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Database: UniProt
Entry: I3WTR7_CARAU
LinkDB: I3WTR7_CARAU
Original site: I3WTR7_CARAU 
ID   I3WTR7_CARAU            Unreviewed;        78 AA.
AC   I3WTR7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
DE   Flags: Fragment;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957 {ECO:0000313|EMBL:AFL46334.1};
RN   [1] {ECO:0000313|EMBL:AFL46334.1}
RP   NUCLEOTIDE SEQUENCE.
RA   An L., Zheng B.;
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00003917}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00010457}.
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DR   EMBL; JQ776518; AFL46334.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3WTR7; -.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProt.
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; 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.
PE   3: Inferred from homology;
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139}.
FT   DOMAIN          1..78
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFL46334.1"
FT   NON_TER         78
FT                   /evidence="ECO:0000313|EMBL:AFL46334.1"
SQ   SEQUENCE   78 AA;  8294 MW;  D59D8D2D1C930C5B CRC64;
     YGDNTNGCTS AGPHYNPHNQ THGGPTDSVR HVGDLGNVIA DKDGVAEIDI VDKMVTLFGE
     YSVIGRTMVI HEKADDLG
//
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