ID   HEPA_HHV2H              Reviewed;         752 AA.
AC   P89431;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   23-FEB-2022, entry version 62.
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=UL8;
OS   Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA   Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT   "The genome sequence of herpes simplex virus type 2.";
RL   J. Virol. 72:2010-2021(1998).
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; Z86099; CAB06768.1; -; Genomic_DNA.
DR   ChEMBL; CHEMBL4630722; -.
DR   PRIDE; P89431; -.
DR   Proteomes; UP000001874; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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.
FT   CHAIN           1..752
FT                   /note="DNA helicase/primase complex-associated protein"
FT                   /id="PRO_0000115857"
SQ   SEQUENCE   752 AA;  80027 MW;  8749B92360B58AD5 CRC64;
     MEAPGIVWVE ESVSAITLYA VWLPPRTRDC LHALLYLVCR DAAGEARARF AEVSVGSSDL
     QDFYGSPDVS APGAVAAARA ATAPAASPLE PLGDPTLWRA LYACVLAALE RQTGRWALFV
     PLRLGWDPQT GLVVRVERAS WGPPAAPRAA LLDVEAKVDV DPLALSARVA EHPGARLAWA
     RLAAIRDSPQ CASSASLAVT ITTRTARFAR EYTTLAFPPT RKEGAFADLV EVCEVGLRPR
     GHPQRVTARV LLPRGYDYFV SAGDGFSAPA LVALFRQWHT TVHAAPGALA PVFAFLGPGF
     EVRGGPVQYF AVLGFPGWPT FTVPAAAAAE SARDLVRGAA ATHAACLGAW PAVGARVVLP
     PRAWPAVASE AAGRLLPAFR EAVARWHPTA TTIQLLDPPA AVGPVWTARF CFSGLQAQLL
     AALAGLGEAG LPEARGRAGL ERLDALVAAA PSEPWARAVL ERLVPDACDA CPALRQLLGG
     VMAAVCLQIE QTASSVKFAV CGGTGAAFWG LFNVDPGDAD AAHGAIQDAR RALEASVRAV
     LSANGIRPRL APSLAPEGVY THVVTWSQTG AWFWNSRDDT DFLQGFPLRG AAYAAAAEVM
     RDALRRILRR PAAGPPEEAV CAARGVMEDA CDRFVLDAFG RRLDAEYWSV LTPPGEADDP
     LPQTAFRGGA LLDAEQYWRR VVRVCPGGGE SVGVPVDLYP RPLVLPPVDC AHHLREILRE
     IQLVFTGVLE GVWGEGGSFV YPFDEKIRFL FP