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Protein

Superoxide dismutase [Cu-Zn]

Gene

SODCC

Organism
Zantedeschia aethiopica (White calla lily) (Calla aethiopica)
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 bindingi45 – 451Copper; catalyticBy similarity
Metal bindingi47 – 471Copper; catalyticBy similarity
Metal bindingi62 – 621Copper; catalyticBy similarity
Metal bindingi62 – 621Zinc; structuralBy similarity
Metal bindingi70 – 701Zinc; structuralBy similarity
Metal bindingi79 – 791Zinc; structuralBy similarity
Metal bindingi82 – 821Zinc; structuralBy similarity
Metal bindingi119 – 1191Copper; 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:SODCC
Synonyms:SOD3
OrganismiZantedeschia aethiopica (White calla lily) (Calla aethiopica)
Taxonomic identifieri69721 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAraceaePhilodendroideaeZantedeschieaeZantedeschia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Superoxide dismutase [Cu-Zn]PRO_0000164159Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 145By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO65174.
SMRiO65174. Positions 1-152.
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.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O65174-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKAVAVLTG SEGVQGTVFF AQEGEGPTTI TGSLSGLKPG LHGFHVHALG
60 70 80 90 100
DTTNGCMSTG PHFNPAGKEH GAPEDGNRHA GDLGNVTVGE DGTVNFTVTD
110 120 130 140 150
SQIPLTGLNS VVGRAVVVHA DSDDLGKGGH ELSKTTGNAG GRLACGVIGL

QA
Length:152
Mass (Da):15,152
Last modified:August 1, 1998 - v1
Checksum:i96C535E190102160
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054150 mRNA. Translation: AAC08581.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF054150 mRNA. Translation: AAC08581.1.

3D structure databases

ProteinModelPortaliO65174.
SMRiO65174. Positions 1-152.
ModBaseiSearch...
MobiDBiSearch...

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.
PS00332. SOD_CU_ZN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Expression of cytosolic Cu/Zn-superoxide dismutase during senescence and regreening of Zantedeschia aethiopica spathe."
    Lino-Neto T., Tavares R.M., Palme K., Pais M.S.S.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leaf.

Entry informationi

Entry nameiSODC_ZANAE
AccessioniPrimary (citable) accession number: O65174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: November 11, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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.