P0C2I5 · YL12B_YEAST
- ProteinTransposon Ty1-LR2 Gag-Pol polyprotein
- GeneTY1B-LR2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1755 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Miscellaneous
Catalytic activity
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 401-402 | Cleavage; by Ty1 protease | ||||
Sequence: HN | ||||||
Active site | 461 | For protease activity; shared with dimeric partner | ||||
Sequence: D | ||||||
Site | 582-583 | Cleavage; by Ty1 protease | ||||
Sequence: NN | ||||||
Binding site | 671 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for integrase activity | ||||
Sequence: D | ||||||
Binding site | 736 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for integrase activity | ||||
Sequence: D | ||||||
Site | 1217-1218 | Cleavage; by Ty1 protease | ||||
Sequence: AA | ||||||
Binding site | 1346 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Binding site | 1427 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Binding site | 1428 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for reverse transcriptase activity | ||||
Sequence: D | ||||||
Binding site | 1610 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: D | ||||||
Binding site | 1652 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for RNase H activity | ||||
Sequence: E | ||||||
Binding site | 1685 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for RNase H 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 | metal ion binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA-directed DNA polymerase activity | |
Molecular Function | RNA-DNA hybrid ribonuclease activity | |
Biological Process | DNA integration | |
Biological Process | DNA recombination | |
Biological Process | proteolysis | |
Biological Process | transposition | |
Biological Process | viral translational frameshifting |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameTransposon Ty1-LR2 Gag-Pol polyprotein
- Alternative names
- Cleaved into 4 chains
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP0C2I5
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000279100 | 1-401 | Capsid protein | |||
Sequence: MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAH | ||||||
Chain | PRO_0000279099 | 1-1755 | Transposon Ty1-LR2 Gag-Pol polyprotein | |||
Sequence: MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAPTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH | ||||||
Chain | PRO_0000279101 | 402-582 | Ty1 protease | |||
Sequence: NVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTIN | ||||||
Modified residue | 416 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000279102 | 583-1217 | Integrase | |||
Sequence: NVHTSESTRKYPYPFIHRMLAHANAPTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIA | ||||||
Chain | PRO_0000279103 | 1218-1755 | Reverse transcriptase/ribonuclease H | |||
Sequence: AVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH |
Post-translational modification
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-36 | Polar residues | ||||
Sequence: MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVS | ||||||
Region | 1-93 | Disordered | ||||
Sequence: MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQ | ||||||
Compositional bias | 47-67 | Polar residues | ||||
Sequence: STKANSQQTTTPASSAVPENP | ||||||
Compositional bias | 71-85 | Pro residues | ||||
Sequence: SPQPASVPPPQNGPY | ||||||
Region | 126-174 | Disordered | ||||
Sequence: PQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPM | ||||||
Compositional bias | 131-164 | Polar residues | ||||
Sequence: PQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTS | ||||||
Region | 299-401 | RNA-binding | ||||
Sequence: NNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAH | ||||||
Region | 352-421 | Disordered | ||||
Sequence: GSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKST | ||||||
Compositional bias | 360-374 | Basic and acidic residues | ||||
Sequence: YRRNLSDEKNDSRSY | ||||||
Compositional bias | 375-421 | Polar residues | ||||
Sequence: TNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKST | ||||||
Region | 583-640 | Integrase-type zinc finger-like | ||||
Sequence: NVHTSESTRKYPYPFIHRMLAHANAPTIRYSLKNNTITYFNESDVDWSSAIDYQCPDC | ||||||
Domain | 660-835 | Integrase catalytic | ||||
Sequence: NSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLP | ||||||
Region | 956-1087 | Disordered | ||||
Sequence: SKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEK | ||||||
Compositional bias | 969-983 | Basic and acidic residues | ||||
Sequence: THTEDSKRVSKTNIR | ||||||
Compositional bias | 993-1018 | Polar residues | ||||
Sequence: SESNILPSKKRSSTPQISNIESTGSG | ||||||
Compositional bias | 1040-1056 | Basic and acidic residues | ||||
Sequence: SHASKSKDFRHSDSYSE | ||||||
Compositional bias | 1057-1080 | Polar residues | ||||
Sequence: NETNHTNVPISSTGGTNNKTVPQI | ||||||
Region | 1092-1111 | Disordered | ||||
Sequence: RSPSIDASPPENNSSHNIVP | ||||||
Compositional bias | 1097-1111 | Polar residues | ||||
Sequence: DASPPENNSSHNIVP | ||||||
Region | 1130-1187 | Disordered | ||||
Sequence: DLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNET | ||||||
Compositional bias | 1134-1148 | Pro residues | ||||
Sequence: PDLPPESPTEFPDPF | ||||||
Compositional bias | 1153-1178 | Polar residues | ||||
Sequence: PINSRQTNSSLGGIGDSNAYTTINSK | ||||||
Motif | 1178-1212 | Bipartite nuclear localization signal | ||||
Sequence: KKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKR | ||||||
Domain | 1338-1476 | Reverse transcriptase Ty1/copia-type | ||||
Sequence: NNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQ | ||||||
Domain | 1610-1752 | RNase H Ty1/copia-type | ||||
Sequence: DASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNK |
Domain
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. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).
P0C2I5-1
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 Ty1-LR2 Gag-Pol polyprotein
- NoteProduced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YLR157C-A ORF.
- Length1,755
- Mass (Da)198,545
- Last updated2007-03-06 v1
- Checksum2916CADCA298D8A7
P0CX72-1
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 Ty1-LR2 Gag polyprotein
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-36 | Polar residues | ||||
Sequence: MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVS | ||||||
Compositional bias | 47-67 | Polar residues | ||||
Sequence: STKANSQQTTTPASSAVPENP | ||||||
Compositional bias | 71-85 | Pro residues | ||||
Sequence: SPQPASVPPPQNGPY | ||||||
Compositional bias | 131-164 | Polar residues | ||||
Sequence: PQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTS | ||||||
Compositional bias | 360-374 | Basic and acidic residues | ||||
Sequence: YRRNLSDEKNDSRSY | ||||||
Compositional bias | 375-421 | Polar residues | ||||
Sequence: TNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKST | ||||||
Compositional bias | 969-983 | Basic and acidic residues | ||||
Sequence: THTEDSKRVSKTNIR | ||||||
Compositional bias | 993-1018 | Polar residues | ||||
Sequence: SESNILPSKKRSSTPQISNIESTGSG | ||||||
Compositional bias | 1040-1056 | Basic and acidic residues | ||||
Sequence: SHASKSKDFRHSDSYSE | ||||||
Compositional bias | 1057-1080 | Polar residues | ||||
Sequence: NETNHTNVPISSTGGTNNKTVPQI | ||||||
Compositional bias | 1097-1111 | Polar residues | ||||
Sequence: DASPPENNSSHNIVP | ||||||
Compositional bias | 1134-1148 | Pro residues | ||||
Sequence: PDLPPESPTEFPDPF | ||||||
Compositional bias | 1153-1178 | Polar residues | ||||
Sequence: PINSRQTNSSLGGIGDSNAYTTINSK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U51921 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BK006945 EMBL· GenBank· DDBJ | DAA09474.1 EMBL· GenBank· DDBJ | Genomic DNA |