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Database: UniProt
Entry: F8QCM7_SERL3
LinkDB: F8QCM7_SERL3
Original site: F8QCM7_SERL3 
ID   F8QCM7_SERL3            Unreviewed;       204 AA.
AC   F8QCM7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   16-JAN-2019, entry version 23.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SERLA73DRAFT_189008 {ECO:0000313|EMBL:EGN93892.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Coniophorineae;
OC   Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M.,
RA   Blumentritt M., Coutinho P.M., Cullen D., de Vries R.P., Gathman A.,
RA   Goodell B., Henrissat B., Ihrmark K., Kauserud H., Kohler A.,
RA   LaButti K., Lapidus A., Lavin J.L., Lee Y.-H., Lindquist E., Lilly W.,
RA   Lucas S., Morin E., Murat C., Oguiza J.A., Park J., Pisabarro A.G.,
RA   Riley R., Rosling A., Salamov A., Schmidt O., Schmutz J., Skrede I.,
RA   Stenlid J., Wiebenga A., Xie X., Kuees U., Hibbett D.S.,
RA   Hoffmeister D., Hoegberg N., Martin F., Grigoriev I.V.,
RA   Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
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; GL945490; EGN93892.1; -; Genomic_DNA.
DR   ProteinModelPortal; F8QCM7; -.
DR   EnsemblFungi; EGN93892; EGN93892; SERLA73DRAFT_189008.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000008063; 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:UP000008063};
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:UP000008063}.
FT   DOMAIN        3     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       97    195       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        73     73       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   204 AA;  22627 MW;  F3154117EEC86FE6 CRC64;
     MSQHTLPDLP YAYDALEPFI SRQIMELHHK KHHQTYVTAL NAAEANYVKT STPKERIALQ
     AAIKFNGGGH INHSLFWKNL APAASEGKGN GGALKDGPLK KAIDEAFGSL DALKKEFNAT
     TAAIQGSGWG WLGLNPKTKR LEITTTANQD PLLTHVPIIG VDIWEHAFYL QYLNVKVDYL
     NAIWSVINFD EAEKRYTDGL SSKL
//
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