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UVRC_STRE4
ID   UVRC_STRE4              Reviewed;         594 AA.
AC   C0M890;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203};
DE            Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203};
DE   AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203};
GN   Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; OrderedLocusNames=SEQ_1368;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. UvrC both incises the 5' and 3' sides of the
CC       lesion. The N-terminal half is responsible for the 3' incision and the
CC       C-terminal half is responsible for the 5' incision. {ECO:0000255|HAMAP-
CC       Rule:MF_00203}.
CC   -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC       {ECO:0000255|HAMAP-Rule:MF_00203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
CC   -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00203}.
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DR   EMBL; FM204883; CAW94194.1; -; Genomic_DNA.
DR   RefSeq; WP_012679702.1; NC_012471.1.
DR   AlphaFoldDB; C0M890; -.
DR   SMR; C0M890; -.
DR   PRIDE; C0M890; -.
DR   EnsemblBacteria; CAW94194; CAW94194; SEQ_1368.
DR   KEGG; seu:SEQ_1368; -.
DR   HOGENOM; CLU_014841_3_2_9; -.
DR   OMA; HIECFDN; -.
DR   OrthoDB; 1036075at2; -.
DR   Proteomes; UP000001365; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.340; -; 1.
DR   Gene3D; 3.40.1440.10; -; 1.
DR   HAMAP; MF_00203; UvrC; 1.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR036876; UVR_dom_sf.
DR   InterPro; IPR004791; UvrC.
DR   InterPro; IPR001162; UvrC_RNase_H_dom.
DR   InterPro; IPR038476; UvrC_RNase_H_dom_sf.
DR   Pfam; PF01541; GIY-YIG; 1.
DR   Pfam; PF02151; UVR; 1.
DR   Pfam; PF08459; UvrC_HhH_N; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF82771; SSF82771; 1.
DR   TIGRFAMs; TIGR00194; uvrC; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
DR   PROSITE; PS50151; UVR; 1.
DR   PROSITE; PS50165; UVRC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA excision; DNA repair; Excision nuclease;
KW   SOS response.
FT   CHAIN           1..594
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000200601"
FT   DOMAIN          14..91
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          196..231
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ   SEQUENCE   594 AA;  68218 MW;  8ECA84DFBBD3E928 CRC64;
     MNELIKHKLE LLPDSPGCYL HKDKAGTIIY VGKAKNLRNR VRSYFRGSHD TKTELLVSEI
     ADFEFIVTGS NTEALLLEIN LIQENMPKYN IKLKDDKSYP FIKITNEPFP RLLITRQIKK
     NDGLYFGPYP DAYTATEVKK LLDRIFPFKK CKNPVNKVCF YYHLGQCQAH TICHTDKAYW
     DSLVADVKQF LNGKDDKIID DLRSKMLEAS HNQEFERAAE YRDLISGIAT MRTKQRVMSK
     DLQDRDIFGY FVDKGWMCVQ VFFVRQGKLI QRDVNMFPYY NEAEEDFLTY VGQFYSDQRH
     LIPKEVFIPE TIDETLVAAI VPARIVKPQR GEKKQLVALA TKNARVSLQQ KFDLLEKDLR
     KTSGAIEHLG QLLGIEKPVR IEAFDNSNIQ GTSPVAAMVV FVDGKPSKKD YRKFKIKTVI
     GPDDYASMRE VIYRRYSRVK HEGLQAPDLI IVDGGQGQVK AARDVIEHQL GLSIPVAGLQ
     KNDKHQTHEL LFGNPLAVVE LPRNSEEFFL LHRIQDEVHR FAITFHRQVR SKNAFSSKLD
     HIAGLGPKRK QLLLKRFKSM TALEQASLEE IQQLGIPKTV AEALFDHLTS KSEV
 
 
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