ID   B3S214_TRIAD            Unreviewed;       251 AA.
AC   B3S214;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Superoxide dismutase copper chaperone {ECO:0000256|ARBA:ARBA00032899};
GN   ORFNames=TRIADDRAFT_58413 {ECO:0000313|EMBL:EDV23287.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV23287.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV23287.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV23287.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
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; DS985247; EDV23287.1; -; Genomic_DNA.
DR   RefSeq; XP_002114197.1; XM_002114161.1.
DR   AlphaFoldDB; B3S214; -.
DR   STRING; 10228.B3S214; -.
DR   EnsemblMetazoa; TriadT58413; TriadP58413; TriadG58413.
DR   GeneID; 6755725; -.
DR   KEGG; tad:TRIADDRAFT_58413; -.
DR   CTD; 6755725; -.
DR   eggNOG; KOG4656; Eukaryota.
DR   HOGENOM; CLU_056632_0_2_1; -.
DR   InParanoid; B3S214; -.
DR   OMA; KNVWEER; -.
DR   OrthoDB; 1693333at2759; -.
DR   PhylomeDB; B3S214; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IBA:GO_Central.
DR   GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   DOMAIN          4..67
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   251 AA;  27063 MW;  FAC50D2DD0BCC6C8 CRC64;
     MATPTRMEFA VHMTCNTCVD KVKDALNGVE GIDNYMISLA EEQVIIDSAL PMAQLHNLLV
     TTGLTVIMRG QGAATEGASH LGAAVSILSG TSVKGLVRFT QLSADKCMIE GTVDNLRPGN
     YDIKIHEYGD LSDGCNNCGD IFNPYEYPHG NNNTSARKLG DIGSMTANKN GRAMFRIEDD
     TVKVWDVIGR SVIIHDKQVE SSGKSLASRI TCGIIARSAG LFENSKKFCA CDGKTLWEDK
     PLTNKSPQAS L
//