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Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.47) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_HV2RO               Reviewed;        1464 AA.
P04584; Q76629;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 194.
RecName: Full=Gag-Pol polyprotein;
AltName: Full=Pr160Gag-Pol;
Contains:
RecName: Full=Matrix protein p17;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Spacer peptide 1 {ECO:0000250|UniProtKB:P12497};
Short=SP1;
AltName: Full=p2;
Contains:
RecName: Full=Nucleocapsid protein p7;
Short=NC;
Contains:
RecName: Full=Transframe peptide;
Short=TF;
Contains:
RecName: Full=p6-pol;
Short=p6*;
Contains:
RecName: Full=Protease;
EC=3.4.23.47;
AltName: Full=PR;
AltName: Full=Retropepsin;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.13;
AltName: Full=Exoribonuclease H;
EC=3.1.13.2;
AltName: Full=p66 RT;
Contains:
RecName: Full=p51 RT;
Contains:
RecName: Full=p15;
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
Name=gag-pol;
Human immunodeficiency virus type 2 subtype A (isolate ROD) (HIV-2).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=11720;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE.
PubMed=3031510; DOI=10.1038/326662a0;
Guyader M., Emerman M., Sonigo P., Clavel F., Montagnier L.,
Alizon M.;
"Genome organization and transactivation of the human immunodeficiency
virus type 2.";
Nature 326:662-669(1987).
[2]
REVIEW.
PubMed=8791726;
Vogt V.M.;
"Proteolytic processing and particle maturation.";
Curr. Top. Microbiol. Immunol. 214:95-131(1996).
[3]
REVIEW.
PubMed=9878383; DOI=10.1006/jmbi.1998.2354;
Turner B.G., Summers M.F.;
"Structural biology of HIV.";
J. Mol. Biol. 285:1-32(1999).
[4]
REVIEW.
PubMed=11700285; DOI=10.1146/annurev.genet.35.102401.090551;
Negroni M., Buc H.;
"Mechanisms of retroviral recombination.";
Annu. Rev. Genet. 35:275-302(2001).
[5]
REVIEW.
PubMed=11983066; DOI=10.1186/gb-2002-3-4-reviews3006;
Dunn B.M., Goodenow M.M., Gustchina A., Wlodawer A.;
"Retroviral proteases.";
Genome Biol. 3:REVIEWS3006.1-REVIEWS3006.7(2002).
[6]
3D-STRUCTURE MODELING OF 514-612.
PubMed=1946342; DOI=10.1002/prot.340100406;
Gustchina A., Weber I.T.;
"Comparative analysis of the sequences and structures of HIV-1 and
HIV-2 proteases.";
Proteins 10:325-339(1991).
[7]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 514-612 IN COMPLEX WITH A
REDUCED AMIDE INHIBITOR.
PubMed=8378311; DOI=10.1073/pnas.90.18.8387;
Tong L., Pav S., Pargellis C., Do F., Lamarre D., Anderson P.C.;
"Crystal structure of human immunodeficiency virus (HIV) type 2
protease in complex with a reduced amide inhibitor and comparison with
HIV-1 protease structures.";
Proc. Natl. Acad. Sci. U.S.A. 90:8387-8391(1993).
[8]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 514-612 IN COMPLEX WITH THE
INHIBITORS U75875 AND U92163.
PubMed=8514751;
Mulichak A.M., Hui J.O., Tomasselli A.G., Heinrikson R.L., Curry K.A.,
Tomich C.S., Thaisrivongs S., Sawyer T.K., Watenpaugh K.D.;
"The crystallographic structure of the protease from human
immunodeficiency virus type 2 with two synthetic peptidic transition
state analog inhibitors.";
J. Biol. Chem. 268:13103-13109(1993).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 514-612 IN COMPLEX WITH THE
INHIBITOR L-736,524.
PubMed=7929352;
Chen Z., Li Y., Chen E., Hall D.L., Darke P.L., Culberson C.,
Shafer J.A., Kuo L.C.;
"Crystal structure at 1.9-A resolution of human immunodeficiency virus
(HIV) II protease complexed with L-735,524, an orally bioavailable
inhibitor of the HIV proteases.";
J. Biol. Chem. 269:26344-26348(1994).
[10]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 514-612 IN COMPLEX WITH THE
INHIBITOR CGP 53820.
PubMed=7613867; DOI=10.1016/S0969-2126(01)00169-1;
Priestle J.P., Fassler A., Rosel J., Tintelnot-Blomley M., Strop P.,
Gruetter M.G.;
"Comparative analysis of the X-ray structures of HIV-1 and HIV-2
proteases in complex with CGP 53820, a novel pseudosymmetric
inhibitor.";
Structure 3:381-389(1995).
[11]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 514-612 IN COMPLEX WITH
INHIBITORS.
PubMed=7743130; DOI=10.1016/S0969-2126(01)00133-2;
Tong L., Pav S., Mui S., Lamarre D., Yoakim C., Beaulieu P.L.,
Anderson P.C.;
"Crystal structures of HIV-2 protease in complex with inhibitors
containing the hydroxyethylamine dipeptide isostere.";
Structure 3:33-40(1995).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 514-612 IN COMPLEX WITH THE
INHIBITORS U096333 AND U097410.
PubMed=7658450; DOI=10.1021/jm00018a023;
Thaisrivongs S., Watenpaugh K.D., Howe W.J., Tomich P.K., Dolak L.A.,
Chong K.-T., Tomich C.C., Tomasselli A.G., Turner S.R.,
Strohbach J.W., Mulichak A.M., Janakiraman M.N., Moon J.B., Lynn J.C.,
Horng M.-M., Hinshaw R.R., Curry K.A., Rothrock D.J.;
"Structure-based design of novel HIV protease inhibitors: carboxamide-
containing 4-hydroxycoumarins and 4-hydroxy-2-pyrones as potent
nonpeptidic inhibitors.";
J. Med. Chem. 38:3624-3637(1995).
[13]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 514-612.
PubMed=7783120; DOI=10.1021/jm00011a008;
Romines K.R., Watenpaugh K.D., Tomich P.K., Howe W.J., Morris J.K.,
Lovasz K.D., Mulichak A.M., Finzel B.C., Lynn J.C., Horng M.-M.,
Schwende F.J., Ruwart M.J., Zipp G.L., Chong K.-T., Dolak L.A.,
Toth L.N., Howard G.M., Rush B.D., Wilkinson K.F., Possert P.L.,
Dalga R.J., Hinshaw R.R.;
"Use of medium-sized cycloalkyl rings to enhance secondary binding:
discovery of a new class of human immunodeficiency virus (HIV)
protease inhibitors.";
J. Med. Chem. 38:1884-1891(1995).
[14]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 514-612 IN COMPLEX WITH
(HYDROXYETHYL)AMIDE ISOSTERE CONTAINING INHIBITORS.
PubMed=9216835; DOI=10.1021/jm9606608;
Beaulieu P.L., Wernic D., Abraham A., Anderson P.C., Bogri T.,
Bousquet Y., Croteau G., Guse I., Lamarre D., Liard F., Paris W.,
Thibeault D., Pav S., Tong L.;
"Potent HIV protease inhibitors containing a novel (hydroxyethyl)amide
isostere.";
J. Med. Chem. 40:2164-2176(1997).
[15]
STRUCTURE BY NMR OF 1172-1226.
PubMed=9368756; DOI=10.1016/S0960-9822(06)00332-0;
Eijkelenboom A.P.A.M., van den Ent F.M.I., Vos A., Doreleijers J.F.,
Hard K., Tullius T.D., Plasterk R.H.A., Kaptein R., Boelens R.;
"The solution structure of the amino-terminal HHCC domain of HIV-2
integrase: a three-helix bundle stabilized by zinc.";
Curr. Biol. 7:739-746(1997).
[16]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 613-1167.
PubMed=12386343; DOI=10.1073/pnas.222366699;
Ren J.S., Bird L.E., Chamberlain P.P., Stewart-Jones G.B.,
Stuart D.I., Stammers D.K.;
"Structure of HIV-2 reverse transcriptase at 2.35-A resolution and the
mechanism of resistance to non-nucleoside inhibitors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14410-14415(2002).
-!- FUNCTION: Gag-Pol polyprotein: Mediates, with Gag polyprotein, the
essential events in virion assembly, including binding the plasma
membrane, making the protein-protein interactions necessary to
create spherical particles, recruiting the viral Env proteins, and
packaging the genomic RNA via direct interactions with the RNA
packaging sequence (Psi). Gag-Pol polyprotein may regulate its own
translation, by the binding genomic RNA in the 5'-UTR. At low
concentration, the polyprotein would promote translation, whereas
at high concentration, the polyprotein would encapsidate genomic
RNA and then shut off translation. {ECO:0000250}.
-!- FUNCTION: Matrix protein p17: Targets the polyprotein to the
plasma membrane via a multipartite membrane-binding signal, that
includes its myristoylated N-terminus. Matrix protein is part of
the pre-integration complex. Implicated in the release from host
cell mediated by Vpu. Binds to RNA.
{ECO:0000250|UniProtKB:P12497}.
-!- FUNCTION: Capsid protein p24: Forms the conical core that
encapsulates the genomic RNA-nucleocapsid complex in the virion.
Most core are conical, with only 7% tubular. The core is
constituted by capsid protein hexamer subunits. The core is
disassembled soon after virion entry (By similarity). Host
restriction factors such as TRIM5-alpha or TRIMCyp bind retroviral
capsids and cause premature capsid disassembly, leading to blocks
in reverse transcription. Capsid restriction by TRIM5 is one of
the factors which restricts HIV-1 to the human species. Host PIN1
apparently facilitates the virion uncoating. On the other hand,
interactions with PDZD8 or CYPA stabilize the capsid.
{ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
-!- FUNCTION: Nucleocapsid protein p7: Encapsulates and protects viral
dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its
zinc fingers. Acts as a nucleic acid chaperone which is involved
in rearangement of nucleic acid secondary structure during gRNA
retrotranscription. Also facilitates template switch leading to
recombination. As part of the polyprotein, participates in gRNA
dimerization, packaging, tRNA incorporation and virion assembly.
{ECO:0000250|UniProtKB:P04585}.
-!- FUNCTION: Protease: Aspartyl protease that mediates proteolytic
cleavages of Gag and Gag-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. Also cleaves Nef and Vif, probably concomitantly with viral
structural proteins on maturation of virus particles. Hydrolyzes
host EIF4GI and PABP1 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|UniProtKB:P04585, ECO:0000255|PROSITE-
ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H: 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(3)-Lys 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 two polypurine tracts (PPTs)
situated at the 5'-end and near the center 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 PPTs that have not
been removed by RNase H as primers. PPTs 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. {ECO:0000250|UniProtKB:P04585}.
-!- 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, Vpr 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 CA
OH's at the 3' ends. In the second step, the PIC enters cell
nucleus. This process is mediated through integrase and Vpr
proteins, and allows the virus to infect a non dividing cell. This
ability to enter the nucleus is specific of lentiviruses, other
retroviruses cannot and rely on cell division to access cell
chromosomes. In 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 are filled in and then ligated. Since this
process occurs at both cuts flanking the HIV genome, a 5 bp
duplication of host DNA is produced at the ends of HIV-1
integration. Alternatively, Integrase may catalyze the excision of
viral DNA just after strand transfer, this is termed
disintegration. {ECO:0000250|UniProtKB:P04585}.
-!- CATALYTIC ACTIVITY:
Reaction=Endopeptidase for which the P1 residue is preferably
hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-
ProRule:PRU00275};
-!- CATALYTIC ACTIVITY:
Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
cleavage modes: 1. sequence-specific internal cleavage of RNA.
Human immunodeficiency virus type 1 and Moloney murine leukemia
virus enzymes prefer to cleave the RNA strand one nucleotide
away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage
13-19 nucleotides from the RNA end. 3. DNA 3'-end directed
cleavage 15-20 nucleotides away from the primer terminus.;
EC=3.1.26.13; Evidence={ECO:0000250};
-!- CATALYTIC ACTIVITY:
Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
hybrid.; EC=3.1.13.2; Evidence={ECO:0000250};
-!- CATALYTIC ACTIVITY:
Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.49;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
-!- CATALYTIC ACTIVITY:
Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
Evidence={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.
Substrate-binding is a precondition for magnesium binding.
{ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Magnesium ions are required for integrase activity. Binds at
least 1, maybe 2 magnesium ions. {ECO:0000250};
-!- ACTIVITY REGULATION: Protease: The viral protease is inhibited by
many synthetic protease inhibitors (PIs), such as amprenavir,
atazanavir, indinavir, loprinavir, nelfinavir, ritonavir and
saquinavir. Use of protease inhibitors in tritherapy regimens
permit more ambitious therapeutic strategies. Reverse
transcriptase/ribonuclease H: RT can be inhibited either by
nucleoside RT inhibitors (NRTIs) or by non nucleoside RT
inhibitors (NNRTIs). NRTIs act as chain terminators, whereas
NNRTIs inhibit DNA polymerization by binding a small hydrophobic
pocket near the RT active site and inducing an allosteric change
in this region. Classical NRTIs are abacavir, adefovir (PMEA),
didanosine (ddI), lamivudine (3TC), stavudine (d4T), tenofovir
(PMPA), zalcitabine (ddC), and zidovudine (AZT). Classical NNRTIs
are atevirdine (BHAP U-87201E), delavirdine, efavirenz (DMP-266),
emivirine (I-EBU), and nevirapine (BI-RG-587). The tritherapies
used as a basic effective treatment of AIDS associate two NRTIs
and one NNRTI. {ECO:0000250}.
-!- SUBUNIT: Matrix protein p17: Homotrimer; further assembles as
hexamers of trimers (By similarity). Matrix protein p17: Interacts
with gp41 (via C-terminus) (By similarity). Matrix protein p17:
interacts with host CALM1; this interaction induces a
conformational change in the Matrix protein, triggering exposure
of the myristate group (By similarity). Matrix protein p17:
interacts with host AP3D1; this interaction allows the polyprotein
trafficking to multivesicular bodies during virus assembly (By
similarity). Matrix protein p17: Part of the pre-integration
complex (PIC) which is composed of viral genome, matrix protein,
Vpr and integrase (By similarity). Capsid protein p24: Homodimer;
the homodimer further multimerizes as homohexamers or
homopentamers. Capsid protein p24: Interacts with human PPIA/CYPA
(By similarity); This interaction stabilizes the capsid. Capsid
protein p24: Interacts with human NUP153 (By similarity). Capsid
protein p24: Interacts with host PDZD8; this interaction
stabilizes the capsid (By similarity). Capsid protein p24:
Interacts with monkey TRIM5; this interaction destabilizes the
capsid (By similarity).Protease: Homodimer, whose active site
consists of two apposed aspartic acid residues. Reverse
transcriptase/ribonuclease H: Heterodimer of p66 RT and p51 RT (RT
p66/p51). Heterodimerization of RT is essential for DNA polymerase
activity. Despite the sequence identities, p66 RT and p51 RT have
distinct folding. Integrase: Homodimer; possibly can form
homotetramer. Integrase: Part of the pre-integration complex (PIC)
which is composed of viral genome, matrix protein, Vpr and
integrase. Integrase: Interacts with human SMARCB1/INI1 and human
PSIP1/LEDGF isoform 1. Integrase: Interacts with human KPNA3; this
interaction might play a role in nuclear import of the pre-
integration complex (By similarity). Integrase: Interacts with
human NUP153; this interaction might play a role in nuclear import
of the pre-integration complex (By similarity).
{ECO:0000250|UniProtKB:P04585, ECO:0000250|UniProtKB:P12497}.
-!- SUBCELLULAR LOCATION: Gag-Pol polyprotein: Host cell membrane;
Lipid-anchor. Host endosome, host multivesicular body. Note=These
locations are linked to virus assembly sites. The main location is
the cell membrane, but under some circumstances, late endosomal
compartments can serve as productive sites for virion assembly.
{ECO:0000250|UniProtKB:P12497}.
-!- SUBCELLULAR LOCATION: Matrix protein p17: Virion membrane; Lipid-
anchor {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p7: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Reverse transcriptase/ribonuclease H: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Integrase: Virion {ECO:0000305}. Host
nucleus {ECO:0000305}. Host cytoplasm {ECO:0000305}. Note=Nuclear
at initial phase, cytoplasmic at assembly. {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=2;
Comment=Translation results in the formation of the Gag
polyprotein most of the time. Ribosomal frameshifting at the
gag-pol genes boundary occurs at low frequency and produces the
Gag-Pol polyprotein. This strategy of translation probably
allows the virus to modulate the quantity of each viral protein.
Maintenance of a correct Gag to Gag-Pol ratio is essential for
RNA dimerization and viral infectivity.;
Name=Gag-Pol polyprotein;
IsoId=P04584-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting.;
Name=Gag polyprotein;
IsoId=P04590-1; Sequence=External;
Note=Produced by conventional translation.;
-!- DOMAIN: Reverse transcriptase/ribonuclease H: RT is 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 RNase H domain
stabilizes the association of RT with primer-template.
{ECO:0000250}.
-!- DOMAIN: Reverse transcriptase/ribonuclease H: The tryptophan
repeat motif is involved in RT p66/p51 dimerization (By
similarity). {ECO:0000250}.
-!- DOMAIN: Integrase: The core domain contains the D-x(n)-D-x(35)-E
motif, named for the phylogenetically conserved glutamic acid and
aspartic acid residues and the invariant 35 amino acid spacing
between the second and third acidic residues. Each acidic residue
of the D,D(35)E motif is independently essential for the 3'-
processing and strand transfer activities of purified integrase
protein. {ECO:0000250}.
-!- PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the
viral protease yield mature proteins. The protease is released by
autocatalytic cleavage. The polyprotein is cleaved during and
after budding, this process is termed maturation. Proteolytic
cleavage of p66 RT removes the RNase H domain to yield the p51 RT
subunit. Nucleocapsid protein p7 might be further cleaved after
virus entry. {ECO:0000250|UniProtKB:P04585, ECO:0000255|PROSITE-
ProRule:PRU00405}.
-!- MISCELLANEOUS: Reverse transcriptase/ribonuclease H: 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. {ECO:0000250}.
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EMBL; X05291; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; M15390; AAB00764.1; ALT_SEQ; Genomic_DNA.
PIR; B26262; GNLJG2.
PDB; 1E0E; NMR; -; A/B=1172-1226.
PDB; 1HII; X-ray; 2.30 A; A/B=514-612.
PDB; 1HSH; X-ray; 1.90 A; A/B/C/D=514-612.
PDB; 1HSI; X-ray; 2.50 A; A/B=514-612.
PDB; 1IDA; X-ray; 1.70 A; A/B=514-612.
PDB; 1IDB; X-ray; 2.20 A; A/B=514-612.
PDB; 1IVP; X-ray; 2.50 A; A/B=514-612.
PDB; 1IVQ; X-ray; 2.60 A; A/B=514-612.
PDB; 1JLD; X-ray; 2.50 A; A/B=514-612.
PDB; 1MU2; X-ray; 2.35 A; A=613-1167, B=618-1043.
PDB; 1PHV; Model; -; A=514-612.
PDB; 2HPE; X-ray; 2.00 A; A/B=514-612.
PDB; 2HPF; X-ray; 3.00 A; A/B=514-612.
PDB; 2K4E; NMR; -; A=2-135.
PDB; 2K4H; NMR; -; A=2-135.
PDB; 2K4I; NMR; -; A=2-135.
PDB; 2MIP; X-ray; 2.20 A; A/B/C/D=514-612.
PDB; 2PHV; Model; -; A/B=514-612.
PDB; 3EBZ; X-ray; 1.20 A; A/B=514-612.
PDB; 3EC0; X-ray; 1.18 A; A/B=514-612.
PDB; 3ECG; X-ray; 1.18 A; A/B=514-612.
PDB; 3F9K; X-ray; 3.20 A; A/B/E/F/I/J/M/N/Q/R/U/V/Y/Z/c/d/g/h/k/l/o/p/s/t=1173-1380.
PDB; 3UPJ; X-ray; 2.50 A; A/B=514-612.
PDB; 4UPJ; X-ray; 1.90 A; A/B=514-612.
PDB; 5UPJ; X-ray; 2.30 A; A/B=514-612.
PDB; 6UPJ; X-ray; 2.34 A; A/B=514-612.
PDBsum; 1E0E; -.
PDBsum; 1HII; -.
PDBsum; 1HSH; -.
PDBsum; 1HSI; -.
PDBsum; 1IDA; -.
PDBsum; 1IDB; -.
PDBsum; 1IVP; -.
PDBsum; 1IVQ; -.
PDBsum; 1JLD; -.
PDBsum; 1MU2; -.
PDBsum; 1PHV; -.
PDBsum; 2HPE; -.
PDBsum; 2HPF; -.
PDBsum; 2K4E; -.
PDBsum; 2K4H; -.
PDBsum; 2K4I; -.
PDBsum; 2MIP; -.
PDBsum; 2PHV; -.
PDBsum; 3EBZ; -.
PDBsum; 3EC0; -.
PDBsum; 3ECG; -.
PDBsum; 3F9K; -.
PDBsum; 3UPJ; -.
PDBsum; 4UPJ; -.
PDBsum; 5UPJ; -.
PDBsum; 6UPJ; -.
ProteinModelPortal; P04584; -.
SMR; P04584; -.
IntAct; P04584; 1.
DrugBank; DB08664; ({3-[1-(4-HYDROXY-2-OXO-2H-CHROMEN-3-YL)-PROPYL]-PHENYLCARBAMOYL}-METHYL)-CARBAMIC ACID TERT-BUTYL ESTER.
DrugBank; DB04245; 2-Hydroxy-3-Amino-4-Phenyl Butane.
DrugBank; DB08425; 3(S)-AMINO-4-PHENYL-BUTAN-2(R)-OL.
DrugBank; DB08474; 3-(CARBOXYAMIDE(2-CARBOXYAMIDE-2-TERTBUTYLETHYL))PENTAN.
DrugBank; DB04490; 3-(Mercaptomethylene)Pyridine.
DrugBank; DB08663; 4-HYDROXY-7-METHOXY-3-(1-PHENYL-PROPYL)-CHROMEN-2-ONE.
DrugBank; DB07581; 5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOPROPYL-HEXANOIC ACID.
DrugBank; DB08231; MYRISTIC ACID.
DrugBank; DB08286; NAPHTHYLOXYACETIC ACID.
DrugBank; DB03149; Phenylalanylmethane.
DrugBank; DB08421; PIPERIDINE-2-CARBOXYLIC ACID TERT-BUTYLAMIDE.
DrugBank; DB02428; Quinaldic Acid.
PRIDE; P04584; -.
OrthoDB; VOG09000135; -.
BioCyc; MetaCyc:MONOMER-16108; -.
BRENDA; 3.4.23.47; 2677.
EvolutionaryTrace; P04584; -.
PRO; PR:P04584; -.
Proteomes; UP000007426; Genome.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0072494; C:host multivesicular body; IEA:UniProtKB-SubCell.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
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-KW.
GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
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.
GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
CDD; cd05482; HIV_retropepsin_like; 1.
Gene3D; 1.10.10.200; -; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.150.90; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.30.30.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR000721; Gag_p24.
InterPro; IPR017856; Integrase-like_N.
InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR000071; Lentvrl_matrix_N.
InterPro; IPR012344; Matrix_HIV/RSV_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR034170; Retropepsin-like_cat_dom.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR000477; RT_dom.
InterPro; IPR010659; RVT_connect.
InterPro; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00540; Gag_p17; 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; PF06815; RVT_connect; 1.
Pfam; PF06817; RVT_thumb; 1.
Pfam; PF00098; zf-CCHC; 2.
PRINTS; PR00234; HIV1MATRIX.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF46919; SSF46919; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 2.
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; 2.
PROSITE; PS50876; ZF_INTEGRASE; 1.
1: Evidence at protein level;
3D-structure; AIDS; Aspartyl protease; Capsid protein;
Complete proteome; DNA integration; DNA recombination; DNA-binding;
DNA-directed DNA polymerase; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus; Host cell membrane;
Host cytoplasm; Host endosome; Host gene expression shutoff by virus;
Host membrane; Host nucleus; Host-virus interaction; Hydrolase;
Lipid-binding; Lipoprotein; Magnesium; Membrane; Metal-binding;
Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
Phosphoprotein; Protease; Repeat; Ribosomal frameshifting;
RNA-binding; RNA-directed DNA polymerase; Transferase;
Viral genome integration; Viral nucleoprotein;
Viral penetration into host nucleus; Viral release from host cell;
Virion; Virion maturation; Virus entry into host cell; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 1464 Gag-Pol polyprotein.
/FTId=PRO_0000261298.
CHAIN 2 135 Matrix protein p17. {ECO:0000250}.
/FTId=PRO_0000042537.
CHAIN 136 365 Capsid protein p24. {ECO:0000250}.
/FTId=PRO_0000042538.
PEPTIDE 366 382 Spacer peptide 1. {ECO:0000250}.
/FTId=PRO_0000042539.
CHAIN 383 431 Nucleocapsid protein p7. {ECO:0000250}.
/FTId=PRO_0000042541.
PEPTIDE 432 445 Transframe peptide. {ECO:0000255}.
/FTId=PRO_0000246747.
CHAIN 446 513 p6-pol. {ECO:0000255}.
/FTId=PRO_0000042543.
CHAIN 514 612 Protease. {ECO:0000250}.
/FTId=PRO_0000038674.
CHAIN 613 1171 Reverse transcriptase/ribonuclease H.
{ECO:0000250}.
/FTId=PRO_0000042544.
CHAIN 613 1051 p51 RT. {ECO:0000250}.
/FTId=PRO_0000042545.
CHAIN 1052 1171 p15. {ECO:0000250}.
/FTId=PRO_0000042546.
CHAIN 1172 1464 Integrase. {ECO:0000250}.
/FTId=PRO_0000042547.
DOMAIN 533 602 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 656 846 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1045 1168 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1224 1375 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 389 406 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 410 427 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1174 1215 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00450}.
DNA_BIND 1394 1441 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
REGION 7 31 Interaction with Gp41.
{ECO:0000250|UniProtKB:P12497}.
REGION 191 228 Interaction with human PPIA/CYPA and
NUP153. {ECO:0000250|UniProtKB:P12497}.
REGION 279 365 Dimerization/Multimerization of capsid
protein p24.
{ECO:0000250|UniProtKB:P04585}.
REGION 514 518 Dimerization of protease.
{ECO:0000250|UniProtKB:P04585}.
REGION 562 568 Dimerization of protease.
{ECO:0000250|UniProtKB:P04585}.
REGION 601 613 Dimerization of protease.
{ECO:0000250|UniProtKB:P04585}.
REGION 839 847 RT 'primer grip'. {ECO:0000250}.
MOTIF 16 22 Nuclear export signal. {ECO:0000250}.
MOTIF 26 32 Nuclear localization signal.
{ECO:0000250}.
MOTIF 1009 1025 Tryptophan repeat motif. {ECO:0000250}.
ACT_SITE 538 538 For protease activity; shared with
dimeric partner. {ECO:0000255|PROSITE-
ProRule:PRU10094}.
METAL 722 722 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 797 797 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 798 798 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1054 1054 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1089 1089 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1109 1109 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1160 1160 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1235 1235 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1287 1287 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1323 1323 Magnesium; catalytic; for integrase
activity. {ECO:0000250|UniProtKB:P04585}.
SITE 135 136 Cleavage; by viral protease.
{ECO:0000250}.
SITE 222 223 Cis/trans isomerization of proline
peptide bond; by human PPIA/CYPA.
{ECO:0000250}.
SITE 365 366 Cleavage; by viral protease.
{ECO:0000250}.
SITE 382 383 Cleavage; by viral protease.
{ECO:0000250}.
SITE 431 432 Cleavage; by viral protease.
{ECO:0000255}.
SITE 445 446 Cleavage; by viral protease.
{ECO:0000250}.
SITE 513 514 Cleavage; by viral protease.
{ECO:0000250}.
SITE 612 613 Cleavage; by viral protease.
{ECO:0000250}.
SITE 1012 1012 Essential for RT p66/p51
heterodimerization. {ECO:0000250}.
SITE 1025 1025 Essential for RT p66/p51
heterodimerization. {ECO:0000250}.
SITE 1051 1052 Cleavage; by viral protease; partial.
{ECO:0000250}.
SITE 1171 1172 Cleavage; by viral protease.
{ECO:0000250}.
MOD_RES 135 135 Phosphotyrosine; by host. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
STRAND 6 8 {ECO:0000244|PDB:2K4E}.
HELIX 10 18 {ECO:0000244|PDB:2K4E}.
STRAND 19 22 {ECO:0000244|PDB:2K4E}.
HELIX 31 44 {ECO:0000244|PDB:2K4E}.
HELIX 49 51 {ECO:0000244|PDB:2K4E}.
HELIX 54 64 {ECO:0000244|PDB:2K4E}.
TURN 65 70 {ECO:0000244|PDB:2K4E}.
HELIX 73 90 {ECO:0000244|PDB:2K4E}.
HELIX 97 115 {ECO:0000244|PDB:2K4E}.
STRAND 515 517 {ECO:0000244|PDB:1IDB}.
STRAND 518 520 {ECO:0000244|PDB:3EC0}.
STRAND 523 528 {ECO:0000244|PDB:3EC0}.
STRAND 531 537 {ECO:0000244|PDB:3EC0}.
STRAND 541 543 {ECO:0000244|PDB:2HPE}.
STRAND 545 548 {ECO:0000244|PDB:3EC0}.
STRAND 556 562 {ECO:0000244|PDB:3EC0}.
STRAND 565 579 {ECO:0000244|PDB:3EC0}.
STRAND 582 591 {ECO:0000244|PDB:3EC0}.
STRAND 594 598 {ECO:0000244|PDB:2HPF}.
HELIX 600 606 {ECO:0000244|PDB:3EC0}.
STRAND 609 611 {ECO:0000244|PDB:3EC0}.
HELIX 640 655 {ECO:0000244|PDB:1MU2}.
STRAND 658 661 {ECO:0000244|PDB:1MU2}.
STRAND 672 674 {ECO:0000244|PDB:1MU2}.
STRAND 685 687 {ECO:0000244|PDB:1MU2}.
HELIX 690 695 {ECO:0000244|PDB:1MU2}.
HELIX 709 711 {ECO:0000244|PDB:1MU2}.
HELIX 712 714 {ECO:0000244|PDB:1MU2}.
STRAND 716 722 {ECO:0000244|PDB:1MU2}.
STRAND 724 726 {ECO:0000244|PDB:1MU2}.
HELIX 727 729 {ECO:0000244|PDB:1MU2}.
TURN 734 736 {ECO:0000244|PDB:1MU2}.
HELIX 737 740 {ECO:0000244|PDB:1MU2}.
STRAND 742 744 {ECO:0000244|PDB:1MU2}.
HELIX 747 749 {ECO:0000244|PDB:1MU2}.
STRAND 755 760 {ECO:0000244|PDB:1MU2}.
HELIX 768 786 {ECO:0000244|PDB:1MU2}.
STRAND 790 795 {ECO:0000244|PDB:1MU2}.
STRAND 798 803 {ECO:0000244|PDB:1MU2}.
HELIX 807 823 {ECO:0000244|PDB:1MU2}.
STRAND 836 841 {ECO:0000244|PDB:1MU2}.
STRAND 844 846 {ECO:0000244|PDB:1MU2}.
STRAND 848 853 {ECO:0000244|PDB:1MU2}.
STRAND 854 856 {ECO:0000244|PDB:1MU2}.
HELIX 866 882 {ECO:0000244|PDB:1MU2}.
HELIX 889 892 {ECO:0000244|PDB:1MU2}.
STRAND 897 899 {ECO:0000244|PDB:1MU2}.
HELIX 909 922 {ECO:0000244|PDB:1MU2}.
STRAND 926 929 {ECO:0000244|PDB:1MU2}.
STRAND 938 943 {ECO:0000244|PDB:1MU2}.
STRAND 945 947 {ECO:0000244|PDB:1MU2}.
STRAND 949 955 {ECO:0000244|PDB:1MU2}.
STRAND 958 965 {ECO:0000244|PDB:1MU2}.
HELIX 975 994 {ECO:0000244|PDB:1MU2}.
STRAND 999 1004 {ECO:0000244|PDB:1MU2}.
HELIX 1006 1015 {ECO:0000244|PDB:1MU2}.
STRAND 1024 1027 {ECO:0000244|PDB:1MU2}.
HELIX 1032 1037 {ECO:0000244|PDB:1MU2}.
STRAND 1040 1043 {ECO:0000244|PDB:1MU2}.
STRAND 1049 1057 {ECO:0000244|PDB:1MU2}.
TURN 1059 1061 {ECO:0000244|PDB:1MU2}.
STRAND 1064 1070 {ECO:0000244|PDB:1MU2}.
STRAND 1075 1082 {ECO:0000244|PDB:1MU2}.
HELIX 1085 1098 {ECO:0000244|PDB:1MU2}.
STRAND 1102 1109 {ECO:0000244|PDB:1MU2}.
HELIX 1111 1118 {ECO:0000244|PDB:1MU2}.
STRAND 1122 1125 {ECO:0000244|PDB:1MU2}.
HELIX 1127 1138 {ECO:0000244|PDB:1MU2}.
STRAND 1140 1146 {ECO:0000244|PDB:1MU2}.
STRAND 1149 1151 {ECO:0000244|PDB:1MU2}.
HELIX 1156 1164 {ECO:0000244|PDB:1MU2}.
TURN 1173 1175 {ECO:0000244|PDB:1E0E}.
HELIX 1176 1186 {ECO:0000244|PDB:3F9K}.
HELIX 1190 1197 {ECO:0000244|PDB:3F9K}.
HELIX 1201 1209 {ECO:0000244|PDB:3F9K}.
TURN 1212 1216 {ECO:0000244|PDB:3F9K}.
STRAND 1231 1239 {ECO:0000244|PDB:3F9K}.
STRAND 1242 1249 {ECO:0000244|PDB:3F9K}.
TURN 1250 1252 {ECO:0000244|PDB:3F9K}.
STRAND 1255 1262 {ECO:0000244|PDB:3F9K}.
HELIX 1265 1276 {ECO:0000244|PDB:3F9K}.
STRAND 1282 1286 {ECO:0000244|PDB:3F9K}.
TURN 1290 1292 {ECO:0000244|PDB:3F9K}.
HELIX 1295 1304 {ECO:0000244|PDB:3F9K}.
STRAND 1307 1312 {ECO:0000244|PDB:3F9K}.
HELIX 1321 1335 {ECO:0000244|PDB:3F9K}.
HELIX 1337 1339 {ECO:0000244|PDB:3F9K}.
HELIX 1343 1356 {ECO:0000244|PDB:3F9K}.
TURN 1361 1364 {ECO:0000244|PDB:3F9K}.
HELIX 1367 1376 {ECO:0000244|PDB:3F9K}.
SEQUENCE 1464 AA; 164645 MW; A594A43F3E9ADB60 CRC64;
MGARNSVLRG KKADELERIR LRPGGKKKYR LKHIVWAANK LDRFGLAESL LESKEGCQKI
LTVLDPMVPT GSENLKSLFN TVCVIWCIHA EEKVKDTEGA KQIVRRHLVA ETGTAEKMPS
TSRPTAPSSE KGGNYPVQHV GGNYTHIPLS PRTLNAWVKL VEEKKFGAEV VPGFQALSEG
CTPYDINQML NCVGDHQAAM QIIREIINEE AAEWDVQHPI PGPLPAGQLR EPRGSDIAGT
TSTVEEQIQW MFRPQNPVPV GNIYRRWIQI GLQKCVRMYN PTNILDIKQG PKEPFQSYVD
RFYKSLRAEQ TDPAVKNWMT QTLLVQNANP DCKLVLKGLG MNPTLEEMLT ACQGVGGPGQ
KARLMAEALK EVIGPAPIPF AAAQQRKAFK CWNCGKEGHS ARQCRAPRRQ GCWKCGKPGH
IMTNCPDRQA GFLRTGPLGK EAPQLPRGPS SAGADTNSTP SGSSSGSTGE IYAAREKTER
AERETIQGSD RGLTAPRAGG DTIQGATNRG LAAPQFSLWK RPVVTAYIEG QPVEVLLDTG
ADDSIVAGIE LGNNYSPKIV GGIGGFINTK EYKNVEIEVL NKKVRATIMT GDTPINIFGR
NILTALGMSL NLPVAKVEPI KIMLKPGKDG PKLRQWPLTK EKIEALKEIC EKMEKEGQLE
EAPPTNPYNT PTFAIKKKDK NKWRMLIDFR ELNKVTQDFT EIQLGIPHPA GLAKKRRITV
LDVGDAYFSI PLHEDFRPYT AFTLPSVNNA EPGKRYIYKV LPQGWKGSPA IFQHTMRQVL
EPFRKANKDV IIIQYMDDIL IASDRTDLEH DRVVLQLKEL LNGLGFSTPD EKFQKDPPYH
WMGYELWPTK WKLQKIQLPQ KEIWTVNDIQ KLVGVLNWAA QLYPGIKTKH LCRLIRGKMT
LTEEVQWTEL AEAELEENRI ILSQEQEGHY YQEEKELEAT VQKDQENQWT YKIHQEEKIL
KVGKYAKVKN THTNGIRLLA QVVQKIGKEA LVIWGRIPKF HLPVEREIWE QWWDNYWQVT
WIPDWDFVST PPLVRLAFNL VGDPIPGAET FYTDGSCNRQ SKEGKAGYVT DRGKDKVKKL
EQTTNQQAEL EAFAMALTDS GPKVNIIVDS QYVMGISASQ PTESESKIVN QIIEEMIKKE
AIYVAWVPAH KGIGGNQEVD HLVSQGIRQV LFLEKIEPAQ EEHEKYHSNV KELSHKFGIP
NLVARQIVNS CAQCQQKGEA IHGQVNAELG TWQMDCTHLE GKIIIVAVHV ASGFIEAEVI
PQESGRQTAL FLLKLASRWP ITHLHTDNGA NFTSQEVKMV AWWIGIEQSF GVPYNPQSQG
VVEAMNHHLK NQISRIREQA NTIETIVLMA IHCMNFKRRG GIGDMTPSER LINMITTEQE
IQFLQAKNSK LKDFRVYFRE GRDQLWKGPG ELLWKGEGAV LVKVGTDIKI IPRRKAKIIR
DYGGRQEMDS GSHLEGARED GEMA


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PCR-505S SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10kunits
PCR-505S SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10000 units
SCH-OBT1906 RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 0.1 mg
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
SCH-OBT1906X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 1 mg
SCH-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
OBT1905X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicat 1 mg
OBT1906 RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 0.1 mg
OBT1906X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 1 mg
SCH-OBT1905X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicat 1 mg
PCR-501L M_MLV Reverse Transcriptase (RNase H_), L pack Reverse Transcriptase 50000units
PCR-501S M_MLV Reverse Transcriptase (RNase H_), S pack Reverse Transcriptase 10000units


 

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