ID UVRC_MYCSJ Reviewed; 676 AA.
AC A3PZ93;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=Mjls_2436;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
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., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-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; CP000580; ABN98220.1; -; Genomic_DNA.
DR AlphaFoldDB; A3PZ93; -.
DR SMR; A3PZ93; -.
DR KEGG; mjl:Mjls_2436; -.
DR HOGENOM; CLU_014841_1_1_11; -.
DR BioCyc; MSP164757:G1G8C-2455-MONOMER; -.
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..676
FT /note="UvrABC system protein C"
FT /id="PRO_1000077810"
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 676 AA; 74750 MW; 21EAA49D126FF01C CRC64;
MPDPSTYRPA PGSIPVEPGV YRFRDPHGRV IYVGKAKSLR SRLNSYFADL SGLAPRTRQM
VMTAAKVEWT VVNTEVEALQ LEYNWIKEFD PRFNIRYRDD KSYPVLAVTL NEEFPRLKVY
RGPRKKGVRY FGPYSHAWAI RETVDLLTRV FPARTCSAGV FKRHNQIDRP CLLGYIDKCS
APCVGRVSAE QHRQIVLDFC DFLAGKTDRL VRDLERKMTA AAEDLDFERA ARLRDDIGAL
RRALEKQTVV FGDGTDADVV AFADDDLEAA VQVFHVRGGR VRGQRGWIVE KSGEPGESGE
GQLVEQFLTQ FYGDQAELGS AGDNAGDSGQ DEATNPVPRQ VLVPCLPDNA DELTEWLSQL
RGSRVALRVP QRGDKKALFE TVQRNAKEAL AQHKLKRAGD FTARTAALQS IQDTLGLADA
PLRIECIDIS HVQGTDVVAS LVVFEDGLPR KSDYRHYAIR EAAGDGRSDD VASIAEVTRR
RFYRHLHDTQ HPTELSAEGK SRKFAYPPNL FVVDGGAPQV NAAQAVLDEL GISDVAVIGL
AKRLEEVWVP SGSDLGPEPI ILPRNSEGLY LLQRVRDEAH RFAITYHRSK RSKRMTASAL
DSVRGLGEHR RKALVTHFGS VARLKEASVE EITAVPGIGV TTARAVLEAL GVPQAAPADS
GTAAAVIDDD QRRVTG
//
