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Protein

Major DNA-binding protein

Gene

DBP

Organism
Human herpesvirus 2 (HHV-2) (Human herpes simplex virus 2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Single-stranded DNA-binding protein required for DNA replication.
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. 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. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA.UniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri499 – 512UniRule annotationAdd BLAST14

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processDNA replication
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Major DNA-binding proteinUniRule annotation
Gene namesi
Name:DBPUniRule annotation
Synonyms:ICP8, UL29
OrganismiHuman herpesvirus 2 (HHV-2) (Human herpes simplex virus 2)
Taxonomic identifieri10310 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

  • Host nucleus UniRule annotation

  • 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).UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001157461 – 1197Major DNA-binding proteinAdd BLAST1197

Interactioni

Subunit structurei

Homooligomers. Forms double-helical filaments necessary for the formation of replication compartments within the host nucleus. Interacts with the origin-binding protein. Interacts with the helicase primase complex; this interaction stimulates primer synthesis activity of the helicase-primase complex. Interacts with the DNA polymerase. Interacts with the alkaline exonuclease; this interaction increases its nuclease processivity.UniRule annotation

Structurei

3D structure databases

SMRiP36384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1172 – 1197Required for nuclear localizationUniRule annotationAdd BLAST26

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi843 – 844Required for filament formationUniRule annotation2
Motifi1142 – 1144Required for filament formationUniRule annotation3

Sequence similaritiesi

Belongs to the herpesviridae major DNA-binding protein family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri499 – 512UniRule annotationAdd BLAST14

Keywords - Domaini

Zinc-finger

Family and domain databases

HAMAPiMF_04007. HSV_DNBI. 1 hit.
InterProiView protein in InterPro
IPR000635. Viral_ssDNA-bd.
PfamiView protein in Pfam
PF00747. Viral_DNA_bp. 1 hit.
SUPFAMiSSF118208. SSF118208. 1 hit.

Sequencei

Sequence statusi: Complete.

P36384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTKPKTTTT VKVPPGPMGY VYGRACPAEG LELLSLLSAR SGDADVAVAP
60 70 80 90 100
LIVGLTVESG FEANVAAVVG SGTTGLGGTA VSLKLMPSHY SPSVYVFHGG
110 120 130 140 150
RHLAPSTQAP NLTRLCERAR RHFGFSDYAP RPCDLKHETT GDALCERLGL
160 170 180 190 200
DPDRALLYLV ITEGFREAVC ISNTFLHLGG MDKVTIGDAE VHRIPVYPLQ
210 220 230 240 250
MFMPDFSRVI ADPFNCNHRS IGENFNYPLP FFNRPLARLL FEAVVGPAAV
260 270 280 290 300
ALRARNVDAV ARAAAHLAFD ENHEGAALPA DITFTAFEAS QGKPQRGARD
310 320 330 340 350
AGNKGPAGGF EQRLASVMAG DAALALESIV SMAVFDEPPP DITTWPLLEG
360 370 380 390 400
QETPAARAGA VGAYLARAAG LVGAMVFSTN SALHLTEVDD AGPADPKDHS
410 420 430 440 450
KPSFYRFFLV PGTHVAANPQ LDREGHVVPG YEGRPTAPLV GGTQEFAGEH
460 470 480 490 500
LAMLCGFSPA LLAKMLFYLE RCDGGVIVGR QEMDVFRYVA DSGQTDVPCN
510 520 530 540 550
LCTFETRHAC AHTTLMRLRA RHPKFASAAR GAIGVFGTMN SAYSDCDVLG
560 570 580 590 600
NYAAFSALKR ADGSENTRTI MQETYRAATE RVMAELEALQ YVDQAVPTAL
610 620 630 640 650
GRLETIIGNR EALHTVVNNI KQLVDREVEQ LMRNLIEGRN FKFRDGLAEA
660 670 680 690 700
NHAMSLSLDP YTCGPCPLLQ LLARRSNLAV YQDLALSQCH GVFAGQSVEG
710 720 730 740 750
RNFRNQFQPV LRRRVMDLFN NGFLSAKTLT VALSEGAAIC APSLTAGQTA
760 770 780 790 800
PAESSFEGDV ARVTLGFPKE LRVKSRVLFA GASANASEAA KARVASLQSA
810 820 830 840 850
YQKPDKRVDI LLGPLGFLLK QFHAVIFPNG KPPGSNQPNP QWFWTALQRN
860 870 880 890 900
QLPARLLSRE DIETIAFIKR FSLDYGAINF INLAPNNVSE LAMYYMANQI
910 920 930 940 950
LRYCDHSTYF INTLTAVIAG SRRPPSVQAA AAWAPQGGAG LEAGARALMD
960 970 980 990 1000
SLDAHPGAWT SMFASCNLLR PVMAARPMVV LGLSISKYYG MAGNDRVFQA
1010 1020 1030 1040 1050
GNWASLLGGK NACPLLIFDR TRKFVLACPR AGFVCAASSL GGGAHEHSLC
1060 1070 1080 1090 1100
EQLRGIIAEG GAAVASSVFV ATVKSLGPRT QQLQIEDWLA LLEDEYLSEE
1110 1120 1130 1140 1150
MMEFTTRALE RGHGEWSTDA ALEVAHEAEA LVSQLGAAGE VFNFGDFGDA
1160 1170 1180 1190
DDHAASFGGL AAAAAGAAGV ARKRAFHGDD PFGEGPPEKK DLTLDML
Length:1,197
Mass (Da):128,413
Last modified:June 1, 1994 - v1
Checksum:iC1576BB5B8865BFB
GO

Sequence databases

PIRiA48350.

Cross-referencesi

Sequence databases

PIRiA48350.

3D structure databases

SMRiP36384.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

HAMAPiMF_04007. HSV_DNBI. 1 hit.
InterProiView protein in InterPro
IPR000635. Viral_ssDNA-bd.
PfamiView protein in Pfam
PF00747. Viral_DNA_bp. 1 hit.
SUPFAMiSSF118208. SSF118208. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDNBI_HHV2
AccessioniPrimary (citable) accession number: P36384
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 10, 2017
This is version 56 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.