AN_EBVA8
ID AN_EBVA8 Reviewed; 470 AA.
AC Q1HVE7;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 02-JUN-2021, entry version 53.
DE RecName: Full=Shutoff alkaline exonuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE Short=SOX {ECO:0000255|HAMAP-Rule:MF_04009};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN ORFNames=BGLF5;
OS Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=82830;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT "The genome of Epstein-Barr virus type 2 strain AG876.";
RL Virology 350:164-170(2006).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17360652; DOI=10.1073/pnas.0611128104;
RA Rowe M., Glaunsinger B., van Leeuwen D., Zuo J., Sweetman D., Ganem D.,
RA Middeldorp J., Wiertz E.J., Ressing M.E.;
RT "Host shutoff during productive Epstein-Barr virus infection is mediated by
RT BGLF5 and may contribute to immune evasion.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3366-3371(2007).
CC -!- FUNCTION: Plays a role in processing non linear or branched viral DNA
CC intermediates in order to promote the production of mature packaged
CC unit-length linear progeny viral DNA molecules. Exhibits endonuclease
CC and exonuclease activities and accepts both double-stranded and single-
CC stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'->
CC 3' direction and the products are 5'-monophosphate nucleosides.
CC Additionally, forms a recombinase with the major DNA-binding protein,
CC which displays strand exchange activity. Also acts as a cytoplasmic RNA
CC endonuclease that induces degradation of the majority of the cellular
CC messenger RNAs during early lytic infection. The resulting inhibition
CC of cellular protein synthesis serves to ensure maximal viral gene
CC expression and evasion from host immune response. Internally cleaves
CC host mRNAs which are then degraded by the cellular exonuclease XRN1.
CC Bypasses therefore the regulatory steps of deadenylation and decapping
CC normally required for XRN1 activation. {ECO:0000255|HAMAP-
CC Rule:MF_04009, ECO:0000269|PubMed:17360652}.
CC -!- SUBUNIT: Forms a complex with the DNA polymerase, the DNA polymerase
CC processivity factor, and the major DNA binding protein.
CC {ECO:0000255|HAMAP-Rule:MF_04009}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04009,
CC ECO:0000269|PubMed:17360652}. Host cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_04009, ECO:0000269|PubMed:17360652}.
CC -!- SIMILARITY: Belongs to the herpesviridae alkaline nuclease family.
CC {ECO:0000255|HAMAP-Rule:MF_04009}.
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; DQ279927; ABB89261.1; -; Genomic_DNA.
DR RefSeq; YP_001129481.1; NC_009334.1.
DR SMR; Q1HVE7; -.
DR PRIDE; Q1HVE7; -.
DR GeneID; 5176208; -.
DR KEGG; vg:5176208; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039595; P:induction by virus of catabolism of host mRNA; IEA:UniProtKB-UniRule.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04009; HSV_AN; 1.
DR InterPro; IPR001616; Herpes_alk_exo.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR034720; Viral_alk_exo.
DR Pfam; PF01771; Viral_alk_exo; 1.
DR PRINTS; PR00924; ALKEXNUCLASE.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 3: Inferred from homology;
KW Decay of host mRNAs by virus; Early protein; Endonuclease;
KW Eukaryotic host gene expression shutoff by virus; Exonuclease;
KW Host cytoplasm; Host gene expression shutoff by virus;
KW Host mRNA suppression by virus; Host nucleus; Host-virus interaction;
KW Hydrolase; Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..470
FT /note="Shutoff alkaline exonuclease"
FT /id="PRO_0000375944"
FT SITE 166
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 203
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 225
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT SITE 227
FT /note="Required for function"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ SEQUENCE 470 AA; 52684 MW; 89199758CDB54227 CRC64;
MADVDELEDP MEEMTSYTFA RFLRSPETEA FVRNLDRPPQ MPAMRYVYLY CLCEQIQEFS
GETGFCDFVS SLVQENDSQD GPSLKSIYWG LQEATDEQRT VLCSYVESMT RGQSENLMWD
ILRNGIISSS KLLSTIKNGP TKVFEPAPIS TNHYFGGPVA FGLRCEDTVK DIVCKLICGD
ASANRQFGFM ISPTDGIFGV SLDLCVNVES QGDFILFTDR SCIYEIKCRF KYLFSKSEFD
PIYPSYTALY KRPCKRSFIR FINSIARPTV EYVPDGRLPS EGDYLLTQDE AWNLKDVRKR
KLGPGHDLVA DSLAANRGVE SMLYVMTDPS ENAGRIGIKD RVPVNIFINP RHNYFYQVLL
QYKIVGDYVR HSGGGKPGRD CSPRVNIVTA FFRKRSPLDP ATCTLGSDLL LDASVEIPVA
VLVTPVVLPD SVIRKTLSTA AGSWKAYADN TFDTAPWVPS GLFADDESTP
