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Database: UniProt/TrEMBL
Entry: Q9ZNQ4_CICAR
LinkDB: Q9ZNQ4_CICAR
Original site: Q9ZNQ4_CICAR 
ID   Q9ZNQ4_CICAR            Unreviewed;       152 AA.
AC   Q9ZNQ4;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   25-OCT-2017, entry version 90.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=sod-1 {ECO:0000313|EMBL:CAA10160.1};
GN   Synonyms=LOC105851841 {ECO:0000313|RefSeq:XP_012569583.1,
GN   ECO:0000313|RefSeq:XP_012569584.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|EMBL:CAA10160.1};
RN   [1] {ECO:0000313|EMBL:CAA10160.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:CAA10160.1};
RA   Hanselle T., Barz W.;
RT   "Isolation of cDNA Encoding Superoxide Dismutase from Infected
RT   Chickpea Plants.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAA10132.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Etiolated epicotyls {ECO:0000313|EMBL:CAA10132.1};
RA   Hernandez-Nistal J., Dopico B., Labrador E.;
RT   "Cold and salt stress regulates the expression and activity of a
RT   chickpea cytosolic Cu/Zn superoxide dismutase.";
RL   Plant Sci. 163:507-514(2002).
RN   [3] {ECO:0000313|Proteomes:UP000087171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CDC Frontier {ECO:0000313|Proteomes:UP000087171};
RX   PubMed=26259924; DOI=10.1038/srep12806;
RA   Parween S., Nawaz K., Roy R., Pole A.K., Venkata Suresh B., Misra G.,
RA   Jain M., Yadav G., Parida S.K., Tyagi A.K., Bhatia S.,
RA   Chattopadhyay D.;
RT   "An advanced draft genome assembly of a desi type chickpea (Cicer
RT   arietinum L.).";
RL   Sci. Rep. 5:12806-12806(2015).
RN   [4] {ECO:0000313|RefSeq:XP_012569583.1, ECO:0000313|RefSeq:XP_012569584.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_012569583.1,
RC   ECO:0000313|RefSeq:XP_012569584.1};
RG   RefSeq;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [5] {ECO:0000313|RefSeq:XP_012569583.1, ECO:0000313|RefSeq:XP_012569584.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_012569583.1,
RC   ECO:0000313|RefSeq:XP_012569584.1};
RG   RefSeq;
RL   Submitted (JUN-2017) to UniProtKB.
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}.
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DR   EMBL; AJ012691; CAA10132.1; -; mRNA.
DR   EMBL; AJ012739; CAA10160.1; -; mRNA.
DR   RefSeq; NP_001296637.1; NM_001309708.1.
DR   RefSeq; XP_012569583.1; XM_012714129.1.
DR   RefSeq; XP_012569584.1; XM_012714130.1.
DR   GeneID; 105851841; -.
DR   KEGG; cam:105851841; -.
DR   KO; K04565; -.
DR   Proteomes; UP000087171; Genome assembly.
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; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
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   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000087171};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:CAA10160.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       11    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15222 MW;  4ED0AF0A54A8A454 CRC64;
     MVKAVAVLGS SDTVSGTINF SQEGDGPTTV TGNLAGLKPG LHGFHIHALG DTTNGCISTG
     PHFNPNGKEH GSPEDPIRHA GDLGNINVGD DGTVSFSITD NQIPLTGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKTTGNAG GRVACGIIGL QG
//
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