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Database: UniProt
Entry: D6BMN3_HBV
LinkDB: D6BMN3_HBV
Original site: D6BMN3_HBV 
ID   D6BMN3_HBV              Unreviewed;       344 AA.
AC   D6BMN3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Protein P {ECO:0000256|ARBA:ARBA00021149};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE   Flags: Fragment;
OS   Hepatitis B virus (HBV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX   NCBI_TaxID=10407 {ECO:0000313|EMBL:ACV03733.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1] {ECO:0000313|EMBL:ACV03733.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S40 {ECO:0000313|EMBL:ACV03733.1};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000077};
CC   -!- SIMILARITY: Belongs to the hepadnaviridae P protein family.
CC       {ECO:0000256|ARBA:ARBA00007994}.
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DR   EMBL; FJ561021; ACV03733.1; -; Genomic_DNA.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; 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; DNA/RNA polymerases; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..254
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACV03733.1"
FT   NON_TER         344
FT                   /evidence="ECO:0000313|EMBL:ACV03733.1"
SQ   SEQUENCE   344 AA;  38867 MW;  894B70E362BA3C93 CRC64;
     EDWGPCSEHG EHRIRTPRTP ARVTGGVFLV DKNPHNTTES RLVVDFSQFS RGNTRVSWPK
     FAVPNLQSLT NLLSSNLSWL SLDVSAAFYH LPLHPAAMPH LLVGSSGLSR YVARLSSNSR
     IINNQHRTMQ NLHISCSRNL YVSLMLLYKT YGRKLHLYSH PIILGFRKIP MGVGLSPFLL
     AQFTSAICSV VRRAFPHCLA FSYMDDVVLG AKSVQHLESL YAAVTNFLLS LGIHLNPHKT
     KRWGYSLNFM GYVIGSWGTL PQEHIVQKIK MCFRKLPVNR PIDWKVCQRI VGLLGFAAPF
     TQCGYPALMP LYACIQAKQA FTFSPTYKAF LSKQYLNLYP VARQ
//
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