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Protein

Protein P

Gene

P

Organism
Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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.UniRule annotation

Miscellaneous

Hepadnaviral virions contain probably just one P protein molecule per particle.UniRule annotation

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).UniRule annotation
Endonucleolytic cleavage to 5'-phosphomonoester.UniRule annotation

Enzyme regulationi

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.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei63Priming of reverse-transcription by covalently linking the first nucleotide of the (-)DNAUniRule annotation1
Metal bindingi418Magnesium; catalyticUniRule annotation1
Metal bindingi540Magnesium; catalyticUniRule annotation1
Metal bindingi541Magnesium; catalyticUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, RNA-directed DNA polymerase, Transferase
Biological processDNA replication, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host RLR pathway by virus, Viral immunoevasion
LigandMagnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PUniRule annotation
Including the following 3 domains:
DNA-directed DNA polymeraseUniRule annotation (EC:2.7.7.7UniRule annotation)
RNA-directed DNA polymeraseUniRule annotation (EC:2.7.7.49UniRule annotation)
Ribonuclease HUniRule annotation (EC:3.1.26.4UniRule annotation)
Gene namesi
Name:PUniRule annotation
OrganismiHepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)
Taxonomic identifieri490133 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesHepadnaviridaeOrthohepadnavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002223441 – 832Protein PAdd BLAST832

Proteomic databases

PRIDEiP03156

Structurei

3D structure databases

ProteinModelPortaliP03156
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini346 – 589Reverse transcriptaseUniRule annotationAdd BLAST244

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 177Terminal protein domain (TP)UniRule annotationAdd BLAST177
Regioni178 – 335SpacerUniRule annotationAdd BLAST158
Regioni336 – 679Polymerase/reverse transcriptase domain (RT)UniRule annotationAdd BLAST344

Domaini

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.UniRule annotation
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.UniRule annotation

Sequence similaritiesi

Belongs to the hepadnaviridae P protein family.UniRule annotation

Phylogenomic databases

OrthoDBiVOG0900002B

Family and domain databases

HAMAPiMF_04073 HBV_DPOL, 1 hit
InterProiView protein in InterPro
IPR001462 DNApol_viral_C
IPR000201 DNApol_viral_N
IPR037531 HBV_DPOL
IPR000477 RT_dom
PfamiView protein in Pfam
PF00336 DNA_pol_viral_C, 1 hit
PF00242 DNA_pol_viral_N, 1 hit
PF00078 RVT_1, 1 hit
PROSITEiView protein in PROSITE
PS50878 RT_POL, 1 hit

Sequencei

Sequence statusi: Complete.

P03156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLSYQHFRR LLLLDDEAGP LEEELPRLAD EGLNRRVAED LNLGNLNVSI
60 70 80 90 100
PWTHKVGNFT GLYSSTVPVF NPHWKTPSFP NIHLHQDIIK KCEQFVGPLT
110 120 130 140 150
VNEKRRLQLI MPARFYPKVT KYLPLDKGIK PYYPEHLVNH YFQTRHYLHT
160 170 180 190 200
LWKAGILYKR ETTHSASFCG SPYSWEQDLQ HGAESFHQQS SGILSRPPVG
210 220 230 240 250
SSLQSKHRKS RLGLQSQQGH LARRQQGRSW SIRAGFHPTA RRPFGVEPSG
260 270 280 290 300
SGHTTNFASK SASCLHQSPV RKAAYPAVST FEKHSSSGHA VEFHNLPPNS
310 320 330 340 350
ARSQSERPVF PCWWLQFRNS KPCSDYCLSL IVNLLEDWGP CAEHGEHHIR
360 370 380 390 400
IPRTPSRVTG GVFLVDKNPH NTAESRLVVD FSQFSRGNYR VSWPKFAVPN
410 420 430 440 450
LQSLTNLLSS NLSWLSLDVS AAFYHLPLHP AAMPHLLVGS SGLSRYVARL
460 470 480 490 500
SSNSRILNNQ HGTMPDLHDY CSRNLYVSLL LLYQTFGRKL HLYSHPIILG
510 520 530 540 550
FRKIPMGVGL SPFLLAQFTS AICSVVRRAF PHCLAFSYMD DVVLGAKSVQ
560 570 580 590 600
HLESLFTAVT NFLLSLGIHL NPNKTKRWGY SLNFMGYVIG CYGSLPQEHI
610 620 630 640 650
IQKIKECFRK LPINRPIDWK VCQRIVGLLG FAAPFTQCGY PALMPLYACI
660 670 680 690 700
QSKQAFTFSP TYKAFLCKQY LNLYPVARQR PGLCQVFADA TPTGWGLVMG
710 720 730 740 750
HQRMRGTFSA PLPIHTAELL AACFARSRSG ANIIGTDNSV VLSRKYTSFP
760 770 780 790 800
WLLGCAANWI LRGTSFVYVP SALNPADDPS RGRLGLSRPL LRLPFRPTTG
810 820 830
RTSLYADSPS VPSHLPDRVH FASPLHVAWR PP
Length:832
Mass (Da):93,677
Last modified:July 21, 1986 - v1
Checksum:i7AB3AAE58A57D0D6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti118K → N in strain: Latvia. 1
Natural varianti136H → Y in strain: Latvia. 1
Natural varianti178D → E in strain: Latvia. 1
Natural varianti236F → I in strain: Latvia. 1
Natural varianti240A → T in strain: Latvia. 1
Natural varianti255 – 257TNF → RNV in strain: Latvia. 3
Natural varianti266H → Y in strain: Latvia. 1
Natural varianti293F → L in strain: Latvia. 1
Natural varianti330L → H in strain: Latvia. 1
Natural varianti356S → A in strain: Latvia. 1
Natural varianti457 – 459LNN → FNY in strain: Latvia. 3
Natural varianti465 – 466PD → QN in strain: Latvia. 2
Natural varianti470Y → S in strain: Latvia. 1
Natural varianti583N → H in strain: Latvia. 1
Natural varianti598E → D in strain: Latvia. 1
Natural varianti613I → V in strain: Latvia. 1
Natural varianti709 – 711SAP → LAR in strain: Latvia. 3
Natural varianti734I → L in strain: Latvia. 1
Natural varianti749F → Y in strain: Latvia. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01460 Genomic DNA No translation available.
X02496 Genomic DNA Translation: CAB41700.1
PIRiA00702 JDVLVA
A00703 JDVLVB

Similar proteinsi

Entry informationi

Entry nameiDPOL_HBVD3
AccessioniPrimary (citable) accession number: P03156
Secondary accession number(s): P04484
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 23, 2018
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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