P03198 (DPOL_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase catalytic subunit
EC=2.7.7.7

Gene names

ORF Names:

BALF5

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]

Taxonomic identifier

10377 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus › Epstein-Barr virus (strain GD1)

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	1015 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	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. Ref.3 Ref.4
Subcellular location	Host nucleus. Note: the protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs. Ref.5
Sequence similarities	Belongs to the DNA polymerase type-B family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Host nucleus
Developmental stage	Early protein
Ligand	DNA-binding
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1015	1015	DNA polymerase catalytic subunit		PRO_0000046505

Sequences

	Sequence		Length	Mass (Da)
	P03198 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0503B5E269399812	FASTA	1,015	113,418
	10 20 30 40 50 60 MSGGLFYNPF LRPNKGLLKK PDKEYLRLIP KCFQTPGAAG VVDVRGPQPP LCFYQDSLTV 70 80 90 100 110 120 VGGDEDGKGM WWRQRAQEGT ARPEADTHGS PLDFHVYDIL ETVYTHEKCA VIPSDKQGYV 130 140 150 160 170 180 VPCGIVIKLL GRRKADGASV CVNVFGQQAY FYASAPQGLD VEFAVLSALK ASTFDRRTPC 190 200 210 220 230 240 RVSVEKVTRR SIMGYGNHAG DYHKITLSHP NSVCHVATWL QDKHGCRIFE ANVDATRRFV 250 260 270 280 290 300 LDNDFVTFGW YSCRRAIPRL QHRDSYAELE YDCEVGDLSV RREDSSWPSY QALAFDIECL 310 320 330 340 350 360 GEEGFPTATN EADLILQISC VLWSTGEEAG RYRRILLTLG TCEDIEGVEV YEFPSELDML 370 380 390 400 410 420 YAFFQLIRDL SVEIVTGYNV ANFDWPYILD RARHIYSINP ASLGKIRAGG VCEVRRPHDA 430 440 450 460 470 480 GKGFLRANTK VRITGLIPID MYAVCRDKLS LSDYKLDTVA RHLLGAKKED VHYKEIPRLF 490 500 510 520 530 540 AAGPEGRRRL GMYCVQDSAL VMDLLNHFVI HVEVAEIAKI AHIPCRRVLD DGQQIRVFSC 550 560 570 580 590 600 LLAAAQKENF ILPMPSASDR DGYQGATVIQ PLSGFYNSPV LVVDFASLYP SIIQAHNLCY 610 620 630 640 650 660 STMITPGEEH RLAGLRPGED YESFRLTGGV YHFVKKHVHE SFLASLLTSW LAKRKAIKKL 670 680 690 700 710 720 LAACEDPRQR TILDKQQLAI KCTCNAVYGF TGVANGLFPC LSIAETVTLQ GRTMLERAKA 730 740 750 760 770 780 FVEALSPANL QALAPSPDAW APLNPEGQLR VIYGDTDSLF IECRGFSESE TLRFADALAA 790 800 810 820 830 840 HTTRSLFVAP ISLEAEKTFS CLMLITKKRY VGVLTDGKTL MKGVELVRKT ACKFVQTRCR 850 860 870 880 890 900 RVLDLVLADA RVKEAASLLS HRPFQESFTQ GLPVGFLPVI DILNQAYTDL REGRVPMGEL 910 920 930 940 950 960 CFSTELSRKL SAYKSTQMPH LAVYQKFVER NEELPQIHDR IQYVFVEPKG GVKGARKTEM 970 980 990 1000 1010 AEDPAYAERH GVPVAVDHYF DKLLQGAANI LQCLFDNNSG AALSVLQNFT ARPPF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8 Epstein-Barr virus." Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G. Mol. Biol. Med. 1:21-45(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"DNA sequence and expression of the B95-8 Epstein-Barr virus genome." Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G. Nature 310:207-211(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"A major DNA binding protein encoded by BALF2 open reading frame of Epstein-Barr virus (EBV) forms a complex with other EBV DNA-binding proteins: DNAase, EA-D, and DNA polymerase." Zeng Y., Middeldorp J., Madjar J.J., Ooka T. Virology 239:285-295(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BALF2, BMRF1, BGL5.
[4]	"The Epstein-Barr virus pol catalytic subunit physically interacts with the BBLF4-BSLF1-BBLF2/3 complex." Fujii K., Yokoyama N., Kiyono T., Kuzushima K., Homma M., Nishiyama Y., Fujita M., Tsurumi T. J. Virol. 74:2550-2557(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH THE PUTATIVE PRIMASE-HELICASE COMPLEX.
[5]	"Architecture of replication compartments formed during Epstein-Barr virus lytic replication." Daikoku T., Kudoh A., Fujita M., Sugaya Y., Isomura H., Shirata N., Tsurumi T. J. Virol. 79:3409-3418(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"A functional and structural basis for TCR cross-reactivity in multiple sclerosis." Lang H.L.E., Jacobsen H., Ikemizu S., Andersson C., Harlos K., Madsen L., Hjorth P., Sondergaard L., Svejgaard A., Wucherpfennig K., Stuart D.I., Bell J.I., Jones E.Y., Fugger L. Nat. Immunol. 3:940-943(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 628-641 IN COMPLEX WITH HLA-DRA/HLA-DRB5 HETERODIMER.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01555 Genomic DNA. Translation: CAA24805.1.
AJ507799 Genomic DNA. Translation: CAD53462.1.

PIR

DJBE2L. A00713.

RefSeq

YP_401712.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H15	X-ray	3.10	C/F	628-641	[»]

ProteinModelPortal

P03198.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3783681.

Phylogenomic databases

ProtClustDB

CLSP2509652.

Family and domain databases

Gene3D

3.90.1600.10. 2 hits.

InterPro

IPR006172. 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]

Pfam

PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
[Graphical view]

PRINTS

PR00106. DNAPOLB.

SMART

SM00486. POLBc. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00194. Vidarabine.

EvolutionaryTrace

P03198.

Entry information

Entry name

DPOL_EBVB9

Accession

Primary (citable) accession number: P03198
Secondary accession number(s): Q777B1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program