ID   PRIM_HCMVT              Reviewed;         946 AA.
AC   B9VXM8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   02-JUN-2021, entry version 28.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN   Name=UL70;
OS   Human cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=10363;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19553388; DOI=10.1099/vir.0.013250-0;
RA   Bradley A.J., Lurain N.S., Ghazal P., Trivedi U., Cunningham C.,
RA   Baluchova K., Gatherer D., Wilkinson G.W., Dargan D.J., Davison A.J.;
RT   "High-throughput sequence analysis of variants of human cytomegalovirus
RT   strains Towne and AD169.";
RL   J. Gen. Virol. 90:2375-2380(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
RN   [3]
RP   INTERACTION WITH HOST SNAPIN.
RX   PubMed=21917956; DOI=10.1128/jvi.05357-11;
RA   Shen A., Lei J., Yang E., Pei Y., Chen Y.C., Gong H., Xiao G., Liu F.;
RT   "Human cytomegalovirus primase UL70 specifically interacts with cellular
RT   factor Snapin.";
RL   J. Virol. 85:11732-11741(2011).
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 (By similarity). Interacts with
CC       host SNAPIN. {ECO:0000255|HAMAP-Rule:MF_04011,
CC       ECO:0000269|PubMed:21917956}.
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; FJ616285; ACM48048.1; -; Genomic_DNA.
DR   Proteomes; UP000006907; 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   1: Evidence at protein level;
KW   DNA replication; Host nucleus; Host-virus interaction; Metal-binding;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..946
FT                   /note="DNA primase"
FT                   /id="PRO_0000416449"
FT   ZN_FING         881..920
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   REGION          596..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            517
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT   SITE            519
FT                   /note="Essential for primase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
SQ   SEQUENCE   946 AA;  107857 MW;  8C25D3483B549DFA CRC64;
     MTLVLFATEY DSAHIVANVL SQTPTDHCVF PLLVKHQVSR RVYFCLQTQK CSDSRRVAPV
     FAVNNETLQL SRYLAARQPI PLSALIASLD EAETQPLYRH LFRTPVLSPE HGGEVREFKH
     LVYFHHAAVL RHLNQVFLCP TSPSWFISVF GHTEGQVLLT MAYYLFEGQY STISTVEEYV
     RSFCTRDLGT IIPTHASMGE FARLLLGSPF RQRVSAFVAY AVARNRRDYT ELEQVDTQIN
     AFRERARLPD TVCVHYVYLA YRTALARARL LEYRRVVAYD ADAAPEAQCT REPGFLGRRL
     STELLDVMQK YFSLDNFLHD YVETHLLRLD ESPHSATSPH GLGLAGYGGR IDGTHLAGFF
     GTSTQLARQL ERINTLSESV FSPLERSLSG LLRLCASLRT AQTYTTGTLT RYSQRRYLLP
     EPALAPLLER PLPVYRVHLP NDQHVFCAVA SETWHRSLFP RDLLRHVPDS RFSDEALTET
     VWLHDDDVAS TSPETQFYYT RHEVFNERLP VFNFVADFDL RLRDGVSGLA RHTVFELCRG
     LRRVWMTVWA SLFGYTHPDR HPVYFFKSAC PPNSVPVDAA GAPFDDDDYL DYRDERDTEE
     DEDGKENKNN VPDNGVFQKT TSSVDTSPPY CRCKGKLGLR IITPFPACTV AVHPSVLRAV
     AQVLNHAVCL DAELHTLLDP ISHPESSLDT GIYHHGRSVR LPYMYKMDQD DGYFMHRRLL
     PLFIVPDAYR EHPLGFVRAQ LDLRNLLHHH PPHDLPALPL SPPPRVILSV RDKICPSTEA
     NFIETRSLNV TRYRRRGLTE VLAYHLYGGD GATAAAISDT DLQRLVVTRV WPPLLEHLTQ
     HYEPHVSEQF TAPHVLLFQP HGACCVAVKR RDGARTRDFR CLNYTHRNPQ ETVQVFIDLR
     TEHSYALWAS LWSRCFTKKC HSNAKNVHIS IKIRPPDAPM PPATAV