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Protein P [Includes: Ribonuclease H (EC 3.1.26.4); DNA-directed DNA polymerase (EC 2.7.7.7); RNA-directed DNA polymerase (EC 2.7.7.49)]

 G3XGU0_HBV              Unreviewed;       839 AA.
G3XGU0;
14-DEC-2011, integrated into UniProtKB/TrEMBL.
14-DEC-2011, sequence version 1.
20-JUN-2018, entry version 34.
RecName: Full=Protein P {ECO:0000256|HAMAP-Rule:MF_04073};
Includes:
RecName: Full=Ribonuclease H {ECO:0000256|HAMAP-Rule:MF_04073};
EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_04073};
Includes:
RecName: Full=RNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04073};
EC=2.7.7.49 {ECO:0000256|HAMAP-Rule:MF_04073};
Includes:
RecName: Full=DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04073};
EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_04073};
Name=P {ECO:0000256|HAMAP-Rule:MF_04073, ECO:0000313|EMBL:BAL03307.1};
HBV recombinant B/C.
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=1052603 {ECO:0000313|EMBL:BAL03307.1, ECO:0000313|Proteomes:UP000002661};
[1] {ECO:0000313|Proteomes:UP000002661}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21925554; DOI=10.1016/j.virusres.2011.09.002;
Mulyanto null, Pancawardani P., Depamede S.N., Wahyono A.,
Jirintai S., Nagashima S., Takahashi M., Nishizawa T., Okamoto H.;
"Identification of four novel subgenotypes (C13-C16) and two inter-
genotypic recombinants (C12/G and C13/B3) of hepatitis B virus in
Papua province, Indonesia.";
Virus Res. 163:129-140(2012).
-!- 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. {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118798}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00517655}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00517675}.
-!- 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. {ECO:0000256|HAMAP-Rule:MF_04073}.
-!- 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. {ECO:0000256|HAMAP-Rule:MF_04073}.
-!- DOMAIN: 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. {ECO:0000256|HAMAP-Rule:MF_04073}.
-!- MISCELLANEOUS: Hepadnaviral virions contain probably just one P
protein molecule per particle. {ECO:0000256|HAMAP-Rule:MF_04073}.
-!- SIMILARITY: Belongs to the hepadnaviridae P protein family.
{ECO:0000256|HAMAP-Rule:MF_04073, ECO:0000256|SAAS:SAAS00585232}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04073}.
-----------------------------------------------------------------------
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EMBL; AB644282; BAL03307.1; -; Genomic_DNA.
Proteomes; UP000002661; Genome.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-UniRule.
HAMAP; MF_04073; HBV_DPOL; 1.
InterPro; IPR001462; DNApol_viral_C.
InterPro; IPR000201; DNApol_viral_N.
InterPro; IPR037531; HBV_DPOL.
InterPro; IPR000477; RT_dom.
Pfam; PF00336; DNA_pol_viral_C; 1.
Pfam; PF00242; DNA_pol_viral_N; 1.
Pfam; PF00078; RVT_1; 1.
PROSITE; PS50878; RT_POL; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000002661};
DNA replication {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00517688};
DNA-binding {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00517690};
DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118729};
Endonuclease {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118727};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00956460};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118727};
Inhibition of host innate immune response by virus {ECO:0000256|HAMAP-
Rule:MF_04073, ECO:0000256|SAAS:SAAS00956460};
Inhibition of host RLR pathway by virus {ECO:0000256|HAMAP-
Rule:MF_04073, ECO:0000256|SAAS:SAAS00956460};
Magnesium {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118750};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118726};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00517683};
Nuclease {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118727};
Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118729, ECO:0000256|SAAS:SAAS00517685};
RNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00517685};
Transferase {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00118729, ECO:0000256|SAAS:SAAS00517685};
Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04073,
ECO:0000256|SAAS:SAAS00956460}.
DOMAIN 353 596 Reverse transcriptase.
{ECO:0000259|PROSITE:PS50878}.
REGION 1 177 Terminal protein domain (TP).
{ECO:0000256|HAMAP-Rule:MF_04073}.
REGION 343 686 Polymerase/reverse transcriptase domain
(RT). {ECO:0000256|HAMAP-Rule:MF_04073}.
METAL 425 425 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_04073}.
METAL 547 547 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_04073}.
METAL 548 548 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_04073}.
SITE 63 63 Priming of reverse-transcription by
covalently linking the first nucleotide
of the (-)DNA. {ECO:0000256|HAMAP-
Rule:MF_04073}.
SEQUENCE 839 AA; 94219 MW; DE994E63A476A93D CRC64;
MPLSYQHFRK LLLLDDEAGP LEEELPRLAD EGLNRRVAED LNLGDPNVSI PWTHKVGNFT
GLYSSTIPVF NPEWQTPSFP DIHLKEDIIN WCQQFVGPLT VNENRRLKLI MPARFYPNVT
KYLPLDKGIK PYYPEHVVNH YFQTRHYLHT LWKAGILYKR ETTRSASFCG SPYSWEQELQ
HGRLVLKTSE RHGDESFCSQ SAGILSRSPV GPCVRSQLKQ TRLGLQPQQG SLAKGKSGRS
GSFRARIHPT TRRYFGVDPS GSGYIDTSTT SASSCLHQSA VRKTAYSHLS TSKRQSSSGH
AVELHHIPPS SARSQSEDCW WLQFRNSKPC SDYCLSHIVN LLEDWGPCTE HGEHHIRIPR
TPARVTGGVF LVDKNPHNTT ESRLVVDFSQ FSRGSSHVSW PKFAVPNLQS LTNLLSSNLS
WLSLDVSAAF YHLPLHPAAM PHLLIGSSGL SRYVARLSST SRNINYQHGP MQDLHDSCSR
NLYVSLMLLY KTFGWKLHLY SHPIILGFRK IPMGVGLSPF LLAQFTSAIC SVVRRAFPHC
LAFSYMDDVV LGAKSVQHLE SLYTSITNFL LSLGIHLNPN KTKRWGYTLN FMGYVIGSWG
TLPQDHIVQK IKQCFRKLPV NRPIDWKVCQ RIVGLLGFAA PFTQCGYPAL MPLYACIHAK
QAFTFSPTYK AFLCKQYLNL YPVARQRSGL CQVFADATPT GWGLALGHQR VRGTFVAPLP
IHTAELLAAC FARSRSGATL IGTDNSVVLS RKYTSFPWLL GCAANWILRG TSFVYVPSAL
NPADDPSRGR LGIYRPLLRL PFRPTTGRTS LYAVSPPVPS HLPVRVHFAS PLHVAWRPP


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