DPOL_DHBV3
ID DPOL_DHBV3 Reviewed; 786 AA.
AC P0C691;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
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 (strain Germany/DHBV-3) (DHBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Avihepadnavirus.
OX NCBI_TaxID=489542;
OH NCBI_TaxID=8835; Anas (ducks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3981148; DOI=10.1002/jmv.1890150402;
RA Sprengel R., Kuhn C., Will H., Schaller H.;
RT "Comparative sequence analysis of duck and human hepatitis B virus
RT genomes.";
RL J. Med. Virol. 15:323-333(1985).
RN [2]
RP REVERSE TRANSCRIPTION PRIMING, AND MUTAGENESIS OF TYR-96; TYR-170; TYR-181
RP AND ASP-513.
RX PubMed=7512155; DOI=10.1128/jvi.68.5.2994-2999.1994;
RA Weber M., Bronsema V., Bartos H., Bosserhoff A., Bartenschlager R.,
RA Schaller H.;
RT "Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to
RT prime reverse transcription.";
RL J. Virol. 68:2994-2999(1994).
RN [3]
RP FUNCTION.
RX PubMed=16051809; DOI=10.1128/jvi.79.16.10164-10170.2005;
RA Cao F., Badtke M.P., Metzger L.M., Yao E., Adeyemo B., Gong Y., Tavis J.E.;
RT "Identification of an essential molecular contact point on the duck
RT hepatitis B virus reverse transcriptase.";
RL J. Virol. 79:10164-10170(2005).
RN [4]
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, ECO:0000269|PubMed:16051809}.
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; DQ195079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR BindingDB; P0C691; -.
DR ChEMBL; CHEMBL4295573; -.
DR Proteomes; UP000007204; 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 1: Evidence at protein level;
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..786
FT /note="Protein P"
FT /id="PRO_0000323249"
FT DOMAIN 374..563
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 36..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..364
FT /note="Spacer"
FT /evidence="ECO:0000250"
FT REGION 207..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..653
FT /note="Polymerase/reverse transcriptase domain (RT)"
FT /evidence="ECO:0000250"
FT REGION 654..786
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 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 513
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 514
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 MUTAGEN 96
FT /note="Y->F: Complete loss of reverse transcription."
FT /evidence="ECO:0000269|PubMed:7512155"
FT MUTAGEN 170
FT /note="Y->F: 90% loss of reverse transcription."
FT /evidence="ECO:0000269|PubMed:7512155"
FT MUTAGEN 181
FT /note="Y->F: No effect on reverse transcription."
FT /evidence="ECO:0000269|PubMed:7512155"
FT MUTAGEN 513
FT /note="D->H: Complete loss of reverse transcription."
FT /evidence="ECO:0000269|PubMed:7512155"
SQ SEQUENCE 786 AA; 89430 MW; 793D209358D18E57 CRC64;
MPQPLKQSLD QSKWLREAEK QLRVLENLVD SNLEEEKLKP QLSMGEDVQS PGKGEPLHPN
VRAPLSHVVR AVTTDLPRLG NKLPARHHLG KLSGLYQMKG CTFNPEWKVP DISDTHFDLE
VINECPSRNW KYLTPAKFWP KSISYFPVQA GVKPKYPDNV MQHESIVGKY LTRLYEAGIL
YKRISKHLVT FKGQPYNWEQ QHLVNQHQIP DGATSSKING RQENRRRRTP IKSTCRQNDT
KRDSDMVGQV SNNRSRIRPC ANNGGDKHPP ATGSLACWGR KASRVIKSGS SRDSSASVDS
RRRSKGPRGF STLPRRETTG NDHHSSDISN SVEATTRRRS TPGESITLGD SSIIPDGTSC
ASDKDSSPKE ENVWYLRGNT SWPNRITGKL FLVDKNSRNT TEARLVVDFS QFSKGKNAMR
FPRYWSPNLS TLRRILPVGM PRISLDLSQA FYHLPLNPAS SSRLAVSDGQ WVYYFRKAPM
GVGLSPFLLH LFTTALGSEI SRRFNVWTFT YMDDFLLCHP NARHLNSISH AVCSFLQELG
IRINFDKTTP SPVTEIRFLG YQIDEHFMKI EESRWKELRT VIKKIKVGEW YDWKCIQRFV
GHLNFVLPFT KGNIEMLKPM YAAITNQVNF SFSSAYRTLL YKLTMGVCKL RINPKSSVPL
PRVATDATPT HGAISHITGG SAVFAFSKVR DIHIQELLMT CLARIMIKPR CLLSDSTFVC
HKRYQTLPWH FAVLAKQLLK PIQLYFVPSK YNPADGPSRH RPPDWTAFPY TPLSKAIYIP
HRLCGT
