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Protein

Protein P

Gene

P

Organism
Hepatitis B virus genotype F2 (isolate Argentina/sa16/2000) (HBV-F)
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

Activity 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 bindingi429Magnesium; catalyticUniRule annotation1
Metal bindingi551Magnesium; catalyticUniRule annotation1
Metal bindingi552Magnesium; 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 F2 (isolate Argentina/sa16/2000) (HBV-F)
Taxonomic identifieri489501 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesHepadnaviridaeOrthohepadnavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
Proteomesi
  • UP000008031 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003232761 – 843Protein PAdd BLAST843

Proteomic databases

PRIDEiQ99HR5

Structurei

3D structure databases

ProteinModelPortaliQ99HR5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini357 – 600Reverse transcriptaseUniRule annotationAdd BLAST244

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 177Terminal protein domain (TP)UniRule annotationAdd BLAST177
Regioni178 – 346SpacerUniRule annotationAdd BLAST169
Regioni347 – 690Polymerase/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.

Q99HR5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPLSYPHFRK LLLLDDEAGP LEEELPRLAD EGLNRRVAED LNLQLPNVSI
60 70 80 90 100
PWTHKVGNFT GLYSSTVPAF NPHWLTPSFP DIHLHQDLIS KCEQFVGPLT
110 120 130 140 150
KNELRRLKLI MPARFFPKLT KYFPLEKGIK PYYPEHAVNH YFKTRHYLHT
160 170 180 190 200
LWKAGILYKR ESTRSASFCG SPYSWEQELQ HGSTSLNDKK GHGTESLCAQ
210 220 230 240 250
STGILSRTSA GSSFQSKFQQ SRLGLQQKQG HLANGKQGRS GRLRSRVHTP
260 270 280 290 300
TRWPVGVEPS GTRCSNNLAS RSASCFHQSA VREEANPSLS TSKRHTSTGN
310 320 330 340 350
AVELNPVPPG LVGSEGKGSV FSCWWLQFRD AEPCSDYCLS HIINLLEDWG
360 370 380 390 400
PCYEHGQHHI RTPRTPARVT GGVFLVDKNP HNTTESRLVV DFSQFSRGTT
410 420 430 440 450
RVSWPKFAVP NLQSLTNLLS SNLSWLSLDV SAAFYHLPLH PAAMPHLLVG
460 470 480 490 500
SSGLSRYVAR LSSNSRIYDH QHGTMQNLHN SCSRNLYVSL LLLFQTLGRK
510 520 530 540 550
LHLYSHPIIL GFRKIPMGVG LSPFLLAQFT SAICSVVRRA FPHCLAFSYM
560 570 580 590 600
DDLVLGAKSV QHLESLYTAV TNFLLSVGIH LNTSKTKRWG YNLHFMGYVI
610 620 630 640 650
GSWGALPQDH IVHKIKECFR KLPVNRPIDW KVCQRIVGLL GFAAPFTQCG
660 670 680 690 700
YPALMPLYTC ITAKQAFVFS PTYKAFLCKQ YMNLYPVARQ RPGLCQVFAD
710 720 730 740 750
ATPTGWGLAI GHQRMRGTFV APLPIHTAEL LAACFARSRS GANIIGTDNS
760 770 780 790 800
VVLSRKYTSF PWLLGCAANW ILRGTSFVYV PSALNPADDP SRGRLGLYRP
810 820 830 840
LLRLPFQPTT GRTSLYADSP SVPSHLPVRV HFASPLHVAW RPP
Length:843
Mass (Da):94,344
Last modified:June 1, 2001 - v1
Checksum:iF5BAAB3381A4488E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF223965 Genomic DNA Translation: AAG49733.1

Similar proteinsi

Cross-referencesi

Web resourcesi

HepSEQ

Hepatitis virus B database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF223965 Genomic DNA Translation: AAG49733.1

3D structure databases

ProteinModelPortaliQ99HR5
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ99HR5

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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
ProtoNetiSearch...

Entry informationi

Entry nameiDPOL_HBVF4
AccessioniPrimary (citable) accession number: Q99HR5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 1, 2001
Last modified: September 12, 2018
This is version 65 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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