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Database: UniProt
Entry: G0RES9_HYPJQ
LinkDB: G0RES9_HYPJQ
Original site: G0RES9_HYPJQ 
ID   G0RES9_HYPJQ            Unreviewed;       248 AA.
AC   G0RES9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Superoxide dismutase 1 copper chaperone {ECO:0000256|ARBA:ARBA00016103};
DE   AltName: Full=Superoxide dismutase copper chaperone {ECO:0000256|ARBA:ARBA00032899};
GN   ORFNames=TRIREDRAFT_120968 {ECO:0000313|EMBL:EGR50173.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR50173.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR50173.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- SIMILARITY: Belongs to the CCS1 family.
CC       {ECO:0000256|ARBA:ARBA00010636}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the Cu-Zn superoxide
CC       dismutase family. {ECO:0000256|ARBA:ARBA00025798}.
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DR   EMBL; GL985060; EGR50173.1; -; Genomic_DNA.
DR   RefSeq; XP_006963698.1; XM_006963636.1.
DR   AlphaFoldDB; G0RES9; -.
DR   STRING; 431241.G0RES9; -.
DR   EnsemblFungi; EGR50173; EGR50173; TRIREDRAFT_120968.
DR   GeneID; 18483010; -.
DR   KEGG; tre:TRIREDRAFT_120968; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_120968; -.
DR   eggNOG; KOG4656; Eukaryota.
DR   HOGENOM; CLU_056632_0_0_1; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000008984; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 2.60.40.200; Superoxide dismutase, copper/zinc binding domain; 1.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003:SF86; COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008984}.
FT   DOMAIN          6..69
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   248 AA;  26595 MW;  9D1472D11429706C CRC64;
     MAVKHSFQTL FAVPLSCDGC VKSVSDSLYK LDGITKVEAN LKDQLISVEG SVAPSAIVEA
     IQATGRDAIL RGSGASNSAA VSILETFADQ QERSDVDNSR EVRGLARMVQ VSPERTLIDL
     TLRGVAPGTY RATIREYGDL KDGAASTGPV WSGGEKEAPK GDLGVVQVSE DGRGSVFVDH
     PFQIWEVIGH AMVLTRQDES TPLKNDDNTV VGVIARSAGV WDNDKTVCSC TGKTLWEERQ
     DEVKKGML
//
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