ID A0A1T4KZX2_9ENTE Unreviewed; 594 AA.
AC A0A1T4KZX2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN02745116_00457 {ECO:0000313|EMBL:SJZ47989.1};
OS Pilibacter termitis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Pilibacter.
OX NCBI_TaxID=263852 {ECO:0000313|EMBL:SJZ47989.1, ECO:0000313|Proteomes:UP000190328};
RN [1] {ECO:0000313|EMBL:SJZ47989.1, ECO:0000313|Proteomes:UP000190328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1030 {ECO:0000313|EMBL:SJZ47989.1,
RC ECO:0000313|Proteomes:UP000190328};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUXI01000004; SJZ47989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4KZX2; -.
DR STRING; 263852.SAMN02745116_00457; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000190328; 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; IPR041663; DisA/LigA_HHH.
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; PF12826; HHH_2; 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:UP000190328};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 14..91
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 196..231
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 247..466
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 594 AA; 68196 MW; 73205D060F8E7D02 CRC64;
MNEKIKAKLT LLPDLPGCYL MKDKDGVIIY VGKAKILKNR VRSYFRGSHD TKTERLVSEI
EDFEIIVTES NIEALLLEIN LIKKNSPKYN IMLKDDKSYP FIKITNEKYP RLLITRKVLK
DNAAYFGPYP DVGAANETKR LLDRLFPLRK CNILPKEVCL YYHMKQCLAP CVFPVKERTY
KEMVAEIKAF LSGGHDKIQQ KLTKEMHIAS ENLEFEKAAE LRDKISSIET LMTNQKMTNA
DMKNRDVFGY HVDKGWMCVQ VFFIRQGKLI ERDVSIFPFY ADEEDDFLTF LGQFYQENEH
FIPSEIYLPT NIDLESAKEM LGTKIVQPKR SEKKKLVDLA MKNARVALSE KFSLIERRQE
RTIGATEALG VAMNIPTPRR IEAFDNSNIM GTNPVSAMVV FIDGKPMKKE YRKFKIKTVT
GPDDYASMRE VIYRRYSRVL KENLPLPDLI LIDGGIGQVN AAKEVLENQL GVDIVIAGLA
KDDKHKTSEL LFGETLSPVP LKRNSDEFFL LHRIQDEVHR FAITFHRQLR SKTSFSSRLD
GISGLGKKRK KLLMTTFKSL KNIREASVED IRAIGIPQAV AKSILEVLND EEKS
//
