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Database: UniProt
Entry: RECR_ACIC1
LinkDB: RECR_ACIC1
Original site: RECR_ACIC1 
ID   RECR_ACIC1              Reviewed;         199 AA.
AC   A0LWH7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN   Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; OrderedLocusNames=Acel_2015;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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; CP000481; ABK53787.1; -; Genomic_DNA.
DR   RefSeq; WP_011720850.1; NC_008578.1.
DR   AlphaFoldDB; A0LWH7; -.
DR   SMR; A0LWH7; -.
DR   STRING; 351607.Acel_2015; -.
DR   KEGG; ace:Acel_2015; -.
DR   eggNOG; COG0353; Bacteria.
DR   HOGENOM; CLU_060739_1_0_11; -.
DR   InParanoid; A0LWH7; -.
DR   OrthoDB; 9802672at2; -.
DR   Proteomes; UP000008221; 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   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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; SM00278; HhH1; 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; DNA recombination; DNA repair; Metal-binding;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..199
FT                   /note="Recombination protein RecR"
FT                   /id="PRO_0000322852"
FT   DOMAIN          79..174
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT   ZN_FING         56..71
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ   SEQUENCE   199 AA;  21806 MW;  EE9EAA2A38B17129 CRC64;
     MYEGVIQDLI DELGKLPGIG PKSAQRIAFH ILGADPSQVR RLAEVLLDVK ERIRFCAICG
     NVAEHEQCRI CADPRRDPTV LCVVEEPKDV VAIEKTREFH GRYHVLGGAI SPIDGIGPDD
     LRIRELLQRL ADGTVKELIL ATDPNLEGEA TATYLARLVK PLGVRVTRLA SGLPVGGDLE
     YADEVTLGRA LEGRRQLDV
//
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