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Q12273

- YO11B_YEAST

UniProt

Q12273 - YO11B_YEAST

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Protein
Transposon Ty1-OL Gag-Pol polyprotein
Gene
TY1B-OL, YOLWTy1-1 POL, YOL103W-B, O0770
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

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.
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.
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.

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 protease By similarity
Active sitei461 – 4611For protease activity; shared with dimeric partner By similarity
Sitei582 – 5832Cleavage; by Ty1 protease By similarity
Metal bindingi671 – 6711Magnesium; catalytic; for integrase activity By similarity
Metal bindingi736 – 7361Magnesium; catalytic; for integrase activity By similarity
Sitei1217 – 12182Cleavage; by Ty1 protease By similarity
Metal bindingi1346 – 13461Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal bindingi1427 – 14271Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal bindingi1428 – 14281Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal bindingi1610 – 16101Magnesium; catalytic; for RNase H activity By similarity
Metal bindingi1652 – 16521Magnesium; catalytic; for RNase H activity By similarity
Metal bindingi1685 – 16851Magnesium; catalytic; for RNase H activity By similarity

GO - Molecular functioni

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

GO - Biological processi

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

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-OL 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
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-OL
Synonyms:YOLWTy1-1 POL
Ordered Locus Names:YOL103W-B
ORF Names:O0770
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOL103w-b.
SGDiS000007350. YOL103W-B.

Subcellular locationi

Cytoplasm. Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17551755Transposon Ty1-OL Gag-Pol polyprotein
PRO_0000279153Add
BLAST
Chaini1 – 401401Capsid protein By similarity
PRO_0000279154Add
BLAST
Chaini402 – 582181Ty1 protease By similarity
PRO_0000279155Add
BLAST
Chaini583 – 1217635Integrase By similarity
PRO_0000279156Add
BLAST
Chaini1218 – 1755538Reverse transcriptase/ribonuclease H By similarity
PRO_0000279157Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei416 – 4161Phosphoserine By 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.

Keywords - PTMi

Phosphoprotein

Expressioni

Gene expression databases

GenevestigatoriQ12273.

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.

Protein-protein interaction databases

BioGridi34299. 3 interactions.
DIPiDIP-8936N.
IntActiQ12273. 1 interaction.
MINTiMINT-473409.
STRINGi4932.YOL103W-B.

Structurei

3D structure databases

ProteinModelPortaliQ12273.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini660 – 835176Integrase catalytic
Add
BLAST
Domaini1338 – 1476139Reverse transcriptase Ty1/copia-type
Add
BLAST
Domaini1610 – 1752143RNase H Ty1/copia-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni299 – 401103RNA-binding By similarity
Add
BLAST
Regioni583 – 64058Integrase-type zinc finger-like
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1178 – 121235Bipartite nuclear localization signal By similarity
Add
BLAST

Compositional bias

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

Domaini

The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities By similarity.1 Publication
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.1 Publication

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00730000111405.
HOGENOMiHOG000280731.
OMAiQISHGSA.
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).

Isoform Transposon Ty1-OL Gag-Pol polyprotein (identifier: Q12273-1) [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

MESQQLSNYP QISHGSACAS 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 TNIINRLNNN 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 YOL103W-A ORF.

Length:1,755
Mass (Da):198,614
Last modified:November 1, 1996 - v1
Checksum:i64062136832619DE
GO
Isoform Transposon Ty1-OL Gag polyprotein (identifier: Q92392-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry Q92392.
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):49,005
GO

Sequence cautioni

The sequence CAA88158.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48149 Genomic DNA. Translation: CAA88158.1. Sequence problems.
Z74845 Genomic DNA. Translation: CAA99118.1.
Z74846 Genomic DNA. Translation: CAA99122.1.
BK006948 Genomic DNA. Translation: DAA10679.1.
PIRiS69975.
RefSeqiNP_058181.1. NM_001184384.1. [Q12273-1]

Genome annotation databases

EnsemblFungiiYOL103W-B; YOL103W-B; YOL103W-B. [Q12273-1]
GeneIDi854049.
KEGGisce:YOL103W-B.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48149 Genomic DNA. Translation: CAA88158.1 . Sequence problems.
Z74845 Genomic DNA. Translation: CAA99118.1 .
Z74846 Genomic DNA. Translation: CAA99122.1 .
BK006948 Genomic DNA. Translation: DAA10679.1 .
PIRi S69975.
RefSeqi NP_058181.1. NM_001184384.1. [Q12273-1 ]

3D structure databases

ProteinModelPortali Q12273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34299. 3 interactions.
DIPi DIP-8936N.
IntActi Q12273. 1 interaction.
MINTi MINT-473409.
STRINGi 4932.YOL103W-B.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOL103W-B ; YOL103W-B ; YOL103W-B . [Q12273-1 ]
GeneIDi 854049.
KEGGi sce:YOL103W-B.

Organism-specific databases

CYGDi YOL103w-b.
SGDi S000007350. YOL103W-B.

Phylogenomic databases

GeneTreei ENSGT00730000111405.
HOGENOMi HOG000280731.
OMAi QISHGSA.
OrthoDBi EOG7TJ3S3.

Miscellaneous databases

NextBioi 975629.

Gene expression databases

Genevestigatori Q12273.

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

« Hide 'large scale' publications
  1. "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element."
    Vandenbol M., Durand P., Portetelle D., Hilger F.
    Yeast 11:1069-1075(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    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.
  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 nameiYO11B_YEAST
AccessioniPrimary (citable) accession number: Q12273
Secondary accession number(s): D6W1W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: November 1, 1996
Last modified: May 14, 2014
This is version 101 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

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