ID A0A1H1T2T0_9FLAO Unreviewed; 597 AA.
AC A0A1H1T2T0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=SAMN04489797_1834 {ECO:0000313|EMBL:SDS54461.1};
OS Winogradskyella sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1382466 {ECO:0000313|EMBL:SDS54461.1, ECO:0000313|Proteomes:UP000198963};
RN [1] {ECO:0000313|EMBL:SDS54461.1, ECO:0000313|Proteomes:UP000198963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA_55 {ECO:0000313|EMBL:SDS54461.1,
RC ECO:0000313|Proteomes:UP000198963};
RA Varghese N., Submissions S.;
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; LT629774; SDS54461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1T2T0; -.
DR STRING; 1249933.SAMN04489797_1834; -.
DR Proteomes; UP000198963; 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; 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; 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; 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; 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 15..93
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 262..476
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 597 AA; 69261 MW; 0D3DEA75839A7CC9 CRC64;
MPESTLDIQI KTLPHQPGVY QYFDADERLI YVGKAKDIKK RVSSYFTKHH DYGKTRVLVK
NIASVKHIVV ETENDALLLE NNLIKKYKPK YNVLLKDDKS YPWICIKKER FPRVFFTRRI
IKDGSEYFGP YTSMKTVKTL LGLIKGLYQL RTCNYDLSES KIEAGKYKVC LEYHLGNCKG
PCEGYETEEE YQANIVAIRE ILKGNFKDSL QQFRIQMRRH AEAMQFEDAQ KIKEKLEILE
NYQAKSTIVN PKISNVDVFS IVSDETYAYV NFLQLSYGSI IRSHTLELKK KLQETDAELL
ELAITEIRQR FNSNSREIYV PFEVNLGDDI KVTVPKLGDK RKILDLSIRN AKYFRMDKFK
QVKLVDPDRH ANRIMAQMKA DLRLSEEPRH IECFDNSNIQ GTNPVAACVV FKNGKPSKKD
YRHFNIKTVE GPDDFASMEE VVYRRYKRLL DEDEPLPQLI IIDGGKGQLS SALKSLDVLG
LRNEIAIIGI AKRLEELFYP DDPIPLYLDK KSETLKIIQH LRNEAHRFGI EHHRNRRSKG
ALTTELENIP GVGEQTIVDL MKQFKTVKRI ANAKLDELEA VIGVSRANKV YNYYHKD
//
