GenomeNet

Database: UniProt
Entry: D8SF57_SELML
LinkDB: D8SF57_SELML
Original site: D8SF57_SELML 
ID   D8SF57_SELML            Unreviewed;       208 AA.
AC   D8SF57;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   16-JAN-2019, entry version 41.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=SELMODRAFT_115358 {ECO:0000313|EMBL:EFJ17097.1};
OS   Selaginella moellendorffii (Spikemoss).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX   NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN   [1] {ECO:0000313|EMBL:EFJ17097.1, ECO:0000313|Proteomes:UP000001514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551031; DOI=10.1126/science.1203810;
RA   Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA   dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A.,
RA   Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L.,
RA   Bonawitz N.D., Chapple C., Cheng C., Correa L.G., Dacre M.,
RA   DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L.,
RA   Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L.,
RA   Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y.,
RA   Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U.,
RA   Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E.,
RA   Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S.,
RA   Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M.,
RA   Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA   Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA   Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA   Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA   Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P.,
RA   Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L.,
RA   Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R.,
RA   Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S.,
RA   Rokhsar D., Grigoriev I.V.;
RT   "The Selaginella genome identifies genetic changes associated with the
RT   evolution of vascular plants.";
RL   Science 332:960-963(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}.
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; GL377616; EFJ17097.1; -; Genomic_DNA.
DR   RefSeq; XP_002982004.1; XM_002981958.1.
DR   ProteinModelPortal; D8SF57; -.
DR   STRING; 88036.EFJ17097; -.
DR   EnsemblPlants; EFJ17097; EFJ17097; SELMODRAFT_115358.
DR   GeneID; 9634234; -.
DR   Gramene; EFJ17097; EFJ17097; SELMODRAFT_115358.
DR   KEGG; smo:SELMODRAFT_115358; -.
DR   eggNOG; KOG0876; Eukaryota.
DR   eggNOG; COG0605; LUCA.
DR   InParanoid; D8SF57; -.
DR   KO; K04564; -.
DR   OMA; YSKHHAT; -.
DR   OrthoDB; 1353361at2759; -.
DR   Proteomes; UP000001514; 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:UP000001514};
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:UP000001514}.
FT   DOMAIN        7     91       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       99    200       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        32     32       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        84     84       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       170    170       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   208 AA;  23335 MW;  EF478745D06AD050 CRC64;
     MSAVVAKFEL PPLPYEMNAL EPFMSKTTLE FHWGKHQRAY IDNLNKQISG TELESLKLED
     IITKTYGGGN AQPAFNNAAQ AWNHDFFFHS MTAKGGKAPS GDISGLINRD LGSYDNFVKE
     FKAAATTQFG SGWAWLSLKD GKLIVQKTAN AVNPLVSGET PLLVLDVWEH AYYLDFQNRR
     PDYVETFLRE LVNWDTVNAR LETATAKL
//
DBGET integrated database retrieval system