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P41962 (SODC_BRUPA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 64. 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:SODC
OrganismBrugia pahangi (Filarial nematode worm)
Taxonomic identifier6280 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeBrugia

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
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.

Subcellular location

Cytoplasm.

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

Chain1 – 158158Superoxide dismutase [Cu-Zn]
PRO_0000164101

Sites

Metal binding461Copper; catalytic By similarity
Metal binding481Copper; catalytic By similarity
Metal binding631Copper; catalytic By similarity
Metal binding631Zinc; structural By similarity
Metal binding711Zinc; structural By similarity
Metal binding801Zinc; structural By similarity
Metal binding831Zinc; structural By similarity
Metal binding1201Copper; catalytic By similarity

Amino acid modifications

Disulfide bond57 ↔ 149 By similarity

Sequences

Sequence LengthMass (Da)Tools
P41962 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 01A9CCEC76C23768

FASTA15816,341
        10         20         30         40         50         60 
MSANRIAVLR GDNVSGIIRF KQEKEGSPTT ISGEIKGLTP GLHGFHVHQY GDTTNGCISA 

        70         80         90        100        110        120 
GPHFNPYNKT HGGPTDEMRH VGDLGNIVAG ADGTAHIDIS DKHVQLLGPN SIIGRSLVVH 

       130        140        150 
ADQDDLGKGV GDKKDESLKT GNAGARVACG IVAVSAAS 

« Hide

References

[1]"Extracellular and cytoplasmic CuZn superoxide dismutases from Brugia lymphatic filarial nematode parasites."
Tang L., Ou X., Henkle K.J., Selkirk M.E.
Infect. Immun. 62:961-967(1994) [PubMed: 8112870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76284 mRNA. Translation: CAA53902.1.

3D structure databases

ProteinModelPortalP41962.
SMRP41962. Positions 3-156.
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_BRUPA
AccessionPrimary (citable) accession number: P41962
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 27, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families