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HELI_EBVB9
ID   HELI_EBVB9              Reviewed;         809 AA.
AC   P03214;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 86.
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}; ORFNames=BBLF4;
OS   Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10377;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6087149; DOI=10.1038/310207a0;
RA   Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA   Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA   Tuffnell P.S., Barrell B.G.;
RT   "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL   Nature 310:207-211(1984).
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; V01555; CAA24821.1; -; Genomic_DNA.
DR   PIR; F43043; QQBE34.
DR   RefSeq; YP_401681.1; NC_007605.1.
DR   BioGRID; 971727; 1.
DR   IntAct; P03214; 1.
DR   MINT; P03214; -.
DR   PRIDE; P03214; -.
DR   DNASU; 3783685; -.
DR   GeneID; 3783685; -.
DR   KEGG; vg:3783685; -.
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; IDA:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
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.
FT   CHAIN           1..809
FT                   /note="DNA replication helicase"
FT                   /id="PRO_0000115854"
FT   BINDING         72..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ   SEQUENCE   809 AA;  89853 MW;  434AA6EDAC01CC50 CRC64;
     MAEEPRAPEA LSSTFMLNMT SDASVRRIVR RIGTLARRRV QQLPDMETFS PEFDPELSEP
     PFLPFSAYVI TGTAGAGKST SVSCLHHTMD CLVTGATTVA AQNLSQTLRA YCPTVYSAFG
     FKSRHINMTQ RVSSHGRSTD AALEELQRRD LAKYWPVLSD IAAEFRRTKP RGLYSGVSGP
     AFEVLRDMHQ GQLWTTNVIV VDEAGTLSVH ILTAVVFCYW FFNAWLRTPL YRRGRIPCIV
     CVGSPTQTDA FQSSFSHETQ VNKIRECDNI LTFLVGNPRA ATYVDVARNW ALFINNKRCT
     DVQFGHLMKT LEYGLELSPD ILAYVDRFVV PRAAIMDPAQ YVGWTRLFLS HAEVKTFLTT
     LHATLKTAGQ GRAARGTGGD GGGVTMFTCP VECEVFLDPL AQYKTLVGLP GLTAHTWLQK
     NYARLGNYSQ FADQDMVPVG TEQDEERVKV TYNVTYVKHS SVSVNCKTKK SICGYTGTFG
     DFMDTLEADS FVEAHGHEQP EYVYSFLARL IYGGIYAFSH GGHSLCENGE YVAELGAVPL
     PGRTWDPEVT AGMELGELPL EVAWDGERSP AAVFYARVLA PPAANSAPLC SLLNIYNDLR
     AYFRQCLDVA VRYGGREFRD LPFCTFTNNM LIRDNIEFTS DEPLLHGLLD YASTTENYTL
     LGYTHLNVFF GIRGKQQPQD AGSSRMPRLM VKDEAGFVCC LEHNTNKLYE TIEDKSLNLC
     SIRDYGISSK LAMTIAKAQG LSLNKVAICF GSHRNIKPGH VYVALSRARH SNCVVMDRNP
     LSEMITGEGN PASGYIVDAL KNSRALLVY
 
 
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