ID A0A229W088_9BIFI Unreviewed; 751 AA.
AC A0A229W088;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=Tam10B_0288 {ECO:0000313|EMBL:OXN01287.1};
OS Bifidobacterium vansinderenii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1984871 {ECO:0000313|EMBL:OXN01287.1, ECO:0000313|Proteomes:UP000215433};
RN [1] {ECO:0000313|EMBL:OXN01287.1, ECO:0000313|Proteomes:UP000215433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tam10B {ECO:0000313|EMBL:OXN01287.1,
RC ECO:0000313|Proteomes:UP000215433};
RA Lugli G.A., Duranti S., Mangifesta M.;
RT "Bifidobacterium vansinderenii sp. nov.";
RL Submitted (MAY-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXN01287.1}.
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DR EMBL; NEWD01000004; OXN01287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229W088; -.
DR Proteomes; UP000215433; 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; 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 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}; SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 37..116
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 230..265
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 281..618
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
FT REGION 364..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 82843 MW; A6D00A7FFE3402C1 CRC64;
MGESGETTPG SAVNINGAPL LGDSRDLFRP KTGDIPAQPG VYKWRDGEGR VIYVGKAKNL
RNRLTNYFQP LYQLHPRTQT MVLTARSLEW TVVGTEIEAL TLEYTWIKEF DPRFNVVFRD
DKTYPYLALS INDEYPRVWI TRSRNRRGTR YFGPYAKVWE VRQSLDLLLK SFPVRTCTDS
AFRKARLTNR PCLLASIGKC SAPCVARIDA GEHRLMCERL VGVMTGRLGR SYVAQLTSEM
KAASAELEFE RAARLRDEIA VLNTVLQRNA VAFDSDVDAD VFGYDADELE ASVHAFFVRS
GAIRGERSWS VERVEDVDDA DLIADLVTQV YADVTGESPA GMDGAAPAGA VSVSRSRDAI
GSTQSVTAVD ASARAQATRS RNSRQEVTGR ADLLAPIAPV PREVIVPVEP SRREDLERWL
TGLRGSAVTI RVAARGEKKE LMDRATANAK QSLQRSKMSR IKDVGTRTEA MNDVARALGL
QRAPLRIECY DISNTVGGIY QVASMVVFED GIAKKSEYRR FAIRGKDGRG AVDDTTALYE
TLTRRFRHGN IAGDSGESMD NERRVAMDAG SHGLSGDADS TSVSSSDAVV QQNTDRRHFA
YKPNLIVVDG GQPQVEAAAR AMADCGVNDV ALCGLAKRLE EVWVPDDDYP IILKRQSEGM
YLLQRVRDES HRFAITYHRE ARTKGGLRSA LDAIPGIGLS HQKKLLQRFG SVKTMRGASI
EELMEVPGIG AKKAQAIYDA LHAEGHERAS S
//
