ID   AN_ALHV1                Reviewed;         485 AA.
AC   O36386;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   02-DEC-2020, entry version 68.
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   Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX   NCBI_TaxID=654901;
OH   NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA   Ensser A., Pflanz R., Fleckenstein B.;
RT   "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL   J. Virol. 71:6517-6525(1997).
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; AF005370; AAC58083.1; -; Genomic_DNA.
DR   PIR; T03131; T03131.
DR   RefSeq; NP_065535.1; NC_002531.1.
DR   SMR; O36386; -.
DR   PRIDE; O36386; -.
DR   GeneID; 911801; -.
DR   KEGG; vg:911801; -.
DR   Proteomes; UP000000941; 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..485
FT                   /note="Shutoff alkaline exonuclease"
FT                   /id="PRO_0000405695"
FT   SITE            178
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            216
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            239
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            241
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ   SEQUENCE   485 AA;  55605 MW;  C7BD602DD81CD388 CRC64;
     MDFLHKATLL EQTLNMEIGE QVKKLATYTF SNFIRCPEVQ QAIASGEIRN DMPHLRFVYI
     FYLFKKIQDF IGDTEVFGIY EKVMGVERAN SAKLVDVVQA CTEMRPHIQA QICEHIERLT
     RGQGENVLWE VLRDGVISSS KLLKFVKQQT PDSKIFNPIP IQKNHYVASP VAFGVRNETV
     VKKLISELVV EEGIGCVTEF GFMLSPNDGI FGVSLDMCTN ASMSDHNTVE FTSTTTIYEI
     KCRYKYLFSK CDYDPIYQAY QKLYNSPGRQ ELIDFIQSIQ KPTVEYVSRG RLPTQNDYLL
     SFDRSWDFGP PKRKRKLTSG HKITEQCMKY NCYTESKVII LTDPALTSGK IEVKGSFFVD
     IYINPRHAYY HQCMLQYKIV TNYVQLTKGD SCKHTHPGVF LVSAFFRKRN SADFPKTYIK
     TERSFVDASV EIPVLLIITP VFVPHGPLVD TLEQAIKFWQ VAVKEEFNHW PWAPTSLSAV
     GDVTP