ID   HELI_HHV6Z              Reviewed;         824 AA.
AC   P52450;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=DNA replication helicase {ECO:0000255|HAMAP-Rule:MF_04030};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04030};
GN   Name=HELI {ECO:0000255|HAMAP-Rule:MF_04030}; OrderedLocusNames=CB4R, U77;
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: Component of the helicase/primase complex. Unwinds the DNA at
CC       the replication forks and generates single-stranded DNA for both
CC       leading and lagging strand synthesis. The primase synthesizes short RNA
CC       primers on the lagging strand that the polymerase elongates using
CC       dNTPs. Possesses helicase-like motifs and therefore may act as the
CC       helicase subunit of the complex. {ECO:0000255|HAMAP-Rule:MF_04030}.
CC   -!- SUBUNIT: Associates with the primase and the primase-associated factor
CC       to form the helicase-primase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_04030}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04030}.
CC   -!- SIMILARITY: Belongs to the herpesviridae helicase family.
CC       {ECO:0000255|HAMAP-Rule:MF_04030}.
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DR   EMBL; AF157706; AAB06360.1; -; Genomic_DNA.
DR   PIR; T44222; T44222.
DR   RefSeq; NP_050256.1; NC_000898.1.
DR   PRIDE; P52450; -.
DR   DNASU; 1497077; -.
DR   GeneID; 1497077; -.
DR   KEGG; vg:1497077; -.
DR   Proteomes; UP000006930; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_04030; HSV_HELI; 1.
DR   InterPro; IPR003840; DNA_helicase.
DR   InterPro; IPR034711; HSV_HELI.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02689; Herpes_Helicase; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; Helicase; Host nucleus; Hydrolase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..824
FT                   /note="DNA replication helicase"
FT                   /id="PRO_0000115850"
FT   BINDING         90..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ   SEQUENCE   824 AA;  93363 MW;  ABD0EF62BAA7FBA4 CRC64;
     MSISSLFGGR YDNKFLLNMS SAPKIELIVD KVASLSERRL EGRLPEDWFR HIMDPETEFN
     GEFADALCIG IDEFAQPLPF LPFKALLVTG TAGAGKTNSI QTLAANLDCI VTATTSIAAQ
     NLSVVLNRSK SAQVKTIFKT FGFNSSHVSM SERQSYIAND ERSIQIQQKQ DLSIYWNVIS
     DIAERALGAV ACKTKELPDL CESSVIVIDE AGVILRHILH TVVFFYWFYN ALYKTPLYEN
     GIVPCIVCVG SPTQSNALVT SFNPLTQNKD VKRGIDVLSA LICDDVLSKY CEVDNNWIIF
     VNNKRCADHA FGDFLKHIEF GLPLKPELIE YVDQFVKPAS YIRNPMNEIE TTRLFLSHNE
     VKNYFRSLHE QVEVTNRNNL FVFPVYFLIK NKTFEDYKSE IGNFSLEIEP WFKSNIHRLN
     TYSQFADQDL SKTVQLEEIV LEDGSVEETL ITCHLKHIRN SSIGVTSKIK ASTVGFSGTY
     EKFVELLQSD LFIEKTSCEQ TIHAYSFLSG LMFGGMYSFC CSEFTTPEVL MEIKNIKMPS
     IEFLESEMSR MSRDVQTVET DERYDFGLVD DGLSDMDLLE IDPCGDPFFT RYSKLPLTNS
     LSFEEISLLY TTFKDIFISR FAILQKHTKG KFGKTLLVTY NRNNVSRKQC GEIYSHLKSF
     YGMLTYAIPA NNYTLEGYTN DNVVHLGTDK QLPQILYKKG LPRLVIKDEM GFISVLDNNV
     SKFVDVVNGQ SFHLCTTVDY ATVSKVSMTI TKSQGLSIQK VAIDFGSDPK NLKLSSIYVG
     MSRVTDPNNL IMNVNPLRLN YENDNFIAPH IVKALKNENT MLIF