ID   O61685_SCAAL            Unreviewed;        94 AA.
AC   O61685;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
DE   Flags: Fragment;
GN   Name=Sod {ECO:0000313|EMBL:AAC39004.1};
OS   Scaptomyza albovittata (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Scaptomyza.
OX   NCBI_TaxID=7299 {ECO:0000313|EMBL:AAC39004.1};
RN   [1] {ECO:0000313|EMBL:AAC39004.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9562982; DOI=10.1006/mpev.1997.0484;
RA   Remsen J., DeSalle R.;
RT   "Character congruence of multiple data partitions and the origin of the
RT   Hawaiian Drosophilidae.";
RL   Mol. Phylogenet. Evol. 9:225-235(1998).
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|ARBA:ARBA00001605};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF059884; AAC39004.1; -; Genomic_DNA.
DR   AlphaFoldDB; O61685; -.
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.
PE   4: Predicted;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          2..94
FT                   /note="Superoxide dismutase copper/zinc binding"
FT                   /evidence="ECO:0000259|Pfam:PF00080"
FT   REGION          31..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAC39004.1"
FT   NON_TER         94
FT                   /evidence="ECO:0000313|EMBL:AAC39004.1"
SQ   SEQUENCE   94 AA;  9770 MW;  F56BD1CAB4B1B26F CRC64;
     PVKVSGEVTG LAKGLHGFHV HEFGDNTNGC MSSGPHFNPH NKEHGAPTDA DRHLGDLGNI
     TASGDGPTQV DICDSKITLF GCNSIIGRTV VVHA
//