ID A0A087EEC7_9BIFI Unreviewed; 826 AA.
AC A0A087EEC7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=BITS_0992 {ECO:0000313|EMBL:KFJ06128.1};
OS Bifidobacterium tsurumiense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=356829 {ECO:0000313|EMBL:KFJ06128.1, ECO:0000313|Proteomes:UP000029080};
RN [1] {ECO:0000313|EMBL:KFJ06128.1, ECO:0000313|Proteomes:UP000029080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13495 {ECO:0000313|EMBL:KFJ06128.1,
RC ECO:0000313|Proteomes:UP000029080};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFJ06128.1}.
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DR EMBL; JGZU01000009; KFJ06128.1; -; Genomic_DNA.
DR RefSeq; WP_026641901.1; NZ_JGZU01000009.1.
DR AlphaFoldDB; A0A087EEC7; -.
DR STRING; 356829.BITS_0992; -.
DR eggNOG; COG0322; Bacteria.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000029080; 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}; Endonuclease {ECO:0000313|EMBL:KFJ06128.1};
KW Excision nuclease {ECO:0000256|ARBA:ARBA00022881, ECO:0000256|HAMAP-
KW Rule:MF_00203}; Hydrolase {ECO:0000313|EMBL:KFJ06128.1};
KW Nuclease {ECO:0000313|EMBL:KFJ06128.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029080};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00203}.
FT DOMAIN 62..141
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 255..290
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 306..587
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
FT REGION 23..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 92171 MW; 4D11984C818D4BB2 CRC64;
MAVFERHSPE VWRRTARLLQ DESTGASGSL AESDQSSVNA NGAPLLGDTR DLFRPKTSDI
PAQPGVYKWR DGDGRVIYVG KAKSLRNRLT NYFQPLNQLH PRTQTMVLTA RSLEWTVVGT
ELEALTLEYT WIKEFDPRFN VVFRDDKTYP YLAVSVGESV PRVWVTRSRK RRDSRYFGPY
AKVWNLRHSL DGLLKTFPVR TCSNGVFRKA QLTGRPCLLA SIGKCSAPCV GRISVKEHRA
QCERLVGVLT GRVGRSYIAQ LTRDMKAASA DLEFEKAAKL RDDIQMLQTV IEQNAVVFDQ
DVDADVFGID SDELEASVHA FFVRSGSIRG ERNWSVERVE DIEDSELMAD LIVQVYSDMM
GERQASDRPE QTEDTSYAHE EDVEDGQNRQ AIAIEERRDA LGVTQSLTAT DSISRAQATR
NRRERQEQTG RSDLLSPISP VPREVIVPIE PARKSELETL LSGMRGSAVT IRVASRGEKK
ALMDRANENA RQALQRSKMS RISDIGARTQ AMNDVAKALG LSQAPLRIEC YDISNTVAGA
FQVASMVVFE DGIAKKSEYR RFAIRGKDGK GAVDDLSALY ETLTRRFRHG NIAGDSGESM
DNERRAQQAQ HNQQAQQATT SPSSIADKPE PDGSAEQTKQ IEPTSQHPAQ QMPQEGIVQQ
HTNRRHFAYK PNLVVVDGGQ PQVMAAARAL ADSGVNDVAV CGLAKRLEEV WVPDDEYPII
LKRQSEGMYL LQRVRDESHR FAITYHRQTR RKGALRSALD DIPGIGEAYQ KRLLNAFGSV
RAMREASIEQ LESVKGVGHA KAESIYQALH SQDQPTNESP NSSPDA
//
