ID   AN_HCMVA                Reviewed;         584 AA.
AC   P16789; Q7M6J3;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   23-FEB-2022, entry version 83.
DE   RecName: Full=Alkaline nuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN   Name=UL98;
OS   Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=10360;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA   Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA   Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA   Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT   "Analysis of the protein-coding content of the sequence of human
RT   cytomegalovirus strain AD169.";
RL   Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 465-584.
RX   PubMed=2535729; DOI=10.1128/jvi.63.1.233-241.1989;
RA   Martinez J., Lahijani R.S., St Jeor S.C.;
RT   "Analysis of a region of the human cytomegalovirus (AD169) genome coding
RT   for a 25-kilodalton virion protein.";
RL   J. Virol. 63:233-241(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 465-584.
RX   PubMed=1845897; DOI=10.1128/jvi.65.1.373-381.1991;
RA   Lahijani R.S., Otteson E.W., Adlish J.D., St Jeor S.C.;
RT   "Characterization of a human cytomegalovirus 1.6-kilobase late mRNA and
RT   identification of its putative protein product.";
RL   J. Virol. 65:373-381(1991).
RN   [4]
RP   GENOME REANNOTATION.
RX   PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA   McGeoch D.J., Hayward G.S.;
RT   "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT   cytomegalovirus genome.";
RL   J. Gen. Virol. 84:17-28(2003).
RN   [5]
RP   ERRATUM OF PUBMED:12533697.
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA   McGeoch D.J., Hayward G.S.;
RL   J. Gen. Virol. 84:1053-1053(2003).
RN   [6]
RP   SEQUENCE REVISION TO 407.
RA   Davison A.J.;
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   EARLY PROTEIN.
RX   PubMed=7636973; DOI=10.1128/jvi.69.9.5304-5310.1995;
RA   Adam B.L., Jervey T.Y., Kohler C.P., Wright G.L. Jr., Nelson J.A.,
RA   Stenberg R.M.;
RT   "The human cytomegalovirus UL98 gene transcription unit overlaps with the
RT   pp28 true late gene (UL99) and encodes a 58-kilodalton early protein.";
RL   J. Virol. 69:5304-5310(1995).
RN   [8]
RP   FUNCTION.
RX   PubMed=9367383; DOI=10.1099/0022-1317-78-11-2953;
RA   Sheaffer A.K., Weinheimer S.P., Tenney D.J.;
RT   "The human cytomegalovirus UL98 gene encodes the conserved herpesvirus
RT   alkaline nuclease.";
RL   J. Gen. Virol. 78:2953-2961(1997).
RN   [9]
RP   FUNCTION.
RX   PubMed=9791036; DOI=10.1006/viro.1998.9344;
RA   Gao M., Robertson B.J., McCann P.J., O'Boyle D.R., Weller S.K.,
RA   Newcomb W.W., Brown J.C., Weinheimer S.P.;
RT   "Functional conservations of the alkaline nuclease of herpes simplex type 1
RT   and human cytomegalovirus.";
RL   Virology 249:460-470(1998).
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, ECO:0000269|PubMed:9367383, ECO:0000269|PubMed:9791036}.
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; X17403; CAA35334.1; -; Genomic_DNA.
DR   EMBL; M62615; AAA45905.1; -; Genomic_DNA.
DR   EMBL; BK000394; DAA00195.2; -; Genomic_DNA.
DR   PIR; S09863; QQBEJ6.
DR   SMR; P16789; -.
DR   PRIDE; P16789; -.
DR   Proteomes; UP000008991; Genome.
DR   Proteomes; UP000008992; 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   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..584
FT                   /note="Alkaline nuclease"
FT                   /id="PRO_0000115701"
FT   REGION          409..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            216
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            254
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            278
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            280
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ   SEQUENCE   584 AA;  65286 MW;  0E8341FB41FC2802 CRC64;
     MWGVSSLDYD DDEELTRLLA VWDDEPLSLF LMNTFLLHQE GFRNLPFTVL RLSYAYRIFA
     KMLRAHGTPV AEDFMTRVAA LARDEGLRDI LGQRHAAEAS RAEIAEALER VAERCDDRHG
     GSDDYVWLSR LLDLAPNYRQ VELFQLLEKE SRGQSRNSVW HLLRMDTVSA TKFYEAFVSG
     CLPGAAAADG SGGGGSHYTG SRAGVSPGIQ FGIKHEGLVK TLVECYVMHG REPVRDGLGL
     LIDPTSGLLG ASMDLCFGVL KQGSGRTLLV EPCARVYEIK CRYKYLRKKE DPFVQNVLRR
     HDAAAVASLL QSHPVPGVEF RGERETPSAR EFLLSHDAAL FRATLKRARP LKPPEPLREY
     LADLLYLNKA ECSEVIVFDA KHLSDDNSDG DATITINASL GLAAGDAAGG GADHHLRGSP
     GDSPPPIPFE DENTPELLGR LNVYEVARFS LPAFVNPRHQ YYFQMLIQQY VLSQYYIKKH
     PDPERIDFRD LPTVYLVSAI FREREESELG CELLAGGRVF HCDHIPLLLI VTPVVFDPQF
     TRHAVSTVLD RWSRDLSRKT NLPIWVPNSA NEYVVSSVPR PVSP