ID A0A1G2VVS7_9BACT Unreviewed; 207 AA.
AC A0A1G2VVS7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Recombination protein RecR {ECO:0000256|HAMAP-Rule:MF_00017};
GN Name=recR {ECO:0000256|HAMAP-Rule:MF_00017};
GN ORFNames=A2542_02010 {ECO:0000313|EMBL:OHB25732.1};
OS Parcubacteria group bacterium RIFOXYD2_FULL_52_8.
OC Bacteria.
OX NCBI_TaxID=1817746 {ECO:0000313|EMBL:OHB25732.1, ECO:0000313|Proteomes:UP000177816};
RN [1] {ECO:0000313|EMBL:OHB25732.1, ECO:0000313|Proteomes:UP000177816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: May play a role in DNA repair. It seems to be involved in an
CC RecBC-independent recombinational process of DNA repair. It may act
CC with RecF and RecO. {ECO:0000256|HAMAP-Rule:MF_00017}.
CC -!- SIMILARITY: Belongs to the RecR family. {ECO:0000256|HAMAP-
CC Rule:MF_00017}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00017}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHB25732.1}.
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DR EMBL; MHXK01000007; OHB25732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2VVS7; -.
DR Proteomes; UP000177816; Unassembled WGS sequence.
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 Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 1.10.8.420; RecR Domain 1; 1.
DR HAMAP; MF_00017; RecR; 1.
DR InterPro; IPR000093; DNA_Rcmb_RecR.
DR InterPro; IPR023627; Rcmb_RecR.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR30446; RECOMBINATION PROTEIN RECR; 1.
DR PANTHER; PTHR30446:SF0; RECOMBINATION PROTEIN RECR; 1.
DR Pfam; PF21176; RecR_HhH; 1.
DR Pfam; PF13662; Toprim_4; 1.
DR SUPFAM; SSF111304; Recombination protein RecR; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00017};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_00017};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00017};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00017};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00017};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW Rule:MF_00017}.
FT DOMAIN 83..186
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 207 AA; 22969 MW; 3DDC8214C9FDD528 CRC64;
MSSAIDQLTE SFARFPGIGP RQAKRFVYHL LQQDPAVLAN LSQQILKLRK EINRCGRCYR
FFSPTENYQE QCDFCRDTSR DAAQLMVVAR DTDLDAMHKS HAYDGYYFVL GGLLSLTERH
PDPSLRGVQL LARVQADVAA GSLKEIILAL SANTEGDHTA EYVESLVSPL TESGQLKLSH
LGRGLSTGTE LEYSDSATIK SALKNRS
//