ID   END4_BPT4               Reviewed;         185 AA.
AC   P39250; D9IEV9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   23-FEB-2022, entry version 62.
DE   RecName: Full=Endonuclease IV {ECO:0000303|PubMed:16971463};
DE            EC=3.1.21.9 {ECO:0000269|PubMed:16971463};
DE   AltName: Full=Deoxyribonuclease IV;
GN   Name=denB;
GN   ORFNames=T4147_276 {ECO:0000312|EMBL:AHY83756.1},
GN   T4Tp278 {ECO:0000312|EMBL:ADJ39995.1},
GN   T4wild_276 {ECO:0000312|EMBL:AHY83560.1};
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21029436; DOI=10.1186/1743-422x-7-292;
RA   Petrov V.M., Ratnayaka S., Nolan J.M., Miller E.S., Karam J.D.;
RT   "Genomes of the T4-related bacteriophages as windows on microbial genome
RT   evolution.";
RL   Virol. J. 7:292-292(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=147 {ECO:0000312|EMBL:AHY83756.1}, and
RC   Wild {ECO:0000312|EMBL:AHY83560.1};
RX   PubMed=26081634; DOI=10.1128/mbio.00648-15;
RA   Bryson A.L., Hwang Y., Sherrill-Mix S., Wu G.D., Lewis J.D., Black L.,
RA   Clark T.A., Bushman F.D.;
RT   "Covalent Modification of Bacteriophage T4 DNA Inhibits CRISPR-Cas9.";
RL   MBio 6:E00648-E00648(2015).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16971463; DOI=10.1093/nar/gkl553;
RA   Hirano N., Ohshima H., Takahashi H.;
RT   "Biochemical analysis of the substrate specificity and sequence preference
RT   of endonuclease IV from bacteriophage T4, a dC-specific endonuclease
RT   implicated in restriction of dC-substituted T4 DNA synthesis.";
RL   Nucleic Acids Res. 34:4743-4751(2006).
RN   [5]
RP   FUNCTION.
RX   PubMed=17940096; DOI=10.1093/nar/gkm721;
RA   Ohshima H., Hirano N., Takahashi H.;
RT   "A hexanucleotide sequence (dC1-dC6 tract) restricts the dC-specific
RT   cleavage of single-stranded DNA by endonuclease IV of bacteriophage T4.";
RL   Nucleic Acids Res. 35:6681-6689(2007).
CC   -!- FUNCTION: Cleaves single-stranded DNA in a dC-specific manner. The
CC       cleavage occurs exclusively at the 5'-proximal position (dC1) within a
CC       dCs tract having a minimal size of 6 bases. These specific cleavages
CC       may have a detrimental effect on the replication of host dC-containing
CC       DNA. {ECO:0000269|PubMed:16971463, ECO:0000269|PubMed:17940096}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of the 5' phosphodiester bond of
CC         deoxycytidine in single-stranded DNA.; EC=3.1.21.9;
CC         Evidence={ECO:0000269|PubMed:16971463};
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DR   EMBL; AF158101; AAD42559.1; -; Genomic_DNA.
DR   EMBL; HM137666; ADJ39995.1; -; Genomic_DNA.
DR   EMBL; KJ477684; AHY83560.1; -; Genomic_DNA.
DR   EMBL; KJ477685; AHY83756.1; -; Genomic_DNA.
DR   RefSeq; NP_049887.1; NC_000866.4.
DR   SMR; P39250; -.
DR   GeneID; 1258726; -.
DR   KEGG; vg:1258726; -.
DR   Proteomes; UP000001092; Genome.
DR   Proteomes; UP000009087; Genome.
DR   Proteomes; UP000185270; Genome.
DR   Proteomes; UP000185271; Genome.
DR   GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Endonuclease; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..185
FT                   /note="Endonuclease IV"
FT                   /id="PRO_0000164933"
SQ   SEQUENCE   185 AA;  21161 MW;  65CBAD51F019058F CRC64;
     MQKTNPGLQR LFQIPTFTLS NSDLTCEMKV KIADTARYSL KQNPNQDKAE VIERCRIAVY
     AEFFVADWLS GYVNKGQEDV DDPYTYAWDV LAHPKYCGLR VEVKTHQTDS RWISVTTGCS
     GEYPYGSGIN LGPILNHQVA DCIIIFNTKE IHPGVIQYTP KFIGDREDLR KVVRKSNYNG
     WYLSI