ID   HELI_EHV1B              Reviewed;         881 AA.
AC   P28934; Q6DLF4;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=57;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
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; AY665713; AAT67314.1; -; Genomic_DNA.
DR   PIR; C36801; WZBEE9.
DR   RefSeq; YP_053101.1; NC_001491.2.
DR   GeneID; 2948565; -.
DR   KEGG; vg:2948565; -.
DR   Proteomes; UP000001189; 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..881
FT                   /note="DNA replication helicase"
FT                   /id="PRO_0000115847"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         105..112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04030"
SQ   SEQUENCE   881 AA;  99453 MW;  F5590589DC492A48 CRC64;
     MESADILPGS RGTVDRRCEG SEEKITPPRP VEDFNPQLFP NEVYLNFTSM HGIQPVVARI
     RELSRKTVSA AMVPPLEWFE RLPRLETPLD IEPLHLPFSV YLISGNAGSG KSTCIQTLNE
     TMDCVITGAT RVAAQNVYTK LSSAFATRHI NTIFQEFGFR GNHVQAQLGK YQYSCSSSPP
     PIEELQKRDI VYYWEVLVDI TRRLFESTAS RGEFENIRAL ERLLGRAPGS LTRLAFCTNG
     SLPAFTRTNI VIIDEAGLLG RHLLTVVVYC WWMLNAAYKS PQYAEGKVPV IVCVGSPTQT
     DSLESRFEHK NLKCHVRSSE NVLTHIITNR TIREYVSLST NWAIFINNKR CQEYEFGELM
     KVLEYGLPIT EEHMRLVDTF VVPEAYINNP ANLPGWTRLY SSHKEVSAYM AKLHAHLKVS
     GERQFVVFTL PAYTFVKTAA FDEYKKITQQ PSLSLDKWLA ANASRVSNYS QSRDQDAGKT
     QCEYYSEHGV VVARTDVTYV LNSQVSVTTR MRKFVFGFSG TFETFDAVLK DDAFIKTQGE
     TSVEYAYRFL STLLFSGMIN FYNFLKRPGL DEGRVREAYR RMAALTAKLI PGASVLESAC
     DNPSGAPLNF RGLTDPPGFT GGTTNDWDDD NDVVFAALNE GAIDMLYCNY EFVRPETTQE
     VYSQFLMLKT MFVGRYSIFM DLFGGDFESS PFDTFVDNIS YKGCEIFVGS MRGGVSSIAL
     QTDSYTLMGY TSAPVYPFVE ELARRKLHEG IAELFGAMNM PRMVLRDQHG FMSVLNVNLS
     EFVESVDDVE LDMATAVDYG LSSKLAMTIA RSQGLSLDKV AICFPRNNLR INSVYVAMSR
     TVSSRFLRMN LNPLRERHER DTVISEHILA ALRDRDVQIV Y