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Database: UniProt
Entry: A0A1G2U676_9BACT
LinkDB: A0A1G2U676_9BACT
Original site: A0A1G2U676_9BACT 
ID   A0A1G2U676_9BACT        Unreviewed;       204 AA.
AC   A0A1G2U676;
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=A3A26_00155 {ECO:0000313|EMBL:OHB04978.1};
OS   Candidatus Zambryskibacteria bacterium RIFCSPLOWO2_01_FULL_47_14.
OC   Bacteria; Candidatus Zambryskibacteria.
OX   NCBI_TaxID=1802763 {ECO:0000313|EMBL:OHB04978.1, ECO:0000313|Proteomes:UP000177068};
RN   [1] {ECO:0000313|EMBL:OHB04978.1, ECO:0000313|Proteomes:UP000177068}
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:OHB04978.1}.
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DR   EMBL; MHWG01000023; OHB04978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2U676; -.
DR   Proteomes; UP000177068; 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          82..180
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   204 AA;  23224 MW;  7C9DCA84EACABE3B CRC64;
     MNSIDKLTEI FRSFPGIGPR QAKRFVYYLL SRNGSYSQEL VQAIQNLKKE ITQCSECQRH
     YAKNGYTSKT CNICSDETRD GSMLMIVPRD IDLEAVERSG SYRGHYFVLG GVVPILEKEP
     EKRIRIKDLG FRIQESLKHG LKEIILAMNA NQDGENTAEY LKERLTTNNP QLTMTVLGRG
     LSTGAELEYA DPETLKNAFL HRTK
//
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