ID   HEPA_HHV7J              Reviewed;         659 AA.
AC   P52376;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   23-FEB-2022, entry version 69.
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=U74;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(1996).
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; U43400; AAC54735.1; -; Genomic_DNA.
DR   PIR; T41975; T41975.
DR   RefSeq; YP_073814.1; NC_001716.2.
DR   SMR; P52376; -.
DR   PRIDE; P52376; -.
DR   DNASU; 3289532; -.
DR   GeneID; 3289532; -.
DR   KEGG; vg:3289532; -.
DR   Proteomes; UP000009246; 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..659
FT                   /note="DNA helicase/primase complex-associated protein"
FT                   /id="PRO_0000115863"
SQ   SEQUENCE   659 AA;  77028 MW;  4A59689522A42462 CRC64;
     MQMRGCVCHL GVYCVHNDWK NKQYRVPIYQ CLFFNAETHS LHTFLVIGNE ISENLLDKIS
     ISKEKIFMWD LNEQIMSITQ KTESICELMF GNKQIIQKLS RTFIFLTIIL NSNMYEIIDV
     CIDSNAVLYM PDLRPMIIRC VGNYSKISSE LLSDSDCTQA TKKMRFDYHV TNFCFSLNVN
     GKKVLFSSTE SSESILEKLL EFFTIQTYKL AEEQFLMVTP KNFFTVLFDE DMCLLLLQTV
     VSFLYDNLFR NKLVVKQVHD YIGPDLWPQG HERAVYFVGF PNMWFLSIYD LDNKIPCIKN
     ICNRILLYCG LPDSLGPDGC QSVPSTQCVD EFEDLPNLGA LQYLKYNSLV VTMETVENSE
     NVYYFFGEQD LFIVKLVDII QSLLELYVPK SFLPDFSDAY IKSEILLKFI SRLHKKSNNI
     FCKIVKKITE FLRCFLNACR LMDLNWMFIR NMHIVYFIGP KKDPSVVLPL LKTSVESCWK
     KILNSSRTPV VNINYIPGYN FLHSSCSFLT SGDINSEDSH WTITASKCLY NCLGASQITV
     DFKNIYTNFQ QMVSVFLSHR YENKYWIEYF EPNNYFLETH EGLLDCNRYT AVWTTENKLI
     RQSVGYPLTD KIDFIHYIQV VIEIFKKWLL TKYSQQEYAE TVRLGSKIIS DHLHLFNVN