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Database: UniProt/TrEMBL
Entry: A0A0T7BSI2_9CYAN
LinkDB: A0A0T7BSI2_9CYAN
Original site: A0A0T7BSI2_9CYAN 
ID   A0A0T7BSI2_9CYAN        Unreviewed;       199 AA.
AC   A0A0T7BSI2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=IJ00_12990 {ECO:0000313|EMBL:AKG22048.1};
OS   Calothrix sp. 336/3.
OC   Bacteria; Cyanobacteria; Nostocales; Rivulariaceae; Calothrix.
OX   NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG22048.1, ECO:0000313|Proteomes:UP000065745};
RN   [1] {ECO:0000313|EMBL:AKG22048.1, ECO:0000313|Proteomes:UP000065745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=336/3 {ECO:0000313|EMBL:AKG22048.1,
RC   ECO:0000313|Proteomes:UP000065745};
RX   PubMed=25614574;
RA   Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA   Battchikova N.;
RT   "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT   cyanobacterium isolated from a finnish lake.";
RL   Genome Announc. 3:0-0(2015).
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; CP011382; AKG22048.1; -; Genomic_DNA.
DR   RefSeq; WP_035153660.1; NZ_CP011382.1.
DR   EnsemblBacteria; AKG22048; AKG22048; IJ00_12990.
DR   KEGG; calh:IJ00_12990; -.
DR   KO; K04564; -.
DR   Proteomes; UP000065745; 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:UP000065745};
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:UP000065745}.
FT   DOMAIN        3     88       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       95    196       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        28     28       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        80     80       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       162    162       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       166    166       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   199 AA;  22285 MW;  1D8212CA25B693D3 CRC64;
     MAFTQPPLPF AMDALEPYGM KAETFEYHYG KHHKAYVDNL NKLTEGKDLA DKSLEEVITI
     AFKDASLTGI FNNAAQVWNH TFFWSCLKPA GGGAPTGDLA ARIDKDFGSF DKFKEDFSTA
     AATQFGSGWA WLVDDNGTLK ITKTPNAENP LVHGQKPLLT LDVWEHAYYV DFRNARPAFI
     KNFLDNLVNW DFVAERLAA
//
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