ID   AN_HHV6U                Reviewed;         488 AA.
AC   P24447;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   23-FEB-2022, entry version 82.
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=16R;
OS   Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS   lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=10370;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2152817; DOI=10.1128/jvi.64.1.287-299.1990;
RA   Lawrence G.L., Chee M., Craxton M.A., Gompels U.A., Honess R.W.,
RA   Barrell B.G.;
RT   "Human herpesvirus 6 is closely related to human cytomegalovirus.";
RL   J. Virol. 64:287-299(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA   Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA   Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT   "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT   genome evolution.";
RL   Virology 209:29-51(1995).
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; X83413; CAA58362.1; -; Genomic_DNA.
DR   EMBL; M68963; AAA65578.1; -; Genomic_DNA.
DR   PIR; F36769; QQBEHS.
DR   RefSeq; NP_042963.1; NC_001664.2.
DR   SMR; P24447; -.
DR   PRIDE; P24447; -.
DR   GeneID; 1487951; -.
DR   KEGG; vg:1487951; -.
DR   Proteomes; UP000009295; 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_0000115694"
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;  56645 MW;  0F38A10597366A5B CRC64;
     MDLDQISETL SSVAEEEPLT MFLLDKLYAI REKIKQVPFS IVRLCHVYCM LIKYNASNNN
     CILGRKLIEE MQQFLCGTRV DGSEDISMDL SELCKLYDYC PLLCSALCRA PCVSVNKLFK
     IVERETRGQS ENPLWHALRK YTVTATKLYD IYTTRCFLEY KGQQFFGEAV IYGAKHERVI
     RHLVATFYVK REVKETLGLL LDPSSGVFGA SLDACFGISF NEDGFLMVKE KALIFEIKFK
     YKYLRDKEDH FVSELLKNPT EKSFSDFILS HPVPVIEFRE RGKIPSSREY LMTYDFQYRP
     QRKLRTCPTP AILAPHIKQL LCLNETQKST VIVFDCKSDL CEQKLSVFQK AVFTVNVFVN
     PKHRYFFQSL LQQYVMTQFY INDHNNPEYI ESTEVPSVHI VTAFFRRRTE EERSLHLVID
     ETEYIEEEIP LALIVTPVAP NPEFTCCVIT DICNLWENNI CKQTSLQVWA QSAVNQYLAA
     CVRKPKTP