Q99315 · YG31B_YEAST
- ProteinTransposon Ty3-G Gag-Pol polyprotein
- GeneTY3B-G
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1547 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Capsid protein
Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the genomic RNA-nucleocapsid complex.
Nucleocapsid protein p11
Nucleocapsid protein p11 (NC) forms the nucleocore that coats the retro-elements dimeric RNA. Binds these RNAs through its zinc fingers (By similarity).
Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription
Promotes primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty3 RNA and initiation of reverse transcription
Ty3 protease
The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.
Reverse transcriptase/ribonuclease H
Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The 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 during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends.
Integrase p61
Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome.
Miscellaneous
Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty3 retrotransposons belong to the gypsy-like elements (metaviridae).
Catalytic activity
Reverse transcriptase/ribonuclease H
a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)Reverse transcriptase/ribonuclease H
a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)Reverse transcriptase/ribonuclease H
Endonucleolytic cleavage to 5'-phosphomonoester.
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 207-208 | Cleavage; by Ty3 protease | ||||
Sequence: GA | ||||||
Site | 233-234 | Cleavage; by Ty3 protease | ||||
Sequence: HT | ||||||
Site | 309-310 | Cleavage; by Ty3 protease | ||||
Sequence: HY | ||||||
Active site | 336 | For protease activity; shared with dimeric partner | ||||
Sequence: D | ||||||
Site | 442-443 | Cleavage; by Ty3 protease | ||||
Sequence: NN | ||||||
Site | 535-536 | Cleavage; by Ty3 protease | ||||
Sequence: ST | ||||||
Binding site | 686 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Binding site | 748 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Binding site | 749 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Binding site | 893 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: D | ||||||
Binding site | 936 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: E | ||||||
Binding site | 961 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: D | ||||||
Site | 1011-1012 | Cleavage; by Ty3 protease | ||||
Sequence: YT | ||||||
Site | 1037-1038 | Cleavage; by Ty3 protease; partial | ||||
Sequence: SA | ||||||
Binding site | 1175 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for integrase activity | ||||
Sequence: D | ||||||
Binding site | 1236 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for integrase activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | aspartic-type endopeptidase activity | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA-directed DNA polymerase activity | |
Molecular Function | RNA-DNA hybrid ribonuclease activity | |
Molecular Function | zinc ion binding | |
Biological Process | DNA integration | |
Biological Process | DNA recombination | |
Biological Process | proteolysis | |
Biological Process | viral translational frameshifting |
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTransposon Ty3-G Gag-Pol polyprotein
- Alternative names
- Cleaved into 8 chains
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ99315
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 267 | Reduces level of VLP formation and maturation. | ||||
Sequence: C → S | ||||||
Mutagenesis | 275 | Reduces level of VLP formation and maturation. | ||||
Sequence: H → Q |
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000279357 | 2-207 | Capsid protein | |||
Sequence: SFMDQIPGGGNYPKLPVECLPNFPIQPSLTFRGRNDSHKLKNFISEIMLNMSMISWPNDASRIVYCRRHLLNPAAQWANDFVQEQGILEITFDTFIQGLYQHFYKPPDINKIFNAITQLSEAKLGIERLNQRFRKIWDRMPPDFMTEKAAIMTYTRLLTKETYNIVRMHKPETLKDAMEEAYQTTALTERFFPGFELDADGDTIIG | ||||||
Chain | PRO_0000279356 | 2-1547 | Transposon Ty3-G Gag-Pol polyprotein | |||
Sequence: SFMDQIPGGGNYPKLPVECLPNFPIQPSLTFRGRNDSHKLKNFISEIMLNMSMISWPNDASRIVYCRRHLLNPAAQWANDFVQEQGILEITFDTFIQGLYQHFYKPPDINKIFNAITQLSEAKLGIERLNQRFRKIWDRMPPDFMTEKAAIMTYTRLLTKETYNIVRMHKPETLKDAMEEAYQTTALTERFFPGFELDADGDTIIGATTHLQEEYDSDYDSEDNLTQNGYVHTVRTRRSYNKPMSNHRNRRNNNPSREECIKNRLCFYCKKEGHRLNECRARKAVLTDLELESKDQQTPFIKTLPIVHYIAIPEMDNTAEKTIKIQNTKVKTLFDSGSPTSFIRRDIVELLKYEIYETPPLRFRGFVATKSAVTSEAVTIDLKINDLHITLAAYILDNMDYQLLIGNPILRRYPKILHTVLNTRESPDSLKPKTYRSETVNNVRTYSAGNRGNPRNIKLSFAPTILEATDPKSAGNRGDSRTKTLSLATTTPAAIDPLTTLDNPGSTQSTFAQFPIPEEASILEEDGKYSNVVSTIQSVEPNATDHSNKDTFCTLPVWLQQKYREIIRNDLPPRPADINNIPVKHDIEIKPGARLPRLQPYHVTEKNEQEINKIVQKLLDNKFIVPSKSPCSSPVVLVPKKDGTFRLCVDYRTLNKATISDPFPLPRIDNLLSRIGNAQIFTTLDLHSGYHQIPMEPKDRYKTAFVTPSGKYEYTVMPFGLVNAPSTFARYMADTFRDLRFVNVYLDDILIFSESPEEHWKHLDTVLERLKNENLIVKKKKCKFASEETEFLGYSIGIQKIAPLQHKCAAIRDFPTPKTVKQAQRFLGMINYYRRFIPNCSKIAQPIQLFICDKSQWTEKQDKAIDKLKDALCNSPVLVPFNNKANYRLTTDASKDGIGAVLEEVDNKNKLVGVVGYFSKSLESAQKNYPAGELELLGIIKALHHFRYMLHGKHFTLRTDHISLLSLQNKNEPARRVQRWLDDLATYDFTLEYLAGPKNVVADAISRAVYTITPETSRPIDTESWKSYYKSDPLCSAVLIHMKELTQHNVTPEDMSAFRSYQKKLELSETFRKNYSLEDEMIYYQDRLVVPIKQQNAVMRLYHDHTLFGGHFGVTVTLAKISPIYYWPKLQHSIIQYIRTCVQCQLIKSHRPRLHGLLQPLPIAEGRWLDISMDFVTGLPPTSNNLNMILVVVDRFSKRAHFIATRKTLDATQLIDLLFRYIFSYHGFPRTITSDRDVRMTADKYQELTKRLGIKSTMSSANHPQTDGQSERTIQTLNRLLRAYASTNIQNWHVYLPQIEFVYNSTPTRTLGKSPFEIDLGYLPNTPAIKSDDEVNARSFTAVELAKHLKALTIQTKEQLEHAQIEMETNNNQRRKPLLLNIGDHVLVHRDAYFKKGAYMKVQQIYVGPFRVVKKINDNAYELDLNSHKKKHRVINVQFLKKFVYRPDAYPKNKPISSTERIKRAHEVTALIGIDTTHKTYLCHMQDVDPTLSVEYSEAEFCQIPERTRRSILANFRQLYETQDNPEREEDVVSQNEICQYDNTSP | ||||||
Peptide | PRO_0000279358 | 208-233 | Spacer peptide p3 | |||
Sequence: ATTHLQEEYDSDYDSEDNLTQNGYVH | ||||||
Chain | PRO_0000279359 | 234-309 | Nucleocapsid protein p11 | |||
Sequence: TVRTRRSYNKPMSNHRNRRNNNPSREECIKNRLCFYCKKEGHRLNECRARKAVLTDLELESKDQQTPFIKTLPIVH | ||||||
Chain | PRO_0000279360 | 310-442 | Ty3 protease | |||
Sequence: YIAIPEMDNTAEKTIKIQNTKVKTLFDSGSPTSFIRRDIVELLKYEIYETPPLRFRGFVATKSAVTSEAVTIDLKINDLHITLAAYILDNMDYQLLIGNPILRRYPKILHTVLNTRESPDSLKPKTYRSETVN | ||||||
Peptide | PRO_0000279361 | 443-535 | Spacer peptide J | |||
Sequence: NVRTYSAGNRGNPRNIKLSFAPTILEATDPKSAGNRGDSRTKTLSLATTTPAAIDPLTTLDNPGSTQSTFAQFPIPEEASILEEDGKYSNVVS | ||||||
Chain | PRO_0000279362 | 536-1011 | Reverse transcriptase/ribonuclease H | |||
Sequence: TIQSVEPNATDHSNKDTFCTLPVWLQQKYREIIRNDLPPRPADINNIPVKHDIEIKPGARLPRLQPYHVTEKNEQEINKIVQKLLDNKFIVPSKSPCSSPVVLVPKKDGTFRLCVDYRTLNKATISDPFPLPRIDNLLSRIGNAQIFTTLDLHSGYHQIPMEPKDRYKTAFVTPSGKYEYTVMPFGLVNAPSTFARYMADTFRDLRFVNVYLDDILIFSESPEEHWKHLDTVLERLKNENLIVKKKKCKFASEETEFLGYSIGIQKIAPLQHKCAAIRDFPTPKTVKQAQRFLGMINYYRRFIPNCSKIAQPIQLFICDKSQWTEKQDKAIDKLKDALCNSPVLVPFNNKANYRLTTDASKDGIGAVLEEVDNKNKLVGVVGYFSKSLESAQKNYPAGELELLGIIKALHHFRYMLHGKHFTLRTDHISLLSLQNKNEPARRVQRWLDDLATYDFTLEYLAGPKNVVADAISRAVY | ||||||
Chain | PRO_0000279363 | 1012-1547 | Integrase p61 | |||
Sequence: TITPETSRPIDTESWKSYYKSDPLCSAVLIHMKELTQHNVTPEDMSAFRSYQKKLELSETFRKNYSLEDEMIYYQDRLVVPIKQQNAVMRLYHDHTLFGGHFGVTVTLAKISPIYYWPKLQHSIIQYIRTCVQCQLIKSHRPRLHGLLQPLPIAEGRWLDISMDFVTGLPPTSNNLNMILVVVDRFSKRAHFIATRKTLDATQLIDLLFRYIFSYHGFPRTITSDRDVRMTADKYQELTKRLGIKSTMSSANHPQTDGQSERTIQTLNRLLRAYASTNIQNWHVYLPQIEFVYNSTPTRTLGKSPFEIDLGYLPNTPAIKSDDEVNARSFTAVELAKHLKALTIQTKEQLEHAQIEMETNNNQRRKPLLLNIGDHVLVHRDAYFKKGAYMKVQQIYVGPFRVVKKINDNAYELDLNSHKKKHRVINVQFLKKFVYRPDAYPKNKPISSTERIKRAHEVTALIGIDTTHKTYLCHMQDVDPTLSVEYSEAEFCQIPERTRRSILANFRQLYETQDNPEREEDVVSQNEICQYDNTSP | ||||||
Chain | PRO_0000279364 | 1038-1547 | Integrase p58 | |||
Sequence: AVLIHMKELTQHNVTPEDMSAFRSYQKKLELSETFRKNYSLEDEMIYYQDRLVVPIKQQNAVMRLYHDHTLFGGHFGVTVTLAKISPIYYWPKLQHSIIQYIRTCVQCQLIKSHRPRLHGLLQPLPIAEGRWLDISMDFVTGLPPTSNNLNMILVVVDRFSKRAHFIATRKTLDATQLIDLLFRYIFSYHGFPRTITSDRDVRMTADKYQELTKRLGIKSTMSSANHPQTDGQSERTIQTLNRLLRAYASTNIQNWHVYLPQIEFVYNSTPTRTLGKSPFEIDLGYLPNTPAIKSDDEVNARSFTAVELAKHLKALTIQTKEQLEHAQIEMETNNNQRRKPLLLNIGDHVLVHRDAYFKKGAYMKVQQIYVGPFRVVKKINDNAYELDLNSHKKKHRVINVQFLKKFVYRPDAYPKNKPISSTERIKRAHEVTALIGIDTTHKTYLCHMQDVDPTLSVEYSEAEFCQIPERTRRSILANFRQLYETQDNPEREEDVVSQNEICQYDNTSP |
Post-translational modification
Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and also contain the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein, and this cleavage is a prerequisite for subsequent processing at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Ty3 protease
The protease is a homodimer, whose active site consists of two apposed aspartic acid residues.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 265-282 | CCHC-type | ||||
Sequence: RLCFYCKKEGHRLNECRA | ||||||
Domain | 620-797 | Reverse transcriptase | ||||
Sequence: LDNKFIVPSKSPCSSPVVLVPKKDGTFRLCVDYRTLNKATISDPFPLPRIDNLLSRIGNAQIFTTLDLHSGYHQIPMEPKDRYKTAFVTPSGKYEYTVMPFGLVNAPSTFARYMADTFRDLRFVNVYLDDILIFSESPEEHWKHLDTVLERLKNENLIVKKKKCKFASEETEFLGYSI | ||||||
Domain | 893-1011 | RNase H Ty3/gyspy-type | ||||
Sequence: DASKDGIGAVLEEVDNKNKLVGVVGYFSKSLESAQKNYPAGELELLGIIKALHHFRYMLHGKHFTLRTDHISLLSLQNKNEPARRVQRWLDDLATYDFTLEYLAGPKNVVADAISRAVY | ||||||
Region | 1106-1145 | Integrase-type zinc finger-like | ||||
Sequence: HTLFGGHFGVTVTLAKISPIYYWPKLQHSIIQYIRTCVQC | ||||||
Domain | 1159-1324 | Integrase catalytic | ||||
Sequence: LQPLPIAEGRWLDISMDFVTGLPPTSNNLNMILVVVDRFSKRAHFIATRKTLDATQLIDLLFRYIFSYHGFPRTITSDRDVRMTADKYQELTKRLGIKSTMSSANHPQTDGQSERTIQTLNRLLRAYASTNIQNWHVYLPQIEFVYNSTPTRTLGKSPFEIDLGYL |
Domain
Integrase p61
Integrase core domain contains the D-x(n)-D-x35-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,D35E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Ribosomal frameshifting. The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift.
Q99315-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameTransposon Ty3-G Gag-Pol polyprotein
- NoteProduced by +1 ribosomal frameshifting between codon Ala-285 and Val-286 of the YGR109W-A ORF.
- Length1,547
- Mass (Da)178,307
- Last updated2007-03-06 v3
- Checksum0E327D91E0575F78
Q12173-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameTransposon Ty3-G Gag polyprotein
Sequence caution
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M34549 EMBL· GenBank· DDBJ | AAA98435.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Z72894 EMBL· GenBank· DDBJ | CAA97115.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Z72895 EMBL· GenBank· DDBJ | CAA97117.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AH003104 EMBL· GenBank· DDBJ | AAA66936.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006941 EMBL· GenBank· DDBJ | DAA08202.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |