Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O13527

- YA11B_YEAST

UniProt

O13527 - YA11B_YEAST

Protein

Truncated transposon Ty1-A Gag-Pol polyprotein

Gene

TY1B-A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 3 (02 Nov 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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
    Metal bindingi112 – 1121Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation
    Metal bindingi177 – 1771Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation
    Sitei658 – 6592Cleavage; by Ty1 proteaseBy similarity
    Metal bindingi787 – 7871Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation
    Metal bindingi868 – 8681Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation
    Metal bindingi869 – 8691Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation
    Metal bindingi1051 – 10511Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1093 – 10931Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation
    Metal bindingi1126 – 11261Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. DNA-directed DNA polymerase activity Source: SGD
    3. metal ion binding Source: UniProtKB-KW
    4. peptidase activity Source: SGD
    5. ribonuclease activity Source: SGD
    6. RNA binding Source: SGD
    7. RNA-directed DNA polymerase activity Source: SGD
    8. 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. proteolysis Source: GOC
    5. RNA-dependent DNA replication Source: GOC
    6. RNA phosphodiester bond hydrolysis Source: GOC
    7. transposition, RNA-mediated Source: SGD

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, RNA-directed DNA polymerase, Transferase

    Keywords - Biological processi

    DNA integration, DNA recombination, Transposition

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Truncated transposon Ty1-A Gag-Pol polyprotein
    Alternative name(s):
    TY1B
    Transposon Ty1 TYB polyprotein
    Cleaved into the following 2 chains:
    Integrase
    Short name:
    IN
    Alternative name(s):
    Pol-p71
    p84
    p90
    Reverse transcriptase/ribonuclease H (EC:2.7.7.49, EC:2.7.7.7, EC:3.1.26.4)
    Short name:
    RT
    Short name:
    RT-RH
    Alternative name(s):
    Pol-p63
    p60
    Gene namesi
    Name:TY1B-A
    Synonyms:YARCTy1-1 POL
    Ordered Locus Names:YAR009C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome I

    Organism-specific databases

    CYGDiYAR009c.
    SGDiS000000067. YAR009C.

    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 – 11961196Truncated transposon Ty1-A Gag-Pol polyproteinPRO_0000278977Add
    BLAST
    Chaini1 – 658658IntegraseBy similarityPRO_0000278980Add
    BLAST
    Chaini659 – 1196538Reverse transcriptase/ribonuclease HBy similarityPRO_0000278981Add
    BLAST

    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

    Expressioni

    Gene expression databases

    GenevestigatoriO13527.

    Interactioni

    Protein-protein interaction databases

    BioGridi31795. 8 interactions.
    DIPiDIP-2632N.
    IntActiO13527. 2 interactions.
    MINTiMINT-601384.
    STRINGi4932.YPR137C-B.

    Structurei

    3D structure databases

    ProteinModelPortaliO13527.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 276176Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini779 – 917139Reverse transcriptase Ty1/copia-typeAdd
    BLAST
    Domaini1051 – 1193143RNase H Ty1/copia-typeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi619 – 65335Bipartite nuclear localization signalBy similarityAdd
    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

    Phylogenomic databases

    GeneTreeiENSGT00730000111405.
    OMAiNINLQEE.
    OrthoDBiEOG7TJ3S3.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR001584. Integrase_cat-core.
    IPR012337. RNaseH-like_dom.
    IPR013103. RVT_2.
    [Graphical view]
    PfamiPF00665. rve. 1 hit.
    PF07727. RVT_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53098. SSF53098. 1 hit.
    PROSITEiPS50994. INTEGRASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O13527-1 [UniParc]FASTAAdd to Basket

    « Hide

    METFTGYLKS TCFHQISPYP PSIMSIQVKV HANILILSFI ECLRMPMHRQ     50
    IRYSLKNNTI TYFNESDVDW SSAIDYQCPD CLIGKSTKHR HIKGSRLKYQ 100
    NSYEPFQYLH TDIFGPVHNL PKSAPSYFIS FTDETTKLRW VYPLHDRRED 150
    SILDVFTTIL AFIKNQFQAS VLVIQMDRGS EYTNRTLHKF LEKNGITPCY 200
    TTTADSRAHG VAERLNRTLL DDCRTQLQCS GLPNHLWFSA IEFSTIVRNS 250
    LASPKSKKSA RQHAGLAGLD ISTLLPFGQP VIVNDHNPNS KIHPRGIPGY 300
    ALHPSRNSYG YIIYLPSLKK TVDTTNYVIL QGKESRLDQF NYDALTFDED 350
    LNRLTASYHS FIASNEIQES NDLNIESDHD FQSDIELHPE QPRNVLSKAV 400
    SPTDSTPPST HTEDSKRVSK TNIRAPREVD PNISESNILP SKKRSSTPQI 450
    SNIESTGSGG MHKLNVPLLA PMSQSNTHES SHASKSKDFR HSDSYSENET 500
    NHTNVPISST GGTNNKTVPQ ISDQETEKRI IHRSPSIDAS PPENNSSHNI 550
    VPIKTPTTVS EQNTEESIIA DLPLPDLPPE SPTEFPDPFK ELPPINSHQT 600
    NSSLGGIGDS NAYTTINSKK RSLEDNETEI KVSRDTWNTK NMRSLEPPRS 650
    KKRIHLIAAV KAVKSIKPIR TTLRYDEAIT YNKDIKEKEK YIEAYHKEVN 700
    QLLKMNTWDT DKYYDRKEID PKRVINSMFI FNKKRDGTHK ARFVARGDIQ 750
    HPDTYDTGMQ SNTVHHYALM TSLSLALDNN YYITQLDISS AYLYADIKEE 800
    LYIRPPPHLG MNDKLIRLKK SLYGLKQSGA NWYETIKSYL IKQCGMEEVR 850
    GWSCVFKNSQ VTICLFVDDM ILFSKDLNAN KKIITTLKKQ YDTKIINLGE 900
    SDNEIQYDIL GLEIKYQRGK YMKLGMEKSL TEKLPKLNVP LNPKGKKLRA 950
    PGQPGLYIDQ DELEIDEDEY KEKVHEMQKL IGLASYVGYK FRFDLLYYIN 1000
    TLAQHILFPS RQVLDMTYEL IQFMWDTRDK QLIWHKNKPT EPDNKLVAIS 1050
    DASYGNQPYY KSQIGNIYLL NGKVIGGKST KASLTCTSTT EAEIHAISES 1100
    VPLLNNLSYL IQELNKKPII KGLLTDSRST ISIIKSTNEE KFRNRFFGTK 1150
    AMRLRDEVSG NNLYVYYIET KKNIADVMTK PLPIKTFKLL TNKWIH 1196
    Length:1,196
    Mass (Da):136,732
    Last modified:November 2, 2010 - v3
    Checksum:i0A3E8CFC5B12C6A2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22015 Genomic DNA. Translation: AAC04967.1.
    BK006935 Genomic DNA. Translation: DAA06991.1.
    PIRiS40908.
    RefSeqiNP_009406.1. NM_001178213.1.

    Genome annotation databases

    EnsemblFungiiYAR009C; YAR009C; YAR009C.
    GeneIDi851268.
    KEGGisce:YAR009C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L22015 Genomic DNA. Translation: AAC04967.1 .
    BK006935 Genomic DNA. Translation: DAA06991.1 .
    PIRi S40908.
    RefSeqi NP_009406.1. NM_001178213.1.

    3D structure databases

    ProteinModelPortali O13527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31795. 8 interactions.
    DIPi DIP-2632N.
    IntActi O13527. 2 interactions.
    MINTi MINT-601384.
    STRINGi 4932.YPR137C-B.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YAR009C ; YAR009C ; YAR009C .
    GeneIDi 851268.
    KEGGi sce:YAR009C.

    Organism-specific databases

    CYGDi YAR009c.
    SGDi S000000067. YAR009C.

    Phylogenomic databases

    GeneTreei ENSGT00730000111405.
    OMAi NINLQEE.
    OrthoDBi EOG7TJ3S3.

    Miscellaneous databases

    NextBioi 968240.

    Gene expression databases

    Genevestigatori O13527.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR001584. Integrase_cat-core.
    IPR012337. RNaseH-like_dom.
    IPR013103. RVT_2.
    [Graphical view ]
    Pfami PF00665. rve. 1 hit.
    PF07727. RVT_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 1 hit.
    PROSITEi PS50994. INTEGRASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
      Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
      Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204511 / S288c / AB972.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "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, IDENTIFICATION OF FRAMESHIFT.
    5. "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.
    6. "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 nameiYA11B_YEAST
    AccessioniPrimary (citable) accession number: O13527
    Secondary accession number(s): D6VPM1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 104 of the entry and version 3 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).

    Caution

    Transposon Ty1-A (YARCTy1-1) contains a frameshift at position 610, which disrupts the ORF coding for protein TY1B. This is the truncated, C-terminal part of TY1B translated from an in-frame start codon, and it is probably not functional.Curated

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome, Transposable element

    Documents

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

    External Data

    Dasty 3