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Database: UniProt
Entry: S9W6E7_SCHCR
LinkDB: S9W6E7_SCHCR
Original site: S9W6E7_SCHCR 
ID   S9W6E7_SCHCR            Unreviewed;       220 AA.
AC   S9W6E7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   16-JAN-2019, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SPOG_03925 {ECO:0000313|EMBL:EPY53400.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS
OS   11777 / NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY53400.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY53400.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K.,
RA   Guo Y., Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K.,
RA   Bayne E.H., Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L.,
RA   FitzGerald M.G., French C., Gujja S., Hansen K., Keifenheim D.,
RA   Levin J.Z., Mosher R.A., Mueller C.A., Pfiffner J., Priest M.,
RA   Russ C., Smialowska A., Swoboda P., Sykes S.M., Vaughn M.,
RA   Vengrova S., Yoder R., Zeng Q., Allshire R., Baulcombe D.,
RA   Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J., Levin H.,
RA   Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(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; KE546988; EPY53400.1; -; Genomic_DNA.
DR   RefSeq; XP_013021643.1; XM_013166189.1.
DR   EnsemblFungi; EPY53400; EPY53400; SPOG_03925.
DR   GeneID; 25038242; -.
DR   OMA; KWGSFDK; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0030145; F:manganese ion binding; IEA:EnsemblFungi.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001320; P:age-dependent response to reactive oxygen species involved in chronological cell aging; IEA:EnsemblFungi.
DR   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
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:UP000015464};
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:UP000015464}.
FT   DOMAIN       29    106       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      119    216       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        52     52       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        98     98       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       183    183       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       187    187       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   220 AA;  24751 MW;  AB68AB57862EF0A6 CRC64;
     MLRFASKNAT LFARNLTVSG ARQLHGKASL PPLPYAYNAL EPAISETIMK LHHDKHHNTY
     VTNLNAAQDK LCQPDLDLKS EIALQAAIKF NGGGHINHSQ FWTIMAPPSE GGGKPITDSS
     LHKSIVEKWG SLEDFQKEMN GALAAIQGSG WAWLVKDKEG SLHITSTQNQ DTVINAKVII
     GIDAWEHAYY PQYENRKAEY FKAFWTVMNW KEAQRRYETN
//
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