ID A0A0G0QD49_9BACT Unreviewed; 728 AA.
AC A0A0G0QD49;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=UT36_C0007G0040 {ECO:0000313|EMBL:KKR08365.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_39_17.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619067 {ECO:0000313|EMBL:KKR08365.1, ECO:0000313|Proteomes:UP000034818};
RN [1] {ECO:0000313|EMBL:KKR08365.1, ECO:0000313|Proteomes:UP000034818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR08365.1}.
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DR EMBL; LBWM01000007; KKR08365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0QD49; -.
DR STRING; 1619067.UT36_C0007G0040; -.
DR PATRIC; fig|1619067.4.peg.796; -.
DR Proteomes; UP000034818; 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:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; 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 CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 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; 2.
DR HAMAP; MF_00203; UvrC; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000305; GIY-YIG_endonuc.
DR InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR InterPro; IPR047296; GIY-YIG_UvrC_Cho.
DR InterPro; IPR000182; GNAT_dom.
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; PF13508; Acetyltransf_7; 1.
DR Pfam; PF01541; GIY-YIG; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF08459; UvrC_RNaseH_dom; 2.
DR SMART; SM00465; GIYc; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF46600; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF82771; GIY-YIG endonuclease; 1.
DR PROSITE; PS50164; GIY_YIG; 1.
DR PROSITE; PS51186; GNAT; 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 13..92
FT /note="GIY-YIG"
FT /evidence="ECO:0000259|PROSITE:PS50164"
FT DOMAIN 229..264
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT DOMAIN 280..506
FT /note="UvrC family homology region profile"
FT /evidence="ECO:0000259|PROSITE:PS50165"
FT DOMAIN 462..626
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 728 AA; 83087 MW; D67CE53EA22742D6 CRC64;
MSSFKSIIIN LPHSPGVYRF LDDKGGVLYV GKAIDLKKRV SSYFRKQKNQ PMRLQKLIEK
TVNIEYTVVD SELEALILET NLIKSYRPRY NILMKDDKNY VYLKITTNED YPRITVTRQV
ERDGARYFGP KASAGELYRT LKWLKKVFPY RHCGLDIRFK GDSTEPLRTG QPGEGGGPFK
VLVTHKVLKY PCIDYHIKRC VGPCIGTVTP EQYKKFILPI VHFFEGKTDE IVKDLKEKMQ
QAAFGKQFEK AARIRDQLLE MEHLMAPQRV SSPDGIDKDV IGLVTEGGMG YVSHFMFRAG
KLKSQENFIL NAVHLESGAE LEDAEILYAF VQQYYEKATD IPREVLLPEP FPQAKTIEEW
LTTLANHPVK FFHPKQGKSK ALIQLANDNA HSFAKKTQVS WQNKEGKGVE DALKGLQKIL
KLPKLPQRIE GYDISHLGGQ DTVGSMVVVE KGLPKKADYR HFKLRTVQER IDDYAAMNEV
LQRRLRYLEP ILSGMRKAKK KEIPQIEKIL TREKLDTDDL IPHKILIIEK RKKIVGIVRT
KPIEKDANEL ASLWVDPSCR GEGLARELVY AVMAKQRKGK LYVLPCQTLI DWYGSLGFHD
VKEIPKFFED KATRCVNACL IEKPVVMVYR FPKGEGDTSL TRKPHLIMVD GGKGQVSVAA
ATLKKAKLSI PLIGLAKKEE AIFMPGQSKP LILPKESAEL QLLQRLRDEA HRFALKYQQG
LRGERLKS
//
