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Database: UniProt
Entry: A0A0D7ARG7_9AGAR
LinkDB: A0A0D7ARG7_9AGAR
Original site: A0A0D7ARG7_9AGAR 
ID   A0A0D7ARG7_9AGAR        Unreviewed;       204 AA.
AC   A0A0D7ARG7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   28-MAR-2018, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=FISHEDRAFT_68497 {ECO:0000313|EMBL:KIY53931.1};
OS   Fistulina hepatica ATCC 64428.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Fistulinaceae;
OC   Fistulina.
OX   NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY53931.1, ECO:0000313|Proteomes:UP000054144};
RN   [1] {ECO:0000313|EMBL:KIY53931.1, ECO:0000313|Proteomes:UP000054144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY53931.1,
RC   ECO:0000313|Proteomes:UP000054144};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H.,
RA   Haridas S., LaButti K., Ohm R.A., Kues U., Blanchette R.A.,
RA   Grigoriev I.V., Minto R.E., Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by
RT   the genome sequences of Fistulina hepatica and Cylindrobasidium
RT   torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {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; KN881583; KIY53931.1; -; Genomic_DNA.
DR   EnsemblFungi; KIY53931; KIY53931; FISHEDRAFT_68497.
DR   Proteomes; UP000054144; 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:UP000054144};
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:UP000054144}.
FT   DOMAIN        3     80       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       96    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        72     72       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   204 AA;  22351 MW;  C1AC7C434E38F557 CRC64;
     MAHVLPNLPY GYDALEPYIS RQIMELHHKK HHQTYVNALN AAEASYAAAS TPKERIALQA
     ALKFNGGGHI NHSLFWKNMA PPASEGKGNG GVLKDGPLKI AIESTFGSLD SMTSKFNTIT
     AGIQGSGWGW LGYNPATKTL EIVTTANQDP LLSHVPIIGV DIWEHAFYLQ YLNVKADYLK
     AIWSVINFEE AEKRYLEAGG SAKL
//
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