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