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APTVMAVVNP + H2O
?
-
-
-
-
?
ATHQVYNphVRKA + H2O
hydrolyzed peptid
-
-
the cysteine residues in M-PMV protease form an intramolecular disulfide bridge and that increases the proteolytic activity significantly
-
?
ATPQVYF(NO2)VRKA + H2O
?
-
-
-
-
?
ATPQVYF(NO2)VRKA + H2O
ATPQVY + F(NO2)VRKA
-
-
-
-
?
CA-NC fusion protein + H2O
?
-
-
-
-
?
capsid protein + H2O
?
-
cleaved in vitro within the major homology region
-
-
?
capsid-nucleocapsid fusion protein + H2O
capsid protein + nucleocapsid protein
-
-
-
-
?
Gag-Pol polyprotein + H2O
?
GPEPPAVSLAMTDHK + H2O
GPEPPAVS + LAMTDHK
-
-
-
-
?
IMMCSPNDI + H2O
IMMCS + PNDI
-
-
-
-
?
IQVHYHRLEQ + H2O
IQVH + YHRLEQ
-
gp22-derived peptide, peptide derived from the cytoplasmic domain of transmembrane protein TM
-
-
?
NC protein + H2O
?
-
cleaved in several sites at the N-terminus
-
-
?
PKDIFPVTET + H2O
PKDIF + PVTET
PKQAYGAVFV + H2O
PKQAY + GAVFV
-
-
-
-
?
PKSIFPVTET + H2O
PKSIF + PVTET
-
-
-
-
?
QGTVSFNFPQITLVWOK + H2O
QGTVSFNF + PQITLVWOK
-
-
-
-
?
SSDIYWVQPI + H2O
SSDIY + WVQPI
-
-
-
-
?
TGPPVVAMPVVIKTEG + H2O
TGPPVVAM + PVVIKTEG
-
-
-
-
?
transmembrane glycoprotein + H2O
?
Val-Ser-Gln-Ala-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ala-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Asn-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Cys-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Cys-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Gly-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Gly-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Ile-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Ile-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Leu-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Leu-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Phe-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Phe-Tyr + Pro-Ile-Val-Gln
-
low activity
-
-
?
Val-Ser-Gln-Thr-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Thr-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
Val-Ser-Gln-Val-Tyr-Pro-Ile-Val-Gln + H2O
Val-Ser-Gln-Val-Tyr + Pro-Ile-Val-Gln
-
-
-
-
?
VFQNYPIVQ + H2O
VFQNY + PIVQ
-
large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VIQNYPIVQ + H2O
VIQNY + PIVQ
-
large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VLQNYPIVQ + H2O
VLQNY + PIVQ
-
large hydrophobic residues as Ile, Leu and Phe are preferred at position P4
-
-
?
VSFNYPIVQ + H2O
VSFNY + PIVQ
-
pronounced preference for the large hydrophobic residues Phe and Leu at position P3
-
-
?
VSLNYPIVQ + H2O
VSLNY + PIVQ
-
pronounced preference for the large hydrophobic residues Phe and Leu at position P3
-
-
?
VSQNFPIVQ + H2O
VSQNF + PIVQ
-
large aromatic residues (Phe and Tyr) are preferred at position P1
-
-
?
VSQNYPIVQ + H2O
VSQNY + PIVQ
-
large aromatic residues (Phe and Tyr) are preferred at position P1
-
-
?
additional information
?
-
Gag polyprotein + H2O
?
-
-
-
-
?
Gag polyprotein + H2O
?
-
processing of the precursor protein into mature proteins and the functional protease
-
-
?
Gag-Pol polyprotein + H2O
?
-
-
-
-
?
Gag-Pol polyprotein + H2O
?
-
processing of the precursor protein into mature proteins and the functional protease
-
-
?
PKDIFPVTET + H2O
PKDIF + PVTET
-
-
-
-
?
PKDIFPVTET + H2O
PKDIF + PVTET
-
a p12/CA cleavage site
-
-
?
transmembrane glycoprotein + H2O
?
-
-
-
-
?
transmembrane glycoprotein + H2O
?
-
cleavage site is in the cytoplasmic domain of the protein
-
-
?
transmembrane glycoprotein + H2O
?
-
cleavage site is in the cytoplasmic domain of the protein. Cleavage takes place as a postbudding event
-
-
?
additional information
?
-
-
peptide substrates spanning the processing sites within the M-PMV Gag, Gag-Pro and Env polyproteins
-
-
?
additional information
?
-
-
processing of Gag polyproteins leads to reorganization of immature retroviral particles and formation of a ribonucleoprotein core. Protease catalyzed cleavage is involved in core disintegration
-
-
?
additional information
?
-
-
the individual forms of M-PMV proteinase may be responsible for cleavage at different locations in the virion or at different stages of maturation
-
-
?
additional information
?
-
-
individual forms of M-PMV proteinase may be responsible for cleavage at different parts of the budding virion, or at different stages of maturation
-
-
?
additional information
?
-
-
the enzyme is released by the autocatalytic cleavage of Gag-Pro and Gag-Pro-POl polypeptide precursors. The enzyme catalyzes the processing of viral precursors to yield the structural proteins and enzymes of the virion
-
-
?
additional information
?
-
-
the enzyme cleaves 17 amino acids of the C-terminal 38-amino-acid cytoplasmic tail of the transmembrane protein TM of the released immature virus, analysis of the cleavage site recognition and specificity for individual amino acids, this processing mediates the fusion with the envelope glycoprotein Env
-
-
?
additional information
?
-
-
the enzyme is involved in core disintegration cleaving the capsid protein within the major homology region, the enzyme also converts the cell-associated transmembrane protein to a virus-associated gp20
-
-
?
additional information
?
-
-
the enzyme is involved in incorporation of the viral glycoprotein Env during virus assembly, the enzyme also converts the cell-associated transmembrane protein TM to a virus-associated gp20, effect of mutation in the cytoplasmic domain of TM, overview
-
-
?
additional information
?
-
-
cleavage site specificity, overview
-
-
?
additional information
?
-
-
study of influence of the P2 position residue on cleavage site specificity of isozyme p12, overview
-
-
?
vimetin + H2O
additional information
-
-
the 12000 Da enzyme form detectably cleaves vimetin only after 10 h
major cleavage product of 48000 Da
?
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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
Mason-Pfizer monkey virus (P07570)
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Rumlova, M.; Ruml, T.; Pohl, J.; Pichova, I.
Specific in vitro cleavage of Mason-Pfizer monkey virus capsid protein: evidence for a potential role of retroviral protease in early stages of infection
Virology
310
310-318
2003
Mason-Pfizer monkey virus
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Snasel, J.; Shoeman, R.; Horejsi, M.; Hruskova-Heidingsfeldova, O.; Sedlacek, J.; Ruml, T.; Pichova, I.
Cleavage of vimentin by different retroviral proteases
Arch. Biochem. Biophys.
377
241-245
2000
Mason-Pfizer monkey virus
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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
Mason-Pfizer monkey virus
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Hruskova-Heidingsfeldova, O.; Andreansky, M.; Fabry, M.; Blaha, I.; Strop, P.; Hunter, E.
Cloning, bacterial expression, and characterization of the Mason-Pfizer monkey virus proteinase
J. Biol. Chem.
270
15053-15058
1995
Mason-Pfizer monkey virus
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Brody, B.A.; Rhee, S.S.; Sommerfelt, M.A.; Hunter, E.
A viral protease-mediated cleavage of the transmembrane glycoprotein of Mason-Pfizer monkey virus can be suppressed by mutations within the matrix protein
Proc. Natl. Acad. Sci. USA
89
3443-3447
1992
Mason-Pfizer monkey virus
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Sommerfelt, M.A.; Petteway, S.R., Jr.; Dreyer, G.B.; Hunter, E.
Effect of retroviral proteinase inhibitors on Mason-Pfizer monkey virus maturation and transmembrane glycoprotein cleavage
J. Virol.
66
4220-4227
1992
Mason-Pfizer monkey virus
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Parker, S.D.; Hunter, E.
Activation of the Mason-Pfizer monkey virus protease within immature capsids in vitro
Proc. Natl. Acad. Sci. USA
98
14631-14636
2001
Mason-Pfizer monkey virus
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Pichova, I.; Zabransky, A.; Kost'alova, I.; Hruskova-Heidingsfeldova, O.; Andreansky, M.; Hunter, E.; Ruml, T.
Analysis of autoprocessing of Mason-Pfizer monkey virus proteinase in vitro. Three active forms of proteinase
Adv. Exp. Med. Biol.
436
105-108
1998
Mason-Pfizer monkey virus
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Bagossi, P.; Sperka, T.; Feher, A.; Kadas, J.; Zahuczky, G.; Miklossy, G.; Boross, P.; Toezser, J.
Amino acid preferences for a critical substrate binding subsite of retroviral proteases in type 1 cleavage sites
J. Virol.
79
4213-4218
2005
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Pichova, I.
Mason-Pfizer monkey virus retropepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
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2004
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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
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Amino acid residues in the cytoplasmic domain of the Mason-Pfizer monkey virus glycoprotein critical for its incorporation into virions
J. Virol.
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2005
Mason-Pfizer monkey virus
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Activity of the Mason-Pfizer monkey virus fusion protein is modulated by single amino acids in the cytoplasmic tail
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The role of the S-S bridge in retroviral protease function and virion maturation
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Three-dimensional structure of a monomeric form of a retroviral protease
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333
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Amino acid preferences of retroviral proteases for amino-terminal positions in a type 1 cleavage site
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NMR structure of the N-terminal domain of capsid protein from the Mason-Pfizer monkey virus
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Feline immunodeficiency virus evolutionarily acquires two proteins, Vif and protease, capable of antagonizing feline APOBEC3
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