GenomeNet

Database: UniProt
Entry: C7ZR16_NECH7
LinkDB: C7ZR16_NECH7
Original site: C7ZR16_NECH7 
ID   C7ZR16_NECH7            Unreviewed;       173 AA.
AC   C7ZR16;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   16-JAN-2019, entry version 51.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=NECHADRAFT_105766 {ECO:0000313|EMBL:EEU33541.1};
OS   Nectria haematococca (strain 77-13-4 / ATCC MYA-4622 / FGSC 9596 /
OS   MPVI) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium solani species complex.
OX   NCBI_TaxID=660122 {ECO:0000313|Proteomes:UP000005206};
RN   [1] {ECO:0000313|EMBL:EEU33541.1, ECO:0000313|Proteomes:UP000005206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=77-13-4 / ATCC MYA-4622 / FGSC 9596 / MPVI
RC   {ECO:0000313|Proteomes:UP000005206};
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A.,
RA   Wasmann C.C., Grimwood J., Schmutz J., Taga M., White G.J., Zhou S.,
RA   Schwartz D.C., Freitag M., Ma L.J., Danchin E.G., Henrissat B.,
RA   Coutinho P.M., Nelson D.R., Straney D., Napoli C.A., Barker B.M.,
RA   Gribskov M., Rep M., Kroken S., Molnar I., Rensing C., Kennell J.C.,
RA   Zamora J., Farman M.L., Selker E.U., Salamov A., Shapiro H.,
RA   Pangilinan J., Lindquist E., Lamers C., Grigoriev I.V., Geiser D.M.,
RA   Covert S.F., Temporini E., Vanetten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; GG699024; EEU33541.1; -; Genomic_DNA.
DR   RefSeq; XP_003039254.1; XM_003039208.1.
DR   ProteinModelPortal; C7ZR16; -.
DR   STRING; 140110.NechaP105766; -.
DR   EnsemblFungi; NechaT105766; NechaP105766; NechaG105766.
DR   GeneID; 9666773; -.
DR   KEGG; nhe:NECHADRAFT_105766; -.
DR   InParanoid; C7ZR16; -.
DR   KO; K04565; -.
DR   OrthoDB; 1574423at2759; -.
DR   Proteomes; UP000005206; 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; 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:UP000005206};
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:UP000005206};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       11    150       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   173 AA;  18289 MW;  95B938FAA9FFC17D CRC64;
     MVKAIATVRG DSTVFGTITF EQLDESSPTT ISWNLRGNDA NSQRAFHIHE FGDNTNGCTS
     AGPHFNPFGR THGAPSHNER HVGDLGNFQT DSSGTSIGTM TDHLVKLIGP ESVLGRTIVI
     HAGTDDLGQG PNEESKITGN AGGRPACGVI GISSSGFQCR YEPVTHSLFG HDN
//
DBGET integrated database retrieval system