ID   CHO_SALTY               Reviewed;         293 AA.
AC   Q8ZPU6;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Excinuclease cho;
DE            EC=3.1.25.-;
DE   AltName: Full=Endonuclease cho;
DE   AltName: Full=UvrC homolog protein;
GN   Name=cho; OrderedLocusNames=STM1309;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Incises the DNA at the 3' side of a lesion during nucleotide
CC       excision repair. Incises the DNA farther away from the lesion than
CC       UvrC. Not able to incise the 5' site of a lesion. When a lesion remains
CC       because UvrC is not able to induce the 3' incision, Cho incises the
CC       DNA. Then UvrC makes the 5' incision. The combined action of Cho and
CC       UvrC broadens the substrate range of nucleotide excision repair (By
CC       similarity). {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL20234.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL20234.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_460275.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZPU6; -.
DR   SMR; Q8ZPU6; -.
DR   STRING; 99287.STM1309; -.
DR   PaxDb; Q8ZPU6; -.
DR   EnsemblBacteria; AAL20234; AAL20234; STM1309.
DR   GeneID; 1252827; -.
DR   KEGG; stm:STM1309; -.
DR   PATRIC; fig|99287.12.peg.1391; -.
DR   HOGENOM; CLU_054721_1_0_6; -.
DR   OMA; RVMSHFR; -.
DR   PhylomeDB; Q8ZPU6; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0009380; C:excinuclease repair complex; IBA:GO_Central.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1440.10; -; 1.
DR   InterPro; IPR000305; GIY-YIG_endonuc.
DR   InterPro; IPR035901; GIY-YIG_endonuc_sf.
DR   SMART; SM00465; GIYc; 1.
DR   SUPFAM; SSF82771; SSF82771; 1.
DR   PROSITE; PS50164; GIY_YIG; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA excision; DNA repair; Excision nuclease; Hydrolase;
KW   Reference proteome; SOS response.
FT   CHAIN           1..293
FT                   /note="Excinuclease cho"
FT                   /id="PRO_0000138374"
FT   DOMAIN          33..108
FT                   /note="GIY-YIG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00977"
SQ   SEQUENCE   293 AA;  33363 MW;  F4222A2222A05656 CRC64;
     MVRRQSAPRL EFEAAAIYEY PEHLRPFLSE APALPGVYIF HSESDTLPLY IGKSVNIRSR
     VLSHLRTPDE ATMLRQARRI SWICTAGEMG ALLLEARLIK EQQPLFNKRL RRNRQLCSLQ
     LSEQKIEVVS ARSVDFSHEP NLFGLFANRR AALQSLQNLA DEQKLCYGLL GLEPVSRGRA
     CFRFALKRCA GACCGQETPQ AHFLRLQASL ERLRVVCWPW KGAIALKESR PQMTQFHIIN
     NWLWLGAVPS LDEAATLVRT PAGFDQDGYK ILCKPLMSGQ YEIIELHTDC RQS