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Database: UniProt
Entry: A0A0C3S166_PHLGI
LinkDB: A0A0C3S166_PHLGI
Original site: A0A0C3S166_PHLGI 
ID   A0A0C3S166_PHLGI        Unreviewed;       206 AA.
AC   A0A0C3S166;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=PHLGIDRAFT_95407 {ECO:0000313|EMBL:KIP02927.1};
OS   Phlebiopsis gigantea 11061_1 CR5-6.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Polyporales; Phanerochaetaceae; Phlebiopsis.
OX   NCBI_TaxID=745531 {ECO:0000313|EMBL:KIP02927.1, ECO:0000313|Proteomes:UP000053257};
RN   [1] {ECO:0000313|EMBL:KIP02927.1, ECO:0000313|Proteomes:UP000053257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11061_1 CR5-6 {ECO:0000313|EMBL:KIP02927.1,
RC   ECO:0000313|Proteomes:UP000053257};
RX   PubMed=25474575;
RA   Hori C., Ishida T., Igarashi K., Samejima M., Suzuki H., Master E.,
RA   Ferreira P., Ruiz-Duenas F.J., Held B., Canessa P., Larrondo L.F.,
RA   Schmoll M., Druzhinina I.S., Kubicek C.P., Gaskell J.A., Kersten P.,
RA   St John F., Glasner J., Sabat G., Splinter BonDurant S., Syed K.,
RA   Yadav J., Mgbeahuruike A.C., Kovalchuk A., Asiegbu F.O., Lackner G.,
RA   Hoffmeister D., Rencoret J., Gutierrez A., Sun H., Lindquist E.,
RA   Barry K., Riley R., Grigoriev I.V., Henrissat B., Kues U., Berka R.M.,
RA   Martinez A.T., Covert S.F., Blanchette R.A., Cullen D.;
RT   "Analysis of the Phlebiopsis gigantea genome, transcriptome and
RT   secretome provides insight into its pioneer colonization strategies of
RT   wood.";
RL   PLoS Genet. 10:E1004759-E1004759(2014).
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; KN840644; KIP02927.1; -; Genomic_DNA.
DR   EnsemblFungi; KIP02927; KIP02927; PHLGIDRAFT_95407.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000053257; 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:UP000053257};
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:UP000053257}.
FT   DOMAIN        4     82       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        29     29       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       163    163       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   206 AA;  22735 MW;  DFC5407BB043FB7F CRC64;
     MSGQHTLPDL PYAYDGLEPF ISRQIMELHH KKHHQTYVNA LNAAEQAYAK TSTPKERIAL
     QAALKFNGGG HINHSLFWKN LAPSASEGKG NGGALQEGPL KKAILESFGS FDNFKKEFNT
     TTAGIQGSGW GWVGVNPSNG RLEITTTANQ DPLLTHVPVI GVDIWEHAFY LQYLNVKVDY
     LNAIWNVINF DEAEKRYLEA AGGAKL
//
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