ID A0A1D9NXQ6_9FIRM Unreviewed; 601 AA.
AC A0A1D9NXQ6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=bhn_I0111 {ECO:0000313|EMBL:AOZ95147.1};
OS Butyrivibrio hungatei.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=185008 {ECO:0000313|EMBL:AOZ95147.1, ECO:0000313|Proteomes:UP000179284};
RN [1] {ECO:0000313|Proteomes:UP000179284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB2003 {ECO:0000313|Proteomes:UP000179284};
RA Palevich N., Kelly W.J., Leahy S.C., Altermann E., Rakonjac J.,
RA Attwood G.T.;
RT "The complete genome sequence of the rumen bacterium Butyrivibrio hungatei
RT MB2003.";
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; CP017831; AOZ95147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D9NXQ6; -.
DR KEGG; bhu:bhn_I0111; -.
DR Proteomes; UP000179284; 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; 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:UP000179284};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 1..73
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 185..220
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 236..478
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 601 AA; 68878 MW; 5C65F250E7612B59 CRC64;
MRDENDTIMY VGKAINLHNR VRSYFRANIG RGPQIDQMVK QIARFEYIVT DSELEALVLE
NNLIKENSPR YNTLLKDDKT YPYIKVTVSE DFPRVLFSRL MKKDKSRYFG PFTSAAAVKD
TIDLINKIYG LRTCNRSLPK EIGADRPCLN YHMKQCCGPC TGNVTKEEYR ERIDKALEFL
NGNYGVIMKD LQQKMEAASE ELDFESAAKY RDLLASVRVV AQKQKMTDSS MEDKDIVAIA
SDDKDAVVQV FFVRDGRLIG REHFYMTHVS ENPSGEILQN FVKQFYAGTP FIPRELILPE
PIEDMEIIEQ WLSQRKGSRV YISVPERGQK EKLMELATQN AELVLSKDKE RIKREEGRTI
GAVKEIEKLL GLKGLNRMEA FDISNISGFA NVGSMVVYEK GKPKKSDYRK FRIKSVAGPD
DYACMHEVLT RRLLHGIEEK HELEVRDIDA QYGSFTKFPD LILMDGGRGQ VNICLQVLDE
LGIHIPVCGM VKDDNHRTRG LYYNNVELPI DTRSEGFKLI TRIQDEAHRF AIEYHRSLRS
KAQVKSSLDD IPGIGPARRK ALMKGFKSIE DIKNASVEEL AAIPEIPENI AQQIYDFFHI
L
//
