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Database: UniProt
Entry: A0A1F8A5Y1_9EURO
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Original site: A0A1F8A5Y1_9EURO 
ID   A0A1F8A5Y1_9EURO        Unreviewed;       191 AA.
AC   A0A1F8A5Y1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Cytosolic Cu/Zn superoxide dismutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ABOM_005022 {ECO:0000313|EMBL:OGM46799.1};
OS   Aspergillus bombycis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM46799.1, ECO:0000313|Proteomes:UP000179179};
RN   [1] {ECO:0000313|EMBL:OGM46799.1, ECO:0000313|Proteomes:UP000179179}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX   PubMed=27664179;
RA   Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT   "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT   bombycis.";
RL   Genome Biol. Evol. 0:0-0(2016).
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:OGM46799.1}.
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DR   EMBL; LYCR01000028; OGM46799.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8A5Y1; -.
DR   STRING; 109264.A0A1F8A5Y1; -.
DR   OrthoDB; 3040041at2759; -.
DR   Proteomes; UP000179179; 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; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   PANTHER; PTHR10003:SF37; CELL SURFACE SUPEROXIDE DISMUTASE [CU-ZN] 4; 1.
DR   PANTHER; PTHR10003; SUPEROXIDE DISMUTASE CU-ZN -RELATED; 1.
DR   SUPFAM; SSF49329; Cu,Zn superoxide dismutase-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..191
FT                   /note="Cytosolic Cu/Zn superoxide dismutase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009534572"
SQ   SEQUENCE   191 AA;  20518 MW;  BB7EFC3C8297B14A CRC64;
     MYLRSIIAAT LATSVIAQTQ DAPEITASFK EHVYEAKLPK NPFFEKGSLV GNIDGSIRAQ
     SAADGKGVDF TVSFSNLPEE GGPFLYHIHN AAVPSDGNCT ATLSHLDPFN RGEKPPCNPS
     AAQTCQIGDL SGKHGKVTQD PFEEEYNDPF VSLSANDEQF IGNKSIVLHF GNRTRITCAN
     FVKEGVADTG L
//
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