ID   HELI_EHV2               Reviewed;         789 AA.
AC   Q66647;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=44;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(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; U20824; AAC13832.1; -; Genomic_DNA.
DR   PIR; S55639; S55639.
DR   RefSeq; NP_042641.1; NC_001650.2.
DR   GeneID; 1461079; -.
DR   KEGG; vg:1461079; -.
DR   Proteomes; UP000007083; 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..789
FT                   /note="DNA replication helicase"
FT                   /id="PRO_0000406057"
FT   BINDING         64..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ   SEQUENCE   789 AA;  88369 MW;  DBB744F04A753382 CRC64;
     MEEPGAGFIL NMTSDSKVRA IVGRIRGLAA KTVPPPEMSW FDSQFDPEDA EGPFLPFSTF
     LITGTAGAGK STSISALYQS LNCLITGATA VAAQNLSNGL KTYCPTIYSA FGFKSRHINI
     LPRHGRNAPA RDMEGIQRNE LCKYWPVISD ILGEFTKKKQ RGQYEHLTGA AFGALAKMGT
     PTLWTTNIIV IDEAGTLSSH ILTAVVFLYW FYNSWLQTPL YKSGAVPCVV CVGSPTQTDA
     IQSTYNHSMQ KHHIQECDNI LTFLMKHEAV SRYVDLNHNW ALFINNKRCT DPEFGHLLKT
     LEYNLDISPR MVDYIDRFVV PKSKILSPLE YVGWTRLFVS HREVKAYLTA LHETLSLNQG
     GATAEADARL FTCPVVCEVF TDTFNEYREA VNLPGLTVTE WLQKNLCRLS NYSQFIDQDL
     SAVHIETGEE STKVTYLVKY VKNSYVSLNG KTKKCICGFM GTFEKFKTIL DNETFIDAHS
     HDQPEYVYSF LNTLLYNGMY AFHKHGLDAG DEGYLDALRR LPIPPNITHL STFQDALDQT
     EAALLNPESD IFYHMTCAPP SASSASLSTL ISFYMSLKSV FLQRLALAVS RFGRDFAERT
     FQTFTINMMI QNGVDFTSAS ERLFGLLGYA SNVDTYKLKG YTFIPVGFGR FNQAELSRDL
     RDKMPVVVVE DPHGFIACLE NNVNKMTEVM ENGDLIHICT AGDYGISSKL AMTIAKAQGM
     SLSRVAVCFG NSKFVRKSHV YVAISRATDP RHMVIDCNPL KNLEEDREDN KTSKYIVQAL
     NNPDTILVY