ID UVRC_LAWIP Reviewed; 621 AA.
AC Q1MQH2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=LI0701;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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; AM180252; CAJ54755.1; -; Genomic_DNA.
DR RefSeq; WP_011526784.1; NC_008011.1.
DR AlphaFoldDB; Q1MQH2; -.
DR SMR; Q1MQH2; -.
DR STRING; 363253.LI0701; -.
DR KEGG; lip:LI0701; -.
DR eggNOG; COG0322; Bacteria.
DR HOGENOM; CLU_014841_3_2_7; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000002430; Chromosome.
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 Reference proteome; SOS response.
FT CHAIN 1..621
FT /note="UvrABC system protein C"
FT /id="PRO_0000264906"
FT DOMAIN 11..90
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 200..235
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 621 AA; 70327 MW; C717D8DA7EA5BB3B CRC64;
MERPHPSSIP TTPGVYLYKD SQGRIIYVGK ARNLRKRVLS YFRDGLVITP KTKAMMNHAN
LLETISTNTE KEALLLEASL IKKHRPRYNI VLRDDKQYLL FRIQKGIPFP RLEIVRQSYK
DNAVYFGPFT SGTSVRDTWK FIHKIFPLRR CSDKVFNNRI RPCLYFYLQQ CLAPCTEEVD
PKDYAVLIQK VELFLSGKSK ELVELLQKDM LYASEALEFE KAATLRDQIQ AIKHTIERQS
VVLPEGGDMD VIGIAVVNNG LALGFLFVRE GKLLDGRTFF WPGLELDDGP ELLGSFLSQF
YSPISSIPPR IIVPWLPEST NNKDEISEDT FETLKYVLED IRNSTVRIEV PKNIIESNLV
DIAVTNAREA VQTKLGEPMS AKLAKVFHTD KPIFRIECVD VSHISGTNTR VGMVVFEDSQ
PLKNDYRIYS TTEDNSPFIK GDDYAALASW AKRRIQSGPP WADLVLIDGG KGQINAVQRV
FNEHHLKDVF ILAGIAKARN EEGRVDRRAG NIGDKIFVVG RMNPLTLKEG SPELLFLQYV
RDTAHNFVLG KHRKARKNTA LLGELLRIPG IGQATAKLLW SHFKTVEAMT CATIKDLEAI
PGIGEAKARM LAERLQSLRN Q
//
