ID I0DD90_HBV Unreviewed; 671 AA.
AC I0DD90;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Protein P {ECO:0000256|ARBA:ARBA00021149};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE Flags: Fragment;
GN Name=P {ECO:0000313|EMBL:AFH87571.1};
OS Hepatitis B virus (HBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10407 {ECO:0000313|EMBL:AFH87571.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:AFH87571.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=477-4136-0 {ECO:0000313|EMBL:AFH87571.1};
RX PubMed=22293432; DOI=10.1093/infdis/jir862;
RG NHLBI-REDS-II Study Group;
RA Delwart E., Slikas E., Stramer S.L., Kamel H., Kessler D., Krysztof D.,
RA Tobler L.H., Carrick D.M., Steele W., Todd D., Wright D.J., Kleinman S.H.,
RA Busch M.P.;
RT "Genetic diversity of recently acquired and prevalent HIV, hepatitis B
RT virus, and hepatitis C virus infections in US blood donors.";
RL J. Infect. Dis. 205:875-885(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077};
CC -!- SIMILARITY: Belongs to the hepadnaviridae P protein family.
CC {ECO:0000256|ARBA:ARBA00007994}.
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DR EMBL; JN604221; AFH87571.1; -; Genomic_DNA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; 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; DNA/RNA polymerases; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 333..576
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 191..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFH87571.1"
FT NON_TER 671
FT /evidence="ECO:0000313|EMBL:AFH87571.1"
SQ SEQUENCE 671 AA; 75329 MW; BA3C0C1D3B5066AA CRC64;
LPRLADEGLN RRVAEDLNLG NLNVSIPWTH KVGNFTGLYS STVPNFNPDW QTPSFPDIHL
QEDIVDRCKQ FVGPLTVNEI RRLKLIMPAR FYPNVTKYLP LDKGIKPYYP EHVVNHYFQT
RHYLHTLWKA GILYKRETTR SASFCGSPYS WEQELQHGRL VFQTSKRHGD KSFCPQSTGI
LPRSSVGPCI QSQLRKSRLG PQSTQGQLAG RQQGGSGSIR ARVHPSPWGP VGVEPSGSGH
THNCASSTSS XLHQSAVRKA AYSLISTSKG HSPSGXAVEL HHXPSNSSRS QSQGSVLSCW
WLQFRNSEPC SEYCLCHIIN LLEDWGPCTE HGEHRIRTPR TPARVTGGVF LVDKNPHNTT
ESRLVVDFSQ FSRGNTRVSW PKFAVPNLQS LTNLLSSNLS WLSLDVSAAF YHLPLHPAAM
PHLLVGSSGL SRYVARLSSN SRIIBHQHRT MQNLHDSCSR NLYVSLMLLY KTYGRKLHLY
SHPIILGFRK IPMGVGLSPF LLAQFTSAVC SVVRRAFPHC LAFSYMDDVV LGAKSVQHLE
SLYAAVTNFL LSLGIHLNPH KTKRWGYSLN FMGYVIGSWG SLPQEHIVQK IKSCFRKLPV
NRPIDWKVCQ RIVGLLGFAA PFTQCGYPAL MPLYACIQAK QAFTFSPTYK AFLSKQYLNL
YPVARQRPGL C
//