ID   HEPA_HHV11              Reviewed;         750 AA.
AC   P10192; B9VQD5; Q09IC5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 89.
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 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2826807; DOI=10.1128/jvi.62.2.444-453.1988;
RA   McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P.,
RA   Challberg M.D.;
RT   "Structures of herpes simplex virus type 1 genes required for replication
RT   of virus DNA.";
RL   J. Virol. 62:444-453(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nonneuroinvasive mutant HF10;
RX   PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA   Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT   "Determination and analysis of the DNA sequence of highly attenuated herpes
RT   simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL   Microbes Infect. 9:142-149(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17 syn+;
RA   Cunningham C., Davison A.J.;
RT   "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH UL9, AND FUNCTION.
RX   PubMed=7931156; DOI=10.1099/0022-1317-75-10-2699;
RA   McLean G.W., Abbotts A.P., Parry M.E., Marsden H.S., Stow N.D.;
RT   "The herpes simplex virus type 1 origin-binding protein interacts
RT   specifically with the viral UL8 protein.";
RL   J. Gen. Virol. 75:2699-2706(1994).
RN   [6]
RP   INTERACTION WITH UL30, AND FUNCTION.
RX   PubMed=9261356; DOI=10.1128/jvi.71.9.6390-6397.1997;
RA   Marsden H.S., McLean G.W., Barnard E.C., Francis G.J., MacEachran K.,
RA   Murphy M., McVey G., Cross A., Abbotts A.P., Stow N.D.;
RT   "The catalytic subunit of the DNA polymerase of herpes simplex virus type 1
RT   interacts specifically with the C terminus of the UL8 component of the
RT   viral helicase-primase complex.";
RL   J. Virol. 71:6390-6397(1997).
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       ECO:0000269|PubMed:7931156, ECO:0000269|PubMed:9261356}.
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, ECO:0000269|PubMed:7931156, ECO:0000269|PubMed:9261356}.
CC   -!- INTERACTION:
CC       P10192; P04293: UL30; NbExp=4; IntAct=EBI-7185538, EBI-8615017;
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; X14112; CAA32344.1; -; Genomic_DNA.
DR   EMBL; AH002360; AAA45823.1; -; Genomic_DNA.
DR   EMBL; DQ889502; ABI63470.1; -; Genomic_DNA.
DR   EMBL; FJ593289; ACM62230.1; -; Genomic_DNA.
DR   PIR; C29890; WMBEX8.
DR   RefSeq; YP_009137082.1; NC_001806.2.
DR   BioGRID; 971456; 1.
DR   DIP; DIP-1097N; -.
DR   IntAct; P10192; 2.
DR   MINT; P10192; -.
DR   ChEMBL; CHEMBL4630721; -.
DR   GeneID; 2703432; -.
DR   KEGG; vg:2703432; -.
DR   Proteomes; UP000009294; Genome.
DR   Proteomes; UP000180652; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   DNA replication; Host nucleus; Reference proteome.
FT   CHAIN           1..750
FT                   /note="DNA helicase/primase complex-associated protein"
FT                   /id="PRO_0000115856"
FT   VARIANT         247
FT                   /note="T -> M (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         330
FT                   /note="A -> T (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         353
FT                   /note="A -> V (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         467
FT                   /note="N -> D (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         471
FT                   /note="A -> V (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         543..544
FT                   /note="AV -> GL (in strain: Nonneuroinvasive mutant HF10
FT                   and 17 syn+)"
FT   VARIANT         612
FT                   /note="C -> G (in strain: Nonneuroinvasive mutant HF10)"
SQ   SEQUENCE   750 AA;  79926 MW;  ECA9ABD0E85CB392 CRC64;
     MDTADIVWVE ESVSAITLYA VWLPPRAREY FHALVYFVCR NAAGEGRARF AEVSVTATEL
     RDFYGSADVS VQAVVAAARA ATTPAASPLE PLENPTLWRA LYACVLAALE RQTGPVALFA
     PLRIGSDPRT GLVVKVERAS WGPPAAPRAA LLVAEANIDI DPMALAARVA EHPDARLAWA
     RLAAIRDTPQ CASAASLTVN ITTGTALFAR EYQTLAFPPI KKEGAFGDLV EVCEVGLRPR
     GHPQRVTARV LLPRDYDYFV SAGEKFSAPA LVALFRQWHT TVHAAPGALA PVFAFLGPEF
     EVRGGPVPYF AVLGFPGWPT FTVPATAESA RDLVRGAAAA YAALLGAWPA VGARVVLPPR
     AWPGVASAAA GCLLPAVREA VARWHPATKI IQLLDPPAAV GPVWTARFCF PGLRAQLLAA
     LADLGGSGLA DPHGRTGLAR LDALVVAAPS EPWAGAVLER LVPDTCNACP ALRQLLGGVM
     AAVCLQIEET ASSVKFAVCG GDGGAFWGVF NVDPQDADAA SGVIEDARRA IETAVGAVLR
     ANAVRLRHPL CLALEGVYTH AVAWSQAGVW FWNSRDNTDH LGGFPLRGPA YTTAAGVVRD
     TLRRVLGLTT ACVPEEDALT ARGLMEDACD RLILDAFNKR LDAEYWSVRV SPFEASDPLP
     PTAFRGGALL DAEHYWRRVV RVCPGGGESV GVPVDLYPRP LVLPPVDCAH HLREILREIE
     LVFTGVLAGV WGEGGKFVYP FDDKMSFLFA
//