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Database: UniProt
Entry: F4RQ23_MELLP
LinkDB: F4RQ23_MELLP
Original site: F4RQ23_MELLP 
ID   F4RQ23_MELLP            Unreviewed;       233 AA.
AC   F4RQ23;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   16-JAN-2019, entry version 30.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=MELLADRAFT_107563 {ECO:0000313|EMBL:EGG05331.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar
OS   leaf rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J.,
RA   Cantarel B.L., Chiu R., Coutinho P.M., Feau N., Field M., Frey P.,
RA   Gelhaye E., Goldberg J., Grabherr M.G., Kodira C.D., Kohler A.,
RA   Kuees U., Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E.,
RA   Murat C., Pangilinan J.L., Park R., Pearson M., Quesneville H.,
RA   Rouhier N., Sakthikumar S., Salamov A.A., Schmutz J., Selles B.,
RA   Shapiro H., Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y.,
RA   Rouze P., Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(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; GL883113; EGG05331.1; -; Genomic_DNA.
DR   RefSeq; XP_007411253.1; XM_007411191.1.
DR   ProteinModelPortal; F4RQ23; -.
DR   EnsemblFungi; EGG05331; EGG05331; MELLADRAFT_107563.
DR   GeneID; 18923208; -.
DR   KEGG; mlr:MELLADRAFT_107563; -.
DR   EuPathDB; FungiDB:MELLADRAFT_107563; -.
DR   InParanoid; F4RQ23; -.
DR   KO; K04564; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000001072; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001072};
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:UP000001072};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25    233       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5005676712.
FT   DOMAIN       39    117       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      132    229       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        62     62       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       110    110       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       196    196       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       200    200       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   233 AA;  25298 MW;  B209F696CEFA9482 CRC64;
     MFNSGVAKLF SLALVLGTPN LAGANPVAPR SLVDQKNVTL PPLTYAYNAL EPAISAKIME
     LHHSKHHQAL VTGLNNALAS YSAAVQAGDL PKQIEIQGLI KFNGGGHINH SLYWKNLQPV
     NLGGGKMKPG VFADAVQAQF GGLDGLKTKM NAVGNTFQGS GWLWLAREKS GKALSIVTTA
     NQDPLVGPLI PIIGIDMWEH SWYLQHYNVR ATYLTDIWNV INFDEAETRY KAI
//
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