ID   RECR_ANADF              Reviewed;         198 AA.
AC   A7HGU3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN   Name=recR {ECO:0000255|HAMAP-Rule:MF_00017};
GN   OrderedLocusNames=Anae109_3760;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RX   PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
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:0000255|HAMAP-Rule:MF_00017}.
CC   -!- SIMILARITY: Belongs to the RecR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00017}.
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DR   EMBL; CP000769; ABS27939.1; -; Genomic_DNA.
DR   RefSeq; WP_012098567.1; NC_009675.1.
DR   AlphaFoldDB; A7HGU3; -.
DR   SMR; A7HGU3; -.
DR   STRING; 404589.Anae109_3760; -.
DR   EnsemblBacteria; ABS27939; ABS27939; Anae109_3760.
DR   KEGG; afw:Anae109_3760; -.
DR   eggNOG; COG0353; Bacteria.
DR   HOGENOM; CLU_060739_1_0_7; -.
DR   OMA; DVMAIEN; -.
DR   OrthoDB; 1661836at2; -.
DR   Proteomes; UP000006382; 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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; SM00278; HhH1; 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;
KW   DNA damage; DNA recombination; DNA repair; Metal-binding;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..198
FT                   /note="Recombination protein RecR"
FT                   /id="PRO_0000322858"
FT   DOMAIN          80..175
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT   ZN_FING         57..72
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ   SEQUENCE   198 AA;  21330 MW;  7B4AE9FC4F9E98DC CRC64;
     MAVADPIARL VKELAKLPGI GEKTAQRLAF HILKAGPGYA GELAGAIAGV VRDVRLCSEC
     QTLTDKDPCA VCADPRRDSR IICVVEGVPD LLAVERTHEF RGRYHVLHGA LSPLDGIGPS
     ELKIRELLLR LEREPAEEIV VATNPDVEGE ATALYLTKLL KPLGVKVTRI AQGIPMGGDL
     EYADQVTLAR ALAGRREL