ID A0A1M6D4W5_9FLAO Unreviewed; 595 AA.
AC A0A1M6D4W5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN04487911_104163 {ECO:0000313|EMBL:SHI68307.1};
OS Arenibacter nanhaiticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=558155 {ECO:0000313|EMBL:SHI68307.1, ECO:0000313|Proteomes:UP000184231};
RN [1] {ECO:0000313|EMBL:SHI68307.1, ECO:0000313|Proteomes:UP000184231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8863 {ECO:0000313|EMBL:SHI68307.1,
RC ECO:0000313|Proteomes:UP000184231};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQYX01000004; SHI68307.1; -; Genomic_DNA.
DR RefSeq; WP_072763387.1; NZ_FQYX01000004.1.
DR AlphaFoldDB; A0A1M6D4W5; -.
DR STRING; 558155.SAMN04487911_104163; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000184231; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184231};
KW 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..472
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 595 AA; 69118 MW; 92D5C2FA234B69DD CRC64;
MTQIPIEVQL SSLPKNPGVY QFYDAEGKIL YVGKAKNLKK RVSSYFSKNH ESGKTRVLVK
KIRSIQHIVV PTESDALLLE NNLIKKYRPR YNVLLKDDKT YPWICIKKER FPRVFATRRL
VKDGSEYFGP YTSMKTLHTL LDLIKSVYPL RTCNYDLSKE KIDHGKYKVC LEYHLGNCKG
PCEDYQSEEE YNRQIQEIRE IVKGDFKASL HYFRGQMTSL AQEMKFEEAQ KIKEKIEVLE
NYQVKTTIVN PKINNVDVFS IISDEEYAYV NFLQLSHGSI IRSHTMEIKK KLEETEEELL
QLAIVEIRQR FQSLSRELYL PFPVSLPPEL KVTVPKLGDK KKILELSERN AKYFRQDRFK
QIKIIDPDRH TNRVMAQLKS DLRLSQEPRH IECFDNSNIQ GAFPVAACVV FKDGKPSKKD
YRHFNIKSVV GPDDFASMEE VVYRRYDRLL REGKDLPQLI VIDGGKGQLS SAVKSLDDLG
LRGKIAIIGI AKRLEEIYFP EDSIPLYLDK KSESLKIIQQ LRNEAHRFGI SFHRDKRSKA
AINSELESID GIGEKTVEDL LKYFKSVKRI KEASLENLIS IVGRSKAKKI YESFH
//
