Protein P - Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)

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P03156 (DPOL_HBVD3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 74. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein P

Including the following 3 domains:

DNA-directed DNA polymerase
EC=2.7.7.7
RNA-directed DNA polymerase
EC=2.7.7.49
Ribonuclease H
EC=3.1.26.4

Gene names

Name:

Organism

Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D) [Complete proteome]

Taxonomic identifier

490133 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Hepadnaviridae › Orthohepadnavirus ›

Virus host

Homo sapiens (Human) [TaxID: 9606]
Pan troglodytes (Chimpanzee) [TaxID: 9598]

Protein attributes

Sequence length	832 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery By similarity.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Endonucleolytic cleavage to 5'-phosphomonoester.
Enzyme regulation	Activated by host HSP70 and HSP40 in vitro to be able to bind the epsilon loop of the pgRNA. Because deletion of the RNase H region renders the protein partly chaperone-independent, the chaperones may be needed indirectly to relieve occlusion of the RNA-binding site by this domain. Inhibited by several reverse-transcriptase inhibitors: Lamivudine, Adefovir and Entecavir By similarity.
Domain	Terminal protein domain (TP) is hepadnavirus-specific. Spacer domain is highly variable and separates the TP and RT domains. Polymerase/reverse-transcriptase domain (RT) and ribonuclease H domain (RH) are similar to retrovirus reverse transcriptase/RNase H By similarity. The polymerase/reverse transcriptase (RT) and ribonuclease H (RH) domains are structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RH domain stabilizes the association of RT with primer-template By similarity.
Miscellaneous	Hepadnaviral virions contain probably just one P protein molecule per particle By similarity.
Sequence similarities	Belongs to the hepadnaviridae P protein family. Contains 1 reverse transcriptase domain.

Ontologies

Keywords
Biological process	DNA replication Host-virus interaction Inhibition of host IFN-mediated response initiation by virus Inhibition of host TBK1-IKBKE-DDX3 complex by virus Inhibition of host innate immune response by virus Viral immunoevasion
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	DNA-directed DNA polymerase Endonuclease Hydrolase Nuclease Nucleotidyltransferase RNA-directed DNA polymerase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC suppression by virus of host innate immune response Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon production Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease H activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 832

832

Protein P

PRO_0000222344

Regions

Domain

346 – 589

244

Reverse transcriptase

Region

1 – 177

177

Terminal protein domain (TP) By similarity

Region

178 – 335

158

Spacer By similarity

Region

336 – 679

344

Polymerase/reverse transcriptase domain (RT) By similarity

Region

680 – 832

153

RnaseH domain (RH) By similarity

Sites

Metal binding

418

Magnesium; catalytic By similarity

Metal binding

540

Magnesium; catalytic By similarity

Metal binding

541

Magnesium; catalytic By similarity

Site

Priming of reverse-transcription by covalently linking the first nucleotide of the (-)DNA By similarity

Natural variations

Natural variant

118

K → N in strain: Latvia.

Natural variant

136

H → Y in strain: Latvia.

Natural variant

178

D → E in strain: Latvia.

Natural variant

236

F → I in strain: Latvia.

Natural variant

240

A → T in strain: Latvia.

Natural variant

255 – 257

TNF → RNV in strain: Latvia.

Natural variant

266

H → Y in strain: Latvia.

Natural variant

293

F → L in strain: Latvia.

Natural variant

330

L → H in strain: Latvia.

Natural variant

356

S → A in strain: Latvia.

Natural variant

457 – 459

LNN → FNY in strain: Latvia.

Natural variant

465 – 466

PD → QN in strain: Latvia.

Natural variant

470

Y → S in strain: Latvia.

Natural variant

583

N → H in strain: Latvia.

Natural variant

598

E → D in strain: Latvia.

Natural variant

613

I → V in strain: Latvia.

Natural variant

709 – 711

SAP → LAR in strain: Latvia.

Natural variant

734

I → L in strain: Latvia.

Natural variant

749

F → Y in strain: Latvia.

Sequences

Sequence

Length

Mass (Da)

Tools

P03156 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 7AB3AAE58A57D0D6
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FASTA

832

93,677

        10         20         30         40         50         60 
MPLSYQHFRR LLLLDDEAGP LEEELPRLAD EGLNRRVAED LNLGNLNVSI PWTHKVGNFT 

        70         80         90        100        110        120 
GLYSSTVPVF NPHWKTPSFP NIHLHQDIIK KCEQFVGPLT VNEKRRLQLI MPARFYPKVT 

       130        140        150        160        170        180 
KYLPLDKGIK PYYPEHLVNH YFQTRHYLHT LWKAGILYKR ETTHSASFCG SPYSWEQDLQ 

       190        200        210        220        230        240 
HGAESFHQQS SGILSRPPVG SSLQSKHRKS RLGLQSQQGH LARRQQGRSW SIRAGFHPTA 

       250        260        270        280        290        300 
RRPFGVEPSG SGHTTNFASK SASCLHQSPV RKAAYPAVST FEKHSSSGHA VEFHNLPPNS 

       310        320        330        340        350        360 
ARSQSERPVF PCWWLQFRNS KPCSDYCLSL IVNLLEDWGP CAEHGEHHIR IPRTPSRVTG 

       370        380        390        400        410        420 
GVFLVDKNPH NTAESRLVVD FSQFSRGNYR VSWPKFAVPN LQSLTNLLSS NLSWLSLDVS 

       430        440        450        460        470        480 
AAFYHLPLHP AAMPHLLVGS SGLSRYVARL SSNSRILNNQ HGTMPDLHDY CSRNLYVSLL 

       490        500        510        520        530        540 
LLYQTFGRKL HLYSHPIILG FRKIPMGVGL SPFLLAQFTS AICSVVRRAF PHCLAFSYMD 

       550        560        570        580        590        600 
DVVLGAKSVQ HLESLFTAVT NFLLSLGIHL NPNKTKRWGY SLNFMGYVIG CYGSLPQEHI 

       610        620        630        640        650        660 
IQKIKECFRK LPINRPIDWK VCQRIVGLLG FAAPFTQCGY PALMPLYACI QSKQAFTFSP 

       670        680        690        700        710        720 
TYKAFLCKQY LNLYPVARQR PGLCQVFADA TPTGWGLVMG HQRMRGTFSA PLPIHTAELL 

       730        740        750        760        770        780 
AACFARSRSG ANIIGTDNSV VLSRKYTSFP WLLGCAANWI LRGTSFVYVP SALNPADDPS 

       790        800        810        820        830 
RGRLGLSRPL LRLPFRPTTG RTSLYADSPS VPSHLPDRVH FASPLHVAWR PP

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References

[1]	"Nucleotide sequence of the hepatitis B virus genome (subtype ayw) cloned in E. coli." Galibert F., Mandart E., Fitoussi F., Tiollais P., Charnay P. Nature 281:646-650(1979) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Subtype ayw variant of hepatitis B virus. DNA primary structure analysis." Bichko V., Pushko P., Dreilina D., Pumpen P., Gren E.Y. FEBS Lett. 185:208-212(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Latvia.
[3]	"Hepatitis B virus replication." Beck J., Nassal M. World J. Gastroenterol. 13:48-64(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Web resources

HepSEQ

Hepatitis virus B database

Cross-references

Sequence databases
EMBL GenBank DDBJ	V01460 Genomic DNA. No translation available. X02496 Genomic DNA. Translation: CAB41700.1.
PIR	JDVLVA. A00702. JDVLVB. A00703.
3D structure databases
ProteinModelPortal	P03156.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	2.7.7.7. 2641.
Family and domain databases
InterPro	IPR001462. DNApol_viral_C. IPR000201. DNApol_viral_N. IPR000477. RVT. [Graphical view]
Pfam	PF00336. DNA_pol_viral_C. 1 hit. PF00242. DNA_pol_viral_N. 1 hit. PF00078. RVT_1. 1 hit. [Graphical view]
PROSITE	PS50878. RT_POL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPOL_HBVD3

Accession

Primary (citable) accession number: P03156
Secondary accession number(s): P04484

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 3 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Natural variations

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents