ID   UVRC_SYNSC              Reviewed;         661 AA.
AC   Q3AJW5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 98.
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};
GN   OrderedLocusNames=Syncc9605_1363;
OS   Synechococcus sp. (strain CC9605).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=110662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9605;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9605.";
RL   Submitted (JUL-2005) 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: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; CP000110; ABB35117.1; -; Genomic_DNA.
DR   RefSeq; WP_011364335.1; NC_007516.1.
DR   AlphaFoldDB; Q3AJW5; -.
DR   SMR; Q3AJW5; -.
DR   STRING; 110662.Syncc9605_1363; -.
DR   EnsemblBacteria; ABB35117; ABB35117; Syncc9605_1363.
DR   KEGG; syd:Syncc9605_1363; -.
DR   eggNOG; COG0322; Bacteria.
DR   HOGENOM; CLU_014841_3_2_3; -.
DR   OMA; HIECFDN; -.
DR   OrthoDB; 1036075at2; -.
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   Gene3D; 3.30.420.340; -; 1.
DR   Gene3D; 3.40.1440.10; -; 1.
DR   HAMAP; MF_00203; UvrC; 1.
DR   InterPro; IPR041663; DisA/LigA_HHH.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
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   Pfam; PF01541; GIY-YIG; 1.
DR   Pfam; PF12826; HHH_2; 1.
DR   Pfam; PF02151; UVR; 1.
DR   Pfam; PF08459; UvrC_HhH_N; 1.
DR   SMART; SM00465; GIYc; 1.
DR   SMART; SM00278; HhH1; 2.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF82771; SSF82771; 1.
DR   TIGRFAMs; TIGR00194; uvrC; 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..661
FT                   /note="UvrABC system protein C"
FT                   /id="PRO_0000264963"
FT   DOMAIN          25..104
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   DOMAIN          214..249
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00203"
FT   REGION          636..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   661 AA;  75777 MW;  D998C660A9B3607F CRC64;
     MDAASGAPLL TQPERLERRL KEIPAEPGCY LMRDCDDRIL YVGKSKALRS RVRSYFRSRH
     DLSPRIRLMT RQVCEIEFIV TDSEAEALVL ESNLIKNHQP HFNVLLKDDK KYPYLCITWS
     EAYPRIFITR RRRFRSPLDR FYGPYVDVGL LRRTLFLVKR VFPLRQRPRP MYPDRTCLNY
     SIGRCPGVCQ EKISSVDYHR TLRKVAMVFQ GRSDELQHLL QEQMERYAER MDYESAARVR
     DQLQGLDQLT ADQKMSLPDS SVSRDVLALA FDERLAAVQL FQMRAGKLVG RLGYTADASG
     LEPGLILQRV IEEHYSQVDS VEVPPELLVQ HALPQQKLME DWLTEQRERR VQIHCPQRQQ
     KADLIELVQR NAEFELLRAK QGQEKQSLAT EDLAQLLELP TPPRRIEGYD ISHIQGSDAV
     ASQVVFIDGL PAKQHYRKYK IRSSSIRAGH SDDFMAMAEI MRRRFRRWAR AKAEGMDVGA
     LRHKGGSALQ TDGLNDWPDV VMIDGGKGQL SAVMEALREL DLHEDLNVCS LAKQREEVFL
     PGESQPLESE PDQLGVVLLR RLRDEAHRFA VSFHRQQRGE RMKRSRLSDI PGVGPKRVKD
     LLAHFHSIDA IQLASIETLS KAPGVGPALA RDIHDFFHPS DEGTDADARA ALEEQPQELS
     A