Q751L8 (SODC_ASHGO) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 57.
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: Superoxide dismutase [Cu-Zn] EC=1.15.1.1 | ||||
| Gene names |
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| Organism | Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome] | ||||
| Taxonomic identifier | 284811 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium |
Protein attributes
| Sequence length | 154 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Destroys radicals which are normally produced within the cells and which are toxic to biological systems By similarity. |
| Catalytic activity | 2 superoxide + 2 H+ = O2 + H2O2. |
| Cofactor | Binds 1 copper ion per subunit By similarity. Binds 1 zinc ion per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the Cu-Zn superoxide dismutase family. |
| Sequence caution | The sequence AAS54170.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Copper Metal-binding Zinc |
| Molecular function | Antioxidant Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | removal of superoxide radicals Inferred from Biological aspect of Ancestor. Source: RefGenome |
| Cellular component | cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome mitochondrionInferred from Biological aspect of Ancestor. Source: RefGenome nucleusInferred from Biological aspect of Ancestor. Source: RefGenome |
| Molecular function | copper ion binding Inferred from Biological aspect of Ancestor. Source: RefGenome superoxide dismutase activityInferred from Biological aspect of Ancestor. Source: RefGenome zinc ion bindingInferred from Biological aspect of Ancestor. Source: RefGenome |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 154 | 153 | Superoxide dismutase [Cu-Zn] | PRO_0000164106 | |||||||
Sites | |||||||||||
| Metal binding | 47 | 1 | Copper By similarity | ||||||||
| Metal binding | 49 | 1 | Copper By similarity | ||||||||
| Metal binding | 64 | 1 | Copper By similarity | ||||||||
| Metal binding | 64 | 1 | Zinc By similarity | ||||||||
| Metal binding | 72 | 1 | Zinc By similarity | ||||||||
| Metal binding | 81 | 1 | Zinc By similarity | ||||||||
| Metal binding | 84 | 1 | Zinc By similarity | ||||||||
| Metal binding | 121 | 1 | Copper By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 58 ↔ 147 | By similarity | |||||||||
Sequences
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References
| [1] | "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016820 Genomic DNA. Translation: AAS54170.1. Sequence problems. |
| RefSeq | NP_986346.2. NM_211408.2. |
3D structure databases | |
| ProteinModelPortal | Q751L8. |
| SMR | Q751L8. Positions 2-154. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q751L8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4622639. |
| GenomeReviews | Gene locus AGL321W in contig AE016820_GR. |
| KEGG | ago:AGOS_AGL321W. |
Organism-specific databases | |
| AGD | AGL321W. |
Phylogenomic databases | |
| eggNOG | fuNOG09621. |
| HOGENOM | HBG609879. |
| OrthoDB | EOG4X3M9S. |
| PhylomeDB | Q751L8. |
Family and domain databases | |
| InterPro | IPR024134. SOD_Cu/Zn_/chaperones. IPR018152. SOD_Cu/Zn_BS. IPR001424. SOD_Cu_Zn_dom. [Graphical view] |
| Gene3D | G3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit. |
| KO | K04565. |
| PANTHER | PTHR10003. SOD_Cu_Zn. 1 hit. |
| Pfam | PF00080. Sod_Cu. 1 hit. [Graphical view] |
| PRINTS | PR00068. CUZNDISMTASE. |
| SUPFAM | SSF49329. SOD_Cu_Zn. 1 hit. |
| PROSITE | PS00087. SOD_CU_ZN_1. 1 hit. PS00332. SOD_CU_ZN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SODC_ASHGO | ||||||||
| Accession | Primary (citable) accession number: Q751L8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with