ID   HEPA_HHV8P              Reviewed;         669 AA.
AC   Q2HR92;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   02-JUN-2021, entry version 48.
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=ORF40;
OS   Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS   sarcoma-associated herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=868565;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA   Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT   "Identification of a spliced gene from Kaposi's sarcoma-associated
RT   herpesvirus encoding a protein with similarities to latent membrane
RT   proteins 1 and 2A of Epstein-Barr virus.";
RL   J. Virol. 73:6953-6963(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA   Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT   "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL   J. Gen. Virol. 87:1781-1804(2006).
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; AF148805; ABD28891.1; -; Genomic_DNA.
DR   RefSeq; YP_001129393.1; NC_009333.1.
DR   PRIDE; Q2HR92; -.
DR   DNASU; 4961438; -.
DR   GeneID; 4961438; -.
DR   KEGG; vg:4961438; -.
DR   Proteomes; UP000000942; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
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; IPR008650; Helicase-primas_cplx_Herpesvir.
DR   InterPro; IPR004996; HSV_HEPA.
DR   Pfam; PF05774; Herpes_heli_pri; 1.
DR   Pfam; PF03324; Herpes_HEPA; 1.
PE   3: Inferred from homology;
KW   DNA replication; Host nucleus; Reference proteome.
FT   CHAIN           1..669
FT                   /note="DNA helicase/primase complex-associated protein"
FT                   /id="PRO_0000423782"
FT   REGION          502..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   669 AA;  74809 MW;  3686012801843E8D CRC64;
     MATSEETAAG YVIGVYFHSV HVHCRIIVWQ VNFLPLDPND GETECYFVVD TLTKEAMERM
     PEIQECVPSI TEHARDLAIW ELALRLQNQT IVKAVRTASL PVVLIMTVGR IVNDVIPCPN
     VRTPRPLACA YLHCEATVTF EVPLTGPAAS TGTWHSSIYR ECAISAIEIC LKTSRGIYSC
     QSNEAPEAKR EKRGLDISDV FVCLTYDIPI AGRVLSLLVP HAPAFHVLWI NEDSKWNGAA
     VEFFRALHHK LFSERNGIPP LWLYVFPGAV EEGTAFAPLL PAFPCIPLRY GSPTSLDRAS
     VQWDLFEPHI LTHFDGIKRT SLADTVFGYD SLAISRECED QYVWPTPVTD ININLCTDSD
     TMAIVREPSG LVAVNLEALL RTDSVLSRVS SIVSLDTLLD LSTPECRRSV ELRYNSLLST
     VLSWSTSRGH KWAAIVKWKL FFLVQALEPE QWSPEFKDLK RACQMAGFTL KGGTSGDLVF
     SSHANLLFST SMGYFLHAGS PRSTAGTGGE PNPRHITGPD TEGNGEHRNS PNLCGFVTWL
     QSLTTCIERA LNMPPDTSWL QLIEEVIPLY FHRRRQTSFW LIPLSHCEGI PVCPPLPFDC
     LAPRLFIVTK SGPMCYRAGF SLPVDVNYLF YLEQTLKAVR QVSPQEHNPQ DAKEMTLQLE
     AWTRLLSLF