ID   EXRN_BPT7               Reviewed;         300 AA.
AC   P00638;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   02-DEC-2020, entry version 85.
DE   RecName: Full=Exonuclease;
DE   AltName: Full=Exonuclease gp6;
DE   AltName: Full=Gene product 6;
DE            Short=Gp6;
DE            EC=3.1.11.3;
GN   OrderedLocusNames=6;
OS   Escherichia phage T7 (Bacteriophage T7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX   NCBI_TaxID=10760;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA   Dunn J.J., Studier F.W.;
RT   "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT   T7 genetic elements.";
RL   J. Mol. Biol. 166:477-535(1983).
RN   [2]
RP   SEQUENCE REVISION.
RA   Dunn J.J.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=2170664; DOI=10.1016/s0022-2836(05)80347-x;
RA   Serwer P., Watson R.H., Son M.;
RT   "Role of gene 6 exonuclease in the replication and packaging of
RT   bacteriophage T7 DNA.";
RL   J. Mol. Biol. 215:287-299(1990).
RN   [4]
RP   FUNCTION IN PACKAGING.
RX   PubMed=1325707; DOI=10.1016/0042-6822(92)90920-k;
RA   Son M., Serwer P.;
RT   "Role of exonuclease in the specificity of bacteriophage T7 DNA
RT   packaging.";
RL   Virology 190:824-833(1992).
CC   -!- FUNCTION: Plays an essential role in phage DNA replication by
CC       participating in the removal of DNA-linked RNA primers. Participates
CC       also in T7 DNA packaging, host DNA degradation and phage genetic
CC       recombination. {ECO:0000269|PubMed:1325707,
CC       ECO:0000269|PubMed:2170664}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.11.3;
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DR   EMBL; V01146; CAA24418.1; -; Genomic_DNA.
DR   PIR; S42316; NDBPT7.
DR   RefSeq; NP_041988.1; NC_001604.1.
DR   GeneID; 1261052; -.
DR   KEGG; vg:1261052; -.
DR   Proteomes; UP000000840; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0099015; P:degradation of host chromosome by virus; IEA:UniProtKB-KW.
DR   GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
DR   GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
PE   1: Evidence at protein level;
KW   Bacterial host gene expression shutoff by virus;
KW   Degradation of host chromosome by virus; Exonuclease;
KW   Host gene expression shutoff by virus; Host-virus interaction; Hydrolase;
KW   Nuclease; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Exonuclease"
FT                   /id="PRO_0000106505"
SQ   SEQUENCE   300 AA;  34502 MW;  750BE36D527E31C4 CRC64;
     MALLDLKQFY ELREGCDDKG ILVMDGDWLV FQAMSAAEFD ASWEEEIWHR CCDHAKARQI
     LEDSIKSYET RKKAWAGAPI VLAFTDSVNW RKELVDPNYK ANRKAVKKPV GYFEFLDALF
     EREEFYCIRE PMLEGDDVMG VIASNPSAFG ARKAVIISCD KDFKTIPNCD FLWCTTGNIL
     TQTEESADWW HLFQTIKGDI TDGYSGIAGW GDTAEDFLNN PFITEPKTSV LKSGKNKGQE
     VTKWVKRDPE PHETLWDCIK SIGAKAGMTE EDIIKQGQMA RILRFNEYNF IDKEIYLWRP