GenomeNet

Database: UniProt/TrEMBL
Entry: V4T4M7_9ROSI
LinkDB: V4T4M7_9ROSI
Original site: V4T4M7_9ROSI 
ID   V4T4M7_9ROSI            Unreviewed;       152 AA.
AC   V4T4M7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   07-JUN-2017, entry version 21.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=CICLE_v10002756mg {ECO:0000313|EMBL:ESR46365.1};
OS   Citrus clementina.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Sapindales; Rutaceae; Aurantioideae;
OC   Citrus.
OX   NCBI_TaxID=85681 {ECO:0000313|EMBL:ESR46365.1, ECO:0000313|Proteomes:UP000030687};
RN   [1] {ECO:0000313|EMBL:ESR46365.1, ECO:0000313|Proteomes:UP000030687}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Jenkins J., Schmutz J., Prochnik S., Rokhsar D., Gmitter F.,
RA   Ollitrault P., Machado M., Talon M., Wincker P., Jaillon O.,
RA   Morgante M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; KI536799; ESR46365.1; -; Genomic_DNA.
DR   RefSeq; XP_006433125.1; XM_006433062.1.
DR   PRIDE; V4T4M7; -.
DR   GeneID; 18042975; -.
DR   KEGG; cic:CICLE_v10002756mg; -.
DR   KO; K04565; -.
DR   Proteomes; UP000030687; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030687};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030687};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       12    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15095 MW;  2CE32D8FB421D45C CRC64;
     MVKAVAVLGG TEGVKGTVSF SQEGDGPTTV SGSLSGLKPG PHGFHVHALG DTTNGCMSTG
     PHFNPAGKEH GPPEDENRHA GDLGNVNVGD DGTATFTVVD NQIPLSGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKTTGNAG GRVACGIIGL QG
//
DBGET integrated database retrieval system