UniProt functional annotation for P07572



	UniProt functional annotation for P07572

UniProt code: P07572.

Organism: Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).

Taxonomy: Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.

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: 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, ECO:0000269|PubMed:22171253};

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, ECO:0000269|PubMed:22171253};

Catalytic activity: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};

Catalytic activity: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={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). {ECO:0000250|UniProtKB:P07570}.

Subunit: [Reverse transcriptase/ribonuclease H]: Interacts with the G- patch peptide (PubMed:22171253). {ECO:0000269|PubMed:22171253}.

Subunit: [G-patch peptide]: Interacts with the reverse transcriptase/ribonuclease H (PubMed:22171253). {ECO:0000269|PubMed:22171253}.

Subunit: [Nucleocapsid protein-dUTPase]: Homotrimer (By similarity). {ECO:0000250|UniProtKB:P07570}.

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}.

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}.

Miscellaneous: [Isoform Gag-Pro-Pol polyprotein]: Produced by -1 ribosomal frameshiftings between gag-pro and pro-pol. {ECO:0000305|PubMed:2421920, ECO:0000305|PubMed:24298557}.

Similarity: Belongs to the retroviral Pol polyprotein family. {ECO:0000305}.

Sequence caution: Sequence=AAA47711.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus).
Taxonomy:		Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Betaretrovirus.



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:		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, ECO:0000269\|PubMed:22171253};
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, ECO:0000269\|PubMed:22171253};
Catalytic activity:		Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255\|PROSITE-ProRule:PRU00408};
Catalytic activity:		Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={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). {ECO:0000250\|UniProtKB:P07570}.
Subunit:		[Reverse transcriptase/ribonuclease H]: Interacts with the G- patch peptide (PubMed:22171253). {ECO:0000269\|PubMed:22171253}.
Subunit:		[G-patch peptide]: Interacts with the reverse transcriptase/ribonuclease H (PubMed:22171253). {ECO:0000269\|PubMed:22171253}.
Subunit:		[Nucleocapsid protein-dUTPase]: Homotrimer (By similarity). {ECO:0000250\|UniProtKB:P07570}.
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}.
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}.
Miscellaneous:		[Isoform Gag-Pro-Pol polyprotein]: Produced by -1 ribosomal frameshiftings between gag-pro and pro-pol. {ECO:0000305\|PubMed:2421920, ECO:0000305\|PubMed:24298557}.
Similarity:		Belongs to the retroviral Pol polyprotein family. {ECO:0000305}.
Sequence caution:		Sequence=AAA47711.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};