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RECR_HAEDU
ID   RECR_HAEDU              Reviewed;         174 AA.
AC   O30823;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN   Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; OrderedLocusNames=HD_0325;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RX   PubMed=9511768; DOI=10.1016/s0378-1119(97)00642-2;
RA   San Mateo L.R., Toffer K.L., Kawula T.H.;
RT   "The sodA gene of Haemophilus ducreyi encodes a hydrogen peroxide-
RT   inhibitable superoxide dismutase.";
RL   Gene 207:251-257(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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:0000255|HAMAP-Rule:MF_00017}.
CC   -!- SIMILARITY: Belongs to the RecR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00017}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP95302.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF017750; AAC46216.1; -; Genomic_DNA.
DR   EMBL; AE017143; AAP95302.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; O30823; -.
DR   SMR; O30823; -.
DR   STRING; 233412.HD_0325; -.
DR   EnsemblBacteria; AAP95302; AAP95302; HD_0325.
DR   KEGG; hdu:HD_0325; -.
DR   eggNOG; COG0353; Bacteria.
DR   HOGENOM; CLU_060739_1_2_6; -.
DR   Proteomes; UP000001022; 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; 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; 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..174
FT                   /note="Recombination protein RecR"
FT                   /id="PRO_0000190327"
FT   DOMAIN          54..149
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT   ZN_FING         30..45
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ   SEQUENCE   174 AA;  19348 MW;  BE4CF6FD3459BC59 CRC64;
     MAYHLLQRNR NGGLNLAKAL NEAMTHIGHC NACRTFTEEE ECTICKNPRR QISGQLCIVE
     MPEDIQAIEQ TGQFSGRYFV LMGHLSPLDG IGPREIGLDL LQQRLEQESF HEIILATNPT
     IEGDATANYI AEICHLYNVK VTRIAHGIPV GGSLEMVDGT TLSHSFAGRR DFLL
 
 
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