ID UVRC_CORGB Reviewed; 696 AA.
AC A4QEG6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=cgR_1640;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
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; AP009044; BAF54632.1; -; Genomic_DNA.
DR RefSeq; WP_011897303.1; NC_009342.1.
DR AlphaFoldDB; A4QEG6; -.
DR SMR; A4QEG6; -.
DR KEGG; cgt:cgR_1640; -.
DR HOGENOM; CLU_014841_3_2_11; -.
DR PhylomeDB; A4QEG6; -.
DR Proteomes; UP000006698; 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 CDD; cd10434; GIY-YIG_UvrC_Cho; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.1440.10; GIY-YIG endonuclease; 1.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR Gene3D; 3.30.420.340; UvrC, RNAse H endonuclease domain; 1.
DR HAMAP; MF_00203; UvrC; 1.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR047296; GIY-YIG_UvrC_Cho.
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 NCBIfam; TIGR00194; uvrC; 1.
DR PANTHER; PTHR30562:SF1; UVRABC SYSTEM PROTEIN C; 1.
DR PANTHER; PTHR30562; UVRC/OXIDOREDUCTASE; 1.
DR Pfam; PF01541; GIY-YIG; 1.
DR Pfam; PF14520; HHH_5; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF08459; UvrC_RNaseH_dom; 1.
DR SMART; SM00465; GIYc; 1.
DR SMART; SM00278; HhH1; 2.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 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..696
FT /note="UvrABC system protein C"
FT /id="PRO_1000077776"
FT DOMAIN 16..95
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 208..243
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 696 AA; 78334 MW; E742491E15C38A8B CRC64;
MADPTTYRPA PGTIPTEPGV YKFRDENRRV IYVGKAKNLR SRLSNYFQDV TQLHPRTRQM
VFAASSVEWT VVSSEVEALQ LEYTWIKRFD PRFNVKYRDD KTYPMLAVST GERFPRAFFF
RGPRRKGVRY FGPYSHAWAV RETLDLLTRV FPMRTCSKGV FNRHESLGRP CLLGYIDKCA
APCVGRVSEE EHREIVDGFT SFMAGHTDKV TRKLNADMMA AAEELDFERA ARLRDDLEAI
DKVMEKQAVV LGDGTDADII AFATDQLEAA VQVFNIRGGR IRGQRGWVVD KPGDYAGLLV
DATTQPEGDA PETDPALPFL MQDFLVQFYG DAVERAETEA KEDAAVIERR GVDKHSFEEA
APVTRASVVP REILVQVAPN EAEQTLKVLE ELRGAGVDAR VPQRGDKRAL METVERNAKE
LLKQHKLKRV GDLTARSAAL QELQEALDME QAPLRIECTD ISHIQGTDVV ASLVVFEDGL
PRKSDYRRYR VKEAAGDGHS NDVASIAEIT RRRFLRHNQD KLAVPEAEEF DGSTFSDEKV
EEMSTDARRF AYPPQIFIVD GGAPQVAAAQ EVFDELGIVD VVLIGLAKRL EEIWLPGDPD
PVILPRNSQA LFLLQQIRDE AHRFAITYHR QQRSKRMRVS ELDSIKGLGQ SRRTELVKHF
GSVAKLKEAS VEDISQVKGF GPKLAEAVYE GLHASK
//
