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Database: UniProt
Entry: A0A0H2VXN2_SHIFL
LinkDB: A0A0H2VXN2_SHIFL
Original site: A0A0H2VXN2_SHIFL 
ID   A0A0H2VXN2_SHIFL        Unreviewed;       588 AA.
AC   A0A0H2VXN2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ECO:0000313|EMBL:AAN43507.2};
GN   OrderedLocusNames=SF1956 {ECO:0000313|EMBL:AAN43507.2};
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623 {ECO:0000313|EMBL:AAN43507.2, ECO:0000313|Proteomes:UP000001006};
RN   [1] {ECO:0000313|EMBL:AAN43507.2, ECO:0000313|Proteomes:UP000001006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
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}.
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DR   EMBL; AE005674; AAN43507.2; -; Genomic_DNA.
DR   RefSeq; NP_707800.4; NC_004337.2.
DR   AlphaFoldDB; A0A0H2VXN2; -.
DR   PaxDb; 198214-SF1956; -.
DR   GeneID; 1025141; -.
DR   KEGG; sfl:SF1956; -.
DR   PATRIC; fig|198214.7.peg.2335; -.
DR   HOGENOM; CLU_014841_3_2_6; -.
DR   Proteomes; UP000001006; 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; 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   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   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}; Reference proteome {ECO:0000313|Proteomes:UP000001006};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   Rule:MF_00203}.
FT   DOMAIN          1..72
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000259|PROSITE:PS50164"
FT   DOMAIN          182..217
FT                   /note="UVR"
FT                   /evidence="ECO:0000259|PROSITE:PS50151"
FT   DOMAIN          232..457
FT                   /note="UvrC family homology region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50165"
SQ   SEQUENCE   588 AA;  65663 MW;  222C6D9FDC93A9E7 CRC64;
     MYDAGGTVIY VGKAKDLKKR LSSYFRSNLA SRKTEALVAQ IQQIDVTVTH TETEALLLEH
     NYIKLYQPRY NVLLRDDKSY PFIFLSGDTH PRLAMHRGAK HAKGEYFGPF PNGYAVRETL
     ALLQKIFPIR QCENSVYRNR SRPCLQYQIG RCLGPCVEGL VSEEEYAQQV EYVRLFLSGK
     DDQVLTQLIS RMETASQNLE FEEAACIRDQ IQAVRRVTEK QFVSNTGDDL DVIGVAFDAG
     MACVHVLFIR QGKVLGSRSY FPKVPGGTEL SEVVETFVGQ FYLQGSQMRT LPGEILLDFN
     LSDKTLLADS LSELAGRKIN VQTKPRGDRA RYLKLARTNA ATALTSKLSQ QSTVHQRLTA
     LASVLKLPEV KRMECFDISH TMGEQTVASC VVFDANGPLR AEYRRYNITG ITPGDDYAAM
     NQVLRRRYGK AIDDSKIPDV ILIDGGKGQL AQAKNVFAEL DVSWDKNHPL LLGVAKGADR
     KAGLETLFFE PEGEGFSLPP DSPALHVIQH IRDESHDHAI GGHRKKRAKV KNTSSLETIE
     GVGPKRRQML LKYMGGLQGL RNASVEEIAK VPGISQGLAE KIFWSLKH
//
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