ID   A0A2K3QGN8_9HYPO        Unreviewed;       226 AA.
AC   A0A2K3QGN8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=TCAP_03357 {ECO:0000313|EMBL:PNY26716.1};
OS   Tolypocladium capitatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX   NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY26716.1, ECO:0000313|Proteomes:UP000236621};
RN   [1] {ECO:0000313|EMBL:PNY26716.1, ECO:0000313|Proteomes:UP000236621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY26716.1,
RC   ECO:0000313|Proteomes:UP000236621};
RA   Quandt C.A., Patterson W., Spatafora J.W.;
RT   "Harnessing the power of phylogenomics to disentangle the directionality
RT   and signatures of interkingdom host jumping in the parasitic fungal genus
RT   Tolypocladium.";
RL   Submitted (AUG-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNY26716.1}.
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DR   EMBL; NRSZ01000507; PNY26716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K3QGN8; -.
DR   STRING; 45235.A0A2K3QGN8; -.
DR   OrthoDB; 1693333at2759; -.
DR   Proteomes; UP000236621; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:InterPro.
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; 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:UP000236621}.
FT   DOMAIN          7..74
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   226 AA;  24794 MW;  39CE83F219F1AC00 CRC64;
     MMTLDHSFQT LFAVPLSCDG CVKAVSDQLY KLRGITKVEG HIEDQLISVE GSVLLGAAVS
     ILETFADRVE RQDENQDREV RGLARMVQVN SERTLVDLTI RGVAPGTYRA TIREYGDLKG
     GVTSTGRVWS GGEKEAKGFL GRIEVGKDGR GAAFVDHAFQ VWEIIGHAMV LTKQDEGTHP
     LQNDENTVVG VVARSAGMWD NDKTVCSCTG KTLWEERKDE VKKGLL
//