ID   UVRC_DEHMB              Reviewed;         607 AA.
AC   A5FQB7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
GN   OrderedLocusNames=DehaBAV1_1026;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 /
OS   BAV1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=216389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Ritalahti K.M., Loeffler F., Richardson P.;
RT   "Complete sequence of Dehalococcoides sp. BAV1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000688; ABQ17606.1; -; Genomic_DNA.
DR   RefSeq; WP_011929262.1; NC_009455.1.
DR   AlphaFoldDB; A5FQB7; -.
DR   SMR; A5FQB7; -.
DR   KEGG; deb:DehaBAV1_1026; -.
DR   PATRIC; fig|216389.18.peg.1081; -.
DR   HOGENOM; CLU_014841_3_2_0; -.
DR   OMA; HIECFDN; -.
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; IPR041663; DisA/LigA_HHH.
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; PF12826; HHH_2; 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..607
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_1000077779"
FT   DOMAIN          15..94
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          204..239
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ   SEQUENCE   607 AA;  68415 MW;  1EC27AA1C0FA5123 CRC64;
     MPNETLQNQI ASLPENPGVY LMKNAQGEII YVGKAAVLKD RVKSYFVPPS RLTPKTCQLV
     SQINELEYLI TGSEQEALIL ELNLIKRHRP YFNVRLKDDK GFPYLKITLN EKWPRIYITR
     SMADDGGRYF GPFANTRSVR HTLQVLKELF RFRSCNRTEP EKRSRPCLEY DIHQCLSPCT
     GKISKSDYDH LISQAILFLE GKQDQVLKLL IRLMNEASAR LDYETAALRR DQIASIKEVI
     EGQQLAARVT GEQDAIAFAQ EGDLSMVQVF FIRRGKLIGR ESFCLQGTRE EKPGDILSEF
     AKQFYHSSTQ IPPKIVTQYP VSDREILEKW LSQRRGDKVH ITAGLRGQPK ELINIVAENA
     REQLKQARIK NLSSSVTLTD ALAELQTALG LSLPPQRIEG YDISNIQGTN AVGSMVVFEN
     GKPQKAHYRR FRIKTVKGAD DFSMLKEVIS RRFGRVHRED AGESFARLPS LMLIDGGKGQ
     LSSVKETLDK LGLEGQAVIG LAKEFEEIYL PHKSEPIRLA ANSPALQLLQ RVRDEAHRFA
     LGYHLHIRQK SGLTSALDGI PGVGPSRRRL LIKTFGSVAG IRQASFEKLS QVKGINQALA
     LSIKELL