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Database: UniProt
Entry: A0A0C1UVT6_9CYAN
LinkDB: A0A0C1UVT6_9CYAN
Original site: A0A0C1UVT6_9CYAN 
ID   A0A0C1UVT6_9CYAN        Unreviewed;       241 AA.
AC   A0A0C1UVT6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-DEC-2018, entry version 17.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=PI95_16740 {ECO:0000313|EMBL:KIF35837.1};
OS   Hassallia byssoidea VB512170.
OC   Bacteria; Cyanobacteria; Nostocales; Tolypothrichaceae; Hassallia.
OX   NCBI_TaxID=1304833 {ECO:0000313|EMBL:KIF35837.1, ECO:0000313|Proteomes:UP000031549};
RN   [1] {ECO:0000313|EMBL:KIF35837.1, ECO:0000313|Proteomes:UP000031549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB512170 {ECO:0000313|EMBL:KIF35837.1,
RC   ECO:0000313|Proteomes:UP000031549};
RA   Singh D., Malar M.C., Panda A., Sen D., Das A., Bhattacharyya S.,
RA   Adhikary S.P., Tripathy S.;
RT   "The genome sequences of Hassallia byssoidea.";
RL   Submitted (NOV-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KIF35837.1}.
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DR   EMBL; JTCM01000018; KIF35837.1; -; Genomic_DNA.
DR   EnsemblBacteria; KIF35837; KIF35837; PI95_16740.
DR   Proteomes; UP000031549; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000031549};
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:UP000031549};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    241       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002140518.
FT   DOMAIN       43    130       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN      138    237       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        67     67       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       122    122       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       204    204       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       208    208       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   241 AA;  26932 MW;  C45780688EF9E89B CRC64;
     MTIDRRHFLF LLAASVGAFA LDSHASAEKA PISQATPTGN TVYSVPPLPY AYDALEPHID
     QATMQFHHDK HHAAYVKNLN AALDKHPELK SKTVEEMLRN LNSVPADIRK MVRNNGGGHV
     NHSMFWQIMK PLGGGEATGA IASAINQSFG SFAAFKKQFN EAGASRFGSG WVWLVRNNGK
     LEITTTANQD SPLSEGKYPI MGNDVWEHAY YLKYQNRRAD YLDAWWNVLN WDEINKRFAA
     A
//
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