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Database: UniProt/SWISS-PROT
Entry: SODC_ASPFU
LinkDB: SODC_ASPFU
Original site: SODC_ASPFU 
ID   SODC_ASPFU              Reviewed;         154 AA.
AC   Q9Y8D9; Q4WUP9; Q8X1S8;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-APR-2018, entry version 116.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=sodC; ORFNames=AFUA_5G09240;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10655345;
RA   Holdom M.D., Lechenne B., Hay R.J., Hamilton A.J., Monod M.;
RT   "Production and characterization of recombinant Aspergillus fumigatus
RT   Cu,Zn superoxide dismutase and its recognition by immune human sera.";
RL   J. Clin. Microbiol. 38:558-562(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Holdom M.D., Hobby P., Lechenne B., Zaugg C., Sutton B., Monod M.,
RA   Hamilton A.J.;
RT   "Homogeneity in 3-dimensional structure of Cu,Zn superoxide dismutases
RT   of Aspergillus fumigatus, Aspergillus flavus and Aspergillus
RT   nidulans.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
RA   Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
RA   Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
RA   Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL91677.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF128886; AAD42060.1; -; mRNA.
DR   EMBL; AF281057; AAL38991.1; -; Genomic_DNA.
DR   EMBL; AAHF01000003; EAL91677.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_753715.1; XM_748622.1.
DR   ProteinModelPortal; Q9Y8D9; -.
DR   SMR; Q9Y8D9; -.
DR   STRING; 5085.CADAFUBP00005560; -.
DR   PRIDE; Q9Y8D9; -.
DR   GeneID; 3511006; -.
DR   KEGG; afm:AFUA_5G09240; -.
DR   EuPathDB; FungiDB:Afu5g09240; -.
DR   HOGENOM; HOG000263447; -.
DR   InParanoid; Q9Y8D9; -.
DR   KO; K04565; -.
DR   OrthoDB; EOG092C578I; -.
DR   BRENDA; 1.15.1.1; 508.
DR   Proteomes; UP000002530; Chromosome 5.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005622; C:intracellular; IDA:AspGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant; Complete proteome; Copper; Cytoplasm; Disulfide bond;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164108.
FT   METAL        47     47       Copper. {ECO:0000250}.
FT   METAL        49     49       Copper. {ECO:0000250}.
FT   METAL        64     64       Copper. {ECO:0000250}.
FT   METAL        64     64       Zinc. {ECO:0000250}.
FT   METAL        72     72       Zinc. {ECO:0000250}.
FT   METAL        81     81       Zinc. {ECO:0000250}.
FT   METAL        84     84       Zinc. {ECO:0000250}.
FT   METAL       121    121       Copper. {ECO:0000250}.
FT   DISULFID     58    147       {ECO:0000250}.
FT   CONFLICT      8      8       Missing (in Ref. 2; AAL38991).
FT                                {ECO:0000305}.
SQ   SEQUENCE   154 AA;  15967 MW;  FB2FC504140DDED6 CRC64;
     MVKAVAVLRG DSKITGTVTF EQADENSPTT VSWNIKGNDP NAKRGFHVHQ FGDNTNGCTS
     AGPHFNPYGK THGAPEDSER HVGDLGNFET DAEGNAVGSK QDKLIKLIGA ESVLGRTLVV
     HAGTDDLGRG GNEESKKTGN AGARPACGVI GIAA
//
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