DPOL_HPBDB
ID DPOL_HPBDB Reviewed; 788 AA.
AC P17192;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein P;
DE Includes:
DE RecName: Full=DNA-directed DNA polymerase;
DE EC=2.7.7.7;
DE Includes:
DE RecName: Full=RNA-directed DNA polymerase;
DE EC=2.7.7.49;
DE Includes:
DE RecName: Full=Ribonuclease H;
DE EC=3.1.26.4;
GN Name=P;
OS Duck hepatitis B virus (isolate brown Shanghai duck S5) (DHBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Avihepadnavirus.
OX NCBI_TaxID=10439;
OH NCBI_TaxID=8835; Anas (ducks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2596031; DOI=10.1016/0042-6822(89)90571-0;
RA Uchida M., Esumi M., Shikata T.;
RT "Molecular cloning and sequence analysis of duck hepatitis B virus genomes
RT of a new variant isolated from Shanghai ducks.";
RL Virology 173:600-606(1989).
RN [2]
RP REVIEW.
RX PubMed=17206754; DOI=10.3748/wjg.v13.i1.48;
RA Beck J., Nassal M.;
RT "Hepatitis B virus replication.";
RL World J. Gastroenterol. 13:48-64(2007).
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 (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- ACTIVITY REGULATION: Activated by host HSP70 and HSP40 in vitro to be
CC able to bind the epsilon loop of the pgRNA. Because deletion of the
CC RNase H region renders the protein partly chaperone-independent, the
CC chaperones may be needed indirectly to relieve occlusion of the RNA-
CC binding site by this domain.
CC -!- DOMAIN: Terminal protein domain (TP) is hepadnavirus-specific. Spacer
CC domain is highly variable and separates the TP and RT domains.
CC Polymerase/reverse-transcriptase domain (RT) and ribonuclease H domain
CC (RH) are similar to retrovirus reverse transcriptase/RNase H (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The polymerase/reverse transcriptase (RT) and ribonuclease H
CC (RH) domains are structured in five subdomains: finger, palm, thumb,
CC connection and RNase H. Within the palm subdomain, the 'primer grip'
CC region is thought to be involved in the positioning of the primer
CC terminus for accommodating the incoming nucleotide. The RH domain
CC stabilizes the association of RT with primer-template (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the hepadnaviridae P protein family.
CC {ECO:0000305}.
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DR EMBL; M32990; AAA45754.1; -; Genomic_DNA.
DR PIR; A33746; JDVLBD.
DR Proteomes; UP000008682; Genome.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001462; DNApol_viral_C.
DR InterPro; IPR000201; DNApol_viral_N.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
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 SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; RNA-directed DNA polymerase; Transferase.
FT CHAIN 1..788
FT /note="Protein P"
FT /id="PRO_0000222329"
FT DOMAIN 376..565
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 1..200
FT /note="Terminal protein domain (TP)"
FT /evidence="ECO:0000250"
FT REGION 201..365
FT /note="Spacer"
FT /evidence="ECO:0000250"
FT REGION 211..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..655
FT /note="Polymerase/reverse transcriptase domain (RT)"
FT /evidence="ECO:0000250"
FT REGION 656..788
FT /note="RnaseH domain (RH)"
FT /evidence="ECO:0000250"
FT COMPBIAS 220..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 448
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 515
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 516
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT SITE 96
FT /note="Priming of reverse-transcription by covalently
FT linking the first nucleotide of the (-)DNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 788 AA; 89379 MW; F482FB578D75BF1B CRC64;
MPQPLKQSLD QSRWLREAEK HLRELENLVD SNLEEEKLKP QLSMGEDVQS PGIGEPLHPN
VRAPLSHVVR AATIDLPRLG NKLPAKHHLG KLSGLYQMKG CTFNPEWKVP DISDTHFDLQ
VINECPSRNW KYLTPAKFWP KSISYFPVQA GVKAKYPDNV MQHEAIVGKY LNRLYEAGIL
YKRISKHLVT FKGKPYNWEL QYLVKQHQVP DGTTTSKING RAENRRRRAP AKSISRPHDS
ERDCNMVGQI SNNRSSIRPC ANNGGGKHYA TTRRLACWGG KTIGTDQSYS SRDTSATVDS
RGRSESSRGF STISGRKATG NHHHCSNVTN SVETTTRGRS TPGKQVVTRD SSALPESRAS
RACHKDSSPQ KEENAWYLRG NTSWPNRITG KLFLVDKNSR NTTEARLVVD FSQFSKGKNA
MRFPRYWSPN LSTLRRILPV GMPRISLDLS QAFYHLPLNP ASSSRLAVSD GQHVYYFRKA
PMGVGLSPFL LHLFTTALGS EIARRFNIWT FTYMDDFLLC HPNARHLNSI SHAVCSFLQE
LGIRINFDKT TPSPVNDIRF LGYQIDQKFM KIEESRWKEL RTVIKKIKIG AWYDWKCIQR
FVGHLNFVLP FTKGNIEMLK PMYAAITNKV NFSFSSAYRT LLYKLTMGVC KLAIRPKSSV
PLPRVATDAT PTHGAISHIT GGSAVFAFSK VRDIHIQELL MVCLAKIMIK PRCILSDSTF
VCHKRYQTLP WHFAMLAKQL LSPIQLYFVP SKYNPADGPS RHKPPDWTAL TYTPLSKAIY
IPHRLCGT
