Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Gag-Pro-Pol polyprotein (Pr180) [Cleaved into: Matrix protein p10; Phosphorylated protein pp24; Phosphorylated protein pp18; p12; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease 17 kDa (EC 3.4.23.-); Protease 13 kDa (EC 3.4.23.-); G-patch peptide; 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_MPMV                Reviewed;        1771 AA.
P07572; O56224;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
28-FEB-2018, sequence version 2.
20-JUN-2018, entry version 108.
RecName: Full=Gag-Pro-Pol polyprotein;
AltName: Full=Pr180;
Contains:
RecName: Full=Matrix protein p10;
Contains:
RecName: Full=Phosphorylated protein pp24;
Contains:
RecName: Full=Phosphorylated protein pp18;
Contains:
RecName: Full=p12;
Contains:
RecName: Full=Capsid protein p27;
Contains:
RecName: Full=Nucleocapsid protein-dUTPase;
Short=NC-dUTPase;
EC=3.6.1.23 {ECO:0000250|UniProtKB:P07570};
Contains:
RecName: Full=Protease 17 kDa {ECO:0000303|PubMed:16257973};
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364};
Contains:
RecName: Full=Protease 13 kDa {ECO:0000303|PubMed:16257973};
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275, ECO:0000269|PubMed:9636364};
Contains:
RecName: Full=G-patch peptide {ECO:0000303|PubMed:22171253};
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
EC=2.7.7.7 {ECO:0000255|PROSITE-ProRule:PRU00405};
EC=3.1.26.4 {ECO:0000255|PROSITE-ProRule:PRU00408};
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P11283};
EC=3.1.-.- {ECO:0000250|UniProtKB:P11283};
Name=gag-pro-pol;
Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Betaretrovirus.
NCBI_TaxID=11855;
NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RIBOSOMAL FRAMESHIFT.
STRAIN=Clone 6A;
PubMed=2421920; DOI=10.1016/0092-8674(86)90323-5;
Sonigo P., Barker C., Hunter E., Wain-Hobson S.;
"Nucleotide sequence of Mason-Pfizer monkey virus: an
immunosuppressive D-type retrovirus.";
Cell 45:375-385(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Chappey C.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEOLYTIC CLEAVAGE (PROTEASE 17 KDA), CATALYTIC ACTIVITY (PROTEASE
17 KDA), FUNCTION (PROTEASE 17 KDA), PROTEOLYTIC CLEAVAGE (GAG-PRO
POLYPROTEIN), SUBCELLULAR LOCATION (PROTEASE 17 KDA), SUBCELLULAR
LOCATION (PROTEASE 13 KDA), CATALYTIC ACTIVITY (PROTEASE 13 KDA), AND
FUNCTION (PROTEASE 13 KDA).
PubMed=9636364; DOI=10.1006/viro.1998.9173;
Zabransky A., Andreansky M., Hruskova-Heidingsfeldova O., Havlicek V.,
Hunter E., Ruml T., Pichova I.;
"Three active forms of aspartic proteinase from Mason-Pfizer monkey
virus.";
Virology 245:250-256(1998).
[4]
DOMAIN (GAG-PRO-POL POLYPROTEIN), AND MUTAGENESIS OF 203-PRO--TYR-205
AND 210-PRO--PRO-211.
PubMed=12915562;
Gottwein E., Bodem J., Mueller B., Schmechel A., Zentgraf H.,
Kraeusslich H.G.;
"The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to
virus release.";
J. Virol. 77:9474-9485(2003).
[5]
PROTEOLYTIC CLEAVAGE (PROTEASE 17 KDA), DOMAIN (PROTEASE 17 KDA), AND
MUTAGENESIS OF ASN-868; ALA-873; GLN-874 AND TYR-880.
PubMed=16257973; DOI=10.1074/jbc.M508031200;
Bauerova-Zabranska H., Stokrova J., Strisovsky K., Hunter E., Ruml T.,
Pichova I.;
"The RNA binding G-patch domain in retroviral protease is important
for infectivity and D-type morphogenesis of Mason-Pfizer monkey
virus.";
J. Biol. Chem. 280:42106-42112(2005).
[6]
DOMAIN (PROTEASE 17 KDA), CATALYTIC ACTIVITY (REVERSE
TRANSCRIPTASE/RIBONUCLEASE H), MUTAGENESIS OF GLY-879; TYR-880;
GLY-883; GLY-885; LEU-886; GLY-887; GLY-892 AND GLY-907, FUNCTION
(G-PATCH PEPTIDE), INTERACTION WITH THE REVERSE
TRANSCRIPTASE/RIBONUCLEASE H (G-PATCH PEPTIDE), AND INTERACTION WITH
THE G-PATCH PEPTIDE (REVERSE TRANSCRIPTASE/RIBONUCLEASE H).
PubMed=22171253; DOI=10.1128/JVI.06638-11;
Krizova I., Hadravova R., Stokrova J., Guenterova J., Dolezal M.,
Ruml T., Rumlova M., Pichova I.;
"The G-patch domain of Mason-Pfizer monkey virus is a part of reverse
transcriptase.";
J. Virol. 86:1988-1998(2012).
[7]
RIBOSOMAL FRAMESHIFT.
PubMed=24298557; DOI=10.1155/2013/984028;
Huang X., Cheng Q., Du Z.;
"A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
ribosomal frameshifting or readthrough in animal viruses.";
Biomed. Res. Int. 2013:984028-984028(2013).
[8]
REVIEW (INTEGRASE).
PubMed=28458055; DOI=10.1016/j.sbi.2017.04.005;
Engelman A.N., Cherepanov P.;
"Retroviral intasomes arising.";
Curr. Opin. Struct. Biol. 47:23-29(2017).
-!- FUNCTION: Matrix protein p10: Matrix protein. {ECO:0000305}.
-!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
{ECO:0000305}.
-!- FUNCTION: Capsid protein p27: Capsid protein. {ECO:0000305}.
-!- FUNCTION: Protease 17 kDa: The aspartyl protease 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. {ECO:0000255|PROSITE-ProRule:PRU00275,
ECO:0000269|PubMed:9636364}.
-!- FUNCTION: Protease 13 kDa: The aspartyl protease 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. {ECO:0000255|PROSITE-ProRule:PRU00275,
ECO:0000269|PubMed:9636364}.
-!- FUNCTION: G-patch peptide: Enhances the activity of the reverse
transcriptase. May be part of the mature RT.
{ECO:0000269|PubMed:22171253}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H: RT is a
multifunctional enzyme that converts the viral dimeric 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 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 perfom 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 perfom 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
primers. 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.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- FUNCTION: Integrase: Catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. {ECO:0000305|PubMed:28458055}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405,
ECO:0000269|PubMed:22171253}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|PROSITE-ProRule:PRU00408}.
-!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
{ECO:0000250|UniProtKB:P07570}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
Note=The RT polymerase active site binds 2 magnesium ions.
{ECO:0000255|PROSITE-ProRule:PRU00405};
-!- SUBUNIT: Protease 17 kDa: Homodimer (By similarity). Reverse
transcriptase/ribonuclease H: Interacts with the G-patch peptide
(PubMed:22171253). G-patch peptide: Interacts with the reverse
transcriptase/ribonuclease H (PubMed:22171253). Nucleocapsid
protein-dUTPase: Homotrimer (By similarity).
{ECO:0000250|UniProtKB:P07570, ECO:0000269|PubMed:22171253}.
-!- SUBCELLULAR LOCATION: Matrix protein p10: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p27: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein-dUTPase: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protease 13 kDa: Virion
{ECO:0000269|PubMed:9636364}.
-!- SUBCELLULAR LOCATION: Protease 17 kDa: Virion
{ECO:0000269|PubMed:9636364}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Gag-Pro-Pol polyprotein;
IsoId=P07572-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshiftings between gag-pro and
pro-pol. {ECO:0000305|PubMed:2421920,
ECO:0000305|PubMed:24298557};
Name=Gag polyprotein;
IsoId=P07567-1; Sequence=External;
Note=Produced by conventional translation.
{ECO:0000305|PubMed:2421920, ECO:0000305|PubMed:24298557};
Name=Gag-Pro polyprotein;
IsoId=P07570-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting between gag-pro.
{ECO:0000305|PubMed:2421920, ECO:0000305|PubMed:24298557};
-!- DOMAIN: Gag-Pro-Pol polyprotein: 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. Phosphorylated protein pp24 and
phosphorylated protein pp18 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 the ubiquitin ligase NEDD4.
Both motifs contribute to viral release. The PSAP motif acts as an
additional L domain and promotes the efficient release of the
virions but requires an intact PPPY motif to perform its function.
{ECO:0000269|PubMed:12915562}.
-!- DOMAIN: Protease 17 kDa: The glycine-rich G-patch domain (GPD) is
present at the C-terminus of the protease from which it is then
detached by the protease itself. {ECO:0000269|PubMed:16257973,
ECO:0000269|PubMed:22171253}.
-!- PTM: Protease 17 kDa: Released by autocatalytic processing. The
protease can undergo further autoprocessing to yield 2 shorter but
enzymatically active forms of 12 kDa and 13 kDa.
{ECO:0000269|PubMed:16257973, ECO:0000269|PubMed:9636364}.
-!- PTM: Gag-Pro-Pol polyprotein: Myristoylated. Myristoylation of the
matrix (MA) domain mediates the transport and binding of Gag
polyproteins to the host plasma membrane and is required for the
assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.
-!- PTM: Gag-Pro-Pol polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. {ECO:0000269|PubMed:9636364}.
-!- 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 swiching 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:0000255|PROSITE-
ProRule:PRU00405}.
-!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA47711.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M12349; AAA47711.1; ALT_SEQ; Genomic_RNA.
EMBL; AF033815; AAC82576.1; -; Genomic_RNA.
PIR; C25839; GNLJMP.
RefSeq; NP_056891.1; NC_001550.1. [P07572-1]
ProteinModelPortal; P07572; -.
GeneID; 2746973; -.
KEGG; vg:2746973; -.
OrthoDB; VOG09000135; -.
Proteomes; UP000008870; Genome.
Proteomes; UP000105838; 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-KW.
GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
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:UniProtKB-EC.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
CDD; cd05482; HIV_retropepsin_like; 1.
CDD; cd07557; trimeric_dUTPase; 1.
Gene3D; 1.10.10.200; -; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.150.490; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.30.30.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 2.70.40.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR003322; B_retro_matrix.
InterPro; IPR038124; B_retro_matrix_sf.
InterPro; IPR029054; dUTPase-like.
InterPro; IPR036157; dUTPase-like_sf.
InterPro; IPR033704; dUTPase_trimeric.
InterPro; IPR000467; G_patch_dom.
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; 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; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00692; dUTPase; 1.
Pfam; PF01585; G-patch; 1.
Pfam; PF02337; Gag_p10; 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.
ProDom; PD004265; B_retro_matrix_N; 1.
SMART; SM00443; G_patch; 1.
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; SSF51283; SSF51283; 1.
SUPFAM; SSF53098; SSF53098; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50174; G_PATCH; 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.
PROSITE; PS50876; ZF_INTEGRASE; 1.
1: Evidence at protein level;
Aspartyl protease; Coiled coil; Complete proteome; DNA integration;
DNA recombination; DNA-binding; DNA-directed DNA polymerase;
Endonuclease; Hydrolase; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
Protease; Repeat; Ribosomal frameshifting; RNA-binding;
RNA-directed DNA polymerase; Transferase; Viral genome integration;
Viral matrix protein; Viral nucleoprotein; Virion;
Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000305}.
CHAIN 2 1771 Gag-Pro-Pol polyprotein.
/FTId=PRO_0000125494.
CHAIN 2 100 Matrix protein p10.
/FTId=PRO_0000443138.
CHAIN 101 216 Phosphorylated protein pp24.
/FTId=PRO_0000443139.
PROPEP 101 161 {ECO:0000305}.
/FTId=PRO_0000443140.
CHAIN 162 216 Phosphorylated protein pp18.
/FTId=PRO_0000443141.
CHAIN 217 299 p12.
/FTId=PRO_0000443142.
CHAIN 300 525 Capsid protein p27.
/FTId=PRO_0000443143.
CHAIN 526 759 Nucleocapsid protein-dUTPase.
/FTId=PRO_0000443144.
CHAIN 760 911 Protease 17 kDa.
/FTId=PRO_0000443145.
CHAIN 760 873 Protease 13 kDa.
/FTId=PRO_0000443146.
PEPTIDE 874 911 G-patch peptide.
/FTId=PRO_0000443147.
CHAIN 912 1496 Reverse transcriptase/ribonuclease H.
/FTId=PRO_0000434773.
CHAIN 1497 1771 Integrase.
/FTId=PRO_0000434774.
DOMAIN 780 856 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 867 913 G-patch. {ECO:0000255|PROSITE-
ProRule:PRU00092,
ECO:0000269|PubMed:22171253}.
DOMAIN 959 1147 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1361 1492 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1550 1719 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 547 564 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 576 593 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1496 1537 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00450}.
DNA_BIND 1716 1765 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
COILED 216 257 {ECO:0000255}.
MOTIF 202 205 PPXY motif.
{ECO:0000269|PubMed:12915562}.
MOTIF 210 213 PTAP/PSAP motif.
{ECO:0000269|PubMed:12915562}.
MOTIF 335 338 PTAP/PSAP motif.
{ECO:0000250|UniProtKB:P03365}.
ACT_SITE 785 785 Protease; shared with dimeric partner.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
METAL 1024 1024 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1099 1099 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1100 1100 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1370 1370 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1399 1399 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1420 1420 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1484 1484 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1561 1561 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
METAL 1618 1618 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
METAL 1654 1654 Magnesium; catalytic; for integrase
activity. {ECO:0000250|UniProtKB:P03354}.
SITE 100 101 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 161 162 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 216 217 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 299 300 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 525 526 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 759 760 Cleavage; by viral protease.
{ECO:0000269|PubMed:9636364}.
SITE 873 874 Cleavage; by viral protease.
{ECO:0000269|PubMed:16257973}.
SITE 911 912 Cleavage; by viral protease.
{ECO:0000269|PubMed:9636364}.
SITE 1496 1497 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03365}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250|UniProtKB:P11283}.
MUTAGEN 203 205 PPY->GAA: 80% loss of virus release.
{ECO:0000269|PubMed:12915562}.
MUTAGEN 210 211 PS->AG: 30% loss of virus release.
{ECO:0000269|PubMed:12915562}.
MUTAGEN 868 868 N->I: Accelerated processing of the
protease C-terminus.
{ECO:0000269|PubMed:16257973}.
MUTAGEN 873 873 A->R: 30% loss of infectivity.
{ECO:0000269|PubMed:16257973}.
MUTAGEN 874 874 Q->I: Accelerated processing of the
protease C-terminus. 50% loss of RT
activity. {ECO:0000269|PubMed:16257973}.
MUTAGEN 879 879 G->A: 85% loss of infectivity and 65%
loss of RT activity.
{ECO:0000269|PubMed:22171253}.
MUTAGEN 880 880 Y->A: 90% loss of infectivity and 65%
loss of RT activity.
{ECO:0000269|PubMed:22171253}.
MUTAGEN 880 880 Y->S: Defective in nucleic acid binding.
80% loss of infectivity. 50% loss of RT
activity. {ECO:0000269|PubMed:16257973}.
MUTAGEN 883 883 G->A: 90% loss of infectivity and 55%
loss of RT activity.
{ECO:0000269|PubMed:22171253}.
MUTAGEN 885 885 G->A: 70% loss of infectivity and 60%
loss of RT activity.
{ECO:0000269|PubMed:22171253}.
MUTAGEN 886 886 L->A: 85% loss of infectivity and 60%
loss of RT activity.
{ECO:0000269|PubMed:22171253}.
MUTAGEN 887 887 G->A: 95% loss of infectivity and 95%
loss of RT activity.
{ECO:0000269|PubMed:22171253}.
MUTAGEN 892 892 G->A: 85% loss of infectivity and 60%
loss of RT activity.
{ECO:0000269|PubMed:22171253}.
MUTAGEN 907 907 G->A: 60% loss of infectivity and 35%
loss of RT activity.
{ECO:0000269|PubMed:22171253}.
SEQUENCE 1771 AA; 198014 MW; BE8BEAB195B4E833 CRC64;
MGQELSQHER YVEQLKQALK TRGVKVKYAD LLKFFDFVKD TCPWFPQEGT IDIKRWRRVG
DCFQDYYNTF GPEKVPVTAF SYWNLIKELI DKKEVNPQVM AAVAQTEEIL KSNSQTDLTK
TSQNPDLDLI SLDSDDEGAK SSSLQDKGLS STKKPKRFPV LLTAQTSKDP EDPNPSEVDW
DGLEDEAAKY HNPDWPPFLT RPPPYNKATP SAPTVMAVVN PKEELKEKIA QLEEQIKLEE
LHQALISKLQ KLKTGNETVT HPDTAGGLSR TPHWPGQHIP KGKCCASREK EEQIPKDIFP
VTETVDGQGQ AWRHHNGFDF AVIKELKTAA SQYGATAPYT LAIVESVADN WLTPTDWNTL
VRAVLSGGDH LLWKSEFFEN CRDTAKRNQQ AGNGWDFDML TGSGNYSSTD AQMQYDPGLF
AQIQAAATKA WRKLPVKGDP GASLTGVKQG PDEPFADFVH RLITTAGRIF GSAEAGVDYV
KQLAYENANP ACQAAIRPYR KKTDLTGYIR LCSDIGPSYQ QGLAMAAAFS GQTVKDFLNN
KNKEKGGCCF KCGKKGHFAK NCHEHAHNNA EPKVPGLCPR CKRGKHWANE CKSKTDNQGN
PIPPHQGNRV EGPAPGPETS LWGSQLCSSQ QKQPISKLTR ATPGSAGLDL CSTSHTVLTP
EMGPQALSTG IYGPLPPNTF GLILGRSSIT MKGLQVYPGV IDNDYTGEIK IMAKAVNNIV
TVSQGNRIAQ LILLPLIETD NKVQQPYRGQ GSFGSSDIYW VQPITCQKPS LTLWLDDKMF
TGLIDTGADV TIIKLEDWPP NWPITDTLTN LRGIGQSNNP KQSSKYLTWR DKENNSGLIK
PFVIPNLPVN LWGRDLLSQM KIMMCSPNDI VTAQMLAQGY SPGKGLGKKE NGILHPIPNQ
GQSNKKGFGN FLTAAIDILA PQQCAEPITW KSDEPVWVDQ WPLTNDKLAA AQQLVQEQLE
AGHITESSSP WNTPIFVIKK KSGKWRLLQD LRAVNATMVL MGALQPGLPS PVAIPQGYLK
IIIDLKDCFF SIPLHPSDQK RFAFSLPSTN FKEPMQRFQW KVLPQGMANS PTLCQKYVAT
AIHKVRHAWK QMYIIHYMDD ILIAGKDGQQ VLQCFDQLKQ ELTAAGLHIA PEKVQLQDPY
TYLGFELNGP KITNQKAVIR KDKLQTLNDF QKLLGDINWL RPYLKLTTGD LKPLFDTLKG
DSDPNSHRSL SKEALASLEK VETAIAEQFV THINYSLPLI FLIFNTALTP TGLFWQDNPI
MWIHLPASPK KVLLPYYDAI ADLIILGRDH SKKYFGIEPS TIIQPYSKSQ IDWLMQNTEM
WPIACASFVG ILDNHYPPNK LIQFCKLHTF VFPQIISKTP LNNALLVFTD GSSTGMAAYT
LTDTTIKFQT NLNSAQLVEL QALIAVLSAF PNQPLNIYTD SAYLAHSIPL LETVAQIKHI
SETAKLFLQC QQLIYNRSIP FYIGHVRAHS GLPGPIAQGN QRADLATKIV ASNINTNLES
AQNAHTLHHL NAQTLRLMFN IPREQARQIV KQCPICVTYL PVPHLGVNPR GLFPNMIWQM
DVTHYSEFGN LKYIHVSIDT FSGFLLATLQ TGETTKHVIT HLLHCFSIIG LPKQIKTDNG
PGYTSKNFQE FCSTLQIKHI TGIPYNPQGQ GIVERAHLSL KTTIEKIKKG EWYPRKGTPR
NILNHALFIL NFLNLDDQNK SAADRFWHNN PKKQFAMVKW KDPLDNTWHG PDPVLIWGRG
SVCVYSQTYD AARWLPERLV RQVSNNNQSR E


Related products :

Catalog number Product name Quantity
orb90082 Thermostable dUTPase protein Thermostable dUTPase (pyrococcus fruriosus) maximizes the efficiency of high-fidelity PCR (using proofreading DNA polymerases). It removes contaminating dUTP present in PC 500 IU
orb90001 GST_HRV Protease Protease Recombinant is fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes subset of sequences whic 100 IU
orb90006 Tobacco Etch Virus Protease protein Recombinant TEV Protease (rTEV) is site-specific protease purified from E.coli The protease can be used for the removal of affinity tags from fusion proteins. The s 300 IU
orb71879 Phosphorylated Protein Kinase C Substrate 1 peptide This is Phosphorylated Protein Kinase C Substrate 1 peptide. For research use only. 1 mg
orb71880 Phosphorylated Protein Kinase C Substrate 2 peptide This is Phosphorylated Protein Kinase C Substrate 2 peptide. For research use only. 1 mg
CSB-E17273r Rat phosphorylated gap junction protein, alpha 1, 43kDa (phosphorylated GJA1)ELISA kit, Species Rat, Sample Type serum, plasma 96T
31-169 Myb-Related Protein B (MYBL2), a member of the MYB family of transcription factor genes, is a nuclear protein involved in cell cycle progression. The encoded protein is phosphorylated by cyclin A_cycl 0.05 mg
orb82817 PreScission Protease enzyme PreScission Protease is a fusion protein of Glutathione S-Transferase (GST) and Human Rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of 1000 U
29-694 SEMG1 is the predominant protein in semen. The secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes 0.1 mg
29-695 SEMG1 is the predominant protein in semen. The secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes 0.1 mg
EIAAB29697 C2orf7,Homo sapiens,hPAP21,Human,PAP21,PRADC1,Protease-associated domain-containing protein 1,Protease-associated domain-containing protein of 21 kDa,UNQ833_PRO1760
EIAAB06612 Carnitine deficiency-associated protein 3,Cdv3,Mouse,Mus musculus,Protein CDV3,TPP36,Tyrosine-phosphorylated protein 36
EIAAB32649 Complement factor D-like protein,Df2,Prss57,Prssl1,Rat,Rattus norvegicus,Serine protease 1-like protein 1,Serine protease 57
29-386 KHDRBS1 recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, KHDRBS1 functions as an adapter protein in signal 0.05 mg
EIAAB29696 Mouse,Mus musculus,Pap21,Pradc1,Protease-associated domain-containing protein 1,Protease-associated domain-containing protein of 21 kDa
18-661-15141 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-001-30061 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-003-42864 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.05 mg Aff Pur
orb90082 Thermostable dUTPase protein Enzymes 500 IU
U0800m CLIA IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,Mouse,Mus musculus,Pappa,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
E0800m ELISA IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,Mouse,Mus musculus,Pappa,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
18-785-210006 4E-BP1 (Ab-45) - 4E-BP1; eIF4E-binding protein 1; Phosphorylated heat- and acid-stable protein regulated by insulin 1; PHAS-I Polyclonal 0.1 mg
18-785-210006 4E-BP1 (Ab-45) - 4E-BP1; eIF4E-binding protein 1; Phosphorylated heat- and acid-stable protein regulated by insulin 1; PHAS-I Polyclonal 0.05 mg
18-785-210005 4E-BP1 (Ab-36) - 4E-BP1; eIF4E-binding protein 1; Phosphorylated heat- and acid-stable protein regulated by insulin 1; PHAS-I Polyclonal 0.1 mg
18-785-210005 4E-BP1 (Ab-36) - 4E-BP1; eIF4E-binding protein 1; Phosphorylated heat- and acid-stable protein regulated by insulin 1; PHAS-I Polyclonal 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur