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RECR_CHLMU
ID   RECR_CHLMU              Reviewed;         200 AA.
AC   Q9PKF4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN   Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; OrderedLocusNames=TC_0511;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39353.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE002160; AAF39353.1; ALT_INIT; Genomic_DNA.
DR   PIR; H81695; H81695.
DR   RefSeq; WP_010230647.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKF4; -.
DR   SMR; Q9PKF4; -.
DR   STRING; 243161.TC_0511; -.
DR   EnsemblBacteria; AAF39353; AAF39353; TC_0511.
DR   GeneID; 1245871; -.
DR   KEGG; cmu:TC_0511; -.
DR   eggNOG; COG0353; Bacteria.
DR   HOGENOM; CLU_060739_1_1_0; -.
DR   OrthoDB; 1661836at2; -.
DR   Proteomes; UP000000800; 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; IPR023627; Rcmb_RecR.
DR   InterPro; IPR015967; Rcmb_RecR_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034137; TOPRIM_RecR.
DR   PANTHER; PTHR30446; PTHR30446; 1.
DR   Pfam; PF13662; Toprim_4; 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; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..200
FT                   /note="Recombination protein RecR"
FT                   /id="PRO_0000190303"
FT   DOMAIN          82..177
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT   ZN_FING         58..75
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ   SEQUENCE   200 AA;  22305 MW;  4DEA32803FE6FBE1 CRC64;
     MLKYPDYISK LISFLKKLPG IGFKSAEKIA FELLEWDPSQ VEAMGLAMQE FSASHATCPD
     CFCLKTSKTS SCDFCSESRD SSFLCIVATP KDVFSFEKSK IFKGRYFVLG NLLSPITGKH
     LSLEKLNILK QRIEDFAPKE MIIALDATLE GDATALFLKQ EFSHLPIKIS RLALGMPVGL
     SFDFIDSNTL ARAFSGRNCF
 
 
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