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Database: UniProt
Entry: A8I2E0_CHLRE
LinkDB: A8I2E0_CHLRE
Original site: A8I2E0_CHLRE 
ID   A8I2E0_CHLRE            Unreviewed;       218 AA.
AC   A8I2E0;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   13-FEB-2019, entry version 80.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=MSD1 {ECO:0000313|EMBL:EDP07754.1};
GN   ORFNames=CHLRE_02g096150v5 {ECO:0000313|EMBL:PNW86799.1},
GN   CHLREDRAFT_53941 {ECO:0000313|EMBL:EDP07754.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
OC   Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1] {ECO:0000313|EMBL:EDP07754.1, ECO:0000313|Proteomes:UP000006906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}, and CC-503 cw92 mt+
RC   {ECO:0000313|EMBL:EDP07754.1};
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K.,
RA   Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R.,
RA   Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P.,
RA   Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J.,
RA   Cardol P., Cerutti H., Chanfreau G., Chen C.L., Cognat V., Croft M.T.,
RA   Dent R., Dutcher S., Fernandez E., Fukuzawa H., Gonzalez-Ballester D.,
RA   Gonzalez-Halphen D., Hallmann A., Hanikenne M., Hippler M., Inwood W.,
RA   Jabbari K., Kalanon M., Kuras R., Lefebvre P.A., Lemaire S.D.,
RA   Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L., Mittag M.,
RA   Mittelmeier T., Moroney J.V., Moseley J., Napoli C., Nedelcu A.M.,
RA   Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G., Purton S.,
RA   Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L., Schroda M.,
RA   Stern D., Umen J., Willows R., Wilson N., Zimmer S.L., Allmer J.,
RA   Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P.,
RA   Jorgensen R., Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T.,
RA   Brokstein P., Dubchak I., Goodstein D., Hornick L., Huang Y.W.,
RA   Jhaveri J., Luo Y., Martinez D., Ngau W.C., Otillar B., Poliakov A.,
RA   Porter A., Szajkowski L., Werner G., Zhou K., Grigoriev I.V.,
RA   Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and
RT   plant functions.";
RL   Science 318:245-250(2007).
RN   [2] {ECO:0000313|EMBL:ACV41090.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Dangeard C-9 {ECO:0000313|EMBL:ACV41090.1};
RA   Page D.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ACV41090.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Dangeard C-9 {ECO:0000313|EMBL:ACV41090.1};
RX   PubMed=22685165; DOI=10.1105/tpc.112.098962;
RA   Page M.D., Allen M.D., Kropat J., Urzica E.I., Karpowicz S.J.,
RA   Hsieh S.I., Loo J.A., Merchant S.S.;
RT   "Fe Sparing and Fe Recycling Contribute to Increased Superoxide
RT   Dismutase Capacity in Iron-Starved Chlamydomonas reinhardtii.";
RL   Plant Cell 24:2649-2665(2012).
RN   [4] {ECO:0000313|EMBL:PNW86799.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CC-503 cw92 mt+ {ECO:0000313|EMBL:PNW86799.1};
RG   Chlamydomonas Annotation Team;
RG   JGI Annotation Team;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K.,
RA   Marechal-Drouard L., Marshall W.F., Qu L.H., Nelson D.R.,
RA   Sanderfoot A.A., Spalding M.H., Kapitonov V.V., Ren Q., Ferris P.,
RA   Lindquist E., Shapiro H., Lucas S.M., Grimwood J., Schmutz J.,
RA   Grigoriev I.V., Rokhsar D.S.;
RT   "WGS assembly of Chlamydomonas reinhardtii.";
RL   Submitted (JUL-2017) 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; GQ413965; ACV41090.1; -; mRNA.
DR   EMBL; DS496112; EDP07754.1; -; Genomic_DNA.
DR   EMBL; CM008963; PNW86799.1; -; Genomic_DNA.
DR   RefSeq; XP_001700058.1; XM_001700006.1.
DR   UniGene; Cre.13231; -.
DR   STRING; 3055.EDP07754; -.
DR   EnsemblPlants; PNW86799; PNW86799; CHLRE_02g096150v5.
DR   GeneID; 5725400; -.
DR   Gramene; PNW86799; PNW86799; CHLRE_02g096150v5.
DR   KEGG; cre:CHLREDRAFT_53941; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; WKVMTNP; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000006906; Chromosome 2.
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   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006906};
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:UP000006906}.
FT   DOMAIN        4     91       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      100    206       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        84     84       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       174    174       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       178    178       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   218 AA;  23900 MW;  728CF66B4130BF09 CRC64;
     MAQALPPLPY DYGSLEPHVD ATTMNIHHTK HHQTYVNNLN AALDKFPELK DLGLVDLNKA
     VGTDKLPKDV ATVIRNNGGG HYNHSFFWKV MTNPSNTNGP NGDVKAAIEA SFGSVDEMKA
     KFNAAAAGRF GSGWAWLSVK PDGSLSIDST PNQDNPLMTA LPDVAGGIPL LGLDVWEHAY
     YLKYQNRRPE YIAAWWNVVN WEQVAENYKA AQAGTVPL
//
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