ID F4MYE1_YEREN Unreviewed; 610 AA.
AC F4MYE1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
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 ECO:0000313|EMBL:CBX70849.1};
GN ORFNames=YEW_LK48450 {ECO:0000313|EMBL:CBX70849.1};
OS Yersinia enterocolitica W22703.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=913028 {ECO:0000313|EMBL:CBX70849.1};
RN [1] {ECO:0000313|EMBL:CBX70849.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21453472; DOI=10.1186/1471-2164-12-168;
RA Fuchs T.M., Brandt K., Starke M., Rattei T.;
RT "Shotgun sequencing of Yersinia enterocolitica strain W22703 (biotype 2,
RT serotype O:9): genomic evidence for oscillation between invertebrates and
RT mammals.";
RL BMC Genomics 12:168-168(2011).
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; FR718551; CBX70849.1; -; Genomic_DNA.
DR AlphaFoldDB; F4MYE1; -.
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};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00203}.
FT DOMAIN 16..94
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 204..239
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 254..479
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 610 AA; 68659 MW; 315F5D45E7CBCEDF CRC64;
MTDCFDSKEF LKTVTSQPGV YRMYDKAGTV IYVGKAKDLK KRLTSYFRAH VASRKTETLV
KNIAQIDVTV THTETEALLL EHNYIKLYQP RYNVLLRDDK SYPLIFLSAD KHPRLAIHRG
AKHEKGEYFG PFPNSYAVRE TLALLQKLFP VRQCENSVYR NRSRPCLQYQ IGRCSGPCVP
GLVSEEEYQR QVDYVRLFLS GKDQQVLTQL ISRMEEASRS LHFEDAARIR DQIQAVRRVT
EQQFVSGDSE DLDVIDVAFD AGLACVHVLF IRQGKVLGSR SYFPKVPAGT ELSEVVQTFV
GQFYLQGSQV RTLPGEILLD FTLAEKDLLA SSLSELAGRK IQIQSRPRGD RARYLKLART
NASTALVTRL SQQSTIHQRM KELAKILNLD EINRMECFDI SHTMGEQTVA SCVVFDANGP
VRSEYRRYNI SGITPGDDYA AMSQVLKRRY GKALDDKKIP DVIFIDGGKG QLSQAFDVFA
SLNVPWDKQK PLLVGVAKGS DRKAGLETLF LAAEGEGFSL PPDSPALHLI QHIRDDSHNH
AITGHRQRRS KVKNTSALEL IEGVGPKRRQ ILLKYMGGLQ PLLNASVEEI AKVPSISQAL
AEKIYNALKH
//
