAILTNTDP | ||||||
Chain | PRO_5008898852 | 21-194 | Superoxide dismutase [Cu-Zn] | |||
Sequence: SRSDAGSDPVNYLFRGPVTAVAAIAGEGEHAGIKGSLTFLQKSLDGRTVINGTISGLPEGKHGLHIVDSGDMTKGCYITTAKGHLNPFNLSHGAPSDSARHVGDLGNIYADDTGISVINLTDTVISLFPTPAFVIGRILVIHTTYDDLGRGGSPVSKVNGNAGGRLACGIISYV | ||||||
Disulfide bond | 96↔188 | |||||
Sequence: CYITTAKGHLNPFNLSHGAPSDSARHVGDLGNIYADDTGISVINLTDTVISLFPTPAFVIGRILVIHTTYDDLGRGGSPVSKVNGNAGGRLAC |
Keywords
- PTM
Interaction
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length194
- Mass (Da)20,109
- Last updated2016-11-30 v1
- Checksum5954031F2E894C1A
Keywords
- Technical term