ID I0DCQ0_HBV Unreviewed; 671 AA.
AC I0DCQ0;
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:AFH87381.1};
OS Hepatitis B virus (HBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10407 {ECO:0000313|EMBL:AFH87381.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:AFH87381.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=478-0079-4 {ECO:0000313|EMBL:AFH87381.1};
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; JN604171; AFH87381.1; -; 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 200..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFH87381.1"
FT NON_TER 671
FT /evidence="ECO:0000313|EMBL:AFH87381.1"
SQ SEQUENCE 671 AA; 75548 MW; B688212EE963E7E9 CRC64;
LPRLADEDLN RRVAEDLNLG NLNVSIPWTH KVGNFTGLYS STVPIFNPEW QTPSFPKIHL
HEDIANRCQQ FVGPLTVNEK RRLKLIMPAR FYPNSTKYLP LDKGIKPYYP DHVVNHYFQT
RHYLHTLWKA GILYKRETTR SASFCGSPYS WEQELHHGRL VIKTSQRHGD EPFCSQPSGI
LSRSSVGPCI RSQFKQSRLG LQPHQGPLAT SQPGRSGSIR ARVHSPTRRC FGVEPSGSGH
IGHSASSASS CLHQSAVRKA AYSHLSTSKR QSSSGHAVEF HSFPPSSARS QSQGPVFSCW
WLQFRNTQPC SNYCLSHIVN LLEDWGPCAE HGEHHIRIPR TPARVTGGVF LVDKNPHNTA
ESRLVVDFSQ FSRGITRVSW PKFAVPNLQS LTNLLSSNLS WLSLDVSAAF YHIPLHPAAM
PHLLIGSSGL SRYVARLSSN SRINNNQHGT LQNLHDSCSR QLYVSLMLLY KTYGWKLHLY
SHPIILGFRK IPMGVGLSPF LLAQFTSAIC SVVRRAFPHC LAFSYMDDVV LGAKSVQHLE
SLYTAVTNFL LSLGIHLNPN KTKRWGYSLN FMGYVIGSWG TLPQDHIVQK IKHCFRKLPV
NRPIDWKVCQ RIVGLLGFAA PFTQCGYPAL MPLYACIQAK QAFTFSPTYK AFLSKQYMNL
YPVARQRPGL C
//