ID I0DCS0_HBV Unreviewed; 671 AA.
AC I0DCS0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:AFH87401.1};
OS Hepatitis B virus (HBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10407 {ECO:0000313|EMBL:AFH87401.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:AFH87401.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=478-2959-6 {ECO:0000313|EMBL:AFH87401.1};
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; JN604176; AFH87401.1; -; 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..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFH87401.1"
FT NON_TER 671
FT /evidence="ECO:0000313|EMBL:AFH87401.1"
SQ SEQUENCE 671 AA; 75781 MW; 97101D828E40C565 CRC64;
LPRLADADLN RRVAEDLNLG NLNVSIPWTH KVGNFTGLYS SXXPIFNPEW QTPSFPKIHL
QEDIINRCQQ FVGPLTVNEK RRLKLIMPAR FYPXHTKYLP LDKGIKPYYP DQVVNHYFQT
RHYLHTLWKA GILYKRETTR SASFCGSPYS WEQELQHGRL VIKTSQRHGD ESFCSQPSGI
LSRSSVGPCI RSQLKQSRLG LQPHQGPLAS SQPGRSGSIR ARAHPSTRRY FGVEPSGSGH
IDHSVNNSSS CLHQSAVRKA AYSHLSTSKR QSSSGHAVEF HCLPPSSAGS QSQGSVFSCW
WLQFRNSKPC SEYCLSHIVN LREDWGPCDE HGEHHIRIPR TPARVTGGVF LVDKNPHNTE
ESRLVVDFSQ FSRGXTRVSW PKFAVPNLQS LTNLLSSNLS WXSLDVSAAF YHIPLHPAAM
PHLLIGSSGL SRYVARLSSN SRINNNQYGT MQNLHDSCSR QLYVSLMLLY KTYGWKLHLY
SHPIVLGFRK IPMGVGLSPF LLAQFTSAIC SVVRRAFPHC LAFSYMDDVV LGAKSVQHLZ
SLXTAVTNFL LSLGIHLNPN KTKRWGYSLN FMGYIIGSWG TLPQDHIVQK IKHCFRKLPV
NRPIDWKVCQ RIVGLLGFAA PFTQCGYPAL MPLYACIQAK QAFTFSPTYK AFLRQQYMNL
YPVARQRPGL C
//