ID   HELI_HHV6U              Reviewed;         824 AA.
AC   P52356;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=HDRF2, U77;
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=7941342; DOI=10.1006/viro.1994.1589;
RA   Nicholas J.;
RT   "Nucleotide sequence analysis of a 21-kbp region of the genome of human
RT   herpesvirus-6 containing homologues of human cytomegalovirus major
RT   immediate-early and replication genes.";
RL   Virology 204:738-750(1994).
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: 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; U13194; AAA68468.1; -; Genomic_DNA.
DR   EMBL; X83413; CAA58369.1; -; Genomic_DNA.
DR   RefSeq; NP_042970.1; NC_001664.2.
DR   PRIDE; P52356; -.
DR   GeneID; 1487959; -.
DR   KEGG; vg:1487959; -.
DR   Proteomes; UP000009295; 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_0000115849"
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;  93287 MW;  5A5507544E06184C CRC64;
     MSISSLFGGR YDNKFLLNMS SAPKIELIVD KVASLSERRL EGRLPEDWFR HIMDPETEFN
     SEFADALCIG IDEFAQPLPF LPFKALLVTG TAGAGKTNSI QTLAANLDCI VTATTSIAAQ
     NLSVVLNRSK SAQVKTIFKT FGFNSSHVSM SERQSYIAND ERSIQIQQKQ DLSIYWNVIS
     DIADRALGAV ACKTKELPDL CESSVIVIDE AGVILRHILH TVVFFYWFYN ALYKTPLYED
     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 LFIEKTSCDQ TIHAYSFLSG LMFGGMYSFC CSKFTTPEVL MEIKNIKMPS
     IEFLESEMSR MSPDVQTVET DERYDFGLVN DGLSDVDLLE IDPCGDPFFT RYSKLPLTNS
     LSFEEISLLY TTFKDIFISR FAILQKHTKG KFGKTLLVTY NRNNVSRKQC GEIYSHLKSF
     YGMLTYAIPA NNYTLEGYTN DNVVHLGTDK QLPQILYKKG LPRLVIKDEM GFISVLDNNV
     SKFIDVVNGQ SFHLCTTVDY ATVSKVSMTI TKSQGLSIQK VAIDFGSDPK NLKLSSIYVG
     MSRVTDPNNL IMNVNPLRLN YENDNFIAPH IVKALKNENT MLIF