ID UVRC_NAUPA Reviewed; 611 AA.
AC B9L9T8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=UvrABC system protein C {ECO:0000255|HAMAP-Rule:MF_00203};
DE Short=Protein UvrC {ECO:0000255|HAMAP-Rule:MF_00203};
DE AltName: Full=Excinuclease ABC subunit C {ECO:0000255|HAMAP-Rule:MF_00203};
GN Name=uvrC {ECO:0000255|HAMAP-Rule:MF_00203}; OrderedLocusNames=NAMH_0996;
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nautiliaceae; Nautilia.
OX NCBI_TaxID=598659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH;
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(2009).
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:0000255|HAMAP-
CC Rule:MF_00203}.
CC -!- SUBUNIT: Interacts with UvrB in an incision complex.
CC {ECO:0000255|HAMAP-Rule:MF_00203}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00203}.
CC -!- SIMILARITY: Belongs to the UvrC family. {ECO:0000255|HAMAP-
CC Rule:MF_00203}.
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DR EMBL; CP001279; ACM92603.1; -; Genomic_DNA.
DR RefSeq; WP_012663974.1; NC_012115.1.
DR AlphaFoldDB; B9L9T8; -.
DR SMR; B9L9T8; -.
DR STRING; 598659.NAMH_0996; -.
DR KEGG; nam:NAMH_0996; -.
DR eggNOG; COG0322; Bacteria.
DR HOGENOM; CLU_014841_3_2_7; -.
DR OrthoDB; 9804933at2; -.
DR Proteomes; UP000000448; Chromosome.
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; DNA damage; DNA excision; DNA repair; Excision nuclease;
KW SOS response.
FT CHAIN 1..611
FT /note="UvrABC system protein C"
FT /id="PRO_1000200595"
FT DOMAIN 12..96
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT DOMAIN 202..237
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
SQ SEQUENCE 611 AA; 70538 MW; 96ABE73323D9D6D6 CRC64;
MSFSEKIKSL PDQPGIYQYF DENGKLLYIG KAKSLKKRVK SYFRFNPFRP ADNLSPRIYK
MISEAKDLNY IVVESENDAL ILENSLIKQL KPKYNILLRD DKTYPYIYID LDEPFPMPQI
TRKVVKGKNI KYFGPFSSGA SAILKTIYEE IPLVQSKSCL RSGKACLYHQ IGRCLAPCEG
KVTSREYMKY VDQAIELIHD KEKILEILNQ KMQKYAENLQ FEEAAEIRDR IKSIESAEIY
SHVDLAKLED LDIFAVEIFN KKAVVIRIFV RQGKVVASSN SVINSQTVPE IGEIYTRAIL
EFYSTETPFT SSKILVGDDF EEREWLSQVL SEKFGKKISI ITPTTKERKS LIKLAKLNAL
EVIKNQKENT VLDELKILFN LQNTPYKIEV FDTSHMQGEA TVGAMVVWED GKFKKSDYRH
YHLEGKDEYS QMRELLTRRA QSFEKSPPPD LWLIDGGKAQ LNLAKEIIDS TGANIDVLAI
SKEKIDAKAH RAKGKAKDKI YFINEKLKVK SEKLNIDKLE LSQSDKRLQF LQMLRDEAHR
FAIEFHRKTK RKKDTQIDLL QVKGIGKAKM TKLLNYFGSF DNIKKASFDE LKDVLNEKDA
KAIKEFFKGQ K
//
