UniProtKB - P03162 (DPOL_DHBV1)
Protein
Protein P
Gene
P
Organism
Duck hepatitis B virus (strain United States/DHBV-16) (DHBV)
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 (By similarity).By similarity
Catalytic activityi
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)PROSITE-ProRule annotationEC:2.7.7.7PROSITE-ProRule annotation EC:2.7.7.49PROSITE-ProRule annotation
- Endonucleolytic cleavage to 5'-phosphomonoester. 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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 146 | Priming of reverse-transcription by covalently linking the first nucleotide of the (-)DNABy similarity | 1 | |
Metal bindingi | 496 | Magnesium; catalyticPROSITE-ProRule annotation | 1 | |
Metal bindingi | 563 | Magnesium; catalyticPROSITE-ProRule annotation | 1 | |
Metal bindingi | 564 | Magnesium; catalyticPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- DNA-directed DNA polymerase activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- RNA-directed DNA polymerase activity Source: UniProtKB
- RNA-DNA hybrid ribonuclease activity Source: UniProtKB
GO - Biological processi
- DNA replication Source: UniProtKB-KW
- RNA phosphodiester bond hydrolysis, endonucleolytic Source: UniProtKB
Keywordsi
Molecular function | DNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, RNA-directed DNA polymerase, Transferase |
Biological process | DNA replication |
Ligand | Magnesium, Metal-binding |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:P |
Organismi | Duck hepatitis B virus (strain United States/DHBV-16) (DHBV) |
Taxonomic identifieri | 489543 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Pararnavirae › Artverviricota › Revtraviricetes › Blubervirales › Hepadnaviridae › Avihepadnavirus › |
Virus hosti | Anas (ducks) [TaxID: 8835] |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000222327 | 1 – 836 | Protein PAdd BLAST | 836 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 424 – 613 | Reverse transcriptasePROSITE-ProRule annotationAdd BLAST | 190 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 51 – 250 | Terminal protein domain (TP)By similarityAdd BLAST | 200 | |
Regioni | 251 – 414 | SpacerBy similarityAdd BLAST | 164 | |
Regioni | 415 – 703 | Polymerase/reverse transcriptase domain (RT)By similarityAdd BLAST | 289 | |
Regioni | 704 – 836 | RnaseH domain (RH)By similarityAdd BLAST | 133 |
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 (By similarity).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).By similarity
Sequence similaritiesi
Belongs to the hepadnaviridae P protein family.Curated
Family and domain databases
Gene3Di | 3.30.70.270, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR001462, DNApol_viral_C IPR000201, DNApol_viral_N 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.
P03162-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQKLTRNHWI GLGDCFGGIT TVYCGEKLKL LTIFLVCVLG CQLLRNIEVE
60 70 80 90 100
MPRPLKQSLD QSRWLREAEK QLRVLENLVD SNLEEEKLKP QLSMGEDVQS
110 120 130 140 150
PGKGEPLHPN VRAPLSHVVR AATIDLPRLG NKLPARHHLG KLSGLYQMKG
160 170 180 190 200
CTFNPEWKVP DISDTHFNLD VVNECPSRNW KYLTPAKFWP KSISYFPVQV
210 220 230 240 250
GVKPKYPDNV MQHESIVGKY LTRLYEAGIL YKRISKHLVT FKGQPYNWEQ
260 270 280 290 300
QHLVNQHHIY DGATSSKING RQTDRRRRNT VKPTCRKDDP KRDFDMVRQV
310 320 330 340 350
SNTRSRVRPC ANNGGDKHPP ESGSLACWGG KESRIIKSDS SRDSSAPVDS
360 370 380 390 400
RGRPKSTRSF SPLSRRKTTG NHHHSSVFPS SVEATTRGRS TPGKSVSPRD
410 420 430 440 450
SSAIPVRTSG ASDKNSPLEE ENVWYLRGNT SWPNRITGKL FLVDKNSRNT
460 470 480 490 500
EEARLVVDFS QFSKGKNAMR FPRYWSPNLS TLRRILPVGM PRISLDLSQA
510 520 530 540 550
FYHLPLNPAS SSRLAVSDGQ RVYYFRKAPM GVGLSPFLLH LFTTALGSEI
560 570 580 590 600
SRRFNVWTFT YMDDFLLCHP NARHLNAISH AVCSFLQELG IRINFDKTTP
610 620 630 640 650
SPVNEIRFLG YQIDENFMKI EESRWKELRT VIKKIKVGEW YDWKCIQRFV
660 670 680 690 700
GHLNFVLPFT KGNIEMLKPM YAAITNQVNF SFSSSYRTLL YKLTMGVCKL
710 720 730 740 750
RIKPKSSVPL PRVATDATPT HGAISHITGG SAVFAFSKVR DIHVQELLMS
760 770 780 790 800
CLAKIMIKPR CLLSDSTFVC HKRYQTLPWH FAMLAKQLLK PIQLYFVPSK
810 820 830
YNPADGPSRH KPPDWTAFPY TPLSKAIYIP HRLCGT
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K01834 Genomic DNA Translation: AAA45742.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | K01834 Genomic DNA Translation: AAA45742.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Family and domain databases
Gene3Di | 3.30.70.270, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR001462, DNApol_viral_C IPR000201, DNApol_viral_N 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_DHBV1 | |
Accessioni | P03162Primary (citable) accession number: P03162 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | October 1, 1996 | |
Last modified: | December 2, 2020 | |
This is version 94 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |