ID   AN_SHV21                Reviewed;         483 AA.
AC   Q01013;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-DEC-2020, entry version 65.
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   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
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; X64346; CAA45660.1; -; Genomic_DNA.
DR   RefSeq; NP_040239.1; NC_001350.1.
DR   SMR; Q01013; -.
DR   GeneID; 1682500; -.
DR   KEGG; vg:1682500; -.
DR   Proteomes; UP000000587; 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   Endonuclease; Exonuclease; Host cytoplasm; Host nucleus;
KW   Host-virus interaction; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..483
FT                   /note="Shutoff alkaline exonuclease"
FT                   /id="PRO_0000115698"
FT   SITE            180
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            218
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"
FT   SITE            243
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ   SEQUENCE   483 AA;  55555 MW;  36591840A4ABD567 CRC64;
     MDLFSEESPI NEIGNMDMTD QQTQLCSSSF SHFLKHPKVQ HFISTYSELV KMPTIRYVYF
     YYLFKKIGGF IGNEKIGTYF SKNVCNNIAA KGVPKLADVY KACEKMNLRQ QSEICLLIEE
     VTRGQYLNSL WDALRDGTIS SSKFYWATKK QNSTKKIFEP WPIKNDYYVA GPLAFGLRCE
     EVIKTVLNEL ICTPKQASCF DCGFMQSPLD GIFGVSLDYC TNVETNKDNL LVFHPDTEVY
     EIKSRFKYLF DKSECDTLYK KYKELYSNPC VKTLIKFIFS VSKPAIEFVP SGRLPSESDY
     LLAYDEEWNL RPTKKRKLNA SHEMIKKCIE YNSYAGSQIY ILSDPAENNG QITVKSKFKA
     GIFMNPRHTY FYQVALQHRV VQSYIGLSES PKSLGTQKNF IVSSFFRKRH FSDPPVCYVG
     KKQLEKTVEI PVFIIITPVY IPRSALLETI SQAVNFWEES AKEAFTEYPW APCALFANGD
     LTP