ID D6BMG7_HBV Unreviewed; 344 AA. AC D6BMG7; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 01-OCT-2014, entry version 11. DE SubName: Full=Polymerase {ECO:0000313|EMBL:ACV03667.1}; DE Flags: Fragment {ECO:0000313|EMBL:ACV03667.1}; OS Hepatitis B virus (HBV). OC Viruses; Retro-transcribing viruses; Hepadnaviridae; OC 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}; RA Baoming L., Tong L., Hui Z.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {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., RA Zhuang H.; RT "Characterization of potential antiviral resistance mutations in RT hepatitis B virus reverse transcriptase sequences in treatment-naive RT Chinese patients."; RL Antiviral Res. 85:512-519(2010). CC -!- FUNCTION: Multifunctional enzyme that converts the viral RNA CC genome into dsDNA in viral cytoplasmic capsids. This enzyme CC displays a DNA polymerase activity that can copy either DNA or RNA CC templates, and a ribonuclease H (RNase H) activity that cleaves CC the RNA strand of RNA-DNA heteroduplexes in a partially processive CC 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA CC (pgRNA) are encapsidated together with the P protein, and reverse- CC transcribed inside the nucleocapsid. Initiation of reverse- CC transcription occurs first by binding the epsilon loop on the CC pgRNA genome, and is initiated by protein priming, thereby the 5'- CC end of (-)DNA is covalently linked to P protein. Partial (+)DNA is CC synthesized from the (-)DNA template and generates the relaxed CC circular DNA (RC-DNA) genome. After budding and infection, the RC- CC DNA migrates in the nucleus, and is converted into a plasmid-like CC covalently closed circular DNA (cccDNA). The activity of P protein CC does not seem to be necessary for cccDNA generation, and is CC presumably released from (+)DNA by host nuclear DNA repair CC machinery. {ECO:0000256|SAAS:SAAS00118798}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000256|SAAS:SAAS00118802}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. {ECO:0000256|SAAS:SAAS00118801}. CC -!- SIMILARITY: Contains 1 reverse transcriptase domain. CC {ECO:0000256|RuleBase:RU000322}. CC -!- SIMILARITY: Contains reverse transcriptase domain. CC {ECO:0000256|SAAS:SAAS00118799}. 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:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro. 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 4: Predicted; KW DNA replication {ECO:0000256|SAAS:SAAS00118795}; KW DNA-binding {ECO:0000256|SAAS:SAAS00118800}; KW DNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00118729}; KW Endonuclease {ECO:0000256|SAAS:SAAS00118727}; KW Hydrolase {ECO:0000256|SAAS:SAAS00118728}; KW Magnesium {ECO:0000256|SAAS:SAAS00118750}; KW Metal-binding {ECO:0000256|SAAS:SAAS00118726}; KW Multifunctional enzyme {ECO:0000256|SAAS:SAAS00118716}; KW Nuclease {ECO:0000256|SAAS:SAAS00118722}; KW Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00118804}; KW RNA-directed DNA polymerase {ECO:0000256|SAAS:SAAS00118797}; KW Transferase {ECO:0000256|SAAS:SAAS00118803}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACV03667.1}. FT NON_TER 344 344 {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 //