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O94178 (SODC_COLGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]

EC=1.15.1.1
Gene names
Name:SOD1
OrganismColletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata)
Taxonomic identifier474922 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeGlomerellalesGlomerellaceaeGlomerella

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processsuperoxide metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

superoxide dismutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 154153Superoxide dismutase [Cu-Zn]
PRO_0000164115

Sites

Metal binding471Copper By similarity
Metal binding491Copper By similarity
Metal binding641Copper By similarity
Metal binding641Zinc By similarity
Metal binding721Zinc By similarity
Metal binding811Zinc By similarity
Metal binding841Zinc By similarity
Metal binding1211Copper By similarity

Amino acid modifications

Disulfide bond58 ↔ 147 By similarity

Sequences

Sequence LengthMass (Da)Tools
O94178 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 177F4962166699AC

FASTA15415,966
        10         20         30         40         50         60 
MVKAVCVVRG DSKVTGSIVF EQESESAPTK ITWDISGNDA NAKRGMHIHT FGDNTNGCTS 

        70         80         90        100        110        120 
AGPHFNPHNK THGAPEDSNR HVGDLGNIET DANGNSKGTV TDSHVKLIGP ESVIGRTIVV 

       130        140        150 
HGGTDDLGKG DNEESLKTGN AGPRPACGVI GISN 

« Hide

References

[1]"A Cu-Zn superoxide dismutase from Glomerella cingulata."
Clark S.J., Templeton M.D., Sullivan P.A.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ICMP 110146.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF076951 Genomic DNA. Translation: AAD19338.1.

3D structure databases

ProteinModelPortalO94178.
SMRO94178. Positions 2-154.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
Gene3DG3DSA:2.60.40.200. SOD_Cu_Zn. 1 hit.
PANTHERPTHR10003. SOD_Cu_Zn. 1 hit.
PfamPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSPR00068. CUZNDISMTASE.
SUPFAMSSF49329. SOD_Cu_Zn. 1 hit.
PROSITEPS00087. SOD_CU_ZN_1. 1 hit.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSODC_COLGL
AccessionPrimary (citable) accession number: O94178
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: July 27, 2011
This is version 58 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families