(data stored in ACNUC10821 zone)

SWISSPROT: C8U2F8_ECO10

ID   C8U2F8_ECO10            Unreviewed;       201 AA.
AC   C8U2F8;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Recombination protein RecR {ECO:0000256|HAMAP-Rule:MF_00017, ECO:0000256|SAAS:SAAS00725297};
GN   Name=recR {ECO:0000256|HAMAP-Rule:MF_00017,
GN   ECO:0000313|EMBL:BAI29316.1};
GN   OrderedLocusNames=ECO103_0448 {ECO:0000313|EMBL:BAI29316.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29316.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29316.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: May play a role in DNA repair. It seems to be involved
CC       in an RecBC-independent recombinational process of DNA repair. It
CC       may act with RecF and RecO. {ECO:0000256|HAMAP-Rule:MF_00017,
CC       ECO:0000256|SAAS:SAAS00725307}.
CC   -!- SIMILARITY: Belongs to the RecR family. {ECO:0000256|HAMAP-
CC       Rule:MF_00017, ECO:0000256|SAAS:SAAS00725273}.
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DR   EMBL; AP010958; BAI29316.1; -; Genomic_DNA.
DR   RefSeq; WP_001195025.1; NC_013353.1.
DR   SMR; C8U2F8; -.
DR   EnsemblBacteria; BAI29316; BAI29316; ECO103_0448.
DR   KEGG; eoh:ECO103_0448; -.
DR   HOGENOM; HOG000103272; -.
DR   KO; K06187; -.
DR   OMA; DVMAIEN; -.
DR   BioCyc; ECOL585395:ECO103_RS02345-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd01025; TOPRIM_recR; 1.
DR   HAMAP; MF_00017; RecR; 1.
DR   InterPro; IPR000093; DNA_Rcmb_RecR.
DR   InterPro; IPR023627; Rcmb_RecR.
DR   InterPro; IPR023628; Rcmb_RecR_C4-type_Zn.
DR   InterPro; IPR015967; Rcmb_RecR_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034137; TOPRIM_RecR.
DR   PANTHER; PTHR30446; PTHR30446; 1.
DR   Pfam; PF02132; RecR; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF111304; SSF111304; 1.
DR   TIGRFAMs; TIGR00615; recR; 1.
DR   PROSITE; PS01300; RECR; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2F8.
DR   SWISS-2DPAGE; C8U2F8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00017,
KW   ECO:0000256|SAAS:SAAS00725304};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00017,
KW   ECO:0000256|SAAS:SAAS00725299};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00017,
KW   ECO:0000256|SAAS:SAAS00725260};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00017,
KW   ECO:0000256|SAAS:SAAS00725312};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00017, ECO:0000256|SAAS:SAAS00725311};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00017,
KW   ECO:0000256|SAAS:SAAS00725288}.
FT   DOMAIN       81    176       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      57     72       C4-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00017}.
SQ   SEQUENCE   201 AA;  21963 MW;  F527EE1C809E47E9 CRC64;
     MQTSPLLTQL MEALRCLPGV GPKSAQRMAF TLLQRDRSGG MRLAQALTRA MSEIGHCADC
     RTFTEQEVCN ICSNPRRQEN GQICVVESPA DIYAIEQTGQ FSGRYFVLMG HLSPLDGIGP
     DDIGLDRLEQ RLAEEKITEV ILATNPTVEG EATANYIAEL CAQYDVEASR IAHGVPVGGE
     LEMVDGTTLS HSLAGRHKIR F
//

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