UniProt functional annotation for O92956



	UniProt functional annotation for O92956

UniProt code: O92956.

Organism: Rous sarcoma virus (strain Schmidt-Ruppin B) (RSV-SRB).

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

Function: Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. {ECO:0000250|UniProtKB:P03322}.

Function: Spacer peptide: Plays a role in the oligomerization of the Gag polyprotein and in the stabilization of the immature particle. Essential layering element during tube assembly. {ECO:0000250|UniProtKB:P03322}.

Function: [Nucleocapsid protein p12]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.

Function: [Protease p15]: 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}.

Function: [Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions (PubMed:9218451). This recombination event is an essential step in the viral replication cycle. Has a strong preference for using the 3'-OH at the viral DNA end as a nucleophile. {ECO:0000250|UniProtKB:P03354, ECO:0000269|PubMed:9218451}.

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};

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

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405};

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|UniProtKB:P03354}; Note=Binds 8 Mg(2+) ions per integrase homotetramer. {ECO:0000250};

Subunit: [Protease p15]: Active as a homodimer. {ECO:0000250|UniProtKB:P03322}.

Subunit: [Integrase]: Homodimer; further associates as a homooctamer. {ECO:0000250|UniProtKB:P03322, ECO:0000303|PubMed:28458055, ECO:0000303|PubMed:9218451}.

Subunit: [Reverse transcriptase beta-subunit]: Heterodimer of alpha and beta subunits. Three forms of RT exist: alpha-alpha (alpha-Pol), beta- beta (beta-Pol), and alpha-beta, with the major form being the heterodimer. Both the polymerase and RNase H active sites are located in the alpha subunit of heterodimeric RT alpha-beta. {ECO:0000250|UniProtKB:P03354}.

Subunit: [Reverse transcriptase alpha-subunit]: Heterodimer of alpha and beta subunits. Three forms of RT exist: alpha-alpha (alpha-Pol), beta-beta (beta-Pol), and alpha-beta, with the major form being the heterodimer. Both the polymerase and RNase H active sites are located in the alpha subunit of heterodimeric RT alpha-beta. {ECO:0000250|UniProtKB:P03354}.

Subcellular location: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03354}.

Subcellular location: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000250|UniProtKB:P03354}.

Subcellular location: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000250|UniProtKB:P03354}.

Subcellular location: [Nucleocapsid protein p12]: Virion {ECO:0000250|UniProtKB:P03354}.

Domain: [Gag-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. P2B contains two L domain: a PPXY motif which probably binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases and a LYPX(n)L domain which is known to bind the Alix adaptator protein. {ECO:0000250|UniProtKB:P03354}.

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 (By similarity). {ECO:0000250}.

Domain: [Gag-Pol polyprotein]: contains a nuclear export signal in p10 and a nucleolar localization signal in nucleocapsid protein p12. {ECO:0000250|UniProtKB:P03322}.

Domain: Capsid protein p27: Proton-driven dimerization of the C- terminus facilitates capsid assembly. {ECO:0000250|UniProtKB:P03322}.

Ptm: [Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000250|UniProtKB:P03354}.

Ptm: Capsid protein p27: The cleavage at the C-terminus is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 amino acids in a ratio of 2:1. {ECO:0000250|UniProtKB:P03322}.

Miscellaneous: Reverse transcriptase: 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:0000255|PROSITE-ProRule:PRU00405}.

Miscellaneous: [Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal frameshifting.

Sequence caution: Sequence=AAC08988.1; Type=Erroneous initiation; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Rous sarcoma virus (strain Schmidt-Ruppin B) (RSV-SRB).
Taxonomy:		Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus.



Function:		Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. {ECO:0000250\|UniProtKB:P03322}.



Function:		Spacer peptide: Plays a role in the oligomerization of the Gag polyprotein and in the stabilization of the immature particle. Essential layering element during tube assembly. {ECO:0000250\|UniProtKB:P03322}.



Function:		[Nucleocapsid protein p12]: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.



Function:		[Protease p15]: 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}.



Function:		[Integrase]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions (PubMed:9218451). This recombination event is an essential step in the viral replication cycle. Has a strong preference for using the 3'-OH at the viral DNA end as a nucleophile. {ECO:0000250\|UniProtKB:P03354, ECO:0000269\|PubMed:9218451}.


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};
Catalytic activity:		Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255\|PROSITE-ProRule:PRU00408};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255\|PROSITE-ProRule:PRU00405};
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\|UniProtKB:P03354}; Note=Binds 8 Mg(2+) ions per integrase homotetramer. {ECO:0000250};
Subunit:		[Protease p15]: Active as a homodimer. {ECO:0000250\|UniProtKB:P03322}.
Subunit:		[Integrase]: Homodimer; further associates as a homooctamer. {ECO:0000250\|UniProtKB:P03322, ECO:0000303\|PubMed:28458055, ECO:0000303\|PubMed:9218451}.
Subunit:		[Reverse transcriptase beta-subunit]: Heterodimer of alpha and beta subunits. Three forms of RT exist: alpha-alpha (alpha-Pol), beta- beta (beta-Pol), and alpha-beta, with the major form being the heterodimer. Both the polymerase and RNase H active sites are located in the alpha subunit of heterodimeric RT alpha-beta. {ECO:0000250\|UniProtKB:P03354}.
Subunit:		[Reverse transcriptase alpha-subunit]: Heterodimer of alpha and beta subunits. Three forms of RT exist: alpha-alpha (alpha-Pol), beta-beta (beta-Pol), and alpha-beta, with the major form being the heterodimer. Both the polymerase and RNase H active sites are located in the alpha subunit of heterodimeric RT alpha-beta. {ECO:0000250\|UniProtKB:P03354}.
Subcellular location:		[Matrix protein p19]: Virion {ECO:0000250\|UniProtKB:P03354}.
Subcellular location:		[Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000250\|UniProtKB:P03354}.
Subcellular location:		[Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000250\|UniProtKB:P03354}.
Subcellular location:		[Nucleocapsid protein p12]: Virion {ECO:0000250\|UniProtKB:P03354}.
Domain:		[Gag-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. P2B contains two L domain: a PPXY motif which probably binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases and a LYPX(n)L domain which is known to bind the Alix adaptator protein. {ECO:0000250\|UniProtKB:P03354}.
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 (By similarity). {ECO:0000250}.
Domain:		[Gag-Pol polyprotein]: contains a nuclear export signal in p10 and a nucleolar localization signal in nucleocapsid protein p12. {ECO:0000250\|UniProtKB:P03322}.
Domain:		Capsid protein p27: Proton-driven dimerization of the C- terminus facilitates capsid assembly. {ECO:0000250\|UniProtKB:P03322}.
Ptm:		[Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000250\|UniProtKB:P03354}.
Ptm:		Capsid protein p27: The cleavage at the C-terminus is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid protein C-terminally extended by 3 amino acids in a ratio of 2:1. {ECO:0000250\|UniProtKB:P03322}.
Miscellaneous:		Reverse transcriptase: 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:0000255\|PROSITE-ProRule:PRU00405}.
Miscellaneous:		[Isoform Gag-Pol polyprotein]: Produced by -1 ribosomal frameshifting.
Sequence caution:		Sequence=AAC08988.1; Type=Erroneous initiation; Evidence={ECO:0000305};