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Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_HTLV2               Reviewed;        1461 AA.
P03363;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
10-MAY-2017, entry version 136.
RecName: Full=Gag-Pro-Pol polyprotein;
AltName: Full=Pr160Gag-Pro-Pol;
Contains:
RecName: Full=Matrix protein p19;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p15-pro;
Short=NC';
Short=NC-pro;
Contains:
RecName: Full=Protease;
Short=PR;
EC=3.4.23.-;
Contains:
RecName: Full=p1;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.4;
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000305|PubMed:8623556};
EC=3.1.-.- {ECO:0000305|PubMed:8623556};
Name=gag-pro-pol;
Human T-cell leukemia virus 2 (HTLV-2).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Deltaretrovirus.
NCBI_TaxID=11909;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2582407; DOI=10.1073/pnas.82.10.3101;
Shimotohno K., Takahashi Y., Shimizu N., Gojobori T., Golde D.W.,
Chen I.S.Y., Miwa M., Sugimura T.;
"Complete nucleotide sequence of an infectious clone of human T-cell
leukemia virus type II: an open reading frame for the protease gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:3101-3105(1985).
[2]
RIBOSOMAL FRAMESHIFT.
PubMed=8371359;
Falk H., Mador N., Udi R., Panet A., Honigman A.;
"Two cis-acting signals control ribosomal frameshift between human T-
cell leukemia virus type II gag and pro genes.";
J. Virol. 67:6273-6277(1993).
[3]
FUNCTION (INTEGRASE).
PubMed=8623556; DOI=10.1006/viro.1996.0224;
Balakrishnan M., Zastrow D., Jonsson C.B.;
"Catalytic activities of the human T-cell leukemia virus type II
integrase.";
Virology 219:77-86(1996).
[4]
RIBOSOMAL FRAMESHIFT.
PubMed=11222762; DOI=10.1093/nar/29.5.1125;
Kim Y.-G., Maas S., Rich A.;
"Comparative mutational analysis of cis-acting RNA signals for
translational frameshifting in HIV-1 and HTLV-2.";
Nucleic Acids Res. 29:1125-1131(2001).
[5]
STRUCTURE BY NMR OF 1-136.
PubMed=9000634; DOI=10.1006/jmbi.1996.0700;
Christensen A.M., Massiah M.A., Turner B.G., Sundquist W.I.,
Summers M.F.;
"Three-dimensional structure of the HTLV-II matrix protein and
comparative analysis of matrix proteins from the different classes of
pathogenic human retroviruses.";
J. Mol. Biol. 264:1117-1131(1996).
-!- FUNCTION: Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol
polyproteins to the plasma membrane via a multipartite membrane
binding signal, that includes its myristoylated N-terminus. Also
mediates nuclear localization of the preintegration complex (By
similarity). {ECO:0000250}.
-!- FUNCTION: Capsid protein p24 forms the conical core of the virus
that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250}.
-!- FUNCTION: Nucleocapsid protein p15 is involved in the packaging
and encapsidation of two copies of the genome. {ECO:0000250}.
-!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of
Gag, Gag-Pro and Gag-Pro-Pol polyproteins during or shortly after
the release of the virion from the plasma membrane. Cleavages take
place as an ordered, step-wise cascade to yield mature proteins.
This process is called maturation. Displays maximal activity
during the budding process just prior to particle release from the
cell. Hydrolyzes host EIF4GI in order to shut off the capped
cellular mRNA translation. The resulting inhibition of cellular
protein synthesis serves to ensure maximal viral gene expression
and to evade host immune response (By similarity). {ECO:0000250}.
-!- FUNCTION: Reverse transcriptase (RT) is a multifunctional enzyme
that converts the viral RNA genome into dsDNA in the cytoplasm,
shortly after virus entry into the cell. 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. Conversion of viral genomic RNA into dsDNA
requires many steps. A tRNA-Pro binds to the primer-binding site
(PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end
of the tRNA primer to perform a short round of RNA-dependent
minus-strand DNA synthesis. The reading proceeds through the U5
region and ends after the repeated (R) region which is present at
both ends of viral RNA. The portion of the RNA-DNA heteroduplex is
digested by the RNase H, resulting in a ssDNA product attached to
the tRNA primer. This ssDNA/tRNA hybridizes with the identical R
region situated at the 3' end of viral RNA. This template
exchange, known as minus-strand DNA strong stop transfer, can be
either intra- or intermolecular. RT uses the 3' end of this newly
synthesized short ssDNA to perform the RNA-dependent minus-strand
DNA synthesis of the whole template. RNase H digests the RNA
template except for a polypurine tract (PPT) situated at the 5'
end of the genome. It is not clear if both polymerase and RNase H
activities are simultaneous. RNase H probably can proceed both in
a polymerase-dependent (RNA cut into small fragments by the same
RT performing DNA synthesis) and a polymerase-independent mode
(cleavage of remaining RNA fragments by free RTs). Secondly, RT
performs DNA-directed plus-strand DNA synthesis using the PPT that
has not been removed by RNase H as primer. PPT and tRNA primers
are then removed by RNase H. The 3' and 5' ssDNA PBS regions
hybridize to form a circular dsDNA intermediate. Strand
displacement synthesis by RT to the PBS and PPT ends produces a
blunt ended, linear dsDNA copy of the viral genome that includes
long terminal repeats (LTRs) at both ends (By similarity).
{ECO:0000250}.
-!- FUNCTION: Integrase catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. This enzyme activity takes place after virion entry
into a cell and reverse transcription of the RNA genome in dsDNA.
The first step in the integration process is 3' processing. This
step requires a complex comprising the viral genome, matrix
protein, and integrase. This complex is called the pre-integration
complex (PIC). The integrase protein removes 2 nucleotides from
each 3' end of the viral DNA, leaving recessed dinucleotides OH's
at the 3' ends. In the second step, the PIC access cell
chromosomes during cell division. The third step, termed strand
transfer, the integrase protein joins the previously processed 3'
ends to the 5'-ends of strands of target cellular DNA at the site
of integration. The 5'-ends are produced by integrase-catalyzed
staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination
intermediate results, with the 5'-ends of the viral DNA strands
and the 3' ends of target DNA strands remaining unjoined, flanking
a gap of 5 bp. The last step is viral DNA integration into host
chromosome. This involves host DNA repair synthesis in which the 5
bp gaps between the unjoined strands (see above) are filled in and
then ligated. {ECO:0000269|PubMed:8623556}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|PROSITE-ProRule:PRU00408}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for reverse transcriptase polymerase
activity. {ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
{ECO:0000250};
-!- SUBUNIT: Interacts with human TSG101. This interaction is
essential for budding and release of viral particles (By
similarity). {ECO:0000250}.
-!- INTERACTION:
O14770:MEIS2 (xeno); NbExp=3; IntAct=EBI-9676133, EBI-2804934;
-!- SUBCELLULAR LOCATION: Matrix protein p19: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p15-pro: Virion
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Comment=This strategy of translation probably allows the virus
to modulate the quantity of each viral protein.;
Name=Gag-Pol polyprotein;
IsoId=P03363-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the gag-pol genes
boundary.;
Name=Gag-Pro polyprotein;
IsoId=P03353-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the gag-pro genes
boundary.;
Name=Gag polyprotein;
IsoId=P03346-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle release. They can occur individually
or in close proximity within structural proteins. They interacts
with sorting cellular proteins of the multivesicular body (MVB)
pathway. Most of these proteins are class E vacuolar protein
sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III
complexes. Matrix protein p19 contains two L domains: a PTAP/PSAP
motif which interacts with the UEV domain of TSG101, and a PPXY
motif which binds to the WW domains of HECT (homologous to E6-AP
C-terminus) E3 ubiquitin ligases (By similarity). {ECO:0000250}.
-!- DOMAIN: The capsid protein N-terminus seems to be involved in Gag-
Gag interactions. {ECO:0000250}.
-!- PTM: Specific enzymatic cleavages by the viral protease yield
mature proteins. The polyprotein is cleaved during and after
budding, this process is termed maturation. The protease is
autoproteolytically processed at its N- and C-termini (By
similarity). {ECO:0000250}.
-!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme
that lacks a proof-reading function. High mutations rate is a
direct consequence of this characteristic. RT also displays
frequent template switching leading to high recombination rate.
Recombination mostly occurs between homologous regions of the two
copackaged RNA genomes. If these two RNA molecules derive from
different viral strains, reverse transcription will give rise to
highly recombinated proviral DNAs (By similarity). {ECO:0000250}.
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EMBL; M10060; AAB59885.1; ALT_SEQ; Genomic_DNA.
PIR; A03962; GNLJH2.
RefSeq; NP_041003.3; NC_001488.1.
PDB; 1JVR; NMR; -; A=1-136.
PDBsum; 1JVR; -.
ProteinModelPortal; P03363; -.
SMR; P03363; -.
IntAct; P03363; 8.
PRIDE; P03363; -.
GeneID; 1491941; -.
KEGG; vg:1491941; -.
OrthoDB; VOG09000135; -.
EvolutionaryTrace; P03363; -.
Proteomes; UP000009254; Genome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
Gene3D; 1.10.10.200; -; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.185.10; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 4.10.60.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR003139; D_retro_matrix.
InterPro; IPR000721; Gag_p24.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR017856; Integrase_Zn-bd_dom-like_N.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR012337; RNaseH-like_dom.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR000477; RT_dom.
InterPro; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
Pfam; PF02228; Gag_p19; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00552; IN_DBD_C; 1.
Pfam; PF02022; Integrase_Zn; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF06817; RVT_thumb; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS51027; INTEGRASE_DBD; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Capsid protein; Complete proteome;
DNA integration; DNA recombination; DNA-binding; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus;
Host gene expression shutoff by virus; Host-virus interaction;
Hydrolase; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
Protease; Reference proteome; Repeat; Ribosomal frameshifting;
RNA-directed DNA polymerase; Transferase; Viral genome integration;
Viral nucleoprotein; Virion; Virus entry into host cell; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 1461 Gag-Pro-Pol polyprotein.
/FTId=PRO_0000085472.
CHAIN 2 136 Matrix protein p19. {ECO:0000250}.
/FTId=PRO_0000259946.
CHAIN 137 350 Capsid protein p24. {ECO:0000250}.
/FTId=PRO_0000259947.
CHAIN 351 446 Nucleocapsid protein p15-pro.
{ECO:0000250}.
/FTId=PRO_0000259948.
CHAIN 447 571 Protease. {ECO:0000250}.
/FTId=PRO_0000261318.
PEPTIDE 572 579 p1. {ECO:0000250}.
/FTId=PRO_0000259949.
CHAIN 580 1166 Reverse transcriptase/ribonuclease H.
{ECO:0000250}.
/FTId=PRO_0000259950.
CHAIN 1167 1461 Integrase. {ECO:0000250}.
/FTId=PRO_0000259951.
DOMAIN 473 551 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 612 802 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1029 1164 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1218 1387 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 361 378 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 384 401 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
DNA_BIND 1392 1441 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
MOTIF 94 97 PTAP/PSAP motif.
MOTIF 124 127 PPXY motif.
COMPBIAS 94 150 Pro-rich.
COMPBIAS 453 456 Poly-Gln.
COMPBIAS 585 588 Poly-Pro.
ACT_SITE 478 478 For protease activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU10094}.
METAL 678 678 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 753 753 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 754 754 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1038 1038 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1073 1073 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1095 1095 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1156 1156 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1229 1229 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1286 1286 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
SITE 136 137 Cleavage; by viral protease.
{ECO:0000250}.
SITE 350 351 Cleavage; by viral protease.
{ECO:0000250}.
SITE 446 447 Cleavage; by viral protease.
{ECO:0000250}.
SITE 571 572 Cleavage; by viral protease.
{ECO:0000250}.
SITE 579 580 Cleavage; by viral protease.
{ECO:0000250}.
SITE 1166 1167 Cleavage; by viral protease.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 2 9 {ECO:0000244|PDB:1JVR}.
HELIX 21 33 {ECO:0000244|PDB:1JVR}.
TURN 40 42 {ECO:0000244|PDB:1JVR}.
HELIX 43 54 {ECO:0000244|PDB:1JVR}.
TURN 60 63 {ECO:0000244|PDB:1JVR}.
TURN 65 67 {ECO:0000244|PDB:1JVR}.
HELIX 68 71 {ECO:0000244|PDB:1JVR}.
HELIX 80 88 {ECO:0000244|PDB:1JVR}.
TURN 89 91 {ECO:0000244|PDB:1JVR}.
STRAND 99 103 {ECO:0000244|PDB:1JVR}.
STRAND 117 119 {ECO:0000244|PDB:1JVR}.
SEQUENCE 1461 AA; 162402 MW; 2D2911076BDD1002 CRC64;
MGQIHGLSPT PIPKAPRGLS THHWLNFLQA AYRLQPRPSD FDFQQLRRFL KLALKTPIWL
NPIDYSLLAS LIPKGYPGRV VEIINILVKN QVSPSAPAAP VPTPICPTTT PPPPPPPSPE
AHVPPPYVEP TTTQCFPILH PPGAPSAHRP WQMKDLQAIK QEVSSSALGS PQFMQTLRLA
VQQFDPTAKD LQDLLQYLCS SLVVSLHHQQ LNTLITEAET RGMTGYNPMA GPLRMQANNP
AQQGLRREYQ NLWLAAFSTL PGNTRDPSWA AILQGLEEPY CAFVERLNVA LDNGLPEGTP
KEPILRSLAY SNANKECQKI LQARGHTNSP LGEMLRTCQA WTPKDKTKVL VVQPRRPPPT
QPCFRCGKVG HWSRDCTQPR PPPGPCPLCQ DPSHWKRDCP QLKPPQEEGE PLLLDLPSTS
GTTEEKNLLK GGDLISPHPD QDISILPLIP LRQQQQPILG VRISVMGQTP QPTQALLDTG
ADLTVIPQTL VPGPVKLHDT LILGASGQTN TQFKLLQTPL HIFLPFRRSP VILSSCLLDT
HNKWTIIGRD ALQQCQGLLY LPDDPSPHQL LPIATPNTIG LEHLPPPPQV DQFPLNLPER
LQALNDLVSK ALEAGHIEPY SGPGNNPVFP VKKPNGKWRF IHDLRATNAI TTTLTSPSPG
PPDLTSLPTA LPHLQTIDLT DAFFQIPLPK QYQPYFAFTI PQPCNYGPGT RYAWTVLPQG
FKNSPTLFEQ QLAAVLNPMR KMFPTSTIVQ YMDDILLASP TNEELQQLSQ LTLQALTTHG
LPISQEKTQQ TPGQIRFLGQ VISPNHITYE STPTIPIKSQ WTLTELQVIL GEIQWVSKGT
PILRKHLQSL YSALHGYRDP RACITLTPQQ LHALHAIQQA LQHNCRGRLN PALPLLGLIS
LSTSGTTSVI FQPKQNWPLA WLHTPHPPTS LCPWGHLLAC TILTLDKYTL QHYGQLCQSF
HHNMSKQALC DFLRNSPHPS VGILIHHMGR FHNLGSQPSG PWKTLLHLPT LLQEPRLLRP
IFTLSPVVLD TAPCLFSDGS PQKAAYVLWD QTILQQDITP LPSHETHSAQ KGELLALICG
LRAAKPWPSL NIFLDSKYLI KYLHSLAIGA FLGTSAHQTL QAALPPLLQG KTIYLHHVRS
HTNLPDPIST FNEYTDSLIL APLVPLTPQG LHGLTHCNQR ALVSFGATPR EAKSLVQTCH
TCQTINSQHH MPRGYIRRGL LPNHIWQGDV THYKYKKYKY CLHVWVDTFS GAVSVSCKKK
ETSCETISAV LQAISLLGKP LHINTDNGPA FLSQEFQEFC TSYRIKHSTH IPYNPTSSGL
VERTNGVIKN LLNKYLLDCP NLPLDNAIHK ALWTLNQLNV MNPSGKTRWQ IHHSPPLPPI
PEASTPPKPP PKWFYYKLPG LTNQRWKGPL QSLQEAAGAA LLSIDGSPRW IPWRFLKKAA
CPRPDASELA EHAATDHQHH G


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OBT1904X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa340_390), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Appli 1 mg
PCR-501S M_MLV Reverse Transcriptase (RNase H_), S pack Reverse Transcriptase 10000units
PCR-501L M_MLV Reverse Transcriptase (RNase H_), L pack Reverse Transcriptase 50000units
orb81556 Hepatitis Virus Nucleocapsid (core) Genotype-1b protein The E.coli derived recombinant multimer protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fus 100
orb81557 Hepatitis Virus Nucleocapsid (core) Genotype-2a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81559 Hepatitis Virus Nucleocapsid (core) Genotype-3a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81558 Hepatitis Virus Nucleocapsid (core) Genotype-2b protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100


 

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