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Q03494 (YD22B_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transposon Ty2-DR2 Gag-Pol polyprotein
Alternative name(s):
TY2A-TY2B
Transposon Ty2 TYA-TYB polyprotein

Cleaved into the following 4 chains:

  1. Capsid protein
    Short name=CA
  2. Ty2 protease
    Short name=PR
    EC=3.4.23.-
  3. Integrase
    Short name=IN
  4. Reverse transcriptase/ribonuclease H
    Short name=RT
    Short name=RT-RH
    EC=2.7.7.49
    EC=2.7.7.7
    EC=3.1.26.4
Gene names
Name:TY2B-DR2
Synonyms:YDRWTy2-2 POL
Ordered Locus Names:YDR210W-B
ORF Names:YD8142A.09
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1770 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 Ty2 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 activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Endonucleolytic cleavage to 5'-phosphomonoester.

Subunit structure

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.

Subcellular location

Cytoplasm. Nucleus By similarity.

Domain

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,D35E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein By similarity.

Post-translational modification

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 By similarity.

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. Ty2 retrotransposons belong to the copia elements (pseudoviridae).

Sequence similarities

Contains 1 integrase catalytic domain.

Contains 1 peptidase A11 domain.

Contains 1 reverse transcriptase Ty1/copia-type domain.

Contains 1 RNase H Ty1/copia-type domain.

Sequence caution

The sequence CAA92351.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processDNA integration
DNA recombination
Transposition
Virion maturation
Virus exit from host cell
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityRibosomal frameshifting
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionAspartyl protease
DNA-directed DNA polymerase
Endonuclease
Hydrolase
Nuclease
Nucleotidyltransferase
Protease
RNA-directed DNA polymerase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Transposable element
Gene Ontology (GO)
   Biological_processDNA integration

Inferred from electronic annotation. Source: UniProtKB-KW

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-dependent DNA replication

Inferred from sequence or structural similarity Ref.3. Source: GOC

RNA phosphodiester bond hydrolysis

Inferred from sequence or structural similarity Ref.3. Source: GOC

RNA-dependent DNA replication

Inferred from sequence or structural similarity Ref.3. Source: GOC

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

transposition, RNA-mediated

Inferred from sequence or structural similarity Ref.3. Source: SGD

viral release from host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 9448009. Source: SGD

retrotransposon nucleocapsid

Inferred from sequence or structural similarity Ref.3. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA-directed DNA polymerase activity

Inferred from sequence or structural similarity Ref.3. Source: SGD

RNA binding

Inferred from sequence or structural similarity Ref.3. Source: SGD

RNA-DNA hybrid ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

RNA-directed DNA polymerase activity

Inferred from sequence or structural similarity Ref.3. Source: SGD

aspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peptidase activity

Inferred from sequence or structural similarity Ref.3. Source: SGD

ribonuclease activity

Inferred from sequence or structural similarity Ref.3. Source: SGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by ribosomal frameshifting. [Align] [Select]

Note: The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift.
Isoform Transposon Ty2-DR2 Gag-Pol polyprotein (identifier: Q03494-1)

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.
Note: Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YDR210W-A ORF.
Isoform Transposon Ty2-DR2 Gag polyprotein (identifier: Q03483-1)

The sequence of this isoform can be found in the external entry Q03483.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17701770Transposon Ty2-DR2 Gag-Pol polyprotein
PRO_0000279292
Chain1 – 397397Capsid protein By similarity
PRO_0000279293
Chain398 – 578181Ty2 protease By similarity
PRO_0000279294
Chain579 – 1232654Integrase By similarity
PRO_0000279295
Chain1233 – 1770538Reverse transcriptase/ribonuclease H By similarity
PRO_0000279296

Regions

Domain656 – 831176Integrase catalytic
Domain1353 – 1491139Reverse transcriptase Ty1/copia-type
Domain1625 – 1767143RNase H Ty1/copia-type
Region295 – 397103RNA-binding By similarity
Region579 – 63658Integrase-type zinc finger-like
Motif1193 – 122735Bipartite nuclear localization signal By similarity

Sites

Active site4571For protease activity; shared with dimeric partner By similarity
Metal binding6671Magnesium; catalytic; for integrase activity By similarity
Metal binding7321Magnesium; catalytic; for integrase activity By similarity
Metal binding13611Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding14421Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding14431Magnesium; catalytic; for reverse transcriptase activity By similarity
Metal binding16251Magnesium; catalytic; for RNase H activity By similarity
Metal binding16671Magnesium; catalytic; for RNase H activity By similarity
Metal binding17001Magnesium; catalytic; for RNase H activity By similarity
Site397 – 3982Cleavage; by Ty2 protease By similarity
Site578 – 5792Cleavage; by Ty2 protease By similarity
Site1232 – 12332Cleavage; by Ty2 protease By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform Transposon Ty2-DR2 Gag-Pol polyprotein [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: 8833D6F4FC6CAC68

FASTA1,770202,095
        10         20         30         40         50         60 
MESQQLHQNP HSQHGSAYAS VTSKEVPSNQ DPLAVSASNL PEFDRDSTKV NSQEETTPGT 

        70         80         90        100        110        120 
SAVPENHHHV SPQPASVPPP QNGQYQQHGM MTPNKAMASN WAHYQQPSMM TCSHYQTSPA 

       130        140        150        160        170        180 
YYQPDPHYPL PQYIPPLSTS SPDPIDSQDQ HSEVPQAKTK VRNNVLPPHT LTSEENFSTW 

       190        200        210        220        230        240 
VKFYIRFLKN SNLGDIIPND QGEIKRQMTY EEHAYIYNTF QAFAPFHLLP TWVKQILEIN 

       250        260        270        280        290        300 
YSDILTVLCK SVSKMQTNNQ ELKDWIALAN LEYNGSTSAD TFEITVSTII QRLKENNINV 

       310        320        330        340        350        360 
SDRLACQLIL KGLSGDFKYL RNQYRTKTNM KLSQLFAEIQ LIYDENKIMN LNKPSQYKQH 

       370        380        390        400        410        420 
SEYKNVSRTS PNTTNTKVTT RNYHRTNSSK PRAAKAHNIA TSSKFSRVNS DHINESTVSS 

       430        440        450        460        470        480 
QYLSDDNELS LGQQQKESKP TRTIDSNDEL PDHLLIDSGA SQTLVRSAHY LHHATPNSEI 

       490        500        510        520        530        540 
NIVDAQKQDI PINAIGNLHF NFQNGTKTSI KALHTPNIAY DLLSLSELAN QNITACFTRN 

       550        560        570        580        590        600 
TLERSDGTVL APIVKHGDFY WLSKKYLIPS HISKLTINNV NKSKSVNKYP YPLIHRMLGH 

       610        620        630        640        650        660 
ANFRSIQKSL KKNAVTYLKE SDIEWSNAST YQCPDCLIGK STKHRHVKGS RLKYQESYEP 

       670        680        690        700        710        720 
FQYLHTDIFG PVHHLPKSAP SYFISFTDEK TRFQWVYPLH DRREESILNV FTSILAFIKN 

       730        740        750        760        770        780 
QFNARVLVIQ MDRGSEYTNK TLHKFFTNRG ITACYTTTAD SRAHGVAERL NRTLLNDCRT 

       790        800        810        820        830        840 
LLHCSGLPNH LWFSAVEFST IIRNSLVSPK NDKSARQHAG LAGLDITTIL PFGQPVIVNN 

       850        860        870        880        890        900 
HNPDSKIHPR GIPGYALHPS RNSYGYIIYL PSLKKTVDTT NYVILQNNQT KLDQFDYDTL 

       910        920        930        940        950        960 
TFDDDLNRLT AHNQSFIEQN ETEQSYDQNT ESDHDYQSEI EINSDPLVND FSSQSLNPLQ 

       970        980        990       1000       1010       1020 
LDKEPVQKVR APKEVDADIS EYNILPSTIR SRTPHIINKE STEMGGTIES DTTSPRHSST 

      1030       1040       1050       1060       1070       1080 
FTARNQKRPG SPNDMIDLTS QDRVNYGLEN IKTTRLGGTE EPYIQRNSDT NIKYRTTNST 

      1090       1100       1110       1120       1130       1140 
PSIDDRSSNS ESTTPIISIE TKAVCDNTPS IDTDPPEYRS SDHATPNIMP DKSSKNVTAD 

      1150       1160       1170       1180       1190       1200 
SILDDLPLPD LTHKSPTDTS DVAKDIPHIH SRQTNSSLGG MDDSNVLTTT KSKKRSLEDN 

      1210       1220       1230       1240       1250       1260 
ETEIEVSRDT WNNKNMRSLE PPRSKKRINL IAAIKGVKSI KPVRTTLRYD EAITYNKDNK 

      1270       1280       1290       1300       1310       1320 
EKDRYVEAYH KEISQLLKMN TWDTNKYYDR NDIDPKKVIN SMFIFNKKRD GTHKARFVAR 

      1330       1340       1350       1360       1370       1380 
GDIQHPDTYD SDMQSNTVHH YALMTSLSIA LDNDYYITQL DISSAYLYAD IKEELYIRPP 

      1390       1400       1410       1420       1430       1440 
PHLGLNDKLL RLRKSLYGLK QSGANWYETI KSYLINCCDM QEVRGWSCVF KNSQVTICLF 

      1450       1460       1470       1480       1490       1500 
VDDMILFSKD LNANKKIITT LKKQYDTKII NLGEGDNEIQ YDILGLEIKY QRSKYMKLGM 

      1510       1520       1530       1540       1550       1560 
EKSLTEKLPK LNVPLNPKGK KLRAPGQPGH YIDQDELEID EDEYKEKVHE MQKLIGLASY 

      1570       1580       1590       1600       1610       1620 
VGYKFRFDLL YYINTLAQHI LFPSRQVLDM TYELIQFMWD TRDKQLIWHK NKPTKPDNKL 

      1630       1640       1650       1660       1670       1680 
VAISDASYGN QPYYKSQIGN IFLLNGKVIG GKSTKASLTC TSTTEAEIHA VSEAIPLLNN 

      1690       1700       1710       1720       1730       1740 
LSHLVQELNK KPIIKGLLTD SRSTISIIKS TNEEKFRNRF FGTKAMRLRD EVSGNNLYVY 

      1750       1760       1770 
YIETKKNIAD VMTKPLPIKT FKLLTNKWIH 

« Hide

Isoform Transposon Ty2-DR2 Gag polyprotein [UniParc].

See Q03483.

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z68194 Genomic DNA. Translation: CAA92351.1. Sequence problems.
BK006938 Genomic DNA. Translation: DAA12051.1.
PIRS69950.
RefSeqNP_058142.3. NM_001184419.3.

3D structure databases

ProteinModelPortalQ03494.
SMRQ03494. Positions 632-833.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32261. 4 interactions.
IntActQ03494. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR210W-B; YDR210W-B; YDR210W-B. [Q03494-1]
GeneID851793.
KEGGsce:YDR210W-B.

Organism-specific databases

SGDS000007393. YDR210W-B.

Phylogenomic databases

GeneTreeENSGT00730000111602.
HOGENOMHOG000280731.
OrthoDBEOG7TJ3S3.

Gene expression databases

GenevestigatorQ03494.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR025724. GAG-pre-integrase_dom.
IPR001584. Integrase_cat-core.
IPR015820. Retrotransposon_Ty1A_N.
IPR012337. RNaseH-like_dom.
IPR013103. RVT_2.
[Graphical view]
PfamPF13976. gag_pre-integrs. 1 hit.
PF00665. rve. 1 hit.
PF07727. RVT_2. 1 hit.
PF01021. TYA. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
PROSITEPS50994. INTEGRASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969618.

Entry information

Entry nameYD22B_YEAST
AccessionPrimary (citable) accession number: Q03494
Secondary accession number(s): D6VSJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries