Skip Header

Contribute Send feedback
Read comments (?) or add your own

P17395 (DPOL_HBVB4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein P

Including the following 3 domains:

  1. DNA-directed DNA polymerase
    EC=2.7.7.7
  2. RNA-directed DNA polymerase
    EC=2.7.7.49
  3. Ribonuclease H
    EC=3.1.26.4
Gene names
Name:P
OrganismHepatitis B virus genotype B/C subtype adw (isolate Okinawa/pODW282/1998) (HBV-B) [Complete proteome]
Taxonomic identifier10415 [NCBI]
Taxonomic lineageViruses › Retro-transcribing viruses › Hepadnaviridae › Orthohepadnavirus ›
Virus hostHomo sapiens (Human) [TaxID: 9606]
Pan troglodytes (Chimpanzee) [TaxID: 9598]

Protein attributes

Sequence length843 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 843843Protein P
PRO_0000222342

Regions

Domain357 – 600244Reverse transcriptase
Region1 – 177177Terminal protein domain (TP) By similarity
Region178 – 346169Spacer By similarity
Region347 – 690344Polymerase/reverse transcriptase domain (RT) By similarity
Region691 – 843153RnaseH domain (RH) By similarity

Sites

Metal binding4291Magnesium; catalytic By similarity
Metal binding5511Magnesium; catalytic By similarity
Metal binding5521Magnesium; catalytic By similarity
Site631Priming of reverse-transcription by covalently linking the first nucleotide of the (-)DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
P17395 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: E2DC1572C6215CAB

FASTA84394,642
        10         20         30         40         50         60 
MPLSYQHFRK LLLLDEEAGP LEEELPRLAD EGLNRRVAED LNLGNLNVSI PWTHKVGNFT 

        70         80         90        100        110        120 
GLYSSTVPCF NPKWQTPSFP DIHLQEDIVD RCKQFVGPLT VNENRRLKLI MPARFYPNVT 

       130        140        150        160        170        180 
KYLPLDKGIK PYYPEYVVNH YFQTRHYLHT LWKAGILYKR ESTRSASFCG SPYSWEQDLQ 

       190        200        210        220        230        240 
HGRLVFQTSK RHGDKSFCPQ SSGILPRSSV GPCIQSQLRK SRLGPQPEQG QLAGRQQGGS 

       250        260        270        280        290        300 
GSIRARVHPS PWGTVGVEPS GSGPTHNCAS SSSSCLHQSA VRKAAYSLIP TSKGHSSSGH 

       310        320        330        340        350        360 
AVELHHFPPN SSRSRSQGPV LSCWWLQFRN SEPCSEYCLC HIVNLIEDWG PCTEHGEHRI 

       370        380        390        400        410        420 
RTPRTPARVT GGVFLVDKNP HNTTESRLVV DFSQFSRGNT RVSWPKFAVP NLQSLTNLLS 

       430        440        450        460        470        480 
SNLSWLSLDV SAAFYHLPLH PAAMPHLLVG SSGLSRYVAR LSSNSRIINN QHRTMQNLHN 

       490        500        510        520        530        540 
SCSRNLYVSL MLLYKTYGWK LHLYSHPIIL GFRKIPMGVG LSPFLLAQFT SAICSVVRRA 

       550        560        570        580        590        600 
FPHCLAFSYM DDMVLGAKSV QHLESLYAAV TNFLLSLGIH LNPHKTKRWG YSLNFMGYVI 

       610        620        630        640        650        660 
GSWGTLPQEH IVQKIKMWFR KLPVNRPIDW KVCQRIVGLL GFAAPFTQCG YPALMPLYAC 

       670        680        690        700        710        720 
IQAKQAFTFS PTYKAFLTKQ YLNLYPVARQ RPGLCQVFAD ATPTGWGLAI GHQRMRGTFV 

       730        740        750        760        770        780 
SPLPIHTAEL LAACFARSRS GAKLIGTDNS VVLSRKYTSF PWLLGCAANW ILRGTSFVYV 

       790        800        810        820        830        840 
PSALNPADDP SRGRLGLYRP LLRLLYRPTT GRTSLYADSP SVPSHLPDRV HFASPLHVAW 


RPP

« Hide

References

[1]"Typing hepatitis B virus by homology in nucleotide sequence: comparison of surface antigen subtypes."
Okamoto H., Tsuda F., Sakugawa H., Sastrosoewignjo R.I., Imai M., Miyakawa Y., Mayumi M.
J. Gen. Virol. 69:2575-2583(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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		D00330 Genomic DNA. No translation available.
PIRJDVLJ2. E28925.

3D structure databases

ProteinModelPortalP17395.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001462. DNApol_viral_C.
IPR000201. DNApol_viral_N.
IPR000477. RVT.
[Graphical view]
PfamPF00336. DNA_pol_viral_C. 1 hit.
PF00242. DNA_pol_viral_N. 1 hit.
PF00078. RVT_1. 1 hit.
[Graphical view]
PROSITEPS50878. RT_POL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDPOL_HBVB4
AccessionPrimary (citable) accession number: P17395
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents