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UVRC_BIFLD
ID   UVRC_BIFLD              Reviewed;         746 AA.
AC   B3DRV5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=BLD_0428;
OS   Bifidobacterium longum (strain DJO10A).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=205913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJO10A;
RX   PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA   Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA   Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA   Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT   "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT   reveals loci susceptible to deletion during pure culture growth.";
RL   BMC Genomics 9:247-247(2008).
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; CP000605; ACD97874.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3DRV5; -.
DR   SMR; B3DRV5; -.
DR   EnsemblBacteria; ACD97874; ACD97874; BLD_0428.
DR   KEGG; blj:BLD_0428; -.
DR   HOGENOM; CLU_014841_3_2_11; -.
DR   OMA; HIECFDN; -.
DR   Proteomes; UP000002419; 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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF82771; SSF82771; 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..746
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000099459"
FT   DOMAIN          18..97
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          211..246
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   REGION          557..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   746 AA;  83169 MW;  1FA03106A165C2F4 CRC64;
     MLGDSRDLFR PKTSDIPAKP GVYKWRDGEG RVIYVGKAKN LRNRLTNYFQ PLYLLHPRTQ
     TMVLTARSLE WTVVATELES LTLEYTWIKE FDPRFNVQFR DDKTYPYLAV STGERIPRVW
     VTRSRKRRDT RYFGPYAKVW ELRHSLDRLL RTFPVRTCTT NVFHKAQLTG RPCLFASIGK
     CSAPCVNRIE ADEHRRLCEQ LVGVMTGRLG RPYIAQLTRD MKEASAELEF EKAARLRDQI
     QMLETVVQQN AVVFDQDVDA DVFGFASDEL EASVHAFYVR AGSIRGERNW SVERVEDIDD
     ADLMADLLVQ VYSDAAGDNH PQSAATISTN REAIGSTQTI TATDAVARAQ ATRERNTRQE
     TTGRADLLAP IAPVPREIIV PVEPARREEL EGWLTNLRGG AVTIRVASRG DKKQLMDRAN
     ENASQALQRS KMSRISDMGA RTQAMNDVAK ALGLAEAPLR IECYDISNTV GGAFQVASMV
     VFEDAIAKKS EYRRFAIRGK DGKGAVDDLS ALYETLTRRF KHGNIAGDSG ESIDAEQRVA
     SAAGKMTTAV AAETIAANGN DNGEGGSDIS GKGHAVPVGV QNDARESPPD IVQQNTNRHH
     FAYKPNLVVV DGGKPQVMAA AKALEDCGVN DVAVCGLAKR LEEVWVPDDD YPIILKRQSE
     GMYLLQRVRD ESHRFAITYH RQQRRKGALR SALDEIPGIG ESYQKRLLNH FGSVKAMREA
     SVEDFEKVKG IGHAKAEALY TALHEQ
 
 
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