ID   D6BMG7_HBV              Unreviewed;       344 AA.
AC   D6BMG7;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   11-DEC-2019, entry version 29.
DE   RecName: Full=Protein P {ECO:0000256|SAAS:SAAS00399868};
DE   Flags: Fragment;
OS   Hepatitis B virus (HBV).
OC   Viruses; Hepadnaviridae; Orthohepadnavirus.
OX   NCBI_TaxID=10407 {ECO:0000313|EMBL:ACV03667.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1] {ECO:0000313|EMBL:ACV03667.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=J-27 {ECO:0000313|EMBL:ACV03667.1};
RX   PubMed=20034521; DOI=10.1016/j.antiviral.2009.12.006;
RA   Liu B.M., Li T., Xu J., Li X.G., Dong J.P., Yan P., Yang J.X., Yan L.,
RA   Gao Z.Y., Li W.P., Sun X.W., Wang Y.H., Jiao X.J., Hou C.S., Zhuang H.;
RT   "Characterization of potential antiviral resistance mutations in hepatitis
RT   B virus reverse transcriptase sequences in treatment-naive Chinese
RT   patients.";
RL   Antiviral Res. 85:512-519(2010).
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|SAAS:SAAS00585225}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|SAAS:SAAS01126698};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130,
CC         Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:83828; EC=2.7.7.49;
CC         Evidence={ECO:0000256|SAAS:SAAS01126708};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:11130,
CC         Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|SAAS:SAAS01126713};
CC   -!- SIMILARITY: Belongs to the hepadnaviridae P protein family.
CC       {ECO:0000256|SAAS:SAAS00585232}.
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DR   EMBL; FJ560988; ACV03667.1; -; Genomic_DNA.
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   InterPro; IPR001462; DNApol_viral_C.
DR   InterPro; IPR000477; RT_dom.
DR   Pfam; PF00336; DNA_pol_viral_C; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|SAAS:SAAS00477507};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00118800};
KW   DNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00477605};
KW   Endonuclease {ECO:0000256|SAAS:SAAS00477542};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00477586};
KW   Magnesium {ECO:0000256|SAAS:SAAS00477628};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00477460};
KW   Multifunctional enzyme {ECO:0000256|SAAS:SAAS00118716};
KW   Nuclease {ECO:0000256|SAAS:SAAS00118722};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00477618};
KW   RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00477537};
KW   Transferase {ECO:0000256|SAAS:SAAS00477589}.
FT   DOMAIN          11..254
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACV03667.1"
FT   NON_TER         344
FT                   /evidence="ECO:0000313|EMBL:ACV03667.1"
SQ   SEQUENCE   344 AA;  38795 MW;  8F8BF871C84BCE7A CRC64;
     EDWGPCTEHG EHNIRIPRTP ARVTGGVFLV DKNPHNTTES RLVVDFSQFS RGSTHVSWPK
     FAVPNLQSLT NLLSSNLSWL SLDVSAAFYH IPLHPAAMPH LLVGSSGLPR YVARLSSTSR
     NINYQHGTMQ DLHDSCSRHL YVSLLLLYKT FGRKLHLYSH PIILGFRKIP MGVGLSPFLL
     AQFTSAICSV VRRAFPHCLA FSYMDDVVLG AKSVQHLESL FTSITNFLLS LGIHLNPNKT
     KRWGYSLNFM GYVIGSWGTL PQEHIVLKLK QCFRKLPVNR PIDWKVCQRI VGLLGFAAPF
     TQCGYPALMP LYACIQSKQA FTFSPTYKAF LCKQYQNLYP VARQ
//