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Database: UniProt
Entry: A0A0C3HUC2_9PEZI
LinkDB: A0A0C3HUC2_9PEZI
Original site: A0A0C3HUC2_9PEZI 
ID   A0A0C3HUC2_9PEZI        Unreviewed;       216 AA.
AC   A0A0C3HUC2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 16.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=OIDMADRAFT_17030 {ECO:0000313|EMBL:KIN05852.1};
OS   Oidiodendron maius Zn.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Myxotrichaceae; Oidiodendron.
OX   NCBI_TaxID=913774 {ECO:0000313|EMBL:KIN05852.1, ECO:0000313|Proteomes:UP000054321};
RN   [1] {ECO:0000313|EMBL:KIN05852.1, ECO:0000313|Proteomes:UP000054321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zn {ECO:0000313|EMBL:KIN05852.1,
RC   ECO:0000313|Proteomes:UP000054321};
RG   DOE Joint Genome Institute;
RA   Kuo A., Martino E., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA   Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zn {ECO:0000313|Proteomes:UP000054321};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (JAN-2015) 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|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|RuleBase:RU000414};
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
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DR   EMBL; KN832871; KIN05852.1; -; Genomic_DNA.
DR   EnsemblFungi; KIN05852; KIN05852; OIDMADRAFT_17030.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000054321; 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; -; 1.
DR   Gene3D; 2.40.500.20; -; 1.
DR   InterPro; IPR001189; Mn/Fe_SOD.
DR   InterPro; IPR019833; Mn/Fe_SOD_BS.
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   Pfam; PF02777; Sod_Fe_C; 1.
DR   Pfam; PF00081; Sod_Fe_N; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   PRINTS; PR01703; MNSODISMTASE.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
DR   PROSITE; PS00088; SOD_MN; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054321};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054321}.
FT   DOMAIN        4     84       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       98    197       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        29     29       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        77     77       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       164    164       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   216 AA;  23966 MW;  4C2A7527E773DAB7 CRC64;
     MATKYTLPPL PYGYDALEPV ISAQIMTIHH TKHHQTYINT LNNALASQAV ATDKNDIVSQ
     IHLQNTINFS AGGHINHTLF WENLVPASSP SAQTHVASKL MAAISARWGS LEKFQEKFNA
     VLLGLKGSGW GWLVQDTESG NLEIVTTKDQ DIVPAGKKPL LGIDMWEHAY YLQYLNDKGS
     YAKKIWNVIN WKKVEERFVG GSDSVFGTLA GLRSNM
//
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