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Protein

Superoxide dismutase [Cu-Zn]

Gene

SOD

Organism
Haemonchus contortus (Barber pole worm)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Copper; catalyticBy similarity
Metal bindingi49 – 491Copper; catalyticBy similarity
Metal bindingi64 – 641Copper; catalyticBy similarity
Metal bindingi64 – 641Zinc; structuralBy similarity
Metal bindingi72 – 721Zinc; structuralBy similarity
Metal bindingi81 – 811Zinc; structuralBy similarity
Metal bindingi84 – 841Zinc; structuralBy similarity
Metal bindingi121 – 1211Copper; catalyticBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
Gene namesi
Name:SOD
OrganismiHaemonchus contortus (Barber pole worm)
Taxonomic identifieri6289 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaStrongylidaTrichostrongyloideaHaemonchidaeHaemonchinaeHaemonchus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 159159Superoxide dismutase [Cu-Zn]PRO_0000164103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 150By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ27666.

Structurei

3D structure databases

ProteinModelPortaliQ27666.
SMRiQ27666. Positions 4-154.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Cu-Zn superoxide dismutase family.Curated

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27666-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNRAVAVLR GDPGVTGTVW FSQDKESDPC VIKGEIKGLT PGLHGFHVHQ
60 70 80 90 100
YGDSTNGCTS AGPHFNPFNK THGGPKDDVR HVGDLGNVEA GADGVAHFEI
110 120 130 140 150
KDHLVKIHGE HTVVGRSLVV HAGTDDLGKG VGEKKEESLK TGNRGARVAC

GVIATAAPQ
Length:159
Mass (Da):16,603
Last modified:November 1, 1996 - v1
Checksum:i40B998876B3754C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69621 mRNA. Translation: CAA93447.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69621 mRNA. Translation: CAA93447.1.

3D structure databases

ProteinModelPortaliQ27666.
SMRiQ27666. Positions 4-154.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ27666.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.40.200. 1 hit.
InterProiIPR024134. SOD_Cu/Zn_/chaperone.
IPR018152. SOD_Cu/Zn_BS.
IPR001424. SOD_Cu_Zn_dom.
[Graphical view]
PANTHERiPTHR10003. PTHR10003. 1 hit.
PfamiPF00080. Sod_Cu. 1 hit.
[Graphical view]
PRINTSiPR00068. CUZNDISMTASE.
SUPFAMiSSF49329. SSF49329. 1 hit.
PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Extracellular and cytoplasmic Cu/Zn superoxide dismutases from Haemonchus contortus."
    Liddell S., Knox D.P.
    Parasitology 116:383-394(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Moredun.

Entry informationi

Entry nameiSODC_HAECO
AccessioniPrimary (citable) accession number: Q27666
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.