ID E0Y102_9PROT Unreviewed; 625 AA.
AC E0Y102;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 48.
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};
OS uncultured alpha proteobacterium EB080_L27A02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; environmental samples.
OX NCBI_TaxID=710796 {ECO:0000313|EMBL:ADI20343.1};
RN [1] {ECO:0000313|EMBL:ADI20343.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x;
RA Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.;
RT "Time-series analyses of Monterey Bay coastal microbial picoplankton using
RT a 'genome proxy' microarray.";
RL Environ. Microbiol. 13:116-134(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; GU474940; ADI20343.1; -; Genomic_DNA.
DR AlphaFoldDB; E0Y102; -.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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 SMART; SM00278; HhH1; 2.
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 28..106
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 216..251
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 267..497
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
SQ SEQUENCE 625 AA; 69944 MW; 01F5E24D2748833F CRC64;
MSETNQQSKP NIIKGHEVIQ SYLKTLDGSP GVYRMLNQDG EVLYVGKARN LKRRVSSYAK
PTGHSARIGR MISNTSSMMF LTTQTETEAL LLEQNLIKQL KPRYNVLLRD DKSFPNIMIS
SSHEFPKIAK HRGRRSKGSE YFGPFASVTS VNRTLHHLQR IFLLRTCTDS DFSSRTRACL
QYQIARCSGP CVGKISSNNY NQLVDDARKF LQGKSTKIQE SMAKEMAEAS RDLQFEKAAS
LRDRIRALTN VQSSQGINPQ TVNEADIVSL YMEGDQACIQ VFFIRANQNW GNRAFYPRNT
SGADADEVME SFLAQFYDNK TPPKLILVSC TVSNLDLLVD ALSSKRGNKV EIIQPKRGER
AELVFNAERN ARESLARKMS ESATQAKLLK GVSDAFSLEN IPKRIEVYDN SHIQGAFAVG
AMIASGPDGY MKSSYRKYNI RYEDTVAGDD FGMMKEVLER RFKSLIKEDP DKKTENWPDL
LLIDGGAGQV SAVAEILTEL GINDVPFVGV AKGIDRDQGK EEFHCKGKPV FALQRNDPVL
YFIQRLRDEA HRFAITTHRA KRSKAIGITT LDEVPGVGAA RKRAILAHFG SAKSASRASL
KDLKAVEGLS SKMAQIIYDF YHDKG
//
