ID   HEPA_EHV2               Reviewed;         706 AA.
AC   Q66643; Q66644;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 2.
DT   02-JUN-2021, entry version 60.
DE   RecName: Full=DNA helicase/primase complex-associated protein {ECO:0000255|HAMAP-Rule:MF_04010};
DE            Short=HEPA {ECO:0000255|HAMAP-Rule:MF_04010};
DE   AltName: Full=Primase-associated factor {ECO:0000255|HAMAP-Rule:MF_04010};
GN   Name=40;
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).
RN   [2]
RP   SEQUENCE REVISION.
RA   Davison A.J.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 presumably elongates
CC       using dNTPs. The primase-associated factor has no known catalytic
CC       activity in the complex and may serve to facilitate the formation of
CC       the replisome by directly interacting with the origin-binding protein
CC       and the polymerase. {ECO:0000255|HAMAP-Rule:MF_04010}.
CC   -!- SUBUNIT: Associates with the primase and the helicase to form the
CC       helicase-primase complex. Interacts with the origin-binding protein.
CC       Interacts with the polymerase catalytic subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_04010}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04010}.
CC   -!- SIMILARITY: Belongs to the herpesviridae HEPA family.
CC       {ECO:0000255|HAMAP-Rule:MF_04010}.
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DR   EMBL; U20824; AAC13828.2; -; Genomic_DNA.
DR   PIR; S55635; S55635.
DR   PIR; S55636; S55636.
DR   RefSeq; NP_042637.2; NC_001650.2.
DR   GeneID; 1461036; -.
DR   KEGG; vg:1461036; -.
DR   Proteomes; UP000007083; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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   HAMAP; MF_04010; HSV_HEPA; 1.
DR   InterPro; IPR008650; Helicase-primas_cplx_Herpesvir.
DR   InterPro; IPR004996; HSV_HEPA.
DR   Pfam; PF05774; Herpes_heli_pri; 1.
DR   Pfam; PF03324; Herpes_HEPA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; Helicase; Host nucleus; Hydrolase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..706
FT                   /note="DNA helicase/primase complex-associated protein"
FT                   /id="PRO_0000406027"
FT   REGION          203..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   706 AA;  76274 MW;  79FB2580AB28226E CRC64;
     MALSPVRVTE GKPLGVYFYN VWREARLVIW YVSYTPSGQT EALDFVFVVQ EVCDEKWSAL
     PASAGEASAF ESGIHTILWE RELRGHNEWI AALEGRGGEV FVFEADAGRV LTGLRVKGEE
     EGVGGGGGGG GEGEYSPETL RNAYFFSQSR QEFSSGRGGD AGREEAGAPV SGKEKLWFRG
     MVEDVCVSDV DIVIRTARGV YSCPGGDGGE EGDGAEGGDG GVGGAGDGAG AGGGSSGKPP
     AGKRGRPTRL RITDLFRPVD CELAWRGRAV KLRPVLADFD VMWANPESAW NCCLPEFFRA
     LLARTTRDFE GLPPALLYVF PAACREGSRF PPHFAGFPFF RVLFEPMRRV TADWLVAGDD
     RPPGGILLHH PPFYRSRLAD RVLCPGLRGD EIVRRARAGG GNCWPLFATE LNEGLCPEGR
     HDLLRVERAH ALLTLDLARA ACSMLGARVE NPGEFLARVV ETGSRDLLNA ATSAYNLLLT
     GVLRWAAEAG FAWAAIDKSR VFLVSEAEPP SEDAEEIEES LWASLGDHPP PCVGLVSGYG
     RENASVFLLW KSDRVLVGKS SDLSCPERRC GSWRESLDAA LSLTLTEAPD PAGILRELMP
     SYHAHRHETK FWLVDRAFAA GRPERAPPMP VDCLRPAPYL LIGEGAVCWH EALDLPLDVD
     FAAYLSETLS CVSAALAPPG GGGEAGEGRN NTDHCLEEFK SVLSLL