ID A0A3Q8T899_9RICK Unreviewed; 199 AA.
AC A0A3Q8T899;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Recombination protein RecR {ECO:0000256|HAMAP-Rule:MF_00017};
GN Name=recR {ECO:0000256|HAMAP-Rule:MF_00017,
GN ECO:0000313|EMBL:AZL16227.1};
GN ORFNames=EF513_06765 {ECO:0000313|EMBL:AZL16227.1};
OS Rickettsiales endosymbiont of Stachyamoeba lipophora.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=2486578 {ECO:0000313|EMBL:AZL16227.1, ECO:0000313|Proteomes:UP000267655};
RN [1] {ECO:0000313|EMBL:AZL16227.1, ECO:0000313|Proteomes:UP000267655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RICK01 {ECO:0000313|EMBL:AZL16227.1,
RC ECO:0000313|Proteomes:UP000267655};
RA Munoz-Gomez S.A., Hess S., Burger G., Lang B.F., Susko E., Slamovits C.H.,
RA Roger A.J.;
RT "An updated phylogeny of the Alphaproteobacteria reveals that the parasitic
RT Rickettsiales and Holosporales have independent origins.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP033611; AZL16227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q8T899; -.
DR KEGG; ren:EF513_06765; -.
DR OrthoDB; 9802672at2; -.
DR Proteomes; UP000267655; 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; 3.40.1360.10; -; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000267655};
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 79..174
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT ZN_FING 56..71
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00017"
SQ SEQUENCE 199 AA; 22084 MW; F1B5050AD2BC6359 CRC64;
MSSNSLEQLI TLFAKMPGLG PRSARRVTLH LIKNRYKLMK PLHDLLGEVM QNVVHCRICN
NLDIYNPCQI CLDENRDKSQ ICIVEEIGDL WAIDKGGIFN GMYHVLGGTL SAIDGIGPEH
LSIDLLVRRV AEGEIEEVIL ANNATIEGKT TAHYITDLLK PYNVKISQLA YGIPVGGEID
YLDEHTLSAA LKARNYVEG
//