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Database: UniProt
Entry: A0A229Z0H6_9EURO
LinkDB: A0A229Z0H6_9EURO
Original site: A0A229Z0H6_9EURO 
ID   A0A229Z0H6_9EURO        Unreviewed;       229 AA.
AC   A0A229Z0H6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   28-MAR-2018, entry version 5.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=CDV55_04167 {ECO:0000313|EMBL:OXN38156.1}, CFD26_05494
GN   {ECO:0000313|EMBL:OXN18153.1};
OS   Aspergillus turcosus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1245748 {ECO:0000313|EMBL:OXN38156.1, ECO:0000313|Proteomes:UP000215394};
RN   [1] {ECO:0000313|EMBL:OXN38156.1, ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR AF 1038 {ECO:0000313|EMBL:OXN18153.1}, and HMR AF 23
RC   {ECO:0000313|EMBL:OXN38156.1};
RA   Dufresne P.J., Fournier E., Martineau C., De Repentigny L.,
RA   Dufresne S.F.;
RT   "Draft genome of two Aspergillus turcosus strains, one azole-
RT   susceptible and the other azole-resistant, isolated from
RT   bronchoalveolarlavage fluid.";
RL   Submitted (OCT-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: 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:OXN38156.1}.
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DR   EMBL; NIDN01000067; OXN18153.1; -; Genomic_DNA.
DR   EMBL; NKHV01000033; OXN38156.1; -; Genomic_DNA.
DR   Proteomes; UP000215289; Unassembled WGS sequence.
DR   Proteomes; UP000215394; Unassembled WGS sequence.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000215289,
KW   ECO:0000313|Proteomes:UP000215394};
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:UP000215289}.
FT   DOMAIN       36    115       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      125    226       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   COILED       64     91       {ECO:0000256|SAM:Coils}.
FT   METAL        59     59       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       107    107       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       193    193       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       197    197       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   229 AA;  25183 MW;  143A5F043041B839 CRC64;
     MAASLIRTSA RTALRSGASA TPRAAASLTF ARGKATLPDL SYDYGALEPS ISGKIMELHH
     KNHHQTYVNS YNQAIEQLQE AQAKNDIASQ IALKPLINFH GGGHLNHTLF WENLAPKNSG
     GGEPPSGALA KAIDEAYGSL ENFQGKMNTA LAGIQGSGWA WLVRDKETGH IGIKTYANQD
     PVVGQFQPLL GIDAWEHAYY LQYQNRKAEY FKAIWEVINW KCVEKRFSA
//
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