Q12414 · YP11B_YEAST
- ProteinTransposon Ty1-PL Gag-Pol polyprotein
- GeneTY1B-PL
- 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-PL 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 accessionQ12414
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000279170 | 1-401 | Capsid protein | |||
Sequence: MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAH | ||||||
Chain | PRO_0000279169 | 1-1755 | Transposon Ty1-PL Gag-Pol polyprotein | |||
Sequence: MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH | ||||||
Chain | PRO_0000279171 | 402-582 | Ty1 protease | |||
Sequence: NVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTIN | ||||||
Modified residue | 416 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000279172 | 583-1217 | Integrase | |||
Sequence: NVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIA | ||||||
Chain | PRO_0000279173 | 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: NVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDC | ||||||
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).
Q12414-1
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-PL Gag-Pol polyprotein
- NoteProduced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YPL257W-A ORF.
- Length1,755
- Mass (Da)198,576
- Last updated1996-11-01 v1
- ChecksumC1D766C7C6070422
P0CX73-1
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-PL 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 | |
---|---|---|---|---|
Z73613 EMBL· GenBank· DDBJ | CAA97984.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z73614 EMBL· GenBank· DDBJ | CAA97988.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11178.1 EMBL· GenBank· DDBJ | Genomic DNA |