CHO_SHIFL
ID CHO_SHIFL Reviewed; 295 AA.
AC P59361;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 25-MAY-2022, entry version 103.
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=SF1485, S1602;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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}.
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DR EMBL; AE005674; AAN43077.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16970.1; -; Genomic_DNA.
DR RefSeq; NP_707370.2; NC_004337.2.
DR RefSeq; WP_000252351.1; NZ_WPGN01000082.1.
DR AlphaFoldDB; P59361; -.
DR SMR; P59361; -.
DR STRING; 198214.SF1485; -.
DR EnsemblBacteria; AAN43077; AAN43077; SF1485.
DR EnsemblBacteria; AAP16970; AAP16970; S1602.
DR GeneID; 1024688; -.
DR KEGG; sfl:SF1485; -.
DR KEGG; sfx:S1602; -.
DR PATRIC; fig|198214.7.peg.1753; -.
DR HOGENOM; CLU_054721_1_0_6; -.
DR OMA; RVMSHFR; -.
DR OrthoDB; 1036075at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
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..295
FT /note="Excinuclease cho"
FT /id="PRO_0000138375"
FT DOMAIN 33..108
FT /note="GIY-YIG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00977"
SQ SEQUENCE 295 AA; 33706 MW; 875D7DF594EF4472 CRC64;
MVRRLTSPRL EFEAAAIYEY PEHLHSFLND LPTRPGVYLF HGESDTMPLY IGKSVNIRSR
VLSHLRTPDE AAMLRQSRRI SWICTAGEIG ALLLEARLIK EQQPLFNKRL RRNRQLCALQ
LNEKRVDVVY AKEVDFSRAP NLFGLFANRR AALQALQSIA DEQKLCYGLL GLEPLSRGRA
CFRSALKRCA GACCGKESHE EHALRLRQSL ERLRVVCWPW QGAVALKEQH PEMTQYHIIQ
NWLWLGAVNS LEEATTLIRT PAGFDHDGYK ILCKPLLSGN YEITELDPAN DQRAS
