ID   Q22H00_TETTS            Unreviewed;       166 AA.
AC   Q22H00;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   ORFNames=TTHERM_00655520 {ECO:0000313|EMBL:EAR84524.1};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR84524.1, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
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. {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. {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
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DR   EMBL; GG662502; EAR84524.1; -; Genomic_DNA.
DR   RefSeq; XP_001032187.1; XM_001032187.3.
DR   AlphaFoldDB; Q22H00; -.
DR   SMR; Q22H00; -.
DR   STRING; 312017.Q22H00; -.
DR   EnsemblProtists; EAR84524; EAR84524; TTHERM_00655520.
DR   GeneID; 7823633; -.
DR   KEGG; tet:TTHERM_00655520; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   HOGENOM; CLU_056632_4_1_1; -.
DR   InParanoid; Q22H00; -.
DR   OMA; DNYSDNP; -.
DR   OrthoDB; 3470597at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Superoxide dismutase, copper/zinc binding domain; 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:SF103; SUPEROXIDE DISMUTASE [CU-ZN]; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   3: Inferred from homology;
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:UP000009168};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN          21..157
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
SQ   SEQUENCE   166 AA;  17900 MW;  742B4B90762A8AB6 CRC64;
     MAQHAPVYAI CLLKNETNTV SAVVRLVEKF ENNKFVTHLK ATFKGLPAGL HGFHVHQYGD
     LSNGCATAGP HFNPFNKQHG GPNDENRHVG DLGNVTAVDG QDTNFEFQSD LIRLSGENTI
     VGRSFVIHAD EDDLGKGNFE DSKTTGHAGA RLACGIIALA APFENF
//