Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 144 (16 Oct 2019)
Sequence version 3 (06 Mar 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Transposon Ty3-G Gag-Pol polyprotein

Gene

TY3B-G

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 similarity4 Publications
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.

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).

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Endonucleolytic cleavage to 5'-phosphomonoester. EC:3.1.26.4

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei336For protease activity; shared with dimeric partnerBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi686Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi748Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi749Magnesium; catalytic; for reverse transcriptase activityBy similarity1
Metal bindingi893Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi936Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi961Magnesium; catalytic; for RNase H activityBy similarity1
Metal bindingi1175Magnesium; catalytic; for integrase activityBy similarity1
Metal bindingi1236Magnesium; catalytic; for integrase activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri265 – 282CCHC-typePROSITE-ProRule annotationAdd BLAST18

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAspartyl protease, DNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed DNA polymerase, Transferase
Biological processDNA integration, DNA recombination, Viral release from host cell, Virion maturation
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Protein family/group databases

MEROPS protease database

More...
MEROPSi
A02.022

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TY3B-G
Synonyms:YGRWTy3-1 POL
Ordered Locus Names:YGR109W-B
ORF Names:G5984
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGR109W-B

Saccharomyces Genome Database

More...
SGDi
S000007347 YGR109W-B

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi267C → S: Reduces level of VLP formation and maturation. 1 Publication1
Mutagenesisi275H → Q: Reduces level of VLP formation and maturation. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002793562 – 1547Transposon Ty3-G Gag-Pol polyproteinAdd BLAST1546
ChainiPRO_00002793572 – 207Capsid proteinAdd BLAST206
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_0000279358208 – 233Spacer peptide p3Add BLAST26
ChainiPRO_0000279359234 – 309Nucleocapsid protein p11Add BLAST76
ChainiPRO_0000279360310 – 442Ty3 proteaseAdd BLAST133
PeptideiPRO_0000279361443 – 535Spacer peptide JSequence analysisAdd BLAST93
ChainiPRO_0000279362536 – 1011Reverse transcriptase/ribonuclease HAdd BLAST476
ChainiPRO_00002793631012 – 1547Integrase p61Add BLAST536
ChainiPRO_00002793641038 – 1547Integrase p58Add BLAST510

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei207 – 208Cleavage; by Ty3 protease2
Sitei233 – 234Cleavage; by Ty3 protease2
Sitei309 – 310Cleavage; by Ty3 protease2
Sitei442 – 443Cleavage; by Ty3 proteaseSequence analysis2
Sitei535 – 536Cleavage; by Ty3 protease2
Sitei1011 – 1012Cleavage; by Ty3 protease2
Sitei1037 – 1038Cleavage; by Ty3 protease; partial2

Keywords - PTMi

Acetylation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q99315

PRoteomics IDEntifications database

More...
PRIDEi
Q99315

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q99315

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q99315

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33356, 1 interactor

STRING: functional protein association networks

More...
STRINGi
4932.YGR109W-B

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11547
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q99315

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini620 – 797Reverse transcriptasePROSITE-ProRule annotationAdd BLAST178
Domaini893 – 1011RNase H Ty3/gyspy-typeAdd BLAST119
Domaini1159 – 1324Integrase catalyticPROSITE-ProRule annotationAdd BLAST166

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1106 – 1145Integrase-type zinc finger-likeAdd BLAST40

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri265 – 282CCHC-typePROSITE-ProRule annotationAdd BLAST18

Keywords - Domaini

Zinc-finger

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000172599

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q99315

KEGG Orthology (KO)

More...
KOi
K07497

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.70.10, 1 hit
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001584 Integrase_cat-core
IPR041588 Integrase_H2C2
IPR024650 Peptidase_A2B
IPR021109 Peptidase_aspartic_dom_sf
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR000477 RT_dom
IPR041577 RT_RNaseH_2
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17921 Integrase_H2C2, 1 hit
PF12384 Peptidase_A2B, 1 hit
PF17919 RT_RNaseH_2, 1 hit
PF00665 rve, 1 hit
PF00078 RVT_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00343 ZnF_C2HC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 1 hit
SSF57756 SSF57756, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50994 INTEGRASE, 1 hit
PS50878 RT_POL, 1 hit
PS50158 ZF_CCHC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

Protein sequence database of the Protein Information Resource

More...
PIRi
S22875
S69842

NCBI Reference Sequences

More...
RefSeqi
NP_011624.1, NM_001184381.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853006

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGR109W-B

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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.
PIRiS22875
S69842
RefSeqiNP_011624.1, NM_001184381.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OL8X-ray3.10A/B/E/F536-1011[»]
SMRiQ99315
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi33356, 1 interactor
STRINGi4932.YGR109W-B

Protein family/group databases

MEROPSiA02.022

PTM databases

iPTMnetiQ99315

Proteomic databases

PaxDbiQ99315
PRIDEiQ99315

Genome annotation databases

GeneIDi853006
KEGGisce:YGR109W-B

Organism-specific databases

EuPathDBiFungiDB:YGR109W-B
SGDiS000007347 YGR109W-B

Phylogenomic databases

HOGENOMiHOG000172599
InParanoidiQ99315
KOiK07497

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
YGR109W-B yeast
PMAP-CutDBiQ99315

Family and domain databases

Gene3Di2.40.70.10, 1 hit
3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR001584 Integrase_cat-core
IPR041588 Integrase_H2C2
IPR024650 Peptidase_A2B
IPR021109 Peptidase_aspartic_dom_sf
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR000477 RT_dom
IPR041577 RT_RNaseH_2
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
PfamiView protein in Pfam
PF17921 Integrase_H2C2, 1 hit
PF12384 Peptidase_A2B, 1 hit
PF17919 RT_RNaseH_2, 1 hit
PF00665 rve, 1 hit
PF00078 RVT_1, 1 hit
SMARTiView protein in SMART
SM00343 ZnF_C2HC, 1 hit
SUPFAMiSSF50630 SSF50630, 1 hit
SSF53098 SSF53098, 1 hit
SSF57756 SSF57756, 1 hit
PROSITEiView protein in PROSITE
PS50994 INTEGRASE, 1 hit
PS50878 RT_POL, 1 hit
PS50158 ZF_CCHC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiYG31B_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q99315
Secondary accession number(s): D6VUP1, Q07096
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: October 16, 2019
This is version 144 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again