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Database: UniProt
Entry: E6RAP5_CRYGW
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Original site: E6RAP5_CRYGW 
ID   E6RAP5_CRYGW            Unreviewed;       225 AA.
AC   E6RAP5;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   16-JAN-2019, entry version 41.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   OrderedLocusNames=CGB_H2330C {ECO:0000313|EMBL:ADV23928.1};
OS   Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS   (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Tremellomycetes; Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV23928.1, ECO:0000313|Proteomes:UP000007805};
RN   [1] {ECO:0000313|EMBL:ADV23928.1, ECO:0000313|Proteomes:UP000007805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T.,
RA   Sawkins J., McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q.,
RA   Bartlett K., Li W., Wang X., Heitman J., Stajich J.E., Fraser J.A.,
RA   Meyer W., Carter D., Schein J., Krzywinski M., Kwon-Chung K.J.,
RA   Varma A., Wang J., Brunham R., Fyfe M., Ouellette B.F., Siddiqui A.,
RA   Marra M., Jones S., Holt R., Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WM276;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T.,
RA   Sawkins J., McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q.,
RA   Bartlett K., Li W., Wang X., Heitman J., Stajich J.E., Fraser J.A.,
RA   Meyer W., Carter D., Schein J., Krzywinski M., Kwong-Chung K.J.,
RA   Varma A., Wang J., Brunham R., Fyfe M., Ouellette B.F.F., Siddiqui A.,
RA   Marra M., Jones S., Holt R., Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 0:0-0(2011).
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; CP000293; ADV23928.1; -; Genomic_DNA.
DR   RefSeq; XP_003195715.1; XM_003195667.1.
DR   STRING; 367775.XP_003195715.1; -.
DR   EnsemblFungi; ADV23928; ADV23928; CGB_H2330C.
DR   GeneID; 10189489; -.
DR   KEGG; cgi:CGB_H2330C; -.
DR   EuPathDB; FungiDB:CGB_H2330C; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   Proteomes; UP000007805; 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:UP000007805};
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:UP000007805}.
FT   DOMAIN       28    109       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      123    220       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        53     53       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       101    101       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       187    187       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       191    191       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   225 AA;  24792 MW;  C9EF40B9F1340623 CRC64;
     MITAITRTAL PRTTLRTSLA TMSTIRAKHT LPPLPYAYDA LEPSISSEIM NLHHTKHHQT
     YVNGLNAAEE SLQKAAAAGD VKAAIALQPA LKFNGGGHIN HSLFWKNLAP TGSAQVKVPT
     SGVFHDHVEA DFGGFKNLKK EMNAKTAAIQ GSGWGWLGYN KDTKKLEIVT TPNQDPLLSH
     VPIIGIDIWE HAFYLQYKNV KPDYLNAIWD VINYEEAESR LKAAL
//
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