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Database: UniProt/TrEMBL
Entry: A0A0K2JT26_9GAMM
LinkDB: A0A0K2JT26_9GAMM
Original site: A0A0K2JT26_9GAMM 
ID   A0A0K2JT26_9GAMM        Unreviewed;       192 AA.
AC   A0A0K2JT26;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   ORFNames=ACH24_06695 {ECO:0000313|EMBL:ALB02242.1}, FSC845_02770
GN   {ECO:0000313|EMBL:ANH77509.1};
OS   Francisella persica ATCC VR-331.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=1086726 {ECO:0000313|EMBL:ALB02242.1};
RN   [1] {ECO:0000313|EMBL:ANH77509.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC VR-331 {ECO:0000313|EMBL:ANH77509.1};
RA   Sjodin A., Larsson P., Backman S., Macellaro A., Nilsson E.,
RA   Karlsson E., Bystrom M., Ohrman C., Stenberg P., Forsman M.;
RT   "Wolbacha persica: a misclassified Francisella.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALB02242.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FSC845 {ECO:0000313|EMBL:ALB02242.1};
RX   PubMed=26747442; DOI=10.1099/ijsem.0.000855;
RA   Larson M.A., Nalbantoglu U., Sayood K., Zentz E.B., Cer R.Z.,
RA   Iwen P.C., Francesconi S.C., Bishop-Lilly K.A., Mokashi V.P.,
RA   Sjostedt A., Hinrichs S.H.;
RT   "Reclassification of Wolbachia persica as Francisella persica comb.
RT   nov. and emended description of the family Francisellaceae.";
RL   Int. J. Syst. Evol. Microbiol. 66:1200-1205(2016).
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; CP012505; ALB02242.1; -; Genomic_DNA.
DR   EMBL; CP013022; ANH77509.1; -; Genomic_DNA.
DR   RefSeq; WP_064461678.1; NZ_CP013022.1.
DR   KEGG; fper:ACH24_06695; -.
DR   PATRIC; fig|1086726.6.peg.1685; -.
DR   KO; K04564; -.
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   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1,
KW   ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414}.
FT   DOMAIN        2     81       Sod_Fe_N. {ECO:0000259|Pfam:PF00081}.
FT   DOMAIN       90    188       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        27     27       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL        74     74       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       156    156       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       160    160       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
SQ   SEQUENCE   192 AA;  21932 MW;  FAC2D04118C979B0 CRC64;
     MKFELPKLPY NVDALEPTIS KETIEYHYGK HHQTYVNNLN NLVEGTEHAG RNLEEIIKNS
     SGGIFNNAAQ VFNHTFYWNC LTPNKTEASS QLKAALIEAC GSVENFKEQF SKAAISIFGS
     GWAWLVKNTD SKLEIVTTSN AGCPLTENKK PLLTFDVWEH AYYIDYRNAR PKYVEALWDI
     VNWEFVSEQF AN
//
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