ID D0UDS9_HBV Unreviewed; 843 AA. AC D0UDS9; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 19-FEB-2014, entry version 12. DE SubName: Full=Polymerase; GN Name=P; OS Hepatitis B virus (HBV). OC Viruses; Retro-transcribing viruses; Hepadnaviridae; OC Orthohepadnavirus. OX NCBI_TaxID=10407; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee). RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KOR11CHB; RX PubMed=20513074; DOI=10.1002/jmv.21844; RA Ahn S.H., Yuen L., Han K.H., Littlejohn M., Chang H.Y., Damerow H., RA Ayres A., Heo J., Locarnini S., Revill P.A.; RT "Molecular and clinical characteristics of hepatitis B virus in RT Korea."; RL J. Med. Virol. 82:1126-1134(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 (By similarity). CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. CC -!- SIMILARITY: Contains 1 reverse transcriptase domain. CC -!- SIMILARITY: Contains reverse transcriptase domain. 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; GQ475315; ACY07345.1; -; 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 GO; GO:0006261; P:DNA-dependent DNA replication; IEA:GOC. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC. DR InterPro; IPR001462; DNApol_viral_C. DR InterPro; IPR000201; DNApol_viral_N. DR InterPro; IPR000477; RVT. DR Pfam; PF00336; DNA_pol_viral_C; 1. DR Pfam; PF00242; DNA_pol_viral_N; 1. DR Pfam; PF00078; RVT_1; 1. DR PROSITE; PS50878; RT_POL; 1. PE 3: Inferred from homology; KW DNA replication; DNA-binding; DNA-directed DNA polymerase; KW Endonuclease; Hydrolase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase; KW RNA-directed DNA polymerase; Transferase. SQ SEQUENCE 843 AA; 94533 MW; BED298CC61D58DE6 CRC64; MPLSYQHFRK LLLLDDEAGP LEEELPRLAD EDLNRRVAED LNLGNLNVSI PWTHKVGNFT GLYSSTVPVF NPEWQTPSFP NIHLKEDIIN RCQQYVGPLT VNEKRRLKLI MPARFYPNLT KYLPLDKGIK PYYPEHAVNH YFKTRHYLHT LWKAGILYKR ETTRSASFCG SPYSWEQELQ HGRLVFQTST RHGDESFCSQ SSGILSRSPV GPCVRSQLKQ SRLGLQPQQG SLARGKSGRS GSIRARVHPT TRRSFGVEPS GSGHIDNSAS SSSSCLHQSA VRKTAYSHLS TSKRQSSSGH AVELHHIPPS SARSQSEGPI FSCWWLQFRN SKPCSDYCLT HIVNLLEDWG PCTEHGEHNI RIPRTPARVT GGVFLVDKNP HNTAESRLVV DFSQFSRGST HVSWPKFAVP NLQSLTNLLS SNLSWLSLDV SAAFYHIPLH PAAMPHLLVG SSGLPRYVAR LSSTSRNINY QHGTMQDLHD SCSRNLYVSL LLLYKTFGRK LHLYSHPIIL GFRKIPMGVG LSPFLLAQFT SAICSVVRRA FPHCLAFSYM DDVVLGAKSV QHLESLFTSI TNFLLSLGIH LNPNKTKRWG YSLNFMGYVI GSWGTLPQEH IILKLKQCFR KLPVNRPIDW KVCQRIVGLL GFAAPFTQCG YPALMPLYAC IQAKQAFTFS PTYKAFLCKQ YLHLYPVARQ RSGLCQVFAD ATPTGWGLAI GHRRMRGTFV APLPIHTAEL LAACFARSRS GAKLIGTDNS VVLSRKYTSF PWLLGCAANW ILRGTSFVYV PSALNPADDP SRGRLGLYRP LLHLPFRPTT GRTSLYAVSP SVPSHLPDRV HFASPLHVAW RPP //