ID   HEPA_EHV1V              Reviewed;         716 AA.
AC   Q6S6V0;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   12-AUG-2020, entry version 38.
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   OrderedLocusNames=54;
OS   Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=310273;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL   Submitted (NOV-2003) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS45938.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY464052; AAS45938.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_053098.2; NC_001491.2.
DR   GeneID; 2948558; -.
DR   KEGG; vg:2948558; -.
DR   Proteomes; UP000008296; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase 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; IPR004996; HSV_HEPA.
DR   Pfam; PF03324; Herpes_HEPA; 1.
PE   3: Inferred from homology;
KW   DNA replication; Host nucleus; Transferase.
FT   CHAIN           1..716
FT                   /note="DNA helicase/primase complex-associated protein"
FT                   /id="PRO_0000115860"
SQ   SEQUENCE   716 AA;  77773 MW;  62AB49A671C6B5F1 CRC64;
     MLCRRGSDYT AEFCHVPVSG ELLKRGARDA SLVTPARVAS AAQTAAVPGC WPLAPLGNAM
     LWKSVYGGIT AALKRAVGSF AFYQPLVLGI NTQTGLLVTL RPAASAGEGG GDHVSPRAAI
     VNVSVEVDLD PAGIEASAAS STGSSLARAR LCTLRDGYFL SKRDIALEVE IATKEVSFYR
     KYDSVQQPAN KRRGDMADLF VVHERTLLLG GCKRMGVKVL LPRTFDCLVA SSQSVSGLAA
     MALYKQWHAT LFSVELPDTV VQIFAYLGPE LNPCGEEVDY CCFVGFPGLP TLKASSSTTE
     AVRDAMAAYR LSDGLWPALG MSAFHFLAPW DPEDRWPGES EAKRVEGAVH RLQLGTEDDW
     GAGRVSCILE SDAVMQGPWF AKFDFSAFFP TLYLLLFPAN ERLAEVVRLR ARGQHPTLKL
     ALVSFFGGLQ HINPVAYRSI IALSNGISKR LEHEVNQRGF AICTYVKDGF WGAAGNLPSD
     SVSYADALVY AEELRSAAQK AALGHVSEMG FSLPEGVHLN LRLEGLFTDA ISWSTHCYWL
     YNRFTKMEDF VGFPAKSGAG RAAKASLSAL LPLVAAVCDS SDMSTLHQSV RGACEQLVAG
     AFAERNNPQF WSTRTGIESS TLLPPAVYRN GSLLDRDCGQ REIVLTRKHD CESPSPVPWT
     LFPPPLVLGR IDCMVYLTSI FKTYLSMLNR AISASCDADE SMNVDFPISD YAFLFT