ID D6BMG7_HBV Unreviewed; 344 AA. AC D6BMG7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 17-JUN-2020, entry version 30. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 Gene3D; 3.30.70.270; -; 1. 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 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:SAAS01262043}; 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:SAAS01262069}; KW RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS01262051}; KW Transferase {ECO:0000256|SAAS:SAAS01262065}. 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 //