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Database: UniProt
Entry: A0A439CXT7_9PEZI
LinkDB: A0A439CXT7_9PEZI
Original site: A0A439CXT7_9PEZI 
ID   A0A439CXT7_9PEZI        Unreviewed;        96 AA.
AC   A0A439CXT7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=superoxide dismutase {ECO:0000256|ARBA:ARBA00012682};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682};
DE   Flags: Fragment;
GN   ORFNames=EKO27_g8100 {ECO:0000313|EMBL:RWA07015.1};
OS   Xylaria grammica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX   NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA07015.1, ECO:0000313|Proteomes:UP000286045};
RN   [1] {ECO:0000313|EMBL:RWA07015.1, ECO:0000313|Proteomes:UP000286045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHI A82 {ECO:0000313|EMBL:RWA07015.1,
RC   ECO:0000313|Proteomes:UP000286045};
RA   Buettner E., Kellner H.;
RT   "Draft genome sequence of Xylaria grammica IHI A82.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714}.
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:RWA07015.1}.
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DR   EMBL; RYZI01000289; RWA07015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A439CXT7; -.
DR   STRING; 363999.A0A439CXT7; -.
DR   Proteomes; UP000286045; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR11404:SF29; SUPEROXIDE DISMUTASE; 1.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286045}.
FT   DOMAIN          1..80
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RWA07015.1"
SQ   SEQUENCE   96 AA;  10687 MW;  A474C7AA71D5602F CRC64;
     FGAALLGIQG SGWGWLVKEA GTGQLRIVTL ANQEAVVVGD TPLVGVDMWE HAYYLQYLNG
     KAAYVDNIWK VINWKTAEAR YTESREDVFK VLKANI
//
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