DPOL_WHV6
ID DPOL_WHV6 Reviewed; 556 AA.
AC P11292;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protein P;
DE Includes:
DE RecName: Full=DNA-directed DNA polymerase;
DE EC=2.7.7.7;
DE Includes:
DE RecName: Full=RNA-directed DNA polymerase;
DE EC=2.7.7.49;
DE Includes:
DE RecName: Full=Ribonuclease H;
DE EC=3.1.26.4;
DE Flags: Fragment;
GN Name=P;
OS Woodchuck hepatitis B virus (isolate w64/pWS23) (WHV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10436;
OH NCBI_TaxID=9995; Marmota monax (Woodchuck).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3582979; DOI=10.1016/0378-1119(86)90325-2;
RA Etiemble J., Moeroey T., Trepo C., Tiollais P., Buendia M.-A.;
RT "Nucleotide sequence of the woodchuck hepatitis virus surface antigen mRNAs
RT and the variability of three overlapping viral genes.";
RL Gene 50:207-214(1986).
RN [2]
RP REVIEW.
RX PubMed=17206754; DOI=10.3748/wjg.v13.i1.48;
RA Beck J., Nassal M.;
RT "Hepatitis B virus replication.";
RL World J. Gastroenterol. 13:48-64(2007).
CC -!- FUNCTION: Multifunctional enzyme that converts the viral RNA genome
CC into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA
CC polymerase activity that can copy either DNA or RNA templates, and a
CC ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-
CC DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic
CC mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together
CC with the P protein, and reverse-transcribed inside the nucleocapsid.
CC Initiation of reverse-transcription occurs first by binding the epsilon
CC loop on the pgRNA genome, and is initiated by protein priming, thereby
CC the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA
CC is synthesized from the (-)DNA template and generates the relaxed
CC circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA
CC migrates in the nucleus, and is converted into a plasmid-like
CC covalently closed circular DNA (cccDNA). The activity of P protein does
CC not seem to be necessary for cccDNA generation, and is presumably
CC released from (+)DNA by host nuclear DNA repair machinery (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- ACTIVITY REGULATION: Activated by host HSP70 and HSP40 in vitro to be
CC able to bind the epsilon loop of the pgRNA. Because deletion of the
CC RNase H region renders the protein partly chaperone-independent, the
CC chaperones may be needed indirectly to relieve occlusion of the RNA-
CC binding site by this domain. Inhibited by several reverse-transcriptase
CC inhibitors: Lamivudine, Adefovir and Entecavir (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: Terminal protein domain (TP) is hepadnavirus-specific. Spacer
CC domain is highly variable and separates the TP and RT domains.
CC Polymerase/reverse-transcriptase domain (RT) and ribonuclease H domain
CC (RH) are similar to retrovirus reverse transcriptase/RNase H (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The polymerase/reverse transcriptase (RT) and ribonuclease H
CC (RH) domains are structured in five subdomains: finger, palm, thumb,
CC connection and RNase H. Within the palm subdomain, the 'primer grip'
CC region is thought to be involved in the positioning of the primer
CC terminus for accommodating the incoming nucleotide. The RH domain
CC stabilizes the association of RT with primer-template (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hepadnaviridae P protein family.
CC {ECO:0000305}.
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DR EMBL; M15954; AAA69573.1; -; mRNA.
DR PIR; A29498; JDVL64.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001462; DNApol_viral_C.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR Pfam; PF00336; DNA_pol_viral_C; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 2: Evidence at transcript level;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; RNA-directed DNA polymerase; Transferase.
FT CHAIN 1..556
FT /note="Protein P"
FT /id="PRO_0000222353"
FT DOMAIN 70..311
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 1..59
FT /note="Spacer"
FT /evidence="ECO:0000250"
FT REGION 60..401
FT /note="Polymerase/reverse transcriptase domain (RT)"
FT /evidence="ECO:0000250"
FT REGION 402..556
FT /note="RnaseH domain (RH)"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT NON_TER 1
SQ SEQUENCE 556 AA; 61872 MW; 135426F9A1438869 CRC64;
SKRYSPPLNY EKSDFSSPGV RGRITRLDNN GTPPQCLWRS FYNTKPCGSY CIHHIVSSLD
DWGPCTVTGD VTIKSPRTPR RITGGVFLVD KNPNNSSESR LVVDFSQFSR GHTRVHWPKF
AVPNLQTLAN LLSTNLQWLS LDVSAAFYHI PISPAAVPHL LVGSPGLERF TTCLSSSTHN
GNDSQLQTMH ALCTRHVYSS LLLLFKTYGR KLHLLAHPFI MGFRKLPMGV GLSPFLLAQF
TSALASMVRR NFPHCVVFAY MDDLVLGART SEHLTAIYSH ICSVFLDLGI HLNVNKTKWW
GNHLHFMGYV ITSSGVLPQD KHVKKLSRYL RSVPVNQPLD YKICERLTGI LNYVAPFTLC
GYAALMPLYH AIASRTAFIF SSLYKSWLLS LYEELWPVVR QRGVVCTVFA DATPTGWGIA
TTCQLLSGTF AFPLPIATAE LIAACLARCW TGARLLGTDN SVVLSGKLTS FPWLLACVAN
WILRGTSFCY VPSALNPADL PSRGLLPVLR PLPRLRLRPQ TSRISLWAAS PPVSPRRPVR
VAWSSPVQTC EPWIPP
