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Database: UniProt/TrEMBL
Entry: L1K0M1_GUITH
LinkDB: L1K0M1_GUITH
Original site: L1K0M1_GUITH 
ID   L1K0M1_GUITH            Unreviewed;       229 AA.
AC   L1K0M1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-2017, entry version 28.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=GUITHDRAFT_91782 {ECO:0000313|EMBL:EKX54109.1};
OS   Guillardia theta CCMP2712.
OC   Eukaryota; Cryptophyta; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX54109.1, ECO:0000313|Proteomes:UP000011087};
RN   [1] {ECO:0000313|EMBL:EKX54109.1, ECO:0000313|EnsemblProtists:EKX54109, ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX54109.1,
RC   ECO:0000313|Proteomes:UP000011087};
RX   PubMed=23201678; DOI=10.1038/nature11681;
RG   DOE Joint Genome Institute;
RA   Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA   Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA   Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA   Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA   Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G.,
RA   Roy S.W., Sarai C., Schaack S., Shirato S., Slamovits C.H.,
RA   Spencer D.F., Suzuki S., Worden A.Z., Zauner S., Barry K., Bell C.,
RA   Bharti A.K., Crow J.A., Grimwood J., Kramer R., Lindquist E.,
RA   Lucas S., Salamov A., McFadden G.I., Lane C.E., Keeling P.J.,
RA   Gray M.W., Grigoriev I.V., Archibald J.M.;
RT   "Algal genomes reveal evolutionary mosaicism and the fate of
RT   nucleomorphs.";
RL   Nature 492:59-65(2012).
RN   [2] {ECO:0000313|EnsemblProtists:EKX54109, ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|EnsemblProtists:EKX54109,
RC   ECO:0000313|Proteomes:UP000011087};
RA   Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA   Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y.,
RA   Hopkins J.F., Rensing S.A., Schmutz J., Symeonidi A., Elias M.,
RA   Eveleigh R.J., Herman E.K., Klute M.J., Nakayama T., Obornik M.,
RA   Reyes-Prieto A., Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P.,
RA   Dacks J.B., Durnford D.G., Fast N.M., Green B.R., Grisdale C.,
RA   Hempe F., Henrissat B., Hoppner M.P., Ishida K.-I., Kim E., Koreny L.,
RA   Kroth P.G., Liu Y., Malik S.-B., Maier U.G., McRose D., Mock T.,
RA   Neilson J.A., Onodera N.T., Poole A.M., Pritham E.J., Richards T.A.,
RA   Rocap G., Roy S.W., Sarai C., Schaack S., Shirato S., Slamovits C.H.,
RA   Spencer D.F., Suzuki S., Worden A.Z., Zauner S., Barry K., Bell C.,
RA   Bharti A.K., Crow J.A., Grimwood J., Kramer R., Lindquist E.,
RA   Lucas S., Salamov A., McFadden G.I., Lane C.E., Keeling P.J.,
RA   Gray M.W., Grigoriev I.V., Archibald J.M.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblProtists:EKX54109}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (MAR-2016) to UniProtKB.
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}.
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DR   EMBL; JH992968; EKX54109.1; -; Genomic_DNA.
DR   RefSeq; XP_005841089.1; XM_005841032.1.
DR   EnsemblProtists; EKX54109; EKX54109; GUITHDRAFT_91782.
DR   GeneID; 17310885; -.
DR   KEGG; gtt:GUITHDRAFT_91782; -.
DR   KO; K04564; -.
DR   OMA; DSPLMHG; -.
DR   Proteomes; UP000011087; 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   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:UP000011087};
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:UP000011087}.
FT   DOMAIN       30    108       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      123    222       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        53     53       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       101    101       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       189    189       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       193    193       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   229 AA;  25378 MW;  7F4642D5C3E55FAC CRC64;
     MFRQGNKLST SISRLSTLAS RAAGVRAKST LPSLPYDFGA LEPVVNSEIM TLHHGKHHAT
     YVNNLNAALE KMSDAMAKQD YATMIALQGA IQFNGGGHLN HSIFWQNLCP VKDVVAPSEA
     NPELAKAIEG QWGSLDNFKT EFNTKTAAIQ GSGWGWLGYN KQSKKLEIAT CANQDPLVMK
     GLVPLLGIDV WEHAYYLQYK NARPEYLKQI WQVVNWKDVA ARYEAAKKA
//
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