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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1093/nar/11.6.1747; PubMed=6300776 [NCBI, ExPASy, EBI, Israel, Japan]
Ono Y.,
Onda H.,
Sasada R.,
Igarashi K.,
Sugino Y.,
Nishioka K.;
"The complete nucleotide sequences of the cloned hepatitis B virus DNA; subtype adr and adw.";
Nucleic Acids Res. 11:1747-1757(1983).
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[2]
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REVIEW.
PubMed=17206754 [NCBI, ExPASy, EBI, Israel, Japan]
Beck J.,
Nassal M.;
"Hepatitis B virus replication.";
World J. Gastroenterol. 13:48-64(2007).
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- FUNCTION: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery (By similarity).
- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-phosphomonoester.
- ENZYME REGULATION: Activated by host HSP70 and HSP40 in vitro to be able to bind the epsilon loop of the pgRNA. Because deletion of the RNase H region renders the protein partly chaperone-independent, the chaperones may be needed indirectly to releive occlusion of the RNA-binding site by this domain. Inhibited by several reverse-transcriptase inhibitors: Lamivudine, Adefovir and Entecavir (By similarity).
- DOMAIN: Terminal protein domain (TP) is hepadnavirus-specific. Spacer domain is highly variable and separates the TP and RT domains. Polymerase/reverse-transcriptase domain (RT) and ribonuclease H domain (RH) are similar to retrovirus reverse transcriptase/RNase H (By similarity).
- DOMAIN: The polymerase/reverse transcriptase (RT) and ribonuclease H (RH) domains are structured in five subdomains: finger, palm, thumb, connection and RNase H. Within the palm subdomain, the 'primer grip' region is thought to be involved in the positioning of the primer terminus for accommodating the incoming nucleotide. The RH domain stabilizes the association of RT with primer-template (By similarity).
- MISCELLANEOUS: Hepadnaviral virions contain probably just one P protein molecule per particle (By similarity).
- SIMILARITY: Belongs to the hepadnaviridae P protein family.
- SIMILARITY: Contains 1 reverse transcriptase domain.
- WEB RESOURCE: Name=HepSEQ; Note=Hepatitis virus B database; URL="http://www.hpa-bioinfodatabases.org.uk/hepatitis_open/main.php";.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 838 AA [This is the length of the unprocessed precursor] |
Molecular weight: 93840 Da [This is the MW of the unprocessed precursor] |
CRC64: B133A77F9C12E91C [This is a checksum on the sequence] |
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10 20 30 40 50 60
MPLSYQHFRK LLLLDDGTEA GPLEEELPRL ADADLNRRVA EDLNLGNLNV SIPWTHKVGN
70 80 90 100 110 120
FTGLYSSTVP IFNPEWQTPS FPKIHLQEDI INRCQQFVGP LTVNEKRRLK LIMPARFYPT
130 140 150 160 170 180
HTKYLPLDKG IKPYYPDQVV NHYFQTRHYL HTLWKAGILY KRETTRSASF CGSPYSWEQE
190 200 210 220 230 240
LQHSQRHGDE SFCSQPSGIP SRSSVGPCIR SQLNKSRLGL QPHQGPLASS QPGRSGSIRA
250 260 270 280 290 300
RAHPSTRRYF GVEPSGSGHI DHSVNNSSSC LHQSAVRKAA YSHLSTSKRQ SSSGHAVEFH
310 320 330 340 350 360
CLAPSSAGSQ SQGSVSSCWW LQFRNSKPCS EYCLSHLVNL REDWGPCDDH GEHHIRIPRT
370 380 390 400 410 420
PARVTGGVFL VDKNPHNTAE SRLVVDFSQF SRGITRVSWP KFAVPNLQSL TNLLSSNLSW
430 440 450 460 470 480
LSLDVSAAFY HIPLHPAAMP HLLIGSSGLS RYVARLSSNS RINNNQYGTM QNLHDSCSRQ
490 500 510 520 530 540
LFVSLMLLYK TYGWKLHLYS HPIVLGFRKI PMGVGLSPFL LAQFTSAICS VVRRAFPHCL
550 560 570 580 590 600
AFSYMDDVVL GAKSVQHRES LYTAVTNFLL SLGIHLNPNK TKRWGYSLNF MGYIIGSWGT
610 620 630 640 650 660
LPQDHIVQKI KHCFRKLPVN RPIDWKVCQR IVGLLGFAAP FTQCGYPALM PLYACIQAKQ
670 680 690 700 710 720
AFTFSPTYKA FLSKQYMNLY PVARQRPGLC QVFADATPTG WGLAIGHQRM RGTFVAPLPI
730 740 750 760 770 780
HTAELLAACF ARSRSGAKLI GTDNSVVLSR KYTSFPWLLG CTANWILRGT SFVYVPSALN
790 800 810 820 830
PADDPSRGRL GLSRPLLRLP FQPTTGRTSL YAVSPSVPSH LPVRVHFASP LHVAWRPP
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P03158 in FASTA format |
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ExPASy Home page
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