GenomeNet

Database: UniProt
Entry: A0A1E4SP47_9ASCO
LinkDB: A0A1E4SP47_9ASCO
Original site: A0A1E4SP47_9ASCO 
ID   A0A1E4SP47_9ASCO        Unreviewed;       204 AA.
AC   A0A1E4SP47;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   16-JAN-2019, entry version 11.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=CANTADRAFT_5249 {ECO:0000313|EMBL:ODV81301.1};
OS   Suhomyces tanzawaensis NRRL Y-17324.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Suhomyces.
OX   NCBI_TaxID=984487 {ECO:0000313|EMBL:ODV81301.1, ECO:0000313|Proteomes:UP000094285};
RN   [1] {ECO:0000313|Proteomes:UP000094285}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-17324 {ECO:0000313|Proteomes:UP000094285};
RG   DOE Joint Genome Institute;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T.,
RA   Goker M., Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K.,
RA   Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K., Lapidus A., Lindquist E.,
RA   Lipzen A., Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Submitted (MAY-2016) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; KV453910; ODV81301.1; -; Genomic_DNA.
DR   RefSeq; XP_020066423.1; XM_020210091.1.
DR   EnsemblFungi; ODV81301; ODV81301; CANTADRAFT_5249.
DR   GeneID; 30984227; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000094285; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UP000094285};
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:UP000094285}.
FT   DOMAIN        7     85       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      101    200       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        30     30       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        78     78       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       167    167       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       171    171       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   204 AA;  22499 MW;  DAC24E333D5BAD91 CRC64;
     MSHTPIELPK LDWAYDALEP HISGEINRIH HSKHHQVYVN GFNAAITALS AAEAKGDVKG
     AVAIQQNIKF HGGGHTNHSL FWKTLAPVSQ GGGVHPSEDS PLGKQIVKQY GSVAKLIELT
     NAKLAGIQGS GWAFIVKNKE NGGTLDVVTT FNQDTVLEPY VPLIAIDAWE HAYYLQYQNV
     KADYFKAIWN VISWKEAEKR FASN
//
DBGET integrated database retrieval system