ID UVRC_BURP0 Reviewed; 747 AA.
AC A3NXK5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=BURPS1106A_2829;
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(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; CP000572; ABN91423.1; -; Genomic_DNA.
DR RefSeq; WP_004527460.1; NC_009076.1.
DR AlphaFoldDB; A3NXK5; -.
DR SMR; A3NXK5; -.
DR GeneID; 56528764; -.
DR KEGG; bpl:BURPS1106A_2829; -.
DR HOGENOM; CLU_014841_3_0_4; -.
DR Proteomes; UP000006738; Chromosome I.
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..747
FT /note="UvrABC system protein C"
FT /id="PRO_1000077762"
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"
FT REGION 363..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 80808 MW; 1B094FBC086E9AB6 CRC64;
MTSPDAPESR FEPKPILAQL PHLPGVYRYY DAQDAVLYVG KARDLKKRVS SYFTKTQLSP
RIAMMITRIA RIETTVTRSE AEALLLENNL IKALAPRYNI LFRDDKSYPY LKLTGHRFPR
MAYYRGAVDK KNQYFGPFPS AWAVRESIQI LQRVFQLRTC EDSVFNNRTR PCLLHQIGRC
SAPCVGAIGE EDYARDVDNA SRFLLGRQGE VMGELERKMH AFAAELKFEQ AAAVRNQMSS
LAKVLHQQAI DVGGDSDVDI LAVVAQGGRV CVNLAMVRGG RHLGDKAYFP AHVETALALA
GDIEALAGEG AGDGVQAAAQ PAQAPLATDA DATDAAATEA KTVTAAAAAR AGARTAQAAG
ARAAASAEGD VERRAEGETH ARADAREAAA LPDGAAAAQE ADADVDAAPL ETEVLEAFIA
QHYLGNRVPP VLVVSHAPAN RELIDLLVEQ AGHKVAVVRQ PQGQKRAWLT MAEQNARLAL
ARLLSEQGSQ QARTRSLADV LGYESDDLAQ LRIECFDISH TMGEATQASC VVYHHHRMQS
SEYRRYNIAG ITPGDDYAAM RQVLTRRYEK MVEEAAAEAS ADEAAGIDGN AVHAAASAGR
LPNVVLIDGG RGQVEIARQV FSELGLDISM LVGVAKGEGR KVGLETLIFA DGRAPLELGK
ESAALMLVAQ IRDEAHRFAI TGMRAKRAKT RQTSRLEELE GVGAKRRQRL LARFGGLRGV
VAASVDELAS VEGISRALAE QIYRQLH
//
