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Database: UniProt/TrEMBL
Entry: A0A0D6AJ93_9CHRO
LinkDB: A0A0D6AJ93_9CHRO
Original site: A0A0D6AJ93_9CHRO 
ID   A0A0D6AJ93_9CHRO        Unreviewed;       201 AA.
AC   A0A0D6AJ93;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   25-OCT-2017, entry version 13.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=GM3708_3299 {ECO:0000313|EMBL:BAQ62893.1};
OS   Geminocystis sp. NIES-3708.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Chroococcaceae; Geminocystis.
OX   NCBI_TaxID=1615909 {ECO:0000313|EMBL:BAQ62893.1, ECO:0000313|Proteomes:UP000060542};
RN   [1] {ECO:0000313|EMBL:BAQ62893.1, ECO:0000313|Proteomes:UP000060542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3708 {ECO:0000313|EMBL:BAQ62893.1,
RC   ECO:0000313|Proteomes:UP000060542};
RA   Hirose Y.;
RT   "Geminocystis sp. NIES-3708 complete genome sequence.";
RL   Submitted (MAR-2015) 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; AP014815; BAQ62893.1; -; Genomic_DNA.
DR   RefSeq; WP_066349009.1; NZ_AP014815.1.
DR   EnsemblBacteria; BAQ62893; BAQ62893; GM3708_3299.
DR   KEGG; gee:GM3708_3299; -.
DR   PATRIC; fig|1615909.3.peg.3354; -.
DR   KO; K04564; -.
DR   Proteomes; UP000060542; 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   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:UP000060542};
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:UP000060542}.
FT   DOMAIN        2     86       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       94    194       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        79     79       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       161    161       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       165    165       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   201 AA;  22166 MW;  9BB15C58D492EA3E CRC64;
     MAYQLPTLPF DYTALEPCIS KSTLEFHHDK HHAAYVNNFN NAVAGTDLDS KSLEEVIKIT
     ATNPSQAGIF NNAAQAWNHS FYWQSIKPNG GGTPSGALAD KIDADFGSFD KFVEAFKTAG
     ATQFGSGWAW LVLDNGTLKV TKTGNADNPL TAGQIPLLTM DVWEHAYYLD YQNKRPDYIS
     DFLSKLVNWD FVAENFAKAT A
//
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