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Q03612

- YE11B_YEAST

UniProt

Q03612 - YE11B_YEAST

Protein

Transposon Ty1-ER1 Gag-Pol polyprotein

Gene

TY1B-ER1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription By similarity.By similarity
    The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.By similarity
    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 By similarity.By similarity
    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 By similarity.By similarity

    Catalytic activityi

    Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
    Endonucleolytic cleavage to 5'-phosphomonoester.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei401 – 4022Cleavage; by Ty1 proteaseBy similarity
    Active sitei461 – 4611For protease activity; shared with dimeric partnerPROSITE-ProRule annotation
    Sitei582 – 5832Cleavage; by Ty1 proteaseBy similarity
    Metal bindingi671 – 6711Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation
    Metal bindingi736 – 7361Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation
    Sitei1217 – 12182Cleavage; by Ty1 proteaseBy similarity
    Metal bindingi1346 – 13461Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation
    Metal bindingi1427 – 14271Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation
    Metal bindingi1428 – 14281Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation
    Metal bindingi1610 – 16101Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1652 – 16521Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1685 – 16851Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW
    2. ATP binding Source: UniProtKB-KW
    3. DNA binding Source: UniProtKB-KW
    4. DNA-directed DNA polymerase activity Source: SGD
    5. metal ion binding Source: UniProtKB-KW
    6. peptidase activity Source: SGD
    7. ribonuclease activity Source: SGD
    8. RNA binding Source: SGD
    9. RNA-directed DNA polymerase activity Source: SGD
    10. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC

    GO - Biological processi

    1. DNA-dependent DNA replication Source: GOC
    2. DNA integration Source: UniProtKB-KW
    3. DNA recombination Source: UniProtKB-KW
    4. RNA-dependent DNA replication Source: GOC
    5. RNA phosphodiester bond hydrolysis Source: GOC
    6. transposition, RNA-mediated Source: SGD
    7. viral release from host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

    Keywords - Biological processi

    DNA integration, DNA recombination, Transposition, Virion maturation, Virus exit from host cell

    Keywords - Ligandi

    ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transposon Ty1-ER1 Gag-Pol polyprotein
    Alternative name(s):
    Gag-Pol-p199
    TY1A-TY1B
    Transposon Ty1 TYA-TYB polyprotein
    p190
    Cleaved into the following 4 chains:
    Capsid protein
    Short name:
    CA
    Alternative name(s):
    Gag-p45
    p54
    Ty1 protease (EC:3.4.23.-)
    Short name:
    PR
    Alternative name(s):
    Pol-p20
    p23
    Integrase
    Short name:
    IN
    Alternative name(s):
    Pol-p71
    p84
    p90
    Alternative name(s):
    Pol-p63
    p60
    Gene namesi
    Name:TY1B-ER1
    Synonyms:YERCTy1-1 POL
    Ordered Locus Names:YER138C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER138c.
    SGDiS000000940. YER138C.

    Subcellular locationi

    Cytoplasm. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: SGD
    3. retrotransposon nucleocapsid Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17551755Transposon Ty1-ER1 Gag-Pol polyproteinPRO_0000279043Add
    BLAST
    Chaini1 – 401401Capsid proteinBy similarityPRO_0000279044Add
    BLAST
    Chaini402 – 582181Ty1 proteaseBy similarityPRO_0000279045Add
    BLAST
    Chaini583 – 1217635IntegraseBy similarityPRO_0000279046Add
    BLAST
    Chaini1218 – 1755538Reverse transcriptase/ribonuclease HBy similarityPRO_0000279047Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei416 – 4161PhosphoserineBy similarity

    Post-translational modificationi

    Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also 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 yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 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 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ03612.

    Expressioni

    Gene expression databases

    GenevestigatoriQ03612.

    Interactioni

    Subunit structurei

    The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues By similarity.By similarity

    Protein-protein interaction databases

    BioGridi36885. 14 interactions.
    DIPiDIP-8790N.
    IntActiQ03612. 4 interactions.
    MINTiMINT-692519.
    STRINGi4932.YER138C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03612.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini660 – 835176Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini1338 – 1476139Reverse transcriptase Ty1/copia-typeAdd
    BLAST
    Domaini1610 – 1752143RNase H Ty1/copia-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni299 – 401103RNA-bindingBy similarityAdd
    BLAST
    Regioni583 – 64058Integrase-type zinc finger-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1178 – 121235Bipartite nuclear localization signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi64 – 14683Pro-richAdd
    BLAST

    Domaini

    The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.By similarity
    Integrase 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.By similarity

    Sequence similaritiesi

    Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
    Contains 1 peptidase A11 domain.Curated

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    GeneTreeiENSGT00730000111405.
    HOGENOMiHOG000280731.
    OrthoDBiEOG7TJ3S3.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR001969. Aspartic_peptidase_AS.
    IPR001584. Integrase_cat-core.
    IPR015820. Retrotransposon_Ty1A_N.
    IPR012337. RNaseH-like_dom.
    IPR013103. RVT_2.
    [Graphical view]
    PfamiPF00665. rve. 1 hit.
    PF07727. RVT_2. 1 hit.
    PF01021. TYA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53098. SSF53098. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 1 hit.
    PS50994. INTEGRASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by ribosomal frameshifting. Align

    Note: 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).By similarity

    Isoform Transposon Ty1-ER1 Gag-Pol polyprotein (identifier: Q03612-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MESQQLSQHS PISHGSACAS VTSKEVHTNQ DPLDVSASKT EECEKASTKA     50
    NSQQTTTPAS SAVPENPHHA SPQPASVPPP QNGPYPQQCM MTQNQANPSG 100
    WSFYGHPSMI PYTPYQMSPM YFPPGPQSQF PQYPSSVGTP LSTPSPESGN 150
    TFTDSSSADS DMTSTKKYVR PPPMLTSPND FPNWVKTYIK FLQNSNLGGI 200
    IPTVNGKPVR QITDDELTFL YNTFQIFAPS QFLPTWVKDI LSVDYTDIMK 250
    ILSKSIEKMQ SDTQEANDIV TLANLQYNGS TPADAFETKV TNIIDRLNNN 300
    GIHINNKVAC QLIMRGLSGE YKFLRYTRHR HLNMTVAELF LDIHAIYEEQ 350
    QGSRNSKPNY RRNLSDEKND SRSYTNTTKP KVIARNPQKT NNSKSKTARA 400
    HNVSTSNNSP STDNDSISKS TTEPIQLNNK HDLHLGQELT ESTVNHTNHS 450
    DDELPGHLLL DSGASRTLIR SAHHIHSASS NPDINVVDAQ KRNIPINAIG 500
    DLQFHFQDNT KTSIKVLHTP NIAYDLLSLN ELAAVDITAC FTKNVLERSD 550
    GTVLAPIVKY GDFYWVSKKY LLPSNISVPT INNVHTSEST RKYPYPFIHR 600
    MLAHANAQTI RYSLKNNTIT YFNESDVDWS SAIDYQCPDC LIGKSTKHRH 650
    IKGSRLKYQN SYEPFQYLHT DIFGPVHNLP KSAPSYFISF TDETTKFRWV 700
    YPLHDRREDS ILDVFTTILA FIKNQFQASV LVIQMDRGSE YTNRTLHKFL 750
    EKNGITPCYT TTADSRAHGV AERLNRTLLD DCRTQLQCSG LPNHLWFSAI 800
    EFSTIVRNSL ASPKSKKSAR QHAGLAGLDI STLLPFGQPV IVNDHNPNSK 850
    IHPRGIPGYA LHPSRNSYGY IIYLPSLKKT VDTTNYVILQ GKESRLDQFN 900
    YDALTFDEDL NRLTASYQSF IASNEIQQSD DLNIESDHDF QSDIELHPEQ 950
    PRNVLSKAVS PTDSTPPSTH TEDSKRVSKT NIRAPREVDP NISESNILPS 1000
    KKRSSTPQIS NIESTGSGGM HKLNVPLLAP MSQSNTHESS HASKSKDFRH 1050
    SDSYSENETN HTNVPISSTG GTNNKTVPQI SDQETEKRII HRSPSIDASP 1100
    PENNSSHNIV PIKTPTTVSE QNTEESIIAD LPLPDLPPES PTEFPDPFKE 1150
    LPPINSHQTN SSLGGIGDSN AYTTINSKKR SLEDNETEIK VSRDTWNTKN 1200
    MRSLEPPRSK KRIHLIAAVK AVKSIKPIRT TLRYDEAITY NKDIKEKEKY 1250
    IEAYHKEVNQ LLKMKTWDTD EYYDRKEIDP KRVINSMFIF NKKRDGTHKA 1300
    RFVARGDIQH PDTYDSGMQS NTVHHYALMT SLSLALDNNY YITQLDISSA 1350
    YLYADIKEEL YIRPPPHLGM NDKLIRLKKS LYGLKQSGAN WYETIKSYLI 1400
    KQCGMEEVRG WSCVFKNSQV TICLFVDDMI LFSKDLNANK KIITTLKKQY 1450
    DTKIINLGES DNEIQYDILG LEIKYQRGKY MKLGMENSLT EKIPKLNVPL 1500
    NPKGRKLSAP GQPGLYIDQD ELEIDEDEYK EKVHEMQKLI GLASYVGYKF 1550
    RFDLLYYINT LAQHILFPSR QVLDMTYELI QFMWDTRDKQ LIWHKNKPTE 1600
    PDNKLVAISD ASYGNQPYYK SQIGNIYLLN GKVIGGKSTK ASLTCTSTTE 1650
    AEIHAISESV PLLNNLSYLI QELNKKPIIK GLLTDSRSTI SIIKSTNEEK 1700
    FRNRFFGTKA MRLRDEVSGN NLYVYYIETK KNIADVMTKP LPIKTFKLLT 1750
    NKWIH 1755

    Note: Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YER137C-A ORF.

    Length:1,755
    Mass (Da):198,562
    Last modified:November 1, 1996 - v1
    Checksum:i6EB17ED89FF1F6FB
    GO
    Isoform Transposon Ty1-ER1 Gag polyprotein (identifier: P0CX71-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry P0CX71.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:440
    Mass (Da):48,953
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18917 Genomic DNA. Translation: AAB64665.1.
    BK006939 Genomic DNA. Translation: DAA07797.1.
    PIRiS50641.
    RefSeqiNP_011064.3. NM_001179028.3. [Q03612-1]

    Genome annotation databases

    EnsemblFungiiYER138C; YER138C; YER138C. [Q03612-1]
    GeneIDi856879.
    KEGGisce:YER138C.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U18917 Genomic DNA. Translation: AAB64665.1 .
    BK006939 Genomic DNA. Translation: DAA07797.1 .
    PIRi S50641.
    RefSeqi NP_011064.3. NM_001179028.3. [Q03612-1 ]

    3D structure databases

    ProteinModelPortali Q03612.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36885. 14 interactions.
    DIPi DIP-8790N.
    IntActi Q03612. 4 interactions.
    MINTi MINT-692519.
    STRINGi 4932.YER138C.

    Proteomic databases

    MaxQBi Q03612.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER138C ; YER138C ; YER138C . [Q03612-1 ]
    GeneIDi 856879.
    KEGGi sce:YER138C.

    Organism-specific databases

    CYGDi YER138c.
    SGDi S000000940. YER138C.

    Phylogenomic databases

    GeneTreei ENSGT00730000111405.
    HOGENOMi HOG000280731.
    OrthoDBi EOG7TJ3S3.

    Miscellaneous databases

    NextBioi 983260.

    Gene expression databases

    Genevestigatori Q03612.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR001969. Aspartic_peptidase_AS.
    IPR001584. Integrase_cat-core.
    IPR015820. Retrotransposon_Ty1A_N.
    IPR012337. RNaseH-like_dom.
    IPR013103. RVT_2.
    [Graphical view ]
    Pfami PF00665. rve. 1 hit.
    PF07727. RVT_2. 1 hit.
    PF01021. TYA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 1 hit.
    PS50994. INTEGRASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence."
      Kim J.M., Vanguri S., Boeke J.D., Gabriel A., Voytas D.F.
      Genome Res. 8:464-478(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    4. "Happy together: the life and times of Ty retrotransposons and their hosts."
      Lesage P., Todeschini A.L.
      Cytogenet. Genome Res. 110:70-90(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    5. "Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element."
      Wilhelm F.-X., Wilhelm M., Gabriel A.
      Cytogenet. Genome Res. 110:269-287(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, DOMAINS.

    Entry informationi

    Entry nameiYE11B_YEAST
    AccessioniPrimary (citable) accession number: Q03612
    Secondary accession number(s): D3DM43
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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. Ty1 retrotransposons belong to the copia elements (pseudoviridae).

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome, Transposable element

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3