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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12124470 [NCBI, ExPASy, EBI, Israel, Japan]
Arauz-Ruiz P.,
Norder H.,
Robertson B.H.,
Magnius L.O.;
"Genotype H: a new Amerindian genotype of hepatitis B virus revealed in Central America.";
J. Gen. Virol. 83:2059-2073(2002).
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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: 843 AA [This is the length of the unprocessed precursor] |
Molecular weight: 94284 Da [This is the MW of the unprocessed precursor] |
CRC64: 4C7E93710D22E280 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MPLSYPHFRK LLLLDDEAGL LEEELPRLAD EGLNRRVAED LNLQLPNVSI PWTHKVGNFT
70 80 90 100 110 120
GLYSSTVPTF NPDWLTPSFP DIHLHQDLIH KCEQFVGPLT KNELRRLKLV MPSRFFPKVT
130 140 150 160 170 180
KYFPMEKGIK PYYPDNVVNH YFKTRHYLHT LWKAGILYKR ESTRSASFCG SPYSWEQELQ
190 200 210 220 230 240
HGSTSINDTK GHGTESLCTQ SSGILSRPSA GSSIQGKFQQ SRLGLQQKQG QLANGKQGRS
250 260 270 280 290 300
GRIRSWVHTP TRWPAGVEPT GTGCAYNIAS RSASCFHQSA VREKTNPSLS TSKRHSSTGH
310 320 330 340 350 360
AVELNPVPPG SVRSEGKGSV LSCWWLQFRD TEPCSDYCLS HIINLLEDWG PCYEHGQHHI
370 380 390 400 410 420
RTPRTPARVT GGVFLVDKNP HNTTESRLVV DFSQFSRGNT RVSWPKFAVP NLQSLTNLLS
430 440 450 460 470 480
SNLSWLSLDV SAAFYHLPLH PAAMPHLLVG SSGLSRYVAR LSSTSRIHDH QHGTMQNLHN
490 500 510 520 530 540
SCSRNLYVSL LLLFKTFGRK LHLYSHPIIL GFRKIPMGVG LSPFLLAQFT SAICSVVRRA
550 560 570 580 590 600
FPHCLAFSYM DDLVLGAKSV QHLESLYTAV TNFLLSVGIH LNTSKTKRWG YTLNFMGYVI
610 620 630 640 650 660
GSWGSLPQDH IVQKIKACFR KLPVNRPIDW KVCQRIVGLL GFAAPFTQCG YPALMPLYAC
670 680 690 700 710 720
ITAKQAFVFS PTYKAFLCQQ YMHLYPVARQ RPGLCQVFAD ATPTGWGLAI GHQRMRGTFV
730 740 750 760 770 780
APLPIHTAEL LAACFARSRS GAKLIGTDNS VVLSRKYTSF PWLLGCAANW ILRGTSFVYV
790 800 810 820 830 840
PSALNPADDP SRGRLGLYRP LLRLPFQPTT GRTSLYAASP SVPSHLPDRV HFASPLHVAW
RPP
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Q8JMY4 in FASTA format |
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