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Q9Y8D9 (SODC_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Superoxide dismutase [Cu-Zn]
EC=1.15.1.1
Gene names
Name:sodC
ORF Names:AFUA_5G09240
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus ›

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

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 EAL91677.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandCopper
Metal-binding
Zinc
   Molecular functionAntioxidant
Oxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
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_0000164108

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

Experimental info

Sequence conflict81Missing in AAL38991. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Y8D9 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: FB2FC504140DDED6

FASTA15415,967
        10         20         30         40         50         60 
MVKAVAVLRG DSKITGTVTF EQADENSPTT VSWNIKGNDP NAKRGFHVHQ FGDNTNGCTS 

        70         80         90        100        110        120 
AGPHFNPYGK THGAPEDSER HVGDLGNFET DAEGNAVGSK QDKLIKLIGA ESVLGRTLVV 

       130        140        150 
HAGTDDLGRG GNEESKKTGN AGARPACGVI GIAA

« Hide

References

« Hide 'large scale' references
[1]"Production and characterization of recombinant Aspergillus fumigatus Cu,Zn superoxide dismutase and its recognition by immune human sera."
Holdom M.D., Lechenne B., Hay R.J., Hamilton A.J., Monod M.
J. Clin. Microbiol. 38:558-562(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Homogeneity in 3-dimensional structure of Cu,Zn superoxide dismutases of Aspergillus fumigatus, Aspergillus flavus and Aspergillus nidulans."
Holdom M.D., Hobby P., Lechenne B., Zaugg C., Sutton B., Monod M., Hamilton A.J.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF128886 mRNA. Translation: AAD42060.1.
AF281057 Genomic DNA. Translation: AAL38991.1.
AAHF01000003 Genomic DNA. Translation: EAL91677.1. Sequence problems.
RefSeqXP_753715.1. XM_748622.1.

3D structure databases

ProteinModelPortalQ9Y8D9.
SMRQ9Y8D9. Positions 2-152.
ModBaseSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00006737.

Proteomic databases

PRIDEQ9Y8D9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3511006.
KEGGafm:AFUA_5G09240.

Phylogenomic databases

eggNOGCOG2032.
HOGENOMHOG000263447.
KOK04565.
OrthoDBEOG4X3M9S.

Enzyme and pathway databases

BRENDA1.15.1.1. 508.

Family and domain databases

Gene3D2.60.40.200. 1 hit.
InterProIPR024134. SOD_Cu/Zn_/chaperones.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERPTHR10003. PTHR10003. 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_ASPFU
AccessionPrimary (citable) accession number: Q9Y8D9
Secondary accession number(s): Q4WUP9, Q8X1S8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 91 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

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