ID   A0A2T3ZXH6_TRIHA        Unreviewed;       292 AA.
AC   A0A2T3ZXH6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=M431DRAFT_512923 {ECO:0000313|EMBL:PTB49478.1};
OS   Trichoderma harzianum CBS 226.95.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB49478.1, ECO:0000313|Proteomes:UP000241690};
RN   [1] {ECO:0000313|EMBL:PTB49478.1, ECO:0000313|Proteomes:UP000241690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB49478.1,
RC   ECO:0000313|Proteomes:UP000241690};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ679692; PTB49478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3ZXH6; -.
DR   STRING; 983964.A0A2T3ZXH6; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000241690; 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:UP000241690}.
FT   DOMAIN          50..113
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   292 AA;  31114 MW;  9FA345EAC9F3E3F2 CRC64;
     MALRNAASSK ILAASFGLFA GYSAYRYRAS HSASPTSSAP TPGNMAVKHS FQTLFAVPLS
     CDGCVKSVSD SLYKLDGITK VEGNLKDQLV SVEGSVAPSA IVEAIQATGR DAILRGSGAS
     NSAAVSILET FADQAEHVED DTSREVRGLA RMVQVSPDRT LIDLTIRGVA PGTYRATIRE
     FGDLKDGAES TGPIWSGGEK EEPKGSLGIV QVSKDGRGSA FVDHAFQIWE VIGHAMVLTR
     QDETQPLKND DNTVVGVIAR SAGMWDNDKT VCSCTGKTLW EEREDEVKKG ML
//