ID   PRIM_HHV8P              Reviewed;         843 AA.
AC   F5HIN0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   23-FEB-2022, entry version 34.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN   Name=ORF56;
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: Essential component of the helicase/primase complex. Unwinds
CC       the DNA at the replication forks and generates single-stranded DNA for
CC       both leading and lagging strand synthesis. The primase initiates primer
CC       synthesis and thereby produces large amount of short RNA primers on the
CC       lagging strand that the polymerase elongates using dNTPs.
CC       {ECO:0000255|HAMAP-Rule:MF_04011}.
CC   -!- SUBUNIT: Associates with the helicase and the primase-associated factor
CC       to form the helicase-primase factor. {ECO:0000255|HAMAP-Rule:MF_04011}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011}.
CC       Note=Requires the presence of the primase associated factor to properly
CC       localize in the host cell nucleus. {ECO:0000255|HAMAP-Rule:MF_04011}.
CC   -!- SIMILARITY: Belongs to the herpesviridae DNA primase family.
CC       {ECO:0000255|HAMAP-Rule:MF_04011}.
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DR   EMBL; AF148805; ABD28907.1; -; Genomic_DNA.
DR   RefSeq; YP_001129409.1; NC_009333.1.
DR   BioGRID; 1776948; 2.
DR   PRIDE; F5HIN0; -.
DR   DNASU; 4961445; -.
DR   GeneID; 4961445; -.
DR   KEGG; vg:4961445; -.
DR   Proteomes; UP000000942; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR   HAMAP; MF_04011; HSV_PRIM; 1.
DR   InterPro; IPR033685; HSV_PRIM.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; Helicase; Host nucleus; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..843
FT                   /note="DNA primase"
FT                   /id="PRO_0000423762"
FT   ZN_FING         785..824
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   SITE            500
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   SITE            502
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ   SEQUENCE   843 AA;  95554 MW;  89248BFCB7DBAB0E CRC64;
     METTYRREAL TVRVIFCTSG DSAETIADVL TGAPTSASFF SVLHDLFYSQ ILAPRVTLKL
     CLPARRPGNG TRCSPVLVLR TDASVASGFL GGRPLEASDI KYMLLSDQTA GLFKPLLEII
     GGARAPPNQD ACTFQSQVAW LRTKFVTALR KLYKMTPSPY WMLSAFGAQE AQFVLTSSFY
     FFEHTVVCTT ETVSHLSRLF SPQQGQTLVS VTSHEELGQL YGTSPFRRRV PAFVAYVKEK
     LARDSLETEA IDRTIDQIRG KLMLSNQDLV HFIYISFYQC LNKRAFLRYS RQTSSSSALR
     ELGEDPQLCG ALHGEFRDHV QSYYHKKTYL STYIDIRYVG GVLPDGYFGG SLVGERCVYW
     CGQSKDTASL LATISQQVPH LRLQNEFAGM LDVAALRGSD DGQFKEGLFS HSQALPLYRC
     EFLGKQFFTM LQEDGLERYW EQSVIFPGDQ DWDMLSDKDL TYRIFYHDLS LSLPTLKEQL
     LVSRHEYFNP RLPVYRWVLD FDLPVCRDID RTFEEVHSLC CSLREAILDI IQLLGPVDPR
     THPVYFFKSA CPPDEWRGED VASTSFCRCH DKLGMRIIVP FPEGVCVVGS EPMVALTGIL
     NRTIKLDPEL VHRFPSIQKK GGPFDCGIYG RGRSVRLPHC YKVGLVGELC RLLKILVCHP
     APNGKAQYVR RAFTLRELLH HSPGHSAGHV GRIIYSIMDR NENFLENKTI SYLPAKIPHI
     FQRIETLSGR SIEDWLHSAV WDKAYDTICK FFPDEKAQQF SHVAFTQQGE NIIQLRPRQG
     RHFLCINHNH KNKSKTVRVF LTLHSIRVSE VTVTLMSQCF ASKCNNNVPT AHFSFVVPVG
     LAS