ID   D0UDS9_HBV              Unreviewed;       843 AA.
AC   D0UDS9;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   09-DEC-2015, entry version 23.
DE   RecName: Full=Protein P {ECO:0000256|SAAS:SAAS00399868};
GN   Name=P {ECO:0000313|EMBL:ACY07345.1};
OS   Hepatitis B virus (HBV).
OC   Viruses; Retro-transcribing viruses; Hepadnaviridae;
OC   Orthohepadnavirus.
OX   NCBI_TaxID=10407 {ECO:0000313|EMBL:ACY07345.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1] {ECO:0000313|EMBL:ACY07345.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KOR11CHB {ECO:0000313|EMBL:ACY07345.1};
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). {ECO:0000256|SAAS:SAAS00399837}.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1). {ECO:0000256|SAAS:SAAS00399746}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester. {ECO:0000256|SAAS:SAAS00399932}.
CC   -!- SIMILARITY: Contains 1 reverse transcriptase domain.
CC       {ECO:0000256|RuleBase:RU000322}.
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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: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; IPR000201; DNApol_viral_N.
DR   InterPro; IPR000477; RT_dom.
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   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   DOMAIN      357    600       Reverse transcriptase.
FT                                {ECO:0000259|PROSITE:PS50878}.
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
//