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Database: UniProt
Entry: A0A1G0WQ95_9BACT
LinkDB: A0A1G0WQ95_9BACT
Original site: A0A1G0WQ95_9BACT 
ID   A0A1G0WQ95_9BACT        Unreviewed;       197 AA.
AC   A0A1G0WQ95;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Recombination protein RecR {ECO:0000256|HAMAP-Rule:MF_00017};
GN   Name=recR {ECO:0000256|HAMAP-Rule:MF_00017};
GN   ORFNames=A2475_07715 {ECO:0000313|EMBL:OGV23586.1};
OS   Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV23586.1, ECO:0000313|Proteomes:UP000177327};
RN   [1] {ECO:0000313|EMBL:OGV23586.1, ECO:0000313|Proteomes:UP000177327}
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: 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:OGV23586.1}.
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DR   EMBL; MHAY01000024; OGV23586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0WQ95; -.
DR   STRING; 1798452.A2475_07715; -.
DR   Proteomes; UP000177327; 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   CDD; cd01025; TOPRIM_recR; 1.
DR   Gene3D; 3.30.60.80; -; 1.
DR   Gene3D; 3.40.1360.10; -; 1.
DR   Gene3D; 6.10.250.240; -; 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; IPR015967; Rcmb_RecR_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034137; TOPRIM_RecR.
DR   NCBIfam; TIGR00615; recR; 1.
DR   PANTHER; PTHR30446; RECOMBINATION PROTEIN RECR; 1.
DR   PANTHER; PTHR30446:SF0; RECOMBINATION PROTEIN RECR; 1.
DR   Pfam; PF21175; RecR_C; 1.
DR   Pfam; PF21176; RecR_HhH; 1.
DR   Pfam; PF02132; RecR_ZnF; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF111304; Recombination protein RecR; 1.
DR   PROSITE; PS01300; 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          81..174
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         58..73
FT                   /note="C4-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00017"
SQ   SEQUENCE   197 AA;  22193 MW;  B0CD3D70D2057D26 CRC64;
     MVYTSDSIEK IVELFSSLPT IGRKTAQRLT FFLLRQPQEF IDQFAESLIS LKKKVKYCSV
     CYNYTETDPC PICSSAKRQS NTICVVEEPN DVMAIEKTGE YYGMYHVLHG TLNPLDGVTP
     EDLKIRELIE RLGNVEEIIL ALNPSVEGEV TTQYLSKQIK PLNIKVTRIA RGLPIGSDLE
     FADEATITRA LEGRVEV
//
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