ID   AN_HHV2                 Reviewed;         620 AA.
AC   P06489; Q69352;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   23-FEB-2022, entry version 79.
DE   RecName: Full=Alkaline nuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN   ORFNames=UL12;
OS   Human herpesvirus 2 (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10310;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3005609; DOI=10.1128/jvi.57.3.1023-1036.1986;
RA   Draper K.G., Devi-Rao G., Costa R.H., Blair E.D., Thompson R.L.,
RA   Wagner E.K.;
RT   "Characterization of the genes encoding herpes simplex virus type 1 and
RT   type 2 alkaline exonucleases and overlapping proteins.";
RL   J. Virol. 57:1023-1036(1986).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA45835.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M11854; AAA45834.1; -; Genomic_DNA.
DR   EMBL; M11854; AAA45835.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_009137163.1; NC_001798.2.
DR   SMR; P06489; -.
DR   PRIDE; P06489; -.
DR   DNASU; 1487295; -.
DR   GeneID; 1487295; -.
DR   KEGG; vg:1487295; -.
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   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.
FT   CHAIN           1..620
FT                   /note="Alkaline nuclease"
FT                   /id="PRO_0000115691"
FT   REGION          1..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..59
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            270
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            330
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            354
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            356
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ   SEQUENCE   620 AA;  66200 MW;  3E4E89AC766414B7 CRC64;
     MAAAATPGAK RPADPARDPD SPPKRPRPNS LDLATVFGPR PAPPRPTSPG APGSHWPQSP
     PRGQPDGGAP GEKARPASPA LSEASSGPPT PDIPLSPGGA HAIDPDCSPG PPDPDPMWSA
     SAIPNALPPH ILAETFERHL RGLLRGVRSP LAIGPLWARL DYLCSLVVSL EAAGMVDRGL
     GRHLWRLTRR APPSAAEAVA PRPLMGFYEA ATQNQADCQL WALLRRGLTT ASTLRWGAQG
     PCFSSQWLTH NASLRLDAQS SAVMFGRVNE PTARNLLFRY CVGRADAGVN DDADAGRFVF
     HQPGDLAEEN VHACGVLMDG HTGMVGASLD ILVCPRDPHG YLAPAPQTPL AFYEVKCRAK
     YAFDPADPGA PAASAYEDLM ARRSPEAFRA FIRSIPNPGV RYFAPGRVPG PEEALVTQDR
     DWLDSRAAGE KRRCSAPDRA LVELNSGVVS EVLLFGVPDL ERRTISPVAW SSGELVRREP
     IFANPRHPNF KQILVQGYVL DSHFPDCPLQ PHLVTFLGRH RAGAEEGVTF RLEDGRGAPA
     GRGGAPGPAK ASILPDQAVP IALIITPVRV EPGIYRDIRR NSRLAFDDTL AKLWASRSPG
     RGPAAADTTS SPPTAGRSSR