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 10-JUN-2026, entry version 94. 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 Autographivirales; Autotranscriptaviridae; Studiervirinae; Teseptimavirus; OC Teseptimavirus T7. 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; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 OrthoDB; 6588at10239; -. DR Proteomes; UP000000840; Segment. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0051908; F:double-stranded DNA 5'-3' DNA exonuclease activity; IEA:UniProtKB-EC. 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:0039657; P:symbiont-mediated suppression of host gene expression; IEA:UniProtKB-KW. DR FunFam; 3.40.50.1010:FF:000085; Exonuclease; 1. DR Gene3D; 3.40.50.1010; 5'-nuclease; 1. 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; PIN domain-like; 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 //