ID   PRIM_SHV21              Reviewed;         835 AA.
AC   P14346;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   02-DEC-2020, entry version 72.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN   Name=56; Synonyms=EDRF4;
OS   Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=10383;
OH   NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA   Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA   Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA   Honess R.W.;
RT   "Primary structure of the herpesvirus saimiri genome.";
RL   J. Virol. 66:5047-5058(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1314457; DOI=10.1016/0042-6822(92)90759-i;
RA   Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.;
RT   "Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus
RT   saimiri (HVS) L-DNA: general conservation of genetic organization between
RT   HVS and Epstein-Barr virus.";
RL   Virology 188:296-310(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 631-835.
RX   PubMed=2841477; DOI=10.1128/jvi.62.9.3250-3257.1988;
RA   Nicholas J., Gompels U.A., Craxton M.A., Honess R.W.;
RT   "Conservation of sequence and function between the product of the 52-
RT   kilodalton immediate-early gene of herpesvirus saimiri and the BMLF1-
RT   encoded transcriptional effector (EB2) of Epstein-Barr virus.";
RL   J. Virol. 62:3250-3257(1988).
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; X64346; CAA45678.1; -; Genomic_DNA.
DR   EMBL; M86409; AAA46133.1; -; Genomic_DNA.
DR   EMBL; M21943; AAA66557.1; -; Genomic_DNA.
DR   RefSeq; NP_040258.1; NC_001350.1.
DR   PRIDE; P14346; -.
DR   GeneID; 1682485; -.
DR   KEGG; vg:1682485; -.
DR   Proteomes; UP000000587; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04011; HSV_PRIM; 1.
DR   InterPro; IPR033685; HSV_PRIM.
PE   3: Inferred from homology;
KW   DNA replication; Host nucleus; Metal-binding; Reference proteome;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..835
FT                   /note="DNA primase"
FT                   /id="PRO_0000116111"
FT   ZN_FING         778..817
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   SITE            496
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   SITE            498
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ   SEQUENCE   835 AA;  96128 MW;  3FA2A47360A937A8 CRC64;
     MNEATEAWPK FKVLFATDGD SAEIITDILT GTDTNAFIYS VLHNCYIYPT EVKIVLILCL
     PAKKPGGGDK CLEVFQLHID TELAIPFLFY TKPLKANDLH KYIDFKAARK NFKPILDIIS
     TNKPSPKTHN SDIKSKIVWF RAKFVNSLRK LYKISSSPYW MITTFGSFEV PFLLTAIFYF
     FEQHNCTINT IFHLSSLFEK KLGTSLIAIT TFEELGGVCS TSDYLKTAPA FINYCHIKLA
     RDSLESQAID TSIDTLRGQL MLSNQDLVHY IYLSFFQCLN KDIFIKYSHL TNSDNIHFVP
     ETEVLAQSLD ENFRKDMLTY YNKSTYLKTY ITHKCIHLPD LIGYAPQDCT SFVYWAGQSK
     NVHNLLNVIN TTHPHINISE DLNGLLDLAA IDSTFNVDNL KDCVFNESQK VPVYRCEFLN
     KTYFVIVQND ILKNVWSTDV LMPMQENWYM LKDTEITSNI SYKETFTSML TLRDQLKISR
     HEYFNPRLPV FNLVLDLDLH IHTSEHEIDE IYNLCCTLRS LILETLQLLG PVDIDTHHVY
     FFKSTCEKPE NWIDNKELKF CYCTKKLGFR IITPLPAGVV LLGSNPVISF VNILNRTIKI
     DKKLLAMYPL IMETDGPFDV GIYHKGRCVR IPHTYKVNSS GRLERLLKLF VCHPHVDNKL
     QYVMDSFDIN NLLYHSHNPE KVKQLKAVYD IADTNENFIL QKAQAQLPQT NHNAVERIES
     ASHMSITDWV AEFAWPRLFE LIKLYLSEEK VSQFYHVSFA ASTGNIIKII SLSGNFSCLN
     FKHRLKTQSV RIFLSLHLTP DNCVTLTLMS QCFASKCNSN KCIAHMSVRV PITDK