ID A0A374TBI9_9BACT Unreviewed; 615 AA.
AC A0A374TBI9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=DXD25_11235 {ECO:0000313|EMBL:RGK28133.1};
OS Prevotella sp. TF12-30.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2292365 {ECO:0000313|EMBL:RGK28133.1, ECO:0000313|Proteomes:UP000262185};
RN [1] {ECO:0000313|EMBL:RGK28133.1, ECO:0000313|Proteomes:UP000262185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF12-30 {ECO:0000313|EMBL:RGK28133.1,
RC ECO:0000313|Proteomes:UP000262185};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGK28133.1}.
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DR EMBL; QSQJ01000030; RGK28133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374TBI9; -.
DR Proteomes; UP000262185; 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; 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; 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; PF08459; UvrC_RNaseH_dom; 1.
DR SMART; SM00465; GIYc; 1.
DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50164; GIY_YIG; 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}; SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 22..100
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 277..486
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 615 AA; 71947 MW; 4056CC1E1D306E45 CRC64;
MTKQENEERL ARLKSIVLSM PEKPGSYQYY DENHTIIYVG KAKNLKRRVS SYFHKEVDRY
KTKVLVSKIF DISYTVVNTE EDALLLENSL IKKYNPRYNV LLKDGKTYPS ICVTNEYFPR
IFKTRHINKK VGTFFGPYPH VGSMYAVLEV IKKLYKPRTC RFPITKEGVA EGKYKPCLEY
HIHNCGAPCI SKQSYEEYQE NMRQAREILK GNTREVSKYL YDLMMKNAEL LRFEIAEEYK
KKYQLLDEFE AKSEVVSHTI TDVDVFTIVN DDANKNAFIN YIHVKNGTIN QSFTYEYKRK
LEESDEELLI TAIPEIRERF HSTSKEIIVP FEMEWKLKDA TFFVPQRGDK KHLLELSEMN
CKQYKFDRLK QAEKLNPEQK QTRLMKELQS KLKLPKMPYQ IECFDNSNIS GTDAVAGCIV
YKGMKPSRKD YRKYNIKTVE GPDDYASMQE VVRRRYSRML EEETPLPDLI ITDGGKGQME
VVREVIEDEL HLEIPIAGLA KDDRHRTNEL LYGFPPQTIA LPPESELFKV LTQIQDEVHR
YAITFHRDKR SKHALHSELD DIKGIGPKAK EALLSKFKSV KKIKEASQEQ LSEVLGPHKA
EILAKYFTEK SENMK
//