ARN_BPT4
ID ARN_BPT4 Reviewed; 92 AA.
AC P39510;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Anti-restriction endonuclease;
DE AltName: Full=Anti-rgl nuclease;
GN Name=arn; Synonyms=asiA.1, motA.-6;
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 [GENOMIC DNA].
RC STRAIN=T4ALC10;
RX PubMed=9387160;
RA Kim B.C., Kim K., Park E.H., Lim C.J.;
RT "Nucleotide sequence and revised map location of the arn gene from
RT bacteriophage T4.";
RL Mol. Cells 7:694-696(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=768783; DOI=10.1038/260454a0;
RA Dharmalingam K., Goldberg E.B.;
RT "Phage-coded protein prevents restriction of unmodified progeny T4 DNA.";
RL Nature 260:454-456(1976).
RN [4]
RP FUNCTION.
RX PubMed=380146; DOI=10.1016/0042-6822(79)90098-9;
RA Dharmalingam K., Goldberg E.B.;
RT "Restriction in vivo. IV. Effect of restriction of parental DNA on the
RT expression of restriction alleviation systems in phage T4.";
RL Virology 96:404-411(1979).
CC -!- FUNCTION: Pays a role in the inhibition of the host restriction-
CC modification system. Strongly inhibits the host mcrA endonuclease that
CC cleaves 5-methyl and 5-hydroxymethylcytosines at the specific DNA
CC sequence C(me)CGG. {ECO:0000269|PubMed:380146,
CC ECO:0000269|PubMed:768783}.
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DR EMBL; L37801; AAA86440.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42538.1; -; Genomic_DNA.
DR RefSeq; NP_049868.1; NC_000866.4.
DR PDB; 3WX4; X-ray; 1.90 A; A=1-92.
DR PDBsum; 3WX4; -.
DR SMR; P39510; -.
DR GeneID; 1258794; -.
DR KEGG; vg:1258794; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Host-virus interaction; Hydrolase; Nuclease;
KW Reference proteome; Restriction-modification system evasion by virus.
FT CHAIN 1..92
FT /note="Anti-restriction endonuclease"
FT /id="PRO_0000164918"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:3WX4"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:3WX4"
FT HELIX 26..43
FT /evidence="ECO:0007829|PDB:3WX4"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:3WX4"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3WX4"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:3WX4"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:3WX4"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:3WX4"
SQ SEQUENCE 92 AA; 10900 MW; 6CFE8EB1711C657D CRC64;
MIIDSQSVVQ YTFKIDILEK LYKFLPNLYH SIVNELVEEL HLENNDFLIG TYKDLSKAGY
FYVIPAPGKN IDDVLKTIMI YVHDYEIEDY FE