PRIM_HHV11
ID PRIM_HHV11 Reviewed; 1058 AA.
AC P10236; B9VQI1; Q09I82;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 89.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04011};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04011};
GN ORFNames=UL52;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2826807; DOI=10.1128/jvi.62.2.444-453.1988;
RA McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P.,
RA Challberg M.D.;
RT "Structures of herpes simplex virus type 1 genes required for replication
RT of virus DNA.";
RL J. Virol. 62:444-453(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH UL8 AND UL5.
RX PubMed=2538835; DOI=10.1073/pnas.86.7.2186;
RA Crute J.J., Tsurumi T., Zhu L.A., Weller S.K., Olivo P.D., Challberg M.D.,
RA Mocarski E.S., Lehman I.R.;
RT "Herpes simplex virus 1 helicase-primase: a complex of three herpes-encoded
RT gene products.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2186-2189(1989).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ASP-628.
RX PubMed=8189507; DOI=10.1128/jvi.68.6.3693-3701.1994;
RA Klinedinst D.K., Challberg M.D.;
RT "Helicase-primase complex of herpes simplex virus type 1: a mutation in the
RT UL52 subunit abolishes primase activity.";
RL J. Virol. 68:3693-3701(1994).
RN [7]
RP FUNCTION.
RX PubMed=7775476; DOI=10.1074/jbc.270.23.14148;
RA Dracheva S., Koonin E.V., Crute J.J.;
RT "Identification of the primase active site of the herpes simplex virus type
RT 1 helicase-primase.";
RL J. Biol. Chem. 270:14148-14153(1995).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=8811024; DOI=10.1099/0022-1317-77-9-2241;
RA Marsden H.S., Cross A.M., Francis G.J., Patel A.H., MacEachran K.,
RA Murphy M., McVey G., Haydon D., Abbotts A., Stow N.D.;
RT "The herpes simplex virus type 1 UL8 protein influences the intracellular
RT localization of the UL52 but not the ICP8 or POL replication proteins in
RT virus-infected cells.";
RL J. Gen. Virol. 77:2241-2249(1996).
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, ECO:0000269|PubMed:7775476,
CC ECO:0000269|PubMed:8189507}.
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 ECO:0000269|PubMed:2538835}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04011,
CC ECO:0000269|PubMed:8811024}. Note=Requires the presence of the primase
CC associated factor to properly localize in the host cell nucleus.
CC {ECO:0000255|HAMAP-Rule:MF_04011, ECO:0000269|PubMed:8811024}.
CC -!- SIMILARITY: Belongs to the herpesviridae DNA primase family.
CC {ECO:0000255|HAMAP-Rule:MF_04011}.
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DR EMBL; X14112; CAA32288.1; -; Genomic_DNA.
DR EMBL; M19122; AAA45826.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63513.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62276.1; -; Genomic_DNA.
DR PIR; E29890; WMBE52.
DR RefSeq; YP_009137128.1; NC_001806.2.
DR BioGRID; 971449; 2.
DR DIP; DIP-1092N; -.
DR BindingDB; P10236; -.
DR ChEMBL; CHEMBL4380; -.
DR PRIDE; P10236; -.
DR DNASU; 2703423; -.
DR GeneID; 2703423; -.
DR KEGG; vg:2703423; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR HAMAP; MF_04011; HSV_PRIM; 1.
DR InterPro; IPR033685; HSV_PRIM.
PE 1: Evidence at protein level;
KW DNA replication; Host nucleus; Metal-binding; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1058
FT /note="DNA primase"
FT /id="PRO_0000116104"
FT ZN_FING 988..1028
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011,
FT ECO:0000305|PubMed:8189507"
FT SITE 628
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT SITE 630
FT /note="Essential for primase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04011"
FT VARIANT 211
FT /note="V -> A (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 364
FT /note="S -> N (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 515
FT /note="P -> T (in strain: Nonneuroinvasive mutant HF10)"
FT MUTAGEN 628
FT /note="D->Q: Complete loss of primase activity."
FT /evidence="ECO:0000269|PubMed:8189507"
SQ SEQUENCE 1058 AA; 114424 MW; CB39341C31B768B4 CRC64;
MGQEDGNRGE RRAAGTPVEV TALYATDGCV ITSSIALLTN SLLGAEPVYI FSYDAYTHDG
RADGPTEQDR FEESRALYQA SGGLNGDSFR VTFCLLGTEV GGTHQARGRT RPMFVCRFER
ADDVAALQDA LAHGTPLQPD HIAATLDAEA TFALHANMIL ALTVAINNAS PRTGRDAAAA
QYDQGASLRS LVGRTSLGQR GLTTLYVHHE VRVLAAYRRA YYGSAQSPFW FLSKFGPDEK
SLVLTTRYYL LQAQRLGGAG ATYDLQAIKD ICATYAIPHA PRPDTVSAAS LTSFAAITRF
CCTSQYARGA AAAGFPLYVE RRIAADVRET SALEKFITHD RSCLRVSDRE FITYIYLAHF
ECFSPPRLAT HLRAVTTHDP NPAASTEQPS PLGREAVEQF FCHVRAQLNI GEYVKHNVTP
RETVLDGDTA KAYLRARTYA PGALTPAPAY CGAVDSATKM MGRLADAEKL LVPRGWPAFA
PASPGEDTAG GTPPPQTCGI VKRLLRLAAT EQQGPTPPAI AALIRNAAVQ TPLPVYRISM
VPTGQAFAAL AWDDWARITR DARLAEAVVS AEAAAHPDHG ALGRRLTDRI RAQGPVMPPG
GLDAGGQMYV NRNEIFNGAL AITNIILDLD IALKEPVPFR RLHEALGHFR RGALAAVQLL
FPAARVDPDA YPCYFFKSAC RPGPASVGSG SGLGNDDDGD WFPCYDDAGD EEWAEDPGAM
DTSHDPPDDE VAYFDLCHEV GPTAEPRETD SPVCSCTDKI GLRVCMPVPA PYVVHGSLTM
RGVARVIQQA VLLDRDFVEA IGSYVKNFLL IDTGVYAHGH SLRLPYFAKI APDGPACGRL
LPVFVIPPAC KDVPAFVAAH ADPRRFHFHA PPTYLASPRE IRVLHSLGGD YVSFFERKAS
RNALEHFGRR ETLTEVLGRY NVQPDAGGTV EGFASELLGR IVACIETHFP EHAGEYQAVS
VRRAVSKDDW VLLQLVPVRG TLQQSLSCLR FKHGRASRAT ARTFVALSVG ANNRLCVSLC
QQCFAAKCDS NRLHTLFTID AGTPCSPSVP CSTSQPSS
