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Q99315

- YG31B_YEAST

UniProt

Q99315 - YG31B_YEAST

Protein

Transposon Ty3-G Gag-Pol polyprotein

Gene

TY3B-G

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 3 (06 Mar 2007)
      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 genomic RNA-nucleocapsid complex.
    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.By similarity
    The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.
    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 (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.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei207 – 2082Cleavage; by Ty3 protease
    Sitei233 – 2342Cleavage; by Ty3 protease
    Sitei309 – 3102Cleavage; by Ty3 protease
    Active sitei336 – 3361For protease activity; shared with dimeric partnerBy similarity
    Sitei442 – 4432Cleavage; by Ty3 proteaseSequence Analysis
    Sitei535 – 5362Cleavage; by Ty3 protease
    Metal bindingi686 – 6861Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi748 – 7481Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi749 – 7491Magnesium; catalytic; for reverse transcriptase activityBy similarity
    Metal bindingi893 – 8931Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi936 – 9361Magnesium; catalytic; for RNase H activityBy similarity
    Metal bindingi961 – 9611Magnesium; catalytic; for RNase H activityBy similarity
    Sitei1011 – 10122Cleavage; by Ty3 protease
    Sitei1037 – 10382Cleavage; by Ty3 protease; partial
    Metal bindingi1175 – 11751Magnesium; catalytic; for integrase activityBy similarity
    Metal bindingi1236 – 12361Magnesium; catalytic; for integrase activityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri265 – 28218CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    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. peptidase activity Source: SGD
    6. ribonuclease activity Source: SGD
    7. RNA binding Source: SGD
    8. RNA-directed DNA polymerase activity Source: SGD
    9. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC
    10. zinc ion binding Source: InterPro

    GO - Biological processi

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

    Keywords - Ligandi

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

    Protein family/group databases

    MEROPSiA02.022.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transposon Ty3-G Gag-Pol polyprotein
    Alternative name(s):
    Gag3-Pol3
    Transposon Ty3-1 TYA-TYB polyprotein
    Cleaved into the following 8 chains:
    Capsid protein
    Short name:
    CA
    Alternative name(s):
    p24
    Ty3 protease (EC:3.4.23.-)
    Short name:
    PR
    Alternative name(s):
    p16
    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):
    p55
    Integrase p61
    Short name:
    IN
    Integrase p58
    Short name:
    IN
    Gene namesi
    Name:TY3B-G
    Synonyms:YGRWTy3-1 POL
    Ordered Locus Names:YGR109W-B
    ORF Names:G5984
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    SGDiS000007347. YGR109W-B.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi267 – 2671C → S: Reduces level of VLP formation and maturation. 1 Publication
    Mutagenesisi275 – 2751H → Q: Reduces level of VLP formation and maturation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 15471546Transposon Ty3-G Gag-Pol polyproteinPRO_0000279356Add
    BLAST
    Chaini2 – 207206Capsid proteinPRO_0000279357Add
    BLAST
    Peptidei208 – 23326Spacer peptide p3PRO_0000279358Add
    BLAST
    Chaini234 – 30976Nucleocapsid protein p11PRO_0000279359Add
    BLAST
    Chaini310 – 442133Ty3 proteasePRO_0000279360Add
    BLAST
    Peptidei443 – 53593Spacer peptide JSequence AnalysisPRO_0000279361Add
    BLAST
    Chaini536 – 1011476Reverse transcriptase/ribonuclease HPRO_0000279362Add
    BLAST
    Chaini1012 – 1547536Integrase p61PRO_0000279363Add
    BLAST
    Chaini1038 – 1547510Integrase p58PRO_0000279364Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    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, 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.2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ99315.

    Miscellaneous databases

    PMAP-CutDBQ99315.

    Expressioni

    Gene expression databases

    GenevestigatoriQ99315.

    Interactioni

    Subunit structurei

    The protease is a homodimer, whose active site consists of two apposed aspartic acid residues.

    Protein-protein interaction databases

    BioGridi33356. 2 interactions.

    Structurei

    Secondary structure

    1
    1547
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi558 – 5636
    Turni565 – 5673
    Helixi608 – 62114
    Beta strandi636 – 6405
    Beta strandi646 – 6505
    Helixi653 – 6564
    Helixi669 – 6735
    Beta strandi681 – 6877
    Helixi690 – 6934
    Beta strandi694 – 6963
    Helixi698 – 7047
    Beta strandi712 – 7176
    Helixi725 – 73713
    Beta strandi743 – 7464
    Beta strandi749 – 7568
    Helixi757 – 77317
    Helixi780 – 7823
    Beta strandi795 – 7973
    Beta strandi802 – 8043
    Helixi806 – 8094
    Turni810 – 8145
    Helixi821 – 83212
    Turni833 – 8375
    Helixi841 – 8444
    Helixi863 – 8719
    Beta strandi884 – 8918
    Beta strandi899 – 9068
    Beta strandi908 – 9114
    Beta strandi913 – 9219
    Helixi932 – 94413
    Helixi948 – 9514
    Beta strandi957 – 9593
    Helixi976 – 98611

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4OL8X-ray3.10A/B/E/F536-1011[»]
    ProteinModelPortaliQ99315.
    SMRiQ99315. Positions 550-1011, 1111-1333.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini620 – 797178Reverse transcriptasePROSITE-ProRule annotationAdd
    BLAST
    Domaini893 – 1011119RNase H Ty3/gyspy-typeAdd
    BLAST
    Domaini1159 – 1324166Integrase catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1106 – 114540Integrase-type zinc finger-likeAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
    Contains 1 peptidase A2 domain.Curated
    Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri265 – 28218CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2801.
    HOGENOMiHOG000172599.
    KOiK07497.
    OrthoDBiEOG7HF1TD.

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    InterProiIPR001584. Integrase_cat-core.
    IPR024650. Peptidase_A2B.
    IPR021109. Peptidase_aspartic_dom.
    IPR005162. Retrotrans_gag_dom.
    IPR012337. RNaseH-like_dom.
    IPR000477. RT_dom.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF12384. Peptidase_A2B. 1 hit.
    PF03732. Retrotrans_gag. 1 hit.
    PF00665. rve. 1 hit.
    PF00078. RVT_1. 1 hit.
    [Graphical view]
    SMARTiSM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    SUPFAMiSSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 1 hit.
    SSF57756. SSF57756. 1 hit.
    PROSITEiPS50994. INTEGRASE. 1 hit.
    PS50878. RT_POL. 1 hit.
    PS50158. ZF_CCHC. 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.1 Publication

    Isoform Transposon Ty3-G Gag-Pol polyprotein (identifier: Q99315-1) [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

    MSFMDQIPGG GNYPKLPVEC LPNFPIQPSL TFRGRNDSHK LKNFISEIML     50
    NMSMISWPND ASRIVYCRRH LLNPAAQWAN DFVQEQGILE ITFDTFIQGL 100
    YQHFYKPPDI NKIFNAITQL SEAKLGIERL NQRFRKIWDR MPPDFMTEKA 150
    AIMTYTRLLT KETYNIVRMH KPETLKDAME EAYQTTALTE RFFPGFELDA 200
    DGDTIIGATT HLQEEYDSDY DSEDNLTQNG YVHTVRTRRS YNKPMSNHRN 250
    RRNNNPSREE CIKNRLCFYC KKEGHRLNEC RARKAVLTDL ELESKDQQTP 300
    FIKTLPIVHY IAIPEMDNTA EKTIKIQNTK VKTLFDSGSP TSFIRRDIVE 350
    LLKYEIYETP PLRFRGFVAT KSAVTSEAVT IDLKINDLHI TLAAYILDNM 400
    DYQLLIGNPI LRRYPKILHT VLNTRESPDS LKPKTYRSET VNNVRTYSAG 450
    NRGNPRNIKL SFAPTILEAT DPKSAGNRGD SRTKTLSLAT TTPAAIDPLT 500
    TLDNPGSTQS TFAQFPIPEE ASILEEDGKY SNVVSTIQSV EPNATDHSNK 550
    DTFCTLPVWL QQKYREIIRN DLPPRPADIN NIPVKHDIEI KPGARLPRLQ 600
    PYHVTEKNEQ EINKIVQKLL DNKFIVPSKS PCSSPVVLVP KKDGTFRLCV 650
    DYRTLNKATI SDPFPLPRID NLLSRIGNAQ IFTTLDLHSG YHQIPMEPKD 700
    RYKTAFVTPS GKYEYTVMPF GLVNAPSTFA RYMADTFRDL RFVNVYLDDI 750
    LIFSESPEEH WKHLDTVLER LKNENLIVKK KKCKFASEET EFLGYSIGIQ 800
    KIAPLQHKCA AIRDFPTPKT VKQAQRFLGM INYYRRFIPN CSKIAQPIQL 850
    FICDKSQWTE KQDKAIDKLK DALCNSPVLV PFNNKANYRL TTDASKDGIG 900
    AVLEEVDNKN KLVGVVGYFS KSLESAQKNY PAGELELLGI IKALHHFRYM 950
    LHGKHFTLRT DHISLLSLQN KNEPARRVQR WLDDLATYDF TLEYLAGPKN 1000
    VVADAISRAV YTITPETSRP IDTESWKSYY KSDPLCSAVL IHMKELTQHN 1050
    VTPEDMSAFR SYQKKLELSE TFRKNYSLED EMIYYQDRLV VPIKQQNAVM 1100
    RLYHDHTLFG GHFGVTVTLA KISPIYYWPK LQHSIIQYIR TCVQCQLIKS 1150
    HRPRLHGLLQ PLPIAEGRWL DISMDFVTGL PPTSNNLNMI LVVVDRFSKR 1200
    AHFIATRKTL DATQLIDLLF RYIFSYHGFP RTITSDRDVR MTADKYQELT 1250
    KRLGIKSTMS SANHPQTDGQ SERTIQTLNR LLRAYASTNI QNWHVYLPQI 1300
    EFVYNSTPTR TLGKSPFEID LGYLPNTPAI KSDDEVNARS FTAVELAKHL 1350
    KALTIQTKEQ LEHAQIEMET NNNQRRKPLL LNIGDHVLVH RDAYFKKGAY 1400
    MKVQQIYVGP FRVVKKINDN AYELDLNSHK KKHRVINVQF LKKFVYRPDA 1450
    YPKNKPISST ERIKRAHEVT ALIGIDTTHK TYLCHMQDVD PTLSVEYSEA 1500
    EFCQIPERTR RSILANFRQL YETQDNPERE EDVVSQNEIC QYDNTSP 1547

    Note: Produced by +1 ribosomal frameshifting between codon Ala-285 and Val-286 of the YGR109W-A ORF.

    Length:1,547
    Mass (Da):178,307
    Last modified:March 6, 2007 - v3
    Checksum:i0E327D91E0575F78
    GO
    Isoform Transposon Ty3-G Gag polyprotein (identifier: Q12173-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry Q12173.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

    Note: Produced by conventional translation.

    Length:290
    Mass (Da):34,027
    GO

    Sequence cautioni

    The sequence AAA98435.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA97115.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA97117.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence DAA08202.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34549 Genomic DNA. Translation: AAA98435.1. Sequence problems.
    Z72894 Genomic DNA. Translation: CAA97115.1. Sequence problems.
    Z72895 Genomic DNA. Translation: CAA97117.1. Sequence problems.
    M18353 Genomic DNA. Translation: AAA66936.1.
    BK006941 Genomic DNA. Translation: DAA08202.1. Sequence problems.
    PIRiS22875.
    S69842.
    RefSeqiNP_011624.1. NM_001184381.1.

    Genome annotation databases

    GeneIDi853006.
    KEGGisce:YGR109W-B.

    Keywords - Coding sequence diversityi

    Ribosomal frameshifting

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34549 Genomic DNA. Translation: AAA98435.1 . Sequence problems.
    Z72894 Genomic DNA. Translation: CAA97115.1 . Sequence problems.
    Z72895 Genomic DNA. Translation: CAA97117.1 . Sequence problems.
    M18353 Genomic DNA. Translation: AAA66936.1 .
    BK006941 Genomic DNA. Translation: DAA08202.1 . Sequence problems.
    PIRi S22875.
    S69842.
    RefSeqi NP_011624.1. NM_001184381.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4OL8 X-ray 3.10 A/B/E/F 536-1011 [» ]
    ProteinModelPortali Q99315.
    SMRi Q99315. Positions 550-1011, 1111-1333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33356. 2 interactions.

    Protein family/group databases

    MEROPSi A02.022.

    Proteomic databases

    PaxDbi Q99315.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 853006.
    KEGGi sce:YGR109W-B.

    Organism-specific databases

    SGDi S000007347. YGR109W-B.

    Phylogenomic databases

    eggNOGi COG2801.
    HOGENOMi HOG000172599.
    KOi K07497.
    OrthoDBi EOG7HF1TD.

    Miscellaneous databases

    NextBioi 972854.
    PMAP-CutDB Q99315.

    Gene expression databases

    Genevestigatori Q99315.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    InterProi IPR001584. Integrase_cat-core.
    IPR024650. Peptidase_A2B.
    IPR021109. Peptidase_aspartic_dom.
    IPR005162. Retrotrans_gag_dom.
    IPR012337. RNaseH-like_dom.
    IPR000477. RT_dom.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF12384. Peptidase_A2B. 1 hit.
    PF03732. Retrotrans_gag. 1 hit.
    PF00665. rve. 1 hit.
    PF00078. RVT_1. 1 hit.
    [Graphical view ]
    SMARTi SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50630. SSF50630. 1 hit.
    SSF53098. SSF53098. 1 hit.
    SSF57756. SSF57756. 1 hit.
    PROSITEi PS50994. INTEGRASE. 1 hit.
    PS50878. RT_POL. 1 hit.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of a transpositionally active Ty3 element and identification of the Ty3 integrase protein."
      Hansen L.J., Sandmeyer S.B.
      J. Virol. 64:2599-2607(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: AB950.
    2. "The sequence of a 23.4 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals CLB6, SPT6, RP28A and NUP57 genes, a Ty3 element and 11 new open reading frames."
      Hansen M., Albers M., Backes U., Coblenz A., Leuther H., Neu R., Schreer A., Schaefer B., Zimmermann M., Wolf K.
      Yeast 12:1273-1277(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "A yeast sigma composite element, TY3, has properties of a retrotransposon."
      Clark D.J., Bilanchone V.W., Haywood L.J., Dildine S.L., Sandmeyer S.B.
      J. Biol. Chem. 263:1413-1423(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    6. "Ty3 GAG3 and POL3 genes encode the components of intracellular particles."
      Hansen L.J., Chalker D.L., Orlinsky K.J., Sandmeyer S.B.
      J. Virol. 66:1414-1424(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF REVERSE TRANSCRIPTASE, SUBCELLULAR LOCATION.
    7. "A novel programed frameshift expresses the POL3 gene of retrotransposon Ty3 of yeast: frameshifting without tRNA slippage."
      Farabaugh P.J., Zhao H., Vimaladithan A.
      Cell 74:93-103(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: RIBOSOMAL FRAMESHIFT SITE.
    8. Erratum
      Farabaugh P.J., Zhao H., Vimaladithan A.
      Cell 75:826-826(1993)
    9. "Proteolytic processing of Ty3 proteins is required for transposition."
      Kirchner J., Sandmeyer S.B.
      J. Virol. 67:19-28(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING, CLEAVAGE SITES.
    10. "The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3 polyproteins."
      Orlinsky K.J., Sandmeyer S.B.
      J. Virol. 68:4152-4166(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF NUCLEOCAPSID, MUTAGENESIS OF CYS-267 AND HIS-275.
    11. "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.
    12. "Characterization of active reverse transcriptase and nucleoprotein complexes of the yeast retrotransposon Ty3 in vitro."
      Cristofari G., Gabus C., Ficheux D., Bona M., Le Grice S.F.J., Darlix J.-L.
      J. Biol. Chem. 274:36643-36648(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF REVERSE TRANSCRIPTASE.
    13. "Ten-kilodalton domain in Ty3 Gag3-Pol3p between PR and RT is dispensable for Ty3 transposition."
      Claypool J.A., Malik H.S., Eickbush T.H., Sandmeyer S.B.
      J. Virol. 75:1557-1560(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF PEPTIDE J.
    14. "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.
    15. "Investigation by atomic force microscopy of the structure of Ty3 retrotransposon particles."
      Kuznetsov Y.G., Zhang M., Menees T.M., McPherson A., Sandmeyer S.B.
      J. Virol. 79:8032-8045(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, CLEAVAGE SITE GLY-207-208-ALA, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiYG31B_YEAST
    AccessioniPrimary (citable) accession number: Q99315
    Secondary accession number(s): D6VUP1, Q07096
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2007
    Last sequence update: March 6, 2007
    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. Ty3 retrotransposons belong to the gypsy-like elements (metaviridae).

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome, Transposable element

    Documents

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

    External Data

    Dasty 3