ID   AN_HHV6Z                Reviewed;         488 AA.
AC   P52448;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   23-FEB-2022, entry version 78.
DE   RecName: Full=Alkaline nuclease {ECO:0000255|HAMAP-Rule:MF_04009};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04009};
GN   Name=U70; Synonyms=CH3R;
OS   Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=36351;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8634027; DOI=10.1007/bf01718406;
RA   Lindquester G.J., Inoue N., Allen R.D., Castelli J.W., Stamey F.R.,
RA   Dambaugh T.R., O'Brian J.J., Danovich R.M., Frenkel N., Pellett P.E.;
RT   "Restriction endonuclease mapping and molecular cloning of the human
RT   herpesvirus 6 variant B strain Z29 genome.";
RL   Arch. Virol. 141:367-379(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA   Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA   Pellett P.E.;
RT   "Human herpesvirus 6B genome sequence: coding content and comparison with
RT   human herpesvirus 6A.";
RL   J. Virol. 73:8040-8052(1999).
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; AF157706; AAB06353.1; -; Genomic_DNA.
DR   PIR; T44215; T44215.
DR   RefSeq; NP_050249.1; NC_000898.1.
DR   SMR; P52448; -.
DR   PRIDE; P52448; -.
DR   DNASU; 1497070; -.
DR   GeneID; 1497070; -.
DR   KEGG; vg:1497070; -.
DR   Proteomes; UP000006930; 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; Reference proteome.
FT   CHAIN           1..488
FT                   /note="Alkaline nuclease"
FT                   /id="PRO_0000115695"
FT   SITE            177
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            213
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            236
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
FT   SITE            238
FT                   /note="Required for function"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04009"
SQ   SEQUENCE   488 AA;  56688 MW;  AE2872028D4B3D90 CRC64;
     MDLNQISETL SAVAEEEPLT MFLLDKLYAI REKIKQVPFS IVRLCHVYCM LIKYNASNNN
     CILGRKLIEE MQQFLCGARV DGSEDVSMDM SELCKLYDYC PLLCSALCRA PCVFVNKLFK
     IVERETRGQS ENPLWHALRR YTVTATKLYD IYTTRNFLEH KGQQFFGEAV IYGAKHERVI
     RHLVAIFYVK REVKETLGLL LDPSSGVFGA SLDACFGISF NEDGFLMVKE KALIFEIKFR
     YKYLRDKEDH FVSELLKNPT EKSFSDFILS HPVPAIEFRE RGKIPSSREY LMTYDFQYRP
     QRKLRTCPTP AILTPHIKQL LCLNETQTST VIVFDCKSHL SEQKLSVFQK AVFTVNVFVN
     PKHRYFFQSL LQQYVMTQFY INDHSNPEYI ESTEVPSVHI VTALFRRRTE EERSLHLVID
     ETEYIEEEIP LALIVTPVAP NPEFTCRVIT DICNLWENNI CKQTSLQVWA QSAVNQYLAA
     CVRKPKTP