ID UVRC_BURCH Reviewed; 681 AA.
AC A0K5W8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=Bcen2424_1143;
OS Burkholderia cenocepacia (strain HI2424).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI2424;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424.";
RL Submitted (AUG-2006) 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; CP000458; ABK07895.1; -; Genomic_DNA.
DR RefSeq; WP_011544950.1; NC_008542.1.
DR AlphaFoldDB; A0K5W8; -.
DR SMR; A0K5W8; -.
DR KEGG; bch:Bcen2424_1143; -.
DR HOGENOM; CLU_014841_3_0_4; -.
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..681
FT /note="UvrABC system protein C"
FT /id="PRO_1000077757"
FT DOMAIN 22..100
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 209..244
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 681 AA; 74629 MW; 851559A03AFE22FF CRC64;
MTSPEASATP FEPKKILAQL PHMPGVYRYY DTTGAVLYVG KARDLKKRVS SYFTKTQLSP
RIAMMVTRIA RIETTVTRSE AEALLLENNL IKALAPRYNI LFRDDKSYPY LKLTAHRFPR
MAYYRGSVDK QNQYFGPFPS AWAVRESIQI LQRVFQLRTC EDSVFNNRTR PCLLHQIGRC
TAPCVGAISE EDYAVDVSNA ARFLLGRQSE VMKELEQKMH AFAAELKFEQ AAAVRNQMSS
LATVLHQQAI EVGSDSDVDI LAVVAQGGRV CVNLAMVRGG RHLGDKAYFP THVESALTLA
EGGLGEEVEP AEAVDATADA PVDTVPDQPA EEAGSARGAA AASVEAEVLD AFIAQHYLGN
RVPPVLVVSH APASRDLLEL LSEQAGHKVS LVRQPQGQRR AWLSMAEQNA RLALARLLSE
QGSQQARTRA LADTLSYDSD DLATLRIECF DISHTMGEAT QASCVVYHHH KMQSSEYRRY
NITGITPGDD YAAMRQVLTR RYEKMVEQAA QAAAVDEAAG IDGESTRQAE ASSLLPNIVL
IDGGKGQVEI ARQVFTELGL DTSMLVGVAK GEGRKVGLET LVFADGRAPL ELGKESAALM
LVAQIRDEAH RFAITGMRAK RAKARQTSRL EELEGVGAKR RQRLLARFGG LRGVVAASVE
ELASVEGISH ALAEQIYKQL H
//
