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Q99315

- YG31B_YEAST

UniProt

Q99315 - YG31B_YEAST

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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

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-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
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, 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-KW
  2. nucleus Source: SGD
  3. retrotransposon nucleocapsid Source: SGD
Complete GO annotation...

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 – 5636Combined sources
Turni565 – 5673Combined sources
Helixi608 – 62114Combined sources
Beta strandi636 – 6405Combined sources
Beta strandi646 – 6505Combined sources
Helixi653 – 6564Combined sources
Helixi669 – 6735Combined sources
Beta strandi681 – 6877Combined sources
Helixi690 – 6934Combined sources
Beta strandi694 – 6963Combined sources
Helixi698 – 7047Combined sources
Beta strandi712 – 7176Combined sources
Helixi725 – 73713Combined sources
Beta strandi743 – 7464Combined sources
Beta strandi749 – 7568Combined sources
Helixi757 – 77317Combined sources
Helixi780 – 7823Combined sources
Beta strandi795 – 7973Combined sources
Beta strandi802 – 8043Combined sources
Helixi806 – 8094Combined sources
Turni810 – 8145Combined sources
Helixi821 – 83212Combined sources
Turni833 – 8375Combined sources
Helixi841 – 8444Combined sources
Helixi863 – 8719Combined sources
Beta strandi884 – 8918Combined sources
Beta strandi899 – 9068Combined sources
Beta strandi908 – 9114Combined sources
Beta strandi913 – 9219Combined sources
Helixi932 – 94413Combined sources
Helixi948 – 9514Combined sources
Beta strandi957 – 9593Combined sources
Helixi976 – 98611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiQ99315.
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

        10         20         30         40         50
MSFMDQIPGG GNYPKLPVEC LPNFPIQPSL TFRGRNDSHK LKNFISEIML
60 70 80 90 100
NMSMISWPND ASRIVYCRRH LLNPAAQWAN DFVQEQGILE ITFDTFIQGL
110 120 130 140 150
YQHFYKPPDI NKIFNAITQL SEAKLGIERL NQRFRKIWDR MPPDFMTEKA
160 170 180 190 200
AIMTYTRLLT KETYNIVRMH KPETLKDAME EAYQTTALTE RFFPGFELDA
210 220 230 240 250
DGDTIIGATT HLQEEYDSDY DSEDNLTQNG YVHTVRTRRS YNKPMSNHRN
260 270 280 290 300
RRNNNPSREE CIKNRLCFYC KKEGHRLNEC RARKAVLTDL ELESKDQQTP
310 320 330 340 350
FIKTLPIVHY IAIPEMDNTA EKTIKIQNTK VKTLFDSGSP TSFIRRDIVE
360 370 380 390 400
LLKYEIYETP PLRFRGFVAT KSAVTSEAVT IDLKINDLHI TLAAYILDNM
410 420 430 440 450
DYQLLIGNPI LRRYPKILHT VLNTRESPDS LKPKTYRSET VNNVRTYSAG
460 470 480 490 500
NRGNPRNIKL SFAPTILEAT DPKSAGNRGD SRTKTLSLAT TTPAAIDPLT
510 520 530 540 550
TLDNPGSTQS TFAQFPIPEE ASILEEDGKY SNVVSTIQSV EPNATDHSNK
560 570 580 590 600
DTFCTLPVWL QQKYREIIRN DLPPRPADIN NIPVKHDIEI KPGARLPRLQ
610 620 630 640 650
PYHVTEKNEQ EINKIVQKLL DNKFIVPSKS PCSSPVVLVP KKDGTFRLCV
660 670 680 690 700
DYRTLNKATI SDPFPLPRID NLLSRIGNAQ IFTTLDLHSG YHQIPMEPKD
710 720 730 740 750
RYKTAFVTPS GKYEYTVMPF GLVNAPSTFA RYMADTFRDL RFVNVYLDDI
760 770 780 790 800
LIFSESPEEH WKHLDTVLER LKNENLIVKK KKCKFASEET EFLGYSIGIQ
810 820 830 840 850
KIAPLQHKCA AIRDFPTPKT VKQAQRFLGM INYYRRFIPN CSKIAQPIQL
860 870 880 890 900
FICDKSQWTE KQDKAIDKLK DALCNSPVLV PFNNKANYRL TTDASKDGIG
910 920 930 940 950
AVLEEVDNKN KLVGVVGYFS KSLESAQKNY PAGELELLGI IKALHHFRYM
960 970 980 990 1000
LHGKHFTLRT DHISLLSLQN KNEPARRVQR WLDDLATYDF TLEYLAGPKN
1010 1020 1030 1040 1050
VVADAISRAV YTITPETSRP IDTESWKSYY KSDPLCSAVL IHMKELTQHN
1060 1070 1080 1090 1100
VTPEDMSAFR SYQKKLELSE TFRKNYSLED EMIYYQDRLV VPIKQQNAVM
1110 1120 1130 1140 1150
RLYHDHTLFG GHFGVTVTLA KISPIYYWPK LQHSIIQYIR TCVQCQLIKS
1160 1170 1180 1190 1200
HRPRLHGLLQ PLPIAEGRWL DISMDFVTGL PPTSNNLNMI LVVVDRFSKR
1210 1220 1230 1240 1250
AHFIATRKTL DATQLIDLLF RYIFSYHGFP RTITSDRDVR MTADKYQELT
1260 1270 1280 1290 1300
KRLGIKSTMS SANHPQTDGQ SERTIQTLNR LLRAYASTNI QNWHVYLPQI
1310 1320 1330 1340 1350
EFVYNSTPTR TLGKSPFEID LGYLPNTPAI KSDDEVNARS FTAVELAKHL
1360 1370 1380 1390 1400
KALTIQTKEQ LEHAQIEMET NNNQRRKPLL LNIGDHVLVH RDAYFKKGAY
1410 1420 1430 1440 1450
MKVQQIYVGP FRVVKKINDN AYELDLNSHK KKHRVINVQF LKKFVYRPDA
1460 1470 1480 1490 1500
YPKNKPISST ERIKRAHEVT ALIGIDTTHK TYLCHMQDVD PTLSVEYSEA
1510 1520 1530 1540
EFCQIPERTR RSILANFRQL YETQDNPERE EDVVSQNEIC QYDNTSP

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi Q99315.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 106 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