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Protein

DNA polymerase catalytic subunit

Gene

BALF5

Organism
Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Replicates viral genomic DNA in the late phase of lytic infection, producing long concatemeric DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein.

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication, Viral DNA replication

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase catalytic subunit (EC:2.7.7.7)
Gene namesi
ORF Names:BALF5
OrganismiEpstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Taxonomic identifieri10377 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeGammaherpesvirinaeLymphocryptovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007640 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Host nucleus

Pathology & Biotechi

Chemistry databases

DrugBankiDB00194. Vidarabine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000465051 – 1015DNA polymerase catalytic subunitAdd BLAST1015

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Forms a complex with the ssDNA-binding protein BALF2, the DNA polymerase processivity factor BMRF1, and the alkaline exonuclease BGLF5. Interacts with the putative helicase-primase complex composed of BBLF4, BSLF1 and BBLF2/3 proteins; these interactions may coordinate leading and lagging strand DNA synthesis at the replication fork.3 Publications

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H15X-ray3.10C/F628-641[»]
ProteinModelPortaliP03198.
SMRiP03198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03198.

Family & Domainsi

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated

Phylogenomic databases

KOiK18964.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03198-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGLFYNPF LRPNKGLLKK PDKEYLRLIP KCFQTPGAAG VVDVRGPQPP
60 70 80 90 100
LCFYQDSLTV VGGDEDGKGM WWRQRAQEGT ARPEADTHGS PLDFHVYDIL
110 120 130 140 150
ETVYTHEKCA VIPSDKQGYV VPCGIVIKLL GRRKADGASV CVNVFGQQAY
160 170 180 190 200
FYASAPQGLD VEFAVLSALK ASTFDRRTPC RVSVEKVTRR SIMGYGNHAG
210 220 230 240 250
DYHKITLSHP NSVCHVATWL QDKHGCRIFE ANVDATRRFV LDNDFVTFGW
260 270 280 290 300
YSCRRAIPRL QHRDSYAELE YDCEVGDLSV RREDSSWPSY QALAFDIECL
310 320 330 340 350
GEEGFPTATN EADLILQISC VLWSTGEEAG RYRRILLTLG TCEDIEGVEV
360 370 380 390 400
YEFPSELDML YAFFQLIRDL SVEIVTGYNV ANFDWPYILD RARHIYSINP
410 420 430 440 450
ASLGKIRAGG VCEVRRPHDA GKGFLRANTK VRITGLIPID MYAVCRDKLS
460 470 480 490 500
LSDYKLDTVA RHLLGAKKED VHYKEIPRLF AAGPEGRRRL GMYCVQDSAL
510 520 530 540 550
VMDLLNHFVI HVEVAEIAKI AHIPCRRVLD DGQQIRVFSC LLAAAQKENF
560 570 580 590 600
ILPMPSASDR DGYQGATVIQ PLSGFYNSPV LVVDFASLYP SIIQAHNLCY
610 620 630 640 650
STMITPGEEH RLAGLRPGED YESFRLTGGV YHFVKKHVHE SFLASLLTSW
660 670 680 690 700
LAKRKAIKKL LAACEDPRQR TILDKQQLAI KCTCNAVYGF TGVANGLFPC
710 720 730 740 750
LSIAETVTLQ GRTMLERAKA FVEALSPANL QALAPSPDAW APLNPEGQLR
760 770 780 790 800
VIYGDTDSLF IECRGFSESE TLRFADALAA HTTRSLFVAP ISLEAEKTFS
810 820 830 840 850
CLMLITKKRY VGVLTDGKTL MKGVELVRKT ACKFVQTRCR RVLDLVLADA
860 870 880 890 900
RVKEAASLLS HRPFQESFTQ GLPVGFLPVI DILNQAYTDL REGRVPMGEL
910 920 930 940 950
CFSTELSRKL SAYKSTQMPH LAVYQKFVER NEELPQIHDR IQYVFVEPKG
960 970 980 990 1000
GVKGARKTEM AEDPAYAERH GVPVAVDHYF DKLLQGAANI LQCLFDNNSG
1010
AALSVLQNFT ARPPF
Length:1,015
Mass (Da):113,418
Last modified:July 21, 1986 - v1
Checksum:i0503B5E269399812
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24805.1.
AJ507799 Genomic DNA. Translation: CAD53462.1.
PIRiA00713. DJBE2L.
RefSeqiYP_401712.1. NC_007605.1.

Genome annotation databases

GeneIDi3783681.
KEGGivg:3783681.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01555 Genomic DNA. Translation: CAA24805.1.
AJ507799 Genomic DNA. Translation: CAD53462.1.
PIRiA00713. DJBE2L.
RefSeqiYP_401712.1. NC_007605.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H15X-ray3.10C/F628-641[»]
ProteinModelPortaliP03198.
SMRiP03198.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB00194. Vidarabine.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3783681.
KEGGivg:3783681.

Phylogenomic databases

KOiK18964.

Miscellaneous databases

EvolutionaryTraceiP03198.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDPOL_EBVB9
AccessioniPrimary (citable) accession number: P03198
Secondary accession number(s): Q777B1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 104 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

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.