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Database: UniProt/TrEMBL
Entry: K9RMB8_9CYAN
LinkDB: K9RMB8_9CYAN
Original site: K9RMB8_9CYAN 
ID   K9RMB8_9CYAN            Unreviewed;       243 AA.
AC   K9RMB8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 25.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=Riv7116_6286 {ECO:0000313|EMBL:AFY58633.1};
OS   Rivularia sp. PCC 7116.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Rivularia.
OX   NCBI_TaxID=373994 {ECO:0000313|EMBL:AFY58633.1, ECO:0000313|Proteomes:UP000010380};
RN   [1] {ECO:0000313|EMBL:AFY58633.1, ECO:0000313|Proteomes:UP000010380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7116 {ECO:0000313|EMBL:AFY58633.1,
RC   ECO:0000313|Proteomes:UP000010380};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A.,
RA   Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X.,
RA   Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Rivularia sp. PCC 7116.";
RL   Submitted (AUG-2012) 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: 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; CP003549; AFY58633.1; -; Genomic_DNA.
DR   RefSeq; WP_015122182.1; NC_019678.1.
DR   EnsemblBacteria; AFY58633; AFY58633; Riv7116_6286.
DR   KEGG; riv:Riv7116_6286; -.
DR   PATRIC; fig|373994.3.peg.6700; -.
DR   KO; K04564; -.
DR   OrthoDB; POG091H03Q7; -.
DR   BioCyc; RSP373994:GLJQ-6071-MONOMER; -.
DR   Proteomes; UP000010380; Chromosome.
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   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:UP000010380};
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:UP000010380}.
FT   DOMAIN       41    127       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      134    235       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        64     64       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       119    119       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       202    202       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       206    206       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   243 AA;  27446 MW;  0E8FB617B10648CD CRC64;
     MTLKRRHFLY LLGVGVSTFA LESCALADNQ KVAQSGSGDI KLPPLPYDYN GLEPHIDAKT
     MKFHHDKHHA GYVKNLNAAL GKYPKLKQQS VEELLGNLDS VPQDIRNTIR NNGGGHVNHS
     MFWEIMKPDG GGEPTGAIAN AIKDNFGSFS EMKNQFNQAG AKRFGSGWAW LVFNKDGKLE
     VMSTANQDSP FSQGKYPVMG NDVWEHAYYL NYQNRRKDYL EAWWNTINWD EVNTRFDAAK
     KFA
//
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