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Database: UniProt
Entry: A0A084G072_9PEZI
LinkDB: A0A084G072_9PEZI
Original site: A0A084G072_9PEZI 
ID   A0A084G072_9PEZI        Unreviewed;       231 AA.
AC   A0A084G072;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   20-JUN-2018, entry version 17.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SAPIO_CDS8679 {ECO:0000313|EMBL:KEZ40734.1};
OS   Scedosporium apiospermum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
OC   Scedosporium.
OX   NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ40734.1, ECO:0000313|Proteomes:UP000028545};
RN   [1] {ECO:0000313|Proteomes:UP000028545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHEM 14462 {ECO:0000313|Proteomes:UP000028545};
RA   Vandeputte P., Rechenmann M., Bouchara J.-P.;
RL   Submitted (JUN-2014) 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: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000414}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000256|RuleBase:RU000414}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KEZ40734.1}.
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DR   EMBL; JOWA01000121; KEZ40734.1; -; Genomic_DNA.
DR   RefSeq; XP_016640533.1; XM_016790270.1.
DR   EnsemblFungi; KEZ40734; KEZ40734; SAPIO_CDS8679.
DR   GeneID; 27727751; -.
DR   Proteomes; UP000028545; 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:UP000028545};
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:UP000028545}.
FT   DOMAIN       38    117       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      127    228       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        61     61       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       109    109       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       195    195       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       199    199       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   231 AA;  25154 MW;  7D8BDB079F6BC861 CRC64;
     MSFSLLRTTP ALRAALRAGA ARPVAALSGT SFARGQATLP DLPYDYNALE PYISAKIMEL
     HHSKHHQTYV NGFNTALQAI AEAESKGDLT KAAAQAPLIN FHGGGHVNHS LFWENLAPSS
     RDGGGEPSGA LRSAIDEDFG SFDALRKEIN AALTGIQGSG WAWLVKDKTT GTLSVVTRAN
     QDPVTGNLAP LLGIDAWEHA YYLQYENRKA EYFDAIWNVL NWKTVAQRFE K
//
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