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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   25-OCT-2017, entry version 38.
DE   SubName: Full=Superoxide dismutase [Fe] {ECO:0000313|EMBL:CCB86686.1};
DE            EC=1.15.1.1 {ECO:0000313|EMBL:CCB86686.1};
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; Parachlamydiales; Parachlamydiaceae;
OC   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).
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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; DSPLMHG; -.
DR   OrthoDB; POG091H03Q7; -.
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; IPR036324; Mn/Fe_SOD_N_sf.
DR   InterPro; IPR036314; SOD_C_sf.
DR   Pfam; PF02777; Sod_Fe_C; 1.
DR   PIRSF; PIRSF000349; SODismutase; 1.
DR   SUPFAM; SSF46609; SSF46609; 1.
DR   SUPFAM; SSF54719; SSF54719; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000495};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000349-1};
KW   Oxidoreductase {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       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003379146.
FT   DOMAIN      126    220       Sod_Fe_C. {ECO:0000259|Pfam:PF02777}.
FT   METAL        54     54       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       103    103       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       187    187       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
FT   METAL       191    191       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000349-1}.
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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