GenomeNet

Database: UniProt
Entry: W4K516_9HOMO
LinkDB: W4K516_9HOMO
Original site: W4K516_9HOMO 
ID   W4K516_9HOMO            Unreviewed;       220 AA.
AC   W4K516;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   28-MAR-2018, entry version 19.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=mnsod3 {ECO:0000313|EMBL:ETW80141.1};
GN   ORFNames=HETIRDRAFT_171368 {ECO:0000313|EMBL:ETW80141.1};
OS   Heterobasidion irregulare TC 32-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Russulales; Bondarzewiaceae; Heterobasidion;
OC   Heterobasidion annosum species complex.
OX   NCBI_TaxID=747525 {ECO:0000313|EMBL:ETW80141.1, ECO:0000313|Proteomes:UP000030671};
RN   [1] {ECO:0000313|EMBL:ETW80141.1, ECO:0000313|Proteomes:UP000030671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC 32-1 {ECO:0000313|EMBL:ETW80141.1,
RC   ECO:0000313|Proteomes:UP000030671};
RX   PubMed=22463738; DOI=10.1111/j.1469-8137.2012.04128.x;
RA   Olson A., Aerts A., Asiegbu F., Belbahri L., Bouzid O., Broberg A.,
RA   Canback B., Coutinho P.M., Cullen D., Dalman K., Deflorio G.,
RA   van Diepen L.T., Dunand C., Duplessis S., Durling M., Gonthier P.,
RA   Grimwood J., Fossdal C.G., Hansson D., Henrissat B., Hietala A.,
RA   Himmelstrand K., Hoffmeister D., Hogberg N., James T.Y., Karlsson M.,
RA   Kohler A., Kues U., Lee Y.H., Lin Y.C., Lind M., Lindquist E.,
RA   Lombard V., Lucas S., Lunden K., Morin E., Murat C., Park J.,
RA   Raffaello T., Rouze P., Salamov A., Schmutz J., Solheim H.,
RA   Stahlberg J., Velez H., de Vries R.P., Wiebenga A., Woodward S.,
RA   Yakovlev I., Garbelotto M., Martin F., Grigoriev I.V., Stenlid J.;
RT   "Insight into trade-off between wood decay and parasitism from the
RT   genome of a fungal forest pathogen.";
RL   New Phytol. 194:1001-1013(2012).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; KI925460; ETW80141.1; -; Genomic_DNA.
DR   RefSeq; XP_009548658.1; XM_009550363.1.
DR   EnsemblFungi; ETW80141; ETW80141; HETIRDRAFT_171368.
DR   GeneID; 20668334; -.
DR   KEGG; hir:HETIRDRAFT_171368; -.
DR   KO; K04564; -.
DR   Proteomes; UP000030671; 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:UP000030671};
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:UP000030671}.
FT   DOMAIN       27    104       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      116    214       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        51     51       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        96     96       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       181    181       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       185    185       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   220 AA;  24255 MW;  7AD5D0318C3962B5 CRC64;
     MFAIARTIAR PALARTFAAP AGAASLHTLP QLPYAYNALE PHISEQIMTL HHTKHHQTYV
     NGLNAAEEAY SKTHDTKQRI ALQSALKFNG GGHINHSLFW KNLAPASEGG GKLADGPLKS
     ALERDFGSVD EFKKKFNTST AAIQGSGWGW LGLNPTTKKL EIVTTANQDP LISHTPIIGV
     DIWEHAFYLQ YKNVKPDYLN AIWNVINFKE AESRLVEASQ
//
DBGET integrated database retrieval system