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Database: UniProt/TrEMBL
Entry: F8L0F2_PARAV
LinkDB: F8L0F2_PARAV
Original site: F8L0F2_PARAV 
ID   F8L0F2_PARAV            Unreviewed;       225 AA.
AC   F8L0F2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   11-MAY-2016, entry version 29.
DE   RecName: Full=Superoxide dismutase {ECO:0000256|RuleBase:RU000414};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000414};
GN   Name=chrC {ECO:0000313|EMBL:CCB86686.1};
GN   OrderedLocusNames=PUV_17360 {ECO:0000313|EMBL:CCB86686.1};
OS   Parachlamydia acanthamoebae (strain UV7).
OC   Bacteria; Chlamydiae; Chlamydiales; Parachlamydiaceae; Parachlamydia.
OX   NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB86686.1, ECO:0000313|Proteomes:UP000000495};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UV7;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E.,
RA   Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S.,
RA   Friedman M.G., Rattei T., Myers G.S.A., Horn M.;
RT   "Unity in variety -- the pan-genome of the Chlamydiae.";
RL   Mol. Biol. Evol. 0:0-0(2011).
RN   [2] {ECO:0000313|EMBL:CCB86686.1, ECO:0000313|Proteomes:UP000000495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX   PubMed=21690563; DOI=10.1093/molbev/msr161;
RA   Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E.,
RA   Brunham R.C., Read T.D., Bavoil P.M., Sachse K., Kahane S.,
RA   Friedman M.G., Rattei T., Myers G.S., Horn M.;
RT   "Unity in variety--the pan-genome of the chlamydiae.";
RL   Mol. Biol. Evol. 28:3253-3270(2011).
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; FR872580; CCB86686.1; -; Genomic_DNA.
DR   STRING; 765952.PUV_17360; -.
DR   EnsemblBacteria; CCB86686; CCB86686; PUV_17360.
DR   KEGG; puv:PUV_17360; -.
DR   eggNOG; ENOG4107XIJ; Bacteria.
DR   eggNOG; COG0605; LUCA.
DR   KO; K04564; -.
DR   OMA; DAHDNGA; -.
DR   BioCyc; PACA765952:GH3O-1771-MONOMER; -.
DR   Proteomes; UP000000495; 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; IPR019832; Mn/Fe_SOD_C.
DR   InterPro; IPR019831; Mn/Fe_SOD_N.
DR   PANTHER; PTHR11404; PTHR11404; 1.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000495};
KW   Metal-binding {ECO:0000256|RuleBase:RU000414};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000414,
KW   ECO:0000313|EMBL:CCB86686.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000495};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    225       Superoxide dismutase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003379146.
FT   DOMAIN      126    220       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
SQ   SEQUENCE   225 AA;  25903 MW;  8CAEBF874755C900 CRC64;
     MKKIWLVAIC LMMGVAQMAM GDETASSTKK YEVRDFDHLL GKVKGLNDDL LKMHFKLYQG
     YVNNTNTLLQ KIGELDQTGK SQSPEFAGFK HMLGWEFDGM LLHEYYFENL GGQTHQLKQD
     DPLFLKMVQD FGGYDQWKSD FQATGAIRGI GWVITYVDPK QGRLVNTWIN EHDVGHLSGG
     KPLLVMDVFE HAYITQFGLD RAKYIQVFFD NIDWNAVSQR YKKTL
//
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