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P04296

- DNBI_HHV11

UniProt

P04296 - DNBI_HHV11

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Protein

Major DNA-binding protein

Gene

DBP

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

Functioni

Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein UL9. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri499 – 51214Sequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. single-stranded DNA binding Source: InterPro

GO - Biological processi

  1. DNA replication Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Major DNA-binding protein
Alternative name(s):
Infected cell protein 8
Short name:
ICP-8 protein
Gene namesi
Name:DBP
Synonyms:ICP8
ORF Names:UL29
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]
ProteomesiUP000009294: Genome

Subcellular locationi

Host nucleus 1 Publication
Note: In the absence of DNA replication, found in the nuclear framework-associated structures (prereplicative sites). As viral DNA replication proceeds, it migrates to globular intranuclear structures (replication compartments).

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11961196Major DNA-binding proteinPRO_0000115743Add
BLAST

Interactioni

Subunit structurei

Interacts with UL9. Interacts with ICP27; this interaction plays a role in the stimulation of late gene transcription. Interacts with the alkaline exonuclease UL12; this interaction increases its nuclease processivity.3 Publications

Protein-protein interaction databases

BioGridi971471. 17 interactions.
IntActiP04296. 53 interactions.
MINTiMINT-191337.

Structurei

Secondary structure

1
1196
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 258Combined sources
Helixi31 – 377Combined sources
Beta strandi47 – 504Combined sources
Beta strandi64 – 7310Combined sources
Beta strandi81 – 9010Combined sources
Beta strandi92 – 987Combined sources
Helixi100 – 1023Combined sources
Helixi112 – 12312Combined sources
Helixi132 – 1376Combined sources
Helixi141 – 1488Combined sources
Beta strandi154 – 1629Combined sources
Turni163 – 1653Combined sources
Helixi166 – 1705Combined sources
Beta strandi174 – 1763Combined sources
Helixi178 – 1803Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi189 – 19810Combined sources
Helixi199 – 2024Combined sources
Helixi234 – 24310Combined sources
Helixi245 – 2517Combined sources
Helixi257 – 26913Combined sources
Helixi310 – 33122Combined sources
Helixi342 – 3443Combined sources
Helixi346 – 3483Combined sources
Beta strandi353 – 3553Combined sources
Helixi358 – 37720Combined sources
Turni382 – 3843Combined sources
Beta strandi385 – 3906Combined sources
Beta strandi406 – 4116Combined sources
Turni413 – 4175Combined sources
Turni430 – 4334Combined sources
Helixi448 – 4547Combined sources
Turni455 – 4573Combined sources
Helixi459 – 46911Combined sources
Helixi485 – 4906Combined sources
Turni491 – 4944Combined sources
Turni504 – 5096Combined sources
Helixi511 – 5177Combined sources
Helixi519 – 5213Combined sources
Beta strandi533 – 5386Combined sources
Helixi575 – 58814Combined sources
Helixi603 – 6064Combined sources
Helixi610 – 63627Combined sources
Helixi643 – 6475Combined sources
Beta strandi651 – 6577Combined sources
Helixi667 – 69327Combined sources
Helixi703 – 71614Combined sources
Turni717 – 7204Combined sources
Beta strandi721 – 73111Combined sources
Turni744 – 7463Combined sources
Beta strandi748 – 7503Combined sources
Beta strandi759 – 7613Combined sources
Beta strandi764 – 77714Combined sources
Helixi810 – 8123Combined sources
Helixi816 – 8216Combined sources
Helixi823 – 8264Combined sources
Helixi840 – 84910Combined sources
Helixi861 – 87818Combined sources
Helixi888 – 90316Combined sources
Beta strandi913 – 92311Combined sources
Beta strandi925 – 9273Combined sources
Helixi928 – 9336Combined sources
Helixi941 – 95010Combined sources
Helixi951 – 9544Combined sources
Beta strandi960 – 9678Combined sources
Helixi969 – 9746Combined sources
Beta strandi978 – 98710Combined sources
Beta strandi999 – 10046Combined sources
Helixi1009 – 10113Combined sources
Beta strandi1022 – 10287Combined sources
Turni1031 – 10333Combined sources
Helixi1049 – 10568Combined sources
Helixi1064 – 107310Combined sources
Helixi1078 – 10825Combined sources
Helixi1085 – 10917Combined sources
Helixi1095 – 111117Combined sources
Helixi1120 – 11256Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1URJX-ray3.00A/B1-1136[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04296.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi929 – 9324Poly-Ala

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri499 – 51214Sequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Family and domain databases

InterProiIPR000635. Viral_ssDNA-bd.
[Graphical view]
PfamiPF00747. Viral_DNA_bp. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04296-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
METKPKTATT IKVPPGPLGY VYARACPSEG IELLALLSAR SGDSDVAVAP
60 70 80 90 100
LVVGLTVESG FEANVAVVVG SRTTGLGGTA VSLKLTPSHY SSSVYVFHGG
110 120 130 140 150
RHLDPSTQAP NLTRLCERAR RHFGFSDYTP RPGDLKHETT GEALCERLGL
160 170 180 190 200
DPDRALLYLV VTEGFKEAVC INNTFLHLGG SDKVTIGGAE VHRIPVYPLQ
210 220 230 240 250
LFMPDFSRVI AEPFNANHRS IGEKFTYPLP FFNRPLNRLL FEAVVGPAAV
260 270 280 290 300
ALRCRNVDAV ARAAAHLAFD ENHEGAALPA DITFTAFEAS QGKTPRGGRD
310 320 330 340 350
GGGKGAAGGF EQRLASVMAG DAALALESIV SMAVFDEPPT DISAWPLFEG
360 370 380 390 400
QDTAAARANA VGAYLARAAG LVGAMVFSTN SALHLTEVDD AGPADPKDHS
410 420 430 440 450
KPSFYRFFLV PGTHVAANPQ VDREGHVVPG FEGRPTAPLV GGTQEFAGEH
460 470 480 490 500
LAMLCGFSPA LLAKMLFYLE RCDGAVIVGR QEMDVFRYVA DSNQTDVPCN
510 520 530 540 550
LCTFDTRHAC VHTTLMRLRA RHPKFASAAR GAIGVFGTMN SMYSDCDVLG
560 570 580 590 600
NYAAFSALKR ADGSETARTI MQETYRAATE RVMAELETLQ YVDQAVPTAM
610 620 630 640 650
GRLETIITNR EALHTVVNNV RQVVDREVEQ LMRNLVEGRN FKFRDGLGEA
660 670 680 690 700
NHAMSLTLDP YACGPCPLLQ LLGRRSNLAV YQDLALSQCH GVFAGQSVEG
710 720 730 740 750
RNFRNQFQPV LRRRVMDMFN NGFLSAKTLT VALSEGAAIC APSLTAGQTA
760 770 780 790 800
PAESSFEGDV ARVTLGFPKE LRVKSRVLFA GASANASEAA KARVASLQSA
810 820 830 840 850
YQKPDKRVDI LLGPLGFLLK QFHAAIFPNG KPPGSNQPNP QWFWTALQRN
860 870 880 890 900
QLPARLLSRE DIETIAFIKK FSLDYGAINF INLAPNNVSE LAMYYMANQI
910 920 930 940 950
LRYCDHSTYF INTLTAIIAG SRRPPSVQAA AAWSAQGGAG LEAGARALMD
960 970 980 990 1000
AVDAHPGAWT SMFASCNLLR PVMAARPMVV LGLSISKYYG MAGNDRVFQA
1010 1020 1030 1040 1050
GNWASLMGGK NACPLLIFDR TRKFVLACPR AGFVCAASSL GGGAHESSLC
1060 1070 1080 1090 1100
EQLRGIISEG GAAVASSVFV ATVKSLGPRT QQLQIEDWLA LLEDEYLSEE
1110 1120 1130 1140 1150
MMELTARALE RGNGEWSTDA ALEVAHEAEA LVSQLGNAGE VFNFGDFGCE
1160 1170 1180 1190
DDNATPFGGP GAPGPAFAGR KRAFHGDDPF GEGPPDKKGD LTLDML
Length:1,196
Mass (Da):128,350
Last modified:March 20, 1987 - v1
Checksum:i453799162E5B99E9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441S → A in strain: Nonneuroinvasive mutant HF10.
Natural varianti224 – 2241K → N in strain: Nonneuroinvasive mutant HF10 and 17 syn+.
Natural varianti306 – 3061A → P in strain: Nonneuroinvasive mutant HF10 and 17 syn+.
Natural varianti428 – 4281V → A in strain: Nonneuroinvasive mutant HF10.
Natural varianti475 – 4751A → G in strain: Nonneuroinvasive mutant HF10 and 17 syn+.
Natural varianti964 – 9641A → T in strain: Nonneuroinvasive mutant HF10.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32322.1.
X03181 Genomic DNA. Translation: CAA26940.1.
M21631 Genomic DNA. Translation: AAA45787.1.
DQ889502 Genomic DNA. Translation: ABI63491.1.
FJ593289 Genomic DNA. Translation: ACM62252.1.
PIRiA03790. DNBEV1.
RefSeqiNP_044631.1. NC_001806.1.

Genome annotation databases

GeneIDi2703458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14112 Genomic DNA. Translation: CAA32322.1 .
X03181 Genomic DNA. Translation: CAA26940.1 .
M21631 Genomic DNA. Translation: AAA45787.1 .
DQ889502 Genomic DNA. Translation: ABI63491.1 .
FJ593289 Genomic DNA. Translation: ACM62252.1 .
PIRi A03790. DNBEV1.
RefSeqi NP_044631.1. NC_001806.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1URJ X-ray 3.00 A/B 1-1136 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 971471. 17 interactions.
IntActi P04296. 53 interactions.
MINTi MINT-191337.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2703458.

Miscellaneous databases

EvolutionaryTracei P04296.

Family and domain databases

InterProi IPR000635. Viral_ssDNA-bd.
[Graphical view ]
Pfami PF00747. Viral_DNA_bp. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence of the region in the genome of herpes simplex virus type 1 containing the genes for DNA polymerase and the major DNA binding protein."
    Quinn J.P., McGeoch D.J.
    Nucleic Acids Res. 13:8143-8163(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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].
  3. "Common epitopes of glycoprotein B map within the major DNA-binding proteins of bovine herpesvirus type 2 (BHV-2) and herpes simplex virus type 1 (HSV-1)."
    Hammerschmidt W., Conraths F., Mankertz J., Buhk H.-J., Pauli G., Ludwig H.
    Virology 165:406-418(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1062-1196.
  4. "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.
  5. "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+.
  6. "Association of origin binding protein and single strand DNA-binding protein, ICP8, during herpes simplex virus type 1 DNA replication in vivo."
    Boehmer P.E., Craigie M.C., Stow N.D., Lehman I.R.
    J. Biol. Chem. 269:29329-29334(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UL9, FUNCTION.
  7. "Herpes simplex virus type 1 prereplicative sites are a heterogeneous population: only a subset are likely to be precursors to replication compartments."
    Lukonis C.J., Burkham J., Weller S.K.
    J. Virol. 71:4771-4781(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "The UL12.5 gene product of herpes simplex virus type 1 exhibits nuclease and strand exchange activities but does not localize to the nucleus."
    Reuven N.B., Antoku S., Weller S.K.
    J. Virol. 78:4599-4608(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UL12, FUNCTION.
  9. "Evidence for a direct interaction between HSV-1 ICP27 and ICP8 proteins."
    Olesky M., McNamee E.E., Zhou C., Taylor T.J., Knipe D.M.
    Virology 331:94-105(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ICP27.
  10. "The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding."
    Mapelli M., Panjikar S., Tucker P.A.
    J. Biol. Chem. 280:2990-2997(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-1136.

Entry informationi

Entry nameiDNBI_HHV11
AccessioniPrimary (citable) accession number: P04296
Secondary accession number(s): B9VQF7, Q09IA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: November 26, 2014
This is version 86 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3