GenomeNet

Database: UniProt
Entry: A0A1G4KE43_9SACH
LinkDB: A0A1G4KE43_9SACH
Original site: A0A1G4KE43_9SACH 
ID   A0A1G4KE43_9SACH        Unreviewed;       237 AA.
AC   A0A1G4KE43;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   16-JAN-2019, entry version 12.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=LAMI_0H02960G {ECO:0000313|EMBL:SCV02784.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV02784.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|EMBL:SCV02784.1, ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ploux O.;
RL   Submitted (MAR-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; LT598468; SCV02784.1; -; Genomic_DNA.
DR   EnsemblFungi; SCV02784; SCV02784; LAMI_0H02960G.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000191024; Chromosome h.
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:UP000191024};
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:UP000191024}.
FT   DOMAIN       34    122       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      132    234       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        57     57       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       114    114       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       201    201       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       205    205       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   237 AA;  26360 MW;  89C31DCD8A545195 CRC64;
     MLALKGLQRV STRGSMGLSP KMGISMMSTR TKVTLPDLDW DFGDLEPHIS GKINELHYTK
     HHQTYVNGFN AATEQLGELE CKLTGDTQQD VPVTTKIVAL QKNLNFHGGG FTNHCLFWKN
     LAPSSQGGGE LPSGKFADQI KDQFGSLEEL QKLTNAKLAG IQGSGWAFIV KNLDNGGAID
     VVQTYNQDTV TGPLRPLVAI DAWEHAYYLQ YQNRKADYFK AIWNVINWKE AARRFDA
//
DBGET integrated database retrieval system