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Protein

Protein P

Gene

P

Organism
Ground squirrel hepatitis virus (strain 27) (GSHV)
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
Sitei68Priming of reverse-transcription by covalently linking the first nucleotide of the (-)DNAUniRule annotation1
Metal bindingi467Magnesium; catalyticUniRule annotation1
Metal bindingi587Magnesium; catalyticUniRule annotation1
Metal bindingi588Magnesium; 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
OrganismiGround squirrel hepatitis virus (strain 27) (GSHV)
Taxonomic identifieri10406 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesHepadnaviridaeOrthohepadnavirus
Virus hostiSpermophilus (old world ground squirrels) [TaxID: 9996]
Proteomesi
  • UP000009156 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002223311 – 881Protein PAdd BLAST881

Proteomic databases

PRIDEiP03161

Structurei

3D structure databases

ProteinModelPortaliP03161
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini395 – 636Reverse transcriptaseUniRule annotationAdd BLAST242

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 184Terminal protein domain (TP)UniRule annotationAdd BLAST184
Regioni185 – 384SpacerUniRule annotationAdd BLAST200
Regioni385 – 726Polymerase/reverse transcriptase domain (RT)UniRule annotationAdd BLAST342

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

KOiK21037
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.

P03161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHPFYQLFRN IQSLGEEEVQ ELLGPPEDAL PLLAGEGLNH RVADALNLQL
60 70 80 90 100
PTADLEWIHK TNVITGLYST QTEKFNCNWK QPVFPKIHLD NNLFQKLENY
110 120 130 140 150
FGPLTTNEKR RLKLVFPARF FPNATKYFPL LKGIKDKYPN YTIEHFFAAA
160 170 180 190 200
NYLWTLWESG ILYLRKNQTT LTFRGKPYSW EHRQLEQHNG QQHKSNIRSQ
210 220 230 240 250
QISCMVANSG NLLYTHYHRD KSSNIQTRNL SDNVFKKSKE STRVRCYTYD
260 270 280 290 300
KIQRNRLGQL ARIPCESKAP SEQQQSSLRS KGRDFRNQIQ AYNSSRNKGY
310 320 330 340 350
TTWHSTTSDS IQSGSKKKTH TSNSSFERHT PSFDNEKSDR SPAGICRGTE
360 370 380 390 400
SSNHLRSSQL CLWRSFYYTK PCGTYCLHHI VSSIDDWGPC TFDGDVTIRS
410 420 430 440 450
PRTPRRITGG IFLVDKNPYN SSESRLVVDF SQFSRGHSRV HWPKFAVPNL
460 470 480 490 500
QTLANLLSTN LQWLSLDVSA AFYHIPVSPA AVPHFLVGSP GLERFASCMS
510 520 530 540 550
HDASNRNNSK LQTMHHICSR HLYNTLLLLF KTYGRKLHLL AHPFIMGFRK
560 570 580 590 600
LPMGVGLSPF LLAQFTSALT SMVRRNFPHC LAFAYMDDLV LGARSYEHLT
610 620 630 640 650
AVYSHICSVF LDLGIHLNVE KTKWWGHTLH FMGYTINGAG VLPQDKHVHK
660 670 680 690 700
VTTYLKSIPI NQPLDYKICE RLTGILNYVA PFTKCGYAAL LPLYQAIASH
710 720 730 740 750
TAFVFSSLYK NWLLSLYGEL WPVARQRGVV CSVFADATPT GWGICTTCQL
760 770 780 790 800
ISGTFGFSLP IATAELIAAC LARCWTGARL LGTDNSVVLS GKLTSFPWLL
810 820 830 840 850
ACVANWILRG TSFCYVPSAD NPADLPSRGL LPALRPLPLL RFRPVTKRIS
860 870 880
LWAASPPVST RRPVRVAWAS PVQTCEPWIP P
Length:881
Mass (Da):99,977
Last modified:July 21, 1986 - v1
Checksum:i1E8D2D81DEFF642C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02715 Genomic DNA Translation: AAA46756.1
PIRiA00709 JDVLS
RefSeqiNP_040994.1, NC_001484.1

Genome annotation databases

GeneIDi1488459
KEGGivg:1488459

Similar proteinsi

Entry informationi

Entry nameiDPOL_GSHV
AccessioniPrimary (citable) accession number: P03161
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 23, 2018
This is version 81 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, Reference proteome

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