ID   AN_EHV2                 Reviewed;         509 AA.
AC   Q66641;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-JUN-2021, entry version 70.
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   Name=37;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
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; U20824; AAC13825.1; -; Genomic_DNA.
DR   PIR; S55632; S55632.
DR   RefSeq; NP_042634.1; NC_001650.2.
DR   SMR; Q66641; -.
DR   GeneID; 1461042; -.
DR   KEGG; vg:1461042; -.
DR   Proteomes; UP000007083; 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..509
FT                   /note="Shutoff alkaline exonuclease"
FT                   /id="PRO_0000405985"
FT   REGION          90..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            207
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            244
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            267
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            269
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ   SEQUENCE   509 AA;  57577 MW;  F73DF3676DDE00F6 CRC64;
     MDFFSRVPLY DELSGLSQPE TKCKLEEFTF SNFLKARRVR EFLRAHAVAK LPAMRYVYVY
     YLFSRIGDYI GDDTVLAIFG EFMGVSDAGK ARGEGDGESD VHGEGEEEGD GGGEAEPGVG
     PDIPEVYRVC ECLPVRTKCR ISLAIEAITR GQYENNLWEI FRDGIISSSK FYHAVRQQNS
     SKKLFQPWPI VNNYYPLSPL AFGLRCEDAV KTLLAEFVCG RKEVMCDVGF LQSPKDGIFG
     VSLDMCANVS VGRDNLLEFR ADAEIYEIKC RFKYNYSKIE CDPLYQKYVS LYNSPSKTTL
     IRFLSGINRP AVEYVPPGKL PTKNDFLLTS DRDWDLSPKR KRNLTPAHKS LYDCLRANEH
     ASSQVLILSD PSETEGKIDI KARFDVDVFI NPEHSYFYQI LLQYKVVKNY IQYHSSPGLG
     SLKTFIVSGF FRKRNHSDPL ECSIGGRGTL DSACEIPVLL ILTPVYIPHC VVTESLKKAS
     QYWNQSAEEE FSHPPWVSSS LFADGDMTP