ID   E2LI04_MONPE            Unreviewed;       172 AA.
AC   E2LI04;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|ARBA:ARBA00012682, ECO:0000256|RuleBase:RU000414};
DE   Flags: Fragment;
GN   ORFNames=MPER_06163 {ECO:0000313|EMBL:EEB94947.1};
OS   Moniliophthora perniciosa (strain FA553 / isolate CP02) (Witches'-broom
OS   disease fungus) (Marasmius perniciosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=554373 {ECO:0000313|EMBL:EEB94947.1, ECO:0000313|Proteomes:UP000000741};
RN   [1] {ECO:0000313|EMBL:EEB94947.1, ECO:0000313|Proteomes:UP000000741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FA553 / isolate CP02 {ECO:0000313|Proteomes:UP000000741};
RX   PubMed=19019209; DOI=10.1186/1471-2164-9-548;
RA   Mondego J.M., Carazzolle M.F., Costa G.G., Formighieri E.F., Parizzi L.P.,
RA   Rincones J., Cotomacci C., Carraro D.M., Cunha A.F., Carrer H., Vidal R.O.,
RA   Estrela R.C., Garcia O., Thomazella D.P., de Oliveira B.V., Pires A.B.,
RA   Rio M.C., Araujo M.R., de Moraes M.H., Castro L.A., Gramacho K.P.,
RA   Goncalves M.S., Neto J.P., Neto A.G., Barbosa L.V., Guiltinan M.J.,
RA   Bailey B.A., Meinhardt L.W., Cascardo J.C., Pereira G.A.;
RT   "A genome survey of Moniliophthora perniciosa gives new insights into
RT   Witches' broom disease of cacao.";
RL   BMC Genomics 9:548-548(2008).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000414}.
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         ECO:0000256|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC       {ECO:0000256|ARBA:ARBA00008714, ECO:0000256|RuleBase:RU000414}.
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:EEB94947.1}.
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; ABRE01010424; EEB94947.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2LI04; -.
DR   STRING; 554373.E2LI04; -.
DR   KEGG; mpr:MPER_06163; -.
DR   HOGENOM; CLU_031625_2_0_1; -.
DR   InParanoid; E2LI04; -.
DR   OMA; GSYEGWK; -.
DR   OrthoDB; 4839at2759; -.
DR   Proteomes; UP000000741; 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; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR   Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   PANTHER; PTHR11404; SUPEROXIDE DISMUTASE 2; 1.
DR   PANTHER; PTHR11404:SF6; SUPEROXIDE DISMUTASE [MN], MITOCHONDRIAL; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR   SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000741}.
FT   DOMAIN          27..104
FT                   /note="Manganese/iron superoxide dismutase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00081"
FT   DOMAIN          115..170
FT                   /note="Manganese/iron superoxide dismutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02777"
FT   BINDING         51
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   BINDING         96
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000349-1"
FT   NON_TER         172
FT                   /evidence="ECO:0000313|EMBL:EEB94947.1"
SQ   SEQUENCE   172 AA;  18827 MW;  4CBEB64691EA8997 CRC64;
     MFALTRNALR PAFARTFAAP STAASLHTLP ELPYAYNDLE PHISEEIMKL HHQKHHQTYV
     NGLNAAEESY AKAPSTKDKI ALQAALKFNG GGHINHSLFW KNLAPANSDG GKLADGPLKQ
     AIERDFGSVE DFKKSFNAKT AAIQGSGWGW LGYNSTTKKL EIVTTPNQDP LL
//