ID A0A1G9VJ66_9FIRM Unreviewed; 611 AA.
AC A0A1G9VJ66;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=UvrABC system protein C {ECO:0000256|HAMAP-Rule:MF_00203};
DE Short=Protein UvrC {ECO:0000256|HAMAP-Rule:MF_00203};
DE AltName: Full=Excinuclease ABC subunit C {ECO:0000256|HAMAP-Rule:MF_00203};
GN Name=uvrC {ECO:0000256|HAMAP-Rule:MF_00203};
GN ORFNames=SAMN05192585_10425 {ECO:0000313|EMBL:SDM72328.1};
OS Acetanaerobacterium elongatum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetanaerobacterium.
OX NCBI_TaxID=258515 {ECO:0000313|EMBL:SDM72328.1, ECO:0000313|Proteomes:UP000199182};
RN [1] {ECO:0000313|EMBL:SDM72328.1, ECO:0000313|Proteomes:UP000199182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5012 {ECO:0000313|EMBL:SDM72328.1,
RC ECO:0000313|Proteomes:UP000199182};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|HAMAP-
CC Rule:MF_00203}.
CC -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC {ECO:0000256|HAMAP-Rule:MF_00203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00203}.
CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000256|HAMAP-
CC Rule:MF_00203}.
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DR EMBL; FNID01000004; SDM72328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9VJ66; -.
DR STRING; 258515.SAMN05192585_10425; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000199182; Unassembled WGS sequence.
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; 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 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00203};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00203};
KW DNA excision {ECO:0000256|ARBA:ARBA00022769, ECO:0000256|HAMAP-
KW Rule:MF_00203};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_00203};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW Rule:MF_00203}; Reference proteome {ECO:0000313|Proteomes:UP000199182};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 18..97
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 208..243
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 259..487
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 611 AA; 69372 MW; B9DCBF5E810B2332 CRC64;
MENERLPYLR EKTKTLTIEP GCYIMRNKQG EIIYIGKAKN LRKRVTSYFR KNADHLPKVE
KMVSHVYDYD YIVTDSEFEA LVLECSLIKQ NSPKYNILLK DDKGYHYIRI SGKSWGRISA
AKQLVDDGAT YIGPYVSSFA VMQAVEEANT AFCLPTCNRK FPQDFKKGRP CLNFHIKRCM
GVCMGKISEQ EYAENLSQAL DFLRSDSANT IKVLTEKMET ASERMDFERA AQLRDRIQAI
RRINEHQKVI YTNTPDQDVI ALSQNTSQAS AVVIKFRNHR LVDKESFMLG EIESIVAARS
EFIIRYYSGD REIPKQISLD GEVEDLELTE RFLTDKAGRK CLLHLPQRGE QARLVEMAKT
NASELLGQHS GASGREVAAL DELARLLNLP KTPEYIEAYD ISNIGSSDMV AGMVVFENGR
PLKSAYKRFS IKTLTEQNDY GAMSEVLSRR LARYFEEKES GKGFGRLPDL ILLDGGKGHV
STIQPIIEQS GLNIPLFGMV KDDRHRTRAI ATNGGEIAIS AYRNAFTFIT RIQDEVHRFS
IEYQRAKHKK TGMESSLTKI DGIGPSRAAK LLRHFKTMHA IKEASVEALL QAPGMTRPAA
ERVYRTFHET E
//
