DPOL_GSHV
ID DPOL_GSHV Reviewed; 881 AA.
AC P03161;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein P {ECO:0000255|HAMAP-Rule:MF_04073};
DE Includes:
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04073};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_04073};
DE Includes:
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04073};
DE EC=2.7.7.49 {ECO:0000255|HAMAP-Rule:MF_04073};
DE Includes:
DE RecName: Full=Ribonuclease H {ECO:0000255|HAMAP-Rule:MF_04073};
DE EC=3.1.26.4 {ECO:0000255|HAMAP-Rule:MF_04073};
GN Name=P {ECO:0000255|HAMAP-Rule:MF_04073};
OS Ground squirrel hepatitis virus (strain 27) (GSHV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10406;
OH NCBI_TaxID=34862; Otospermophilus beecheyi (California ground squirrel) (Spermophilus beecheyi).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6086950; DOI=10.1128/jvi.51.2.367-375.1984;
RA Seeger C., Ganem D., Varmus H.E.;
RT "Nucleotide sequence of an infectious molecularly cloned genome of ground
RT squirrel hepatitis virus.";
RL J. Virol. 51:367-375(1984).
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.
CC {ECO:0000255|HAMAP-Rule:MF_04073}.
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|HAMAP-
CC Rule:MF_04073};
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|HAMAP-
CC Rule:MF_04073};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04073};
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. Inhibited by several reverse-transcriptase
CC inhibitors: Lamivudine, Adefovir and Entecavir. {ECO:0000255|HAMAP-
CC Rule:MF_04073}.
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.
CC {ECO:0000255|HAMAP-Rule:MF_04073}.
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.
CC {ECO:0000255|HAMAP-Rule:MF_04073}.
CC -!- MISCELLANEOUS: Hepadnaviral virions contain probably just one P protein
CC molecule per particle. {ECO:0000255|HAMAP-Rule:MF_04073}.
CC -!- SIMILARITY: Belongs to the hepadnaviridae P protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04073}.
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DR EMBL; K02715; AAA46756.1; -; Genomic_DNA.
DR PIR; A00709; JDVLS.
DR RefSeq; NP_040994.1; NC_001484.1.
DR PRIDE; P03161; -.
DR GeneID; 1488459; -.
DR KEGG; vg:1488459; -.
DR Proteomes; UP000009156; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.270; -; 1.
DR HAMAP; MF_04073; HBV_DPOL; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001462; DNApol_viral_C.
DR InterPro; IPR000201; DNApol_viral_N.
DR InterPro; IPR037531; HBV_DPOL.
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 Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host RLR pathway by virus; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Reference proteome; RNA-directed DNA polymerase; Transferase;
KW Viral immunoevasion.
FT CHAIN 1..881
FT /note="Protein P"
FT /id="PRO_0000222331"
FT DOMAIN 395..636
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04073"
FT REGION 1..184
FT /note="Terminal protein domain (TP)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04073"
FT REGION 185..384
FT /note="Spacer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04073"
FT REGION 263..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..726
FT /note="Polymerase/reverse transcriptase domain (RT)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04073"
FT COMPBIAS 268..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04073"
FT BINDING 587
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04073"
FT BINDING 588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04073"
FT SITE 68
FT /note="Priming of reverse-transcription by covalently
FT linking the first nucleotide of the (-)DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04073"
SQ SEQUENCE 881 AA; 99977 MW; 1E8D2D81DEFF642C CRC64;
MHPFYQLFRN IQSLGEEEVQ ELLGPPEDAL PLLAGEGLNH RVADALNLQL PTADLEWIHK
TNVITGLYST QTEKFNCNWK QPVFPKIHLD NNLFQKLENY FGPLTTNEKR RLKLVFPARF
FPNATKYFPL LKGIKDKYPN YTIEHFFAAA NYLWTLWESG ILYLRKNQTT LTFRGKPYSW
EHRQLEQHNG QQHKSNIRSQ QISCMVANSG NLLYTHYHRD KSSNIQTRNL SDNVFKKSKE
STRVRCYTYD KIQRNRLGQL ARIPCESKAP SEQQQSSLRS KGRDFRNQIQ AYNSSRNKGY
TTWHSTTSDS IQSGSKKKTH TSNSSFERHT PSFDNEKSDR SPAGICRGTE SSNHLRSSQL
CLWRSFYYTK PCGTYCLHHI VSSIDDWGPC TFDGDVTIRS PRTPRRITGG IFLVDKNPYN
SSESRLVVDF SQFSRGHSRV HWPKFAVPNL QTLANLLSTN LQWLSLDVSA AFYHIPVSPA
AVPHFLVGSP GLERFASCMS HDASNRNNSK LQTMHHICSR HLYNTLLLLF KTYGRKLHLL
AHPFIMGFRK LPMGVGLSPF LLAQFTSALT SMVRRNFPHC LAFAYMDDLV LGARSYEHLT
AVYSHICSVF LDLGIHLNVE KTKWWGHTLH FMGYTINGAG VLPQDKHVHK VTTYLKSIPI
NQPLDYKICE RLTGILNYVA PFTKCGYAAL LPLYQAIASH TAFVFSSLYK NWLLSLYGEL
WPVARQRGVV CSVFADATPT GWGICTTCQL ISGTFGFSLP IATAELIAAC LARCWTGARL
LGTDNSVVLS GKLTSFPWLL ACVANWILRG TSFCYVPSAD NPADLPSRGL LPALRPLPLL
RFRPVTKRIS LWAASPPVST RRPVRVAWAS PVQTCEPWIP P
