UniProtKB - Q05486 (DPOL_HBVF1)
Protein
Protein P
Gene
P
Organism
Hepatitis B virus genotype F2 (isolate Brazil/w4B) (HBV-F)
Status
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
- Endonucleolytic cleavage to 5'-phosphomonoester.UniRule annotation EC:3.1.26.4
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 63 | Priming of reverse-transcription by covalently linking the first nucleotide of the (-)DNAUniRule annotation | 1 | |
Metal bindingi | 429 | Magnesium; catalyticUniRule annotation | 1 | |
Metal bindingi | 551 | Magnesium; catalyticUniRule annotation | 1 | |
Metal bindingi | 552 | Magnesium; catalyticUniRule annotation | 1 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-UniRule
- DNA-directed DNA polymerase activity Source: UniProtKB-UniRule
- metal ion binding Source: UniProtKB-UniRule
- RNA-directed DNA polymerase activity Source: UniProtKB-UniRule
- RNA-DNA hybrid ribonuclease activity Source: UniProtKB-UniRule
GO - Biological processi
- DNA replication Source: UniProtKB-UniRule
- suppression by virus of host innate immune response Source: UniProtKB-UniRule
Keywordsi
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:PUniRule annotation |
Organismi | Hepatitis B virus genotype F2 (isolate Brazil/w4B) (HBV-F) |
Taxonomic identifieri | 45410 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Pararnavirae › Artverviricota › Revtraviricetes › Blubervirales › Hepadnaviridae › Orthohepadnavirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] Pan troglodytes (Chimpanzee) [TaxID: 9598] |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000222338 | 1 – 843 | Protein PAdd BLAST | 843 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 357 – 600 | Reverse transcriptaseUniRule annotationAdd BLAST | 244 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 177 | Terminal protein domain (TP)UniRule annotationAdd BLAST | 177 | |
Regioni | 178 – 346 | SpacerUniRule annotationAdd BLAST | 169 | |
Regioni | 347 – 690 | Polymerase/reverse transcriptase domain (RT)UniRule annotationAdd BLAST | 344 |
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
Family and domain databases
Gene3Di | 3.30.70.270, 1 hit |
HAMAPi | MF_04073, HBV_DPOL, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR001462, DNApol_viral_C IPR000201, DNApol_viral_N IPR037531, HBV_DPOL IPR043128, Rev_trsase/Diguanyl_cyclase IPR000477, RT_dom |
Pfami | View protein in Pfam PF00336, DNA_pol_viral_C, 1 hit PF00242, DNA_pol_viral_N, 1 hit PF00078, RVT_1, 1 hit |
SUPFAMi | SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS50878, RT_POL, 1 hit |
i Sequence
Sequence statusi: Complete.
Q05486-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPLSYPHFRK LLLLDDEAGP LEEELPRLAD EDLNRRVAAD LNLQLPNVSI
60 70 80 90 100
PWTHKVGNFT GLYSSTVPAF NPNWSTPSFP DIHLHQDLIS KCEQFVGPLT
110 120 130 140 150
KNELRRLKLV MPARFYPKVT KYFPMDKGIK PYYPEHAVNH YFKTRHYLHT
160 170 180 190 200
LWKAGILYKR ESTRSASFCG SPYSWEQELQ HGSTSLNDTK RHGTESLCAQ
210 220 230 240 250
SSGILSRPSA GSAIQSKFQQ SRLGLQHKQG QLANGKQGRS GRLRSRVHTP
260 270 280 290 300
TRWPAGVEPS STRCVNNLAS RSASCFHQSA VREKANPSLS TSKRHTSTGN
310 320 330 340 350
AVELNPVPPS SVGSQGKGSV LPCWWLQFRD TEPCSDYCLS HIINLLEDWG
360 370 380 390 400
PCYEHGQHYI RTPRTPARVT GGVFLVDKNP HNTTESRLVV DFSQFSRGTT
410 420 430 440 450
RVSWPKFAVP NLQSLTNLLS SNLSWLSLDV SAAFYHLPLH PAAMPHLLVG
460 470 480 490 500
SSGLSRYVAR LSSTSRIHDH QHGTLQNLHN SCTRNLYVSL LLLFQTLGRK
510 520 530 540 550
LHLYSHPIIL GFRKIPMGVG LSPFLLAQFT SAICSVVRRA FPHCLAFSYM
560 570 580 590 600
DDLVLGAKSV QHLESLYTAV TNFLLSVGIH LNTSKTKRWG YSLHFMGYVI
610 620 630 640 650
GSWGSLPQDH IVHKIKECFR KLPVNRPIDW KVCQRIVGLL GFAAPFTQCG
660 670 680 690 700
YPALMPLYAC ITAKQAFVFS PTYKAFLCKQ YMNLYPVARQ RPGLCQVFAD
710 720 730 740 750
ATPTGWGLAI GHQRMRGTFV APLPIHTAEL LAACFARSRS GATLIGTDNS
760 770 780 790 800
VVLSRKYTSF PWLLGCAANW ILRGTSFVYV PSALNPADDP SRGRLGLYRP
810 820 830 840
LLRLPFQPTT GRTSLYADSP SVPSHLPDRV HFASPLHVAW RPP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X69798 Genomic DNA Translation: CAA49456.1 |
PIRi | JQ2229 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X69798 Genomic DNA Translation: CAA49456.1 |
PIRi | JQ2229 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Chemistry databases
DrugBanki | DB00709, Lamivudine DB01265, Telbivudine |
Family and domain databases
Gene3Di | 3.30.70.270, 1 hit |
HAMAPi | MF_04073, HBV_DPOL, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR001462, DNApol_viral_C IPR000201, DNApol_viral_N IPR037531, HBV_DPOL IPR043128, Rev_trsase/Diguanyl_cyclase IPR000477, RT_dom |
Pfami | View protein in Pfam PF00336, DNA_pol_viral_C, 1 hit PF00242, DNA_pol_viral_N, 1 hit PF00078, RVT_1, 1 hit |
SUPFAMi | SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS50878, RT_POL, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DPOL_HBVF1 | |
Accessioni | Q05486Primary (citable) accession number: Q05486 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | December 2, 2020 | |
This is version 89 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |