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Database: UniProt
Entry: H6C6T6_EXODN
LinkDB: H6C6T6_EXODN
Original site: H6C6T6_EXODN 
ID   H6C6T6_EXODN            Unreviewed;       220 AA.
AC   H6C6T6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   16-JAN-2019, entry version 26.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=HMPREF1120_07422 {ECO:0000313|EMBL:EHY59432.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656)
OS   (Black yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY59432.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|Proteomes:UP000007304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34100 / CBS 525.76 / NIH/UT8656
RC   {ECO:0000313|Proteomes:UP000007304};
RX   PubMed=24496724; DOI=10.1534/g3.113.009241;
RA   Chen Z., Martinez D.A., Gujja S., Sykes S.M., Zeng Q., Szaniszlo P.J.,
RA   Wang Z., Cuomo C.A.;
RT   "Comparative genomic and transcriptomic analysis of Wangiella
RT   dermatitidis, a major cause of phaeohyphomycosis and a model black
RT   yeast human pathogen.";
RL   G3 (Bethesda) 0:0-0(2014).
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; JH226135; EHY59432.1; -; Genomic_DNA.
DR   RefSeq; XP_009159893.1; XM_009161645.1.
DR   ProteinModelPortal; H6C6T6; -.
DR   EnsemblFungi; EHY59432; EHY59432; HMPREF1120_07422.
DR   GeneID; 20312061; -.
DR   InParanoid; H6C6T6; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000007304; 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   Complete proteome {ECO:0000313|Proteomes:UP000007304};
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:UP000007304}.
FT   DOMAIN        5     86       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      100    201       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       168    168       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       172    172       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   220 AA;  24615 MW;  93F437710500D3A9 CRC64;
     MSVEKYELPR LPYALDALEP AISGQIMDLH YNKHHQTYIT NLNNALAAQA EAFQSKNLLK
     QIELQPAIRF NAGGHINHTL FWQSLSPASS GDSNIQAVAG SLHSAIVKKW GSFDNFKAKF
     EATALAIQGS GWAWLVKDTE NSGTQLEITT SKDQDLPPGG KQIVLGVDMW EHAYYLQYYN
     NKKEYVSKIW SVINWKVAEK RFQGDAKTIY GELIGLASKL
//
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