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Database: UniProt
Entry: M0S4H9_MUSAM
LinkDB: M0S4H9_MUSAM
Original site: M0S4H9_MUSAM 
ID   M0S4H9_MUSAM            Unreviewed;       152 AA.
AC   M0S4H9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   13-FEB-2019, entry version 33.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=103970087 {ECO:0000313|EnsemblPlants:GSMUA_Achr2P02380_001};
OS   Musa acuminata subsp. malaccensis (Wild banana) (Musa malaccensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Zingiberales; Musaceae;
OC   Musa.
OX   NCBI_TaxID=214687 {ECO:0000313|EnsemblPlants:GSMUA_Achr2P02380_001, ECO:0000313|Proteomes:UP000012960};
RN   [1] {ECO:0000313|EnsemblPlants:GSMUA_Achr2P02380_001, ECO:0000313|Proteomes:UP000012960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Doubled-haploid Pahang [DH-Pahang]
RC   {ECO:0000313|EnsemblPlants:GSMUA_Achr2P02380_001,
RC   ECO:0000313|Proteomes:UP000012960};
RX   PubMed=22801500; DOI=10.1038/nature11241;
RA   D Hont A., Denoeud F., Aury J.M., Baurens F.C., Carreel F.,
RA   Garsmeur O., Noel B., Bocs S., Droc G., Rouard M., Da Silva C.,
RA   Jabbari K., Cardi C., Poulain J., Souquet M., Labadie K., Jourda C.,
RA   Lengelle J., Roudier-Goud M., Alberti A., Bernard M., Correa M.,
RA   Ayyampalayam S., Mckain M.R., Leebens-Mack J., Burgess D.,
RA   Freeling M., Mbeguie-A-Mbeguie D., Chabannes M., Wicker T., Panaud O.,
RA   Barbosa J., Hribova E., Heslop-Harrison P., Habas R., Rivallan R.,
RA   Francois P., Poiron C., Kilian A., Burthia D., Jenny C., Bakry F.,
RA   Brown S., Guignon V., Kema G., Dita M., Waalwijk C., Joseph S.,
RA   Dievart A., Jaillon O., Leclercq J., Argout X., Lyons E., Almeida A.,
RA   Jeridi M., Dolezel J., Roux N., Risterucci A.M., Weissenbach J.,
RA   Ruiz M., Glaszmann J.C., Quetier F., Yahiaoui N., Wincker P.;
RT   "The banana (Musa acuminata) genome and the evolution of
RT   monocotyledonous plants.";
RL   Nature 488:213-217(2012).
RN   [2] {ECO:0000313|EnsemblPlants:GSMUA_Achr2P02380_001}
RP   IDENTIFICATION.
RC   STRAIN=subsp. malaccensis
RC   {ECO:0000313|EnsemblPlants:GSMUA_Achr2P02380_001};
RG   EnsemblPlants;
RL   Submitted (JUN-2013) 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:
CC       Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:18421; EC=1.15.1.1;
CC         Evidence={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   RefSeq; XP_009382001.1; XM_009383726.2.
DR   RefSeq; XP_009382009.1; XM_009383734.2.
DR   ProteinModelPortal; M0S4H9; -.
DR   STRING; 4641.GSMUA_Achr2P02380_001; -.
DR   EnsemblPlants; GSMUA_Achr2T02380_001; GSMUA_Achr2P02380_001; GSMUA_Achr2G02380_001.
DR   GeneID; 103970087; -.
DR   Gramene; GSMUA_Achr2T02380_001; GSMUA_Achr2P02380_001; GSMUA_Achr2G02380_001.
DR   KEGG; mus:103970087; -.
DR   KO; K04565; -.
DR   OMA; HKGDIGN; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000012960; Chromosome 2.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000012960};
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:UP000012960};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       11    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   152 AA;  15229 MW;  CF256BA89DEF4BAE CRC64;
     MVKAVVVLGG SEDVKGTVYF SQEGDGPTTV TGSISGLKPG LHGFHVHALG DTTNGCMSTG
     PHFNPVGKEH GAPEDDNRHA GDLGNVTAGE DGTVTISKVD NQIPLSGPNS IIGRAVVVHA
     DPDDLGKGGH ELSKSTGNAG GRVACGIIGL QG
//
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