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Database: UniProt/SWISS-PROT
Entry: SODM_NEUCR
LinkDB: SODM_NEUCR
Original site: SODM_NEUCR 
ID   SODM_NEUCR              Reviewed;         245 AA.
AC   Q9Y783; Q7RVD9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   05-DEC-2018, entry version 125.
DE   RecName: Full=Superoxide dismutase [Mn], mitochondrial;
DE            EC=1.15.1.1;
DE   Flags: Precursor;
GN   Name=sod-2; ORFNames=18F11.030, NCU01213;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Dvorachek W.H. Jr., Natvig D.O.;
RT   "Characterization of sod-2, the Neurospora crassa gene for manganese
RT   superoxide dismutase.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA   Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC       produced within the cells and which are toxic to biological
CC       systems.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase
CC       family. {ECO:0000305}.
DR   EMBL; AF118809; AAD28503.1; -; Genomic_DNA.
DR   EMBL; AL670011; CAD21408.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA32343.3; -; Genomic_DNA.
DR   RefSeq; XP_961579.3; XM_956486.3.
DR   ProteinModelPortal; Q9Y783; -.
DR   SMR; Q9Y783; -.
DR   EnsemblFungi; EAA32343; EAA32343; NCU01213.
DR   GeneID; 3877711; -.
DR   KEGG; ncr:NCU01213; -.
DR   EuPathDB; FungiDB:NCU01213; -.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; Q9Y783; -.
DR   KO; K04564; -.
DR   OrthoDB; EOG092C4NQ6; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR   GO; GO:0004784; F:superoxide dismutase activity; IBA:GO_Central.
DR   GO; GO:0007568; P:aging; IBA:GO_Central.
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; Manganese; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT       1     32       Mitochondrion. {ECO:0000255}.
FT   CHAIN        33    245       Superoxide dismutase [Mn], mitochondrial.
FT                                /FTId=PRO_0000032885.
FT   METAL        58     58       Manganese. {ECO:0000250}.
FT   METAL       106    106       Manganese. {ECO:0000250}.
FT   METAL       196    196       Manganese. {ECO:0000250}.
FT   METAL       200    200       Manganese. {ECO:0000250}.
SQ   SEQUENCE   245 AA;  27020 MW;  FF288947FB7676AD CRC64;
     MVNLGSIWQN LLASQAPLQS MTGNATTMAG LATYSLPQLP YAYNALEPYI SAQIMELHHS
     KHHQTYVTNL NNALKVHVAA IASSDIPAQI AQQPAIKFNG GGHINHSLFW KNLAPAETPE
     TNYSKAAPSL AAEIEKTWGS FDEFKKAFSA ALLGIQGSGW GWLVKESTAE KGRLRIITTK
     DQDPVVGGEV PVFGVDMWEH AYYLQYLNGK AAYVENIWKV INWKTAEERF QGSREDAFAD
     LKALL
//
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