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Database: UniProt
Entry: A0A1D2VKE0_9ASCO
LinkDB: A0A1D2VKE0_9ASCO
Original site: A0A1D2VKE0_9ASCO 
ID   A0A1D2VKE0_9ASCO        Unreviewed;       207 AA.
AC   A0A1D2VKE0;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   16-JAN-2019, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ASCRUDRAFT_33283 {ECO:0000313|EMBL:ODV62069.1};
OS   Ascoidea rubescens DSM 1968.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Ascoideaceae; Ascoidea.
OX   NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV62069.1, ECO:0000313|Proteomes:UP000095038};
RN   [1] {ECO:0000313|Proteomes:UP000095038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
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}.
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DR   EMBL; KV454478; ODV62069.1; -; Genomic_DNA.
DR   RefSeq; XP_020048376.1; XM_020190413.1.
DR   EnsemblFungi; ODV62069; ODV62069; ASCRUDRAFT_33283.
DR   GeneID; 30964049; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000095038; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; 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:0001324; P:age-dependent response to oxidative stress involved in chronological 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:UP000095038};
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:UP000095038}.
FT   DOMAIN       10     89       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      106    204       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        33     33       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        81     81       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       171    171       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       175    175       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   207 AA;  23808 MW;  8D99867519D0E47D CRC64;
     MPSLVRTKVT LPDLEWDFGD LEPYISGQIN EIHYTKHHQT YVNGYNQAIE QHAEAKAKGD
     VKATIELQQN IKFHGGGFTN HCLFWKNLSP SSKKGGNYHD LDQNSDFYKQ VVTNYGSFDN
     LINVTNNKLA GIQGSGWAFI VKNKENNSID VVQTYNQDTV LNNLTPLVAI DAWEHAYYLQ
     YRNQKVDYFK AIWNVINWNE AAKRYAQ
//
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