ID   AN_EBVG                 Reviewed;         470 AA.
AC   Q3KSR5;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   23-FEB-2022, 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 GD1) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10376;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA   Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA   Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT   "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT   nasopharyngeal carcinoma patient.";
RL   J. Virol. 79:15323-15330(2005).
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}.
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       Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04009}.
CC   -!- SIMILARITY: Belongs to the herpesviridae alkaline nuclease family.
CC       {ECO:0000255|HAMAP-Rule:MF_04009}.
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DR   EMBL; AY961628; AAY41134.1; -; Genomic_DNA.
DR   SMR; Q3KSR5; -.
DR   IntAct; Q3KSR5; 6.
DR   MINT; Q3KSR5; -.
DR   Proteomes; UP000007641; 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; RNA-binding.
FT   CHAIN           1..470
FT                   /note="Shutoff alkaline exonuclease"
FT                   /id="PRO_0000375943"
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;  52683 MW;  967C00655D41CFC0 CRC64;
     MADVDELEDP MEEMTSYTFA RFLRSPETEA FVRNLDRPPQ MPAMRYVYLY CLCKQIQEFS
     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