ID I0DDR7_HBV Unreviewed; 671 AA.
AC I0DDR7;
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:AFH87748.1};
OS Hepatitis B virus (HBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10407 {ECO:0000313|EMBL:AFH87748.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:AFH87748.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=476-6804-3 {ECO:0000313|EMBL:AFH87748.1};
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; JN604269; AFH87748.1; -; 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 196..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFH87748.1"
FT NON_TER 671
FT /evidence="ECO:0000313|EMBL:AFH87748.1"
SQ SEQUENCE 671 AA; 75634 MW; 24CBB531BC26C4A6 CRC64;
LPRLADADLN RRVAEDLNLG NLNVSIPWTH KVGNFTGLYS STVPIFNPEW QTPSFPRIHL
QEDIINRCQQ FVGPLTANEK RRLKLIMPAR FYPNHTKYLP LDKGIKPYYP DQVVNHYFQT
RHYLHTLWKA GILYKRETTR SASFCGSPYS WEQELQHGRL VIKTSQRHGD ESFCSQPSGI
LSRSSVGPCI RSQLKQSRLG LQPHQGPLAS SQPGRSGSIR ARAHPSTRRY FGVEPSGSGH
IDHSVNNSSS CLHQSAVRKA AYSHLSTSKR QSSSGHAVEF HCLPPSSAGS QSQGSISSCW
WLQFRDSKPC SEYCLSHLVN LREDWGPCDE HGEHHIRIPR TPARVTGGVF LVDKNPHNTA
ESRLVVDFSQ FSRGITRVSW PKFAVPNLQS LTNLLSSNLS WLSLDVSAAF YHIPLHPAAM
PHLLIGSSGL SRYVARVSSN SRINNNQYGT MQNLHDSCSR QLYXSLMLLY KTYGWKLHLY
SHPIVLGFRK IPMGVGLSPF LLAQFTSAIC SVVRRAFPHC LAFSYMDDVV LGAKSVQHRE
ALYTAVTNFL LSLGIHLNPN KTKRWGYSLN FMGYIIGSWG TLPQDHIVQK IKHCFRKLPV
NRPIDWKVCQ RIVGLLGFAA PFTQCGYPAL MPLYACIQAK QAXTFSPTYK AFLSKQYMNL
YPVARQRPGL C
//