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Database: UniProt
Entry: B7FPQ3_PHATC
LinkDB: B7FPQ3_PHATC
Original site: B7FPQ3_PHATC 
ID   B7FPQ3_PHATC            Unreviewed;       226 AA.
AC   B7FPQ3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   16-JAN-2019, entry version 44.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=SOD2 {ECO:0000313|EMBL:EEC51716.1};
GN   ORFNames=PHATRDRAFT_42832 {ECO:0000313|EMBL:EEC51716.1};
OS   Phaeodactylum tricornutum (strain CCAP 1055/1).
OC   Eukaryota; Stramenopiles; Bacillariophyta; Bacillariophyceae;
OC   Bacillariophycidae; Naviculales; Phaeodactylaceae; Phaeodactylum.
OX   NCBI_TaxID=556484 {ECO:0000313|Proteomes:UP000000759};
RN   [1] {ECO:0000313|EMBL:EEC51716.1, ECO:0000313|Proteomes:UP000000759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC51716.1,
RC   ECO:0000313|Proteomes:UP000000759};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E.,
RA   Salamov A., Vandepoele K., Beszteri B., Gruber A., Heijde M.,
RA   Katinka M., Mock T., Valentin K., Verret F., Berges J.A., Brownlee C.,
RA   Cadoret J.P., Chiovitti A., Choi C.J., Coesel S., De Martino A.,
RA   Detter J.C., Durkin C., Falciatore A., Fournet J., Haruta M.,
RA   Huysman M.J., Jenkins B.D., Jiroutova K., Jorgensen R.E., Joubert Y.,
RA   Kaplan A., Kroger N., Kroth P.G., La Roche J., Lindquist E.,
RA   Lommer M., Martin-Jezequel V., Lopez P.J., Lucas S., Mangogna M.,
RA   McGinnis K., Medlin L.K., Montsant A., Oudot-Le Secq M.P., Napoli C.,
RA   Obornik M., Parker M.S., Petit J.L., Porcel B.M., Poulsen N.,
RA   Robison M., Rychlewski L., Rynearson T.A., Schmutz J., Shapiro H.,
RA   Siaut M., Stanley M., Sussman M.R., Taylor A.R., Vardi A.,
RA   von Dassow P., Vyverman W., Willis A., Wyrwicz L.S., Rokhsar D.S.,
RA   Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
RN   [2] {ECO:0000313|EMBL:EEC51716.1, ECO:0000313|Proteomes:UP000000759}
RP   GENOME REANNOTATION.
RC   STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC51716.1,
RC   ECO:0000313|Proteomes:UP000000759};
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A.,
RA   Detter J.C., Lindquist E., Shapiro H., Lucas S., Glavina del Rio T.,
RA   Pitluck S., Rokhsar D., Bowler C.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CM000605; EEC51716.1; -; Genomic_DNA.
DR   RefSeq; XP_002177253.1; XM_002177217.1.
DR   UniGene; Ptc.3632; -.
DR   ProteinModelPortal; B7FPQ3; -.
DR   STRING; 2850.Phatr42832; -.
DR   PRIDE; B7FPQ3; -.
DR   EnsemblProtists; Phatr3_J42832.t1; Phatr3_J42832.p1; Phatr3_J42832.
DR   GeneID; 7196432; -.
DR   KEGG; pti:PHATRDRAFT_42832; -.
DR   HOGENOM; HOG000013583; -.
DR   InParanoid; B7FPQ3; -.
DR   KO; K04564; -.
DR   OMA; YEHAYFI; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000000759; Chromosome 1.
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:UP000000759};
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:UP000000759}.
FT   DOMAIN       43    121       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      121    221       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        68     68       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       116    116       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       188    188       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       192    192       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   226 AA;  24778 MW;  0C6BC265970545E2 CRC64;
     MSGSKIIVDS ALRAAVNLRS SKIPTELAKS SAALFSAYGG AKKHELPTLT YDYASLEPAI
     SAETMELHHS KHHNTYVTNL NVTLEKMDSA LTSSDISALI GLQGALKFNG GGHLNHTLFW
     DLESAIKESF GDFEKLKTEM SAKTVAVQGS GWGWLGYNKS TGRLEIATCA NQDPLEATTG
     LAPLLGIDVW EHAYYVDYRN VRPDYVKNIW DIINWDTVAQ RLSATK
//
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