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Database: UniProt
Entry: B4ZYU9_HBV
LinkDB: B4ZYU9_HBV
Original site: B4ZYU9_HBV 
ID   B4ZYU9_HBV              Unreviewed;       832 AA.
AC   B4ZYU9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   03-MAY-2023, entry version 63.
DE   RecName: Full=Protein P {ECO:0000256|HAMAP-Rule:MF_04073};
DE   Includes:
DE     RecName: Full=DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04073};
DE              EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_04073};
DE   Includes:
DE     RecName: Full=RNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_04073};
DE              EC=2.7.7.49 {ECO:0000256|HAMAP-Rule:MF_04073};
DE   Includes:
DE     RecName: Full=Ribonuclease H {ECO:0000256|HAMAP-Rule:MF_04073};
DE              EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_04073};
GN   Name=P {ECO:0000256|HAMAP-Rule:MF_04073, ECO:0000313|EMBL:ACG68646.1};
OS   Hepatitis B virus (HBV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX   NCBI_TaxID=10407 {ECO:0000313|EMBL:ACG68646.1, ECO:0000313|Proteomes:UP000133850};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1] {ECO:0000313|EMBL:ACG68646.1, ECO:0000313|Proteomes:UP000133850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=165 {ECO:0000313|EMBL:ACG68646.1};
RA   Sun X.-F., Zhang Y.-X., Hou J.-L., Wang Z.-H.;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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.
CC       {ECO:0000256|HAMAP-Rule:MF_04073}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|HAMAP-
CC         Rule:MF_04073};
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:0000256|HAMAP-
CC         Rule:MF_04073};
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:0000256|HAMAP-
CC         Rule:MF_04073};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_04073}.
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.
CC       {ECO:0000256|HAMAP-Rule:MF_04073}.
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.
CC       {ECO:0000256|HAMAP-Rule:MF_04073}.
CC   -!- MISCELLANEOUS: Hepadnaviral virions contain probably just one P protein
CC       molecule per particle. {ECO:0000256|HAMAP-Rule:MF_04073}.
CC   -!- SIMILARITY: Belongs to the hepadnaviridae P protein family.
CC       {ECO:0000256|ARBA:ARBA00007994, ECO:0000256|HAMAP-Rule:MF_04073}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_04073}.
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DR   EMBL; EU787436; ACG68646.1; -; Genomic_DNA.
DR   Proteomes; UP000133850; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.270; -; 1.
DR   HAMAP; MF_04073; HBV_DPOL; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001462; DNApol_viral_C.
DR   InterPro; IPR000201; DNApol_viral_N.
DR   InterPro; IPR037531; HBV_DPOL.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR000477; RT_dom.
DR   Pfam; PF00336; DNA_pol_viral_C; 1.
DR   Pfam; PF00242; DNA_pol_viral_N; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_04073}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_04073};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|HAMAP-Rule:MF_04073};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_04073}; Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04073};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_04073};
KW   Inhibition of host innate immune response by virus
KW   {ECO:0000256|ARBA:ARBA00022632, ECO:0000256|HAMAP-Rule:MF_04073};
KW   Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482,
KW   ECO:0000256|HAMAP-Rule:MF_04073};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_04073};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_04073};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04073};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_04073};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_04073};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918,
KW   ECO:0000256|HAMAP-Rule:MF_04073};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_04073};
KW   Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280, ECO:0000256|HAMAP-
KW   Rule:MF_04073}.
FT   DOMAIN          346..589
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          1..177
FT                   /note="Terminal protein domain (TP)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04073"
FT   REGION          189..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..679
FT                   /note="Polymerase/reverse transcriptase domain (RT)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04073"
FT   COMPBIAS        189..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         418
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04073"
FT   BINDING         540
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04073"
FT   BINDING         541
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04073"
FT   SITE            63
FT                   /note="Priming of reverse-transcription by covalently
FT                   linking the first nucleotide of the (-)DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04073"
SQ   SEQUENCE   832 AA;  93781 MW;  9CEF91ED63AF477C CRC64;
     MPLSYQHFRR LLLLDDEAGP LEEELPRLAD EGLNRRVAED LNLGNLNVSI PWTHKVGNFT
     GLYSSTVPVF NPHWKTPSFP NIHLHQDIIK KCEQFVGPLT VNEKRRLQLI MPARFYPNVT
     KYLPLDKGIK PYYPEHLVNH YFQTRHYLHT LWKAGILYKR ETTHSASFCG SPYSWEQELQ
     HGAESFHKQS SGILSRPPVG SSLQSKHRKS RLGLQSQQGH LARRQQGRSW SIRAGIHPTA
     RRPFGVEPSG SGHTTNFASK SASCLYQSPV RKAAYPSVST FEKHSSSGHA VELHNLPPNS
     ARSQSERPVF PCWWLQFRNS KPCSDYCLSH IVNLLEDWGP CAEHGEHHIR IPRTPARVTG
     GVFLVDKNPH NTAESRLVVD FSQFSRGNYR VSWPKFAVPN LQSLTNLLSS NLSWLSLDVS
     AAFYHLPLHP AAMPHLLVGS SGLSRYVARL SSNSRIFNHQ HGTMQNLHDS CSRNLYVSLL
     LLYQTFGRKL HLYSHPIILG FRKIPMGVGL SPFLLAQFTS AICSVVRRAF PHCLAFSYMD
     DVVLGAKSVQ HLESLFTAVT NFLLSLGIHL NPNKTKRWGY SLHFMGYVIG CYGSLPQEHI
     IQKIKECFRK LPVNRPIDWK VCQRIVGLLG FAAPFTQCGY PALMPLYACI QSKQAFTFSP
     TYKAFLCKQY LNLYPVARQR PGLCQVFADA TPTGWGLVMG HQRMRGTFLA PLPIHTAELL
     AACFARSRSG ANILGTDNSV VLSRKYTSFP WLLGCAANWI LRGTSFVYVP SALNPADDPS
     RGRLGLYRPL LRLPFRPTTG RTSLYADSPS VPSHLPDRVH FASPLHVAWR PP
//
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