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Protein

DNA primase

Gene

UL52

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs.UniRule annotation2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei628 – 6281Essential for primase activityUniRule annotation
Sitei630 – 6301Essential for primase activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri988 – 102841CHC2-typeUniRule annotation1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • bidirectional double-stranded viral DNA replication Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DNA primaseUniRule annotation (EC:2.7.7.-UniRule annotation)
Gene namesi
ORF Names:UL52
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000009294 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi628 – 6281D → Q: Complete loss of primase activity. 1 Publication

Chemistry

ChEMBLiCHEMBL4380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10581058DNA primasePRO_0000116104Add
BLAST

Interactioni

Subunit structurei

Associates with the helicase and the primase-associated factor to form the helicase-primase factor.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi971449. 2 interactions.
DIPiDIP-1092N.

Chemistry

BindingDBiP10236.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi177 – 1804Poly-Ala
Compositional biasi310 – 3134Poly-Ala

Sequence similaritiesi

Belongs to the herpesviridae DNA primase family.UniRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri988 – 102841CHC2-typeUniRule annotation1 PublicationAdd
BLAST

Keywords - Domaini

Zinc-finger

Family and domain databases

HAMAPiMF_04011. HSV_PRIM.
InterProiIPR004340. DNA_primase_UL52/UL70_Herpvir.
[Graphical view]
PfamiPF03121. Herpes_UL52. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQEDGNRGE RRAAGTPVEV TALYATDGCV ITSSIALLTN SLLGAEPVYI
60 70 80 90 100
FSYDAYTHDG RADGPTEQDR FEESRALYQA SGGLNGDSFR VTFCLLGTEV
110 120 130 140 150
GGTHQARGRT RPMFVCRFER ADDVAALQDA LAHGTPLQPD HIAATLDAEA
160 170 180 190 200
TFALHANMIL ALTVAINNAS PRTGRDAAAA QYDQGASLRS LVGRTSLGQR
210 220 230 240 250
GLTTLYVHHE VRVLAAYRRA YYGSAQSPFW FLSKFGPDEK SLVLTTRYYL
260 270 280 290 300
LQAQRLGGAG ATYDLQAIKD ICATYAIPHA PRPDTVSAAS LTSFAAITRF
310 320 330 340 350
CCTSQYARGA AAAGFPLYVE RRIAADVRET SALEKFITHD RSCLRVSDRE
360 370 380 390 400
FITYIYLAHF ECFSPPRLAT HLRAVTTHDP NPAASTEQPS PLGREAVEQF
410 420 430 440 450
FCHVRAQLNI GEYVKHNVTP RETVLDGDTA KAYLRARTYA PGALTPAPAY
460 470 480 490 500
CGAVDSATKM MGRLADAEKL LVPRGWPAFA PASPGEDTAG GTPPPQTCGI
510 520 530 540 550
VKRLLRLAAT EQQGPTPPAI AALIRNAAVQ TPLPVYRISM VPTGQAFAAL
560 570 580 590 600
AWDDWARITR DARLAEAVVS AEAAAHPDHG ALGRRLTDRI RAQGPVMPPG
610 620 630 640 650
GLDAGGQMYV NRNEIFNGAL AITNIILDLD IALKEPVPFR RLHEALGHFR
660 670 680 690 700
RGALAAVQLL FPAARVDPDA YPCYFFKSAC RPGPASVGSG SGLGNDDDGD
710 720 730 740 750
WFPCYDDAGD EEWAEDPGAM DTSHDPPDDE VAYFDLCHEV GPTAEPRETD
760 770 780 790 800
SPVCSCTDKI GLRVCMPVPA PYVVHGSLTM RGVARVIQQA VLLDRDFVEA
810 820 830 840 850
IGSYVKNFLL IDTGVYAHGH SLRLPYFAKI APDGPACGRL LPVFVIPPAC
860 870 880 890 900
KDVPAFVAAH ADPRRFHFHA PPTYLASPRE IRVLHSLGGD YVSFFERKAS
910 920 930 940 950
RNALEHFGRR ETLTEVLGRY NVQPDAGGTV EGFASELLGR IVACIETHFP
960 970 980 990 1000
EHAGEYQAVS VRRAVSKDDW VLLQLVPVRG TLQQSLSCLR FKHGRASRAT
1010 1020 1030 1040 1050
ARTFVALSVG ANNRLCVSLC QQCFAAKCDS NRLHTLFTID AGTPCSPSVP

CSTSQPSS
Length:1,058
Mass (Da):114,424
Last modified:July 1, 1989 - v1
Checksum:iCB39341C31B768B4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111V → A in strain: Nonneuroinvasive mutant HF10.
Natural varianti364 – 3641S → N in strain: Nonneuroinvasive mutant HF10.
Natural varianti515 – 5151P → T in strain: Nonneuroinvasive mutant HF10.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32288.1.
M19122 Genomic DNA. Translation: AAA45826.1.
DQ889502 Genomic DNA. Translation: ABI63513.1.
FJ593289 Genomic DNA. Translation: ACM62276.1.
PIRiE29890. WMBE52.
RefSeqiYP_009137128.1. NC_001806.2.

Genome annotation databases

GeneIDi2703423.
KEGGivg:2703423.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32288.1.
M19122 Genomic DNA. Translation: AAA45826.1.
DQ889502 Genomic DNA. Translation: ABI63513.1.
FJ593289 Genomic DNA. Translation: ACM62276.1.
PIRiE29890. WMBE52.
RefSeqiYP_009137128.1. NC_001806.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi971449. 2 interactions.
DIPiDIP-1092N.

Chemistry

BindingDBiP10236.
ChEMBLiCHEMBL4380.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2703423.
KEGGivg:2703423.

Family and domain databases

HAMAPiMF_04011. HSV_PRIM.
InterProiIPR004340. DNA_primase_UL52/UL70_Herpvir.
[Graphical view]
PfamiPF03121. Herpes_UL52. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
    McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
    J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "Structures of herpes simplex virus type 1 genes required for replication of virus DNA."
    McGeoch D.J., Dalrymple M.A., Dolan A., McNab D., Perry L.J., Taylor P., Challberg M.D.
    J. Virol. 62:444-453(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
    Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
    Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Nonneuroinvasive mutant HF10.
  4. "Herpes simplex virus type 1 bacterial artificial chromosome."
    Cunningham C., Davison A.J.
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 17 syn+.
  5. "Herpes simplex virus 1 helicase-primase: a complex of three herpes-encoded gene products."
    Crute J.J., Tsurumi T., Zhu L.A., Weller S.K., Olivo P.D., Challberg M.D., Mocarski E.S., Lehman I.R.
    Proc. Natl. Acad. Sci. U.S.A. 86:2186-2189(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UL8 AND UL5.
  6. "Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity."
    Klinedinst D.K., Challberg M.D.
    J. Virol. 68:3693-3701(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-628.
  7. "Identification of the primase active site of the herpes simplex virus type 1 helicase-primase."
    Dracheva S., Koonin E.V., Crute J.J.
    J. Biol. Chem. 270:14148-14153(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The herpes simplex virus type 1 UL8 protein influences the intracellular localization of the UL52 but not the ICP8 or POL replication proteins in virus-infected cells."
    Marsden H.S., Cross A.M., Francis G.J., Patel A.H., MacEachran K., Murphy M., McVey G., Haydon D., Abbotts A., Stow N.D.
    J. Gen. Virol. 77:2241-2249(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPRIM_HHV11
AccessioniPrimary (citable) accession number: P10236
Secondary accession number(s): B9VQI1, Q09I82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 13, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.