ID   UVRC_CUPPJ              Reviewed;         663 AA.
AC   Q46Z26;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=Reut_A2244;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ61607.1; -; Genomic_DNA.
DR   RefSeq; WP_011298400.1; NC_007347.1.
DR   AlphaFoldDB; Q46Z26; -.
DR   SMR; Q46Z26; -.
DR   STRING; 264198.Reut_A2244; -.
DR   PRIDE; Q46Z26; -.
DR   EnsemblBacteria; AAZ61607; AAZ61607; Reut_A2244.
DR   KEGG; reu:Reut_A2244; -.
DR   eggNOG; COG0322; Bacteria.
DR   HOGENOM; CLU_014841_3_0_4; -.
DR   OMA; HIECFDN; -.
DR   OrthoDB; 1036075at2; -.
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..663
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_0000227466"
FT   DOMAIN          32..110
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          219..254
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   663 AA;  72741 MW;  39DF9B84ECB648EA CRC64;
     MSDQLPDASA QPPDPAQAEP FDPKPVIARL PGLPGVYRYI DSAGNVLYVG KARNLKKRVS
     SYFNKTQLSP RIAMMVAKIA RIDTTVVRTE AEALLLENNL IKALAPRYNI LFRDDKSYPF
     LKLTGHRFPR MAYYRGATDR KHQYFGPFPS AYAVRESMQI LQKVFQLRTC EDTVFNNRTR
     PCLLHQIHRC TGPCVGAISE ADYARDVGNA ASFLQGRETE VLEGLQSKME EHAMQLEFEQ
     AAAVRDQIAA LSTVLKRQAV EEVGQARDID VLAVAVEGGR ACVNLAMVRG GRHLGDKAYF
     PAHADEAAMI VEDGDEGAEG GETEPAPAVP LGVERIAARV LSAFMVQHYL DQAPPPIIVV
     SHVPDDAALL EALALHAGRK IALVRQPQGQ RKAWLEMAQQ GAALALARRL SEQGSQEART
     RALAETIGID LEDLALLRVE CFDISHTAGE ATQASCVVFH HHDMQNGEYR RYNIQDITPG
     DDYAAMRQVL TRRYQKLVEL MQEQGGLDPA GEASSPMPHV VLIDGGKGQV EVARQVFEEL
     GLDIGLLVGV AKGEGRKVGL ETLVFADGRP SLELGQGSAA LMLVAQIRDE AHRFAITGMR
     ARRAKARTTS RLEEIEGVGA RRRQKLLTRF GGLRGVMAAS IDELASVDGI SRGLAEEIYR
     QLH