ID   AN_VZVO                 Reviewed;         551 AA.
AC   Q4JQS7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   23-FEB-2022, entry version 46.
DE   RecName: Full=Alkaline nuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN   ORFNames=ORF48;
OS   Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=341980;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC   Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA   Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT   "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT   its parental virus.";
RL   J. Virol. 76:11447-11459(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC   Oka varicella vaccine Varivax (V-Oka-Merk);
RX   PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA   Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA   Vassilev V.;
RT   "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL   J. Virol. 82:11023-11044(2008).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_04009}.
CC   -!- SUBUNIT: Interacts with major DNA-binding protein; this interaction
CC       increases the nuclease processivity of the alkaline exonuclease.
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; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ008354; AAY57657.1; -; Genomic_DNA.
DR   EMBL; DQ008355; AAY57728.1; -; Genomic_DNA.
DR   SMR; Q4JQS7; -.
DR   IntAct; Q4JQS7; 2.
DR   Proteomes; UP000002603; Genome.
DR   Proteomes; UP000008504; Genome.
DR   Proteomes; UP000008505; Genome.
DR   Proteomes; UP000008506; 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:0016032; P:viral process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.320.10; -; 1.
DR   HAMAP; MF_04009; HSV_AN; 1.
DR   InterPro; IPR001616; Herpes_alk_exo.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
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.
FT   CHAIN           1..551
FT                   /note="Alkaline nuclease"
FT                   /id="PRO_0000385137"
FT   SITE            188
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            260
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            286
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            288
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ   SEQUENCE   551 AA;  61252 MW;  B94D1A226AD42EDE CRC64;
     MARSGLDRID ISPQPAKKIA RVGGLQHPFV KTDINTINVE HHFIDTLQKT SPNMDCRGMT
     AGIFIRLSHM YKILTTLESP NDVTYTTPGS TNALFFKTST QPQEPHPEEL ASKLTQDDIK
     RILLTIESET RGQGDNAIWT LLRRNLITAS TLKWSVSGPV IPPQWFYHHN TTDTYGDAAA
     MAFGKTNEPA ARAIVEALFI DPADIRTPDH LTPEATTKFF NFDMLNTKSP SLLVGTPRIG
     TYECGLLIDV RTGLIGASLD VLVCDRDPLT GTLNPHPAET DISFFEIKCR AKYLFDPDDK
     NNPLGRTYTT LINRPTMANL RDFLYTIKNP CVSFFGPSAN PSTREALITD HVEWKRLGFK
     GGRALTELDA HHLGLNRTIS SRVWVFNDPD IQKGTITTIA WATGDTALQI PVFANPRHAN
     FKQIAVQTYV LSGYFPALKL RPFLVTFIGR VRRPHEVGVP LRVDTQAAAI YEYNWPTIPP
     HCAVPVIAVL TPIEVDVPRV TKILKDTGNN AITSALRSLR WDNLHPAVEE ESVDCANGTT
     SLLRATEKPL L