ID   HEPA_VZVD               Reviewed;         771 AA.
AC   P09300;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-JUN-2021, entry version 66.
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   ORFNames=ORF52;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27935.1; -; Genomic_DNA.
DR   PIR; H27344; WZBE52.
DR   PRIDE; P09300; -.
DR   Proteomes; UP000002602; 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; Reference proteome; Transferase.
FT   CHAIN           1..771
FT                   /note="DNA helicase/primase complex-associated protein"
FT                   /id="PRO_0000115864"
SQ   SEQUENCE   771 AA;  86348 MW;  FAABCA800586CC5F CRC64;
     MDATQITLVR ESGHICAASI YTSWTQSGQL TQNGLSVLYY LLCKNSCGKY VPKFAEITVQ
     QEDLCRYSRH GGSVSAATFA SICRAASSAA LDAWPLEPLG NADTWRCLHG TALATLRRVL
     GFKSFYSPVT FETDTNTGLL LKTIPDEHAL NNDNTPSTGV LRANFPVAID VSAVSACNAH
     TQGTSLAYAR LTALKSNGDT QQQTPLDVEV ITPKAYIRRK YKSTFSPPIE REGQTSDLFN
     LEERRLVLSG NRAIVVRVLL PCYFDCLTTD STVTSSLSIL ATYRLWYAAA FGKPGVVRPI
     FAYLGPELNP KGEDRDYFCT VGFPGWTTLR TQTPAVESIR TATEMYMETD GLWPVTGIQA
     FHYLAPWGQH PPLPPRVQDL IGQIPQDTGH ADATVNWDAG RISTVFKQPV QLQDRWMAKF
     DFSAFFPTIY CAMFPMHFRL GKIVLARMRR GMGCLKPALV SFFGGLRHIL PSIYKAIIFI
     ANEISLCVEQ TALEQGFAIC TYIKDGFWGI FTDLHTRNVC SDQARCSALN LAATCERAVT
     GLLRIQLGLN FTPAMEPVLR VEGVYTHAFT WCTTGSWLWN LQTNTPPDLV GVPWRSQAAR
     DLKERLSGLL CTATKIRERI QENCIWDHVL YDIWAGQVVE AARKTYVDFF EHVFDRRYTP
     VYWSLQEQNS ETKAIPASYL TYGHMQDKDY KPRQIIMVRN PNPHGPPTVV YWELLPSCAC
     IPPIDCAAHL KPLIHTFVTI INHLLDAHND FSSPSLKFTD DPLASYNFLF L