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Entry version 135 (18 Sep 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Transposon Ty2-DR3 Gag-Pol polyprotein

Gene

TY2B-DR3

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>
-Protein inferred from homologyi <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 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).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).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).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).

<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 sitei457For 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 bindingi667Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi732Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi1361Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1442Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1443Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1625Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1667Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1700Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1

<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, Transposition, Viral release from host cell, Virion maturation
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

<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 Ty2-DR3 Gag-Pol polyprotein
Alternative name(s):
TY2A-TY2B
Transposon Ty2 TYA-TYB polyprotein
Cleaved into the following 4 chains:
Capsid protein
Short name:
CA
Ty2 protease (EC:3.4.23.-)
Short name:
PR
Integrase
Short name:
IN
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
<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:TY2B-DR3
Synonyms:YDRWTy2-3 POL
Ordered Locus Names:YDR261W-B
ORF Names:YD9320A.14
<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 IV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YDR261W-B

Saccharomyces Genome Database

More...
SGDi
S000007397 YDR261W-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 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 ‘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_00002793001 – 1770Transposon Ty2-DR3 Gag-Pol polyproteinAdd BLAST1770
ChainiPRO_00002793011 – 397Capsid proteinBy similarityAdd BLAST397
ChainiPRO_0000279302398 – 578Ty2 proteaseBy similarityAdd BLAST181
ChainiPRO_0000279303579 – 1232IntegraseBy similarityAdd BLAST654
ChainiPRO_00002793041233 – 1770Reverse transcriptase/ribonuclease HBy similarityAdd BLAST538

<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 (By similarity).By similarity

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>Sitei397 – 398Cleavage; by Ty2 proteaseBy similarity2
Sitei578 – 579Cleavage; by Ty2 proteaseBy similarity2
Sitei1232 – 1233Cleavage; by Ty2 proteaseBy similarity2

Proteomic databases

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

More...
PaxDbi
Q07791

PRoteomics IDEntifications database

More...
PRIDEi
Q07791

<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 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).

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
32314, 7 interactors

Database of interacting proteins

More...
DIPi
DIP-8840N

Protein interaction database and analysis system

More...
IntActi
Q07791, 3 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YDR261W-B

<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>Domaini656 – 831Integrase catalyticPROSITE-ProRule annotationAdd BLAST176
Domaini1353 – 1491Reverse transcriptase Ty1/copia-typeAdd BLAST139
Domaini1625 – 1767RNase H Ty1/copia-typeAdd BLAST143

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>Regioni295 – 397RNA-bindingBy similarityAdd BLAST103
Regioni579 – 636Integrase-type zinc finger-likeAdd BLAST58

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1193 – 1227Bipartite nuclear localization signalBy similarityAdd BLAST35

<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

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,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).By similarity

Keywords - Domaini

Zinc-finger

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000280731

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q07791

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.420.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025724 GAG-pre-integrase_dom
IPR001584 Integrase_cat-core
IPR039537 Retrotran_Ty1/copia-like
IPR015820 Retrotransposon_Ty1A_N
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR013103 RVT_2

The PANTHER Classification System

More...
PANTHERi
PTHR11439 PTHR11439, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF13976 gag_pre-integrs, 1 hit
PF00665 rve, 1 hit
PF07727 RVT_2, 1 hit
PF01021 TYA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53098 SSF53098, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50994 INTEGRASE, 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.
Isoform Transposon Ty2-DR3 Gag-Pol polyprotein (identifier: Q07791-1) [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
MESQQLHQNP HSLHGSAAAS VTSKEVPSNQ DPLAVSASNL PEFDRDSTKV
60 70 80 90 100
NSQQETTPGT SAVPENHHHV SPQPASVPPP QNGQYQQHGM MTPNKAMASN
110 120 130 140 150
WAHYQQPSMM TCSHYQTSPA YYQPDPHYPL PQYIPPLSTS SPDPIDSQNQ
160 170 180 190 200
HSEVPQAKTK VRNNVLPPHT LTSEENFSTW VKFYIRFLKN SNLGDIIPND
210 220 230 240 250
QGEIKRQMTY EEHAYIYNTF QAFAPFHLLP TWVKQILEIN YADILTVLCK
260 270 280 290 300
SVSKMQTNNQ ELKDWIALAN LEYDGSTSAD TFEITVSTII QRLKENNINV
310 320 330 340 350
SDRLACQLIL KGLSGDFKYL RNQYRTKTNM KLSQLFAEIQ LIYDENKIMN
360 370 380 390 400
LNKPSQYKQH SEYKNVSRTS PNTTNTKVTS RNYHRTNSSK PRAAKAHNIA
410 420 430 440 450
TSSKFSRVNN DHINESTVSS QYLSDDNELS LGQQQKESKP TRTIDSNDEL
460 470 480 490 500
PDHLLIDSGA SQTLVRSAHY LHHATPNSEI NIVDAQKQDI PINAIGNLHF
510 520 530 540 550
NFQNGTKTSI KALHTPNIAY DLLSLSELAN QNITACFTRN TLERSDGTVL
560 570 580 590 600
APIVKHGDFY WLSKKYLIPS HISKLTINNV NKSKSVNKYP YPLIHRMLGH
610 620 630 640 650
ANFRSIQKSL KKNAVTYLKE SDIEWSNAST YQCPDCLIGK STKHRHIKGS
660 670 680 690 700
RLKYQESYEP FQYLHTDIFG PVHHLPKSAP SYFISFTDEK TRFQWVYPLH
710 720 730 740 750
DRREESILNV FTSILAFIKN QFNARVLVIQ MDRGSEYTNK TLHKFFTNRG
760 770 780 790 800
ITACYTTTAD SRAHGVAERL NRTLLNDCRT LLHCSGLPNH LWFSAVEFST
810 820 830 840 850
IIRNSLVSPK NDKSARQHAG LAGLDITTIL PFGQPVIVNN HNPDSKIHPR
860 870 880 890 900
GIPGYALHPS RNSYGYIIYL PSLKKTVDTT NYVILQDNQS KLDQFNYDTL
910 920 930 940 950
TFDDDLNRLT AHNQSFIEQN ETEQSYDQNT ESDHDYQSEI EINSDPLVND
960 970 980 990 1000
FSSQSLNPLQ LDKEPVQKVR APKEVDADIS EYNILPSTIR SRTPHIINKE
1010 1020 1030 1040 1050
STEMGGTIES DTTSPRHSST FTARNQKRPG SPNDMIDLTS QDRVNYGLEN
1060 1070 1080 1090 1100
IKTTRLGGTE EPYIQRNSDT NIKYRTTNST PSIDDRSSNS ESTTPIISIE
1110 1120 1130 1140 1150
TKAVCDNTPS IDTDPPEYRS SDHATPNIMP DKSSKNVTAD SILDDLPLPD
1160 1170 1180 1190 1200
LTNKSPTDTS DVSKDIPHIH SRQTNSSLGG MDDSNVLTTT KSKKRSLEDN
1210 1220 1230 1240 1250
ETEIEVSRDT WNNKNMRSLE PPRSKKRINL IAAIKGVKSI KPVRTTLRYD
1260 1270 1280 1290 1300
EAITYNKDNK EKDRYVEAYH KEISQLLKMN TWDTNKYYDR NDIDPKKVIN
1310 1320 1330 1340 1350
SMFIFNKKRD GTHKARFVAR GDIQHPDTYD SDMQSNTVHH YALMTSLSIA
1360 1370 1380 1390 1400
LDNDYYITQL DISSAYLYAD IKEELYIRPP PHLGLNDKLL RLRKSLYGLK
1410 1420 1430 1440 1450
QSGANWYETI KSYLINCCDM QEVRGWSCVF KNSQVTICLF VDDMILFSKD
1460 1470 1480 1490 1500
LNANKKIITT LKKQYDTKII NLGEGDNEIQ YDILGLEIKY QRSKYMKLGM
1510 1520 1530 1540 1550
EKSLTEKLPK LNVPLNPKGK KLRAPGQPGH YIDQDELEID EDEYKEKVHE
1560 1570 1580 1590 1600
MQKLIGLASY VGYKFRFDLL YYINTLAQHI LFPSRQVLDM TYELIQFIWN
1610 1620 1630 1640 1650
TRDKQLIWHK SKPVKPTNKL VVISDASYGN QPYYKSQIGN IYLLNGKVIG
1660 1670 1680 1690 1700
GKSTKASLTC TSTTEAEIHA VSEAIPLLNN LSHLVQELNK KPIIKGLLTD
1710 1720 1730 1740 1750
SRSTISIIKS TNEEKFRNRF FGTKAMRLRD EVSGNNLYVY YIETKMNIAD
1760 1770
VMTKPLPIKT FKLLTNKWIH
Note: Produced by +1 ribosomal frameshifting between codon Leu-431 and Gly-432 of the YDR261W-A ORF.
Length:1,770
Mass (Da):201,962
Last modified:November 1, 1996 - v1
<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:iC7D9F5E2103BD6F9
GO
Isoform Transposon Ty2-DR3 Gag polyprotein (identifier: Q99303-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry Q99303.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:438
Mass (Da):49,724
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 CAA92721 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z68329 Genomic DNA Translation: CAA92721.1 Sequence problems.
Z74387 Genomic DNA Translation: CAA98914.1
BK006938 Genomic DNA Translation: DAA12102.1

Protein sequence database of the Protein Information Resource

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PIRi
S69953

NCBI Reference Sequences

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RefSeqi
NP_058146.3, NM_001184423.4 [Q07791-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
851851

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR261W-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
Z68329 Genomic DNA Translation: CAA92721.1 Sequence problems.
Z74387 Genomic DNA Translation: CAA98914.1
BK006938 Genomic DNA Translation: DAA12102.1
PIRiS69953
RefSeqiNP_058146.3, NM_001184423.4 [Q07791-1]

3D structure databases

Database of comparative protein structure models

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ModBasei
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SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
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Protein-protein interaction databases

BioGridi32314, 7 interactors
DIPiDIP-8840N
IntActiQ07791, 3 interactors
STRINGi4932.YDR261W-B

Proteomic databases

PaxDbiQ07791
PRIDEiQ07791

Genome annotation databases

GeneIDi851851
KEGGisce:YDR261W-B

Organism-specific databases

EuPathDBiFungiDB:YDR261W-B
SGDiS000007397 YDR261W-B

Phylogenomic databases

HOGENOMiHOG000280731
InParanoidiQ07791

Family and domain databases

Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR025724 GAG-pre-integrase_dom
IPR001584 Integrase_cat-core
IPR039537 Retrotran_Ty1/copia-like
IPR015820 Retrotransposon_Ty1A_N
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
IPR013103 RVT_2
PANTHERiPTHR11439 PTHR11439, 1 hit
PfamiView protein in Pfam
PF13976 gag_pre-integrs, 1 hit
PF00665 rve, 1 hit
PF07727 RVT_2, 1 hit
PF01021 TYA, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS50994 INTEGRASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiYD23B_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: Q07791
Secondary accession number(s): D6VSP2, Q03934
<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: November 1, 1996
Last modified: September 18, 2019
This is version 135 of the entry and version 1 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

Complete proteome, Reference proteome, Transposable element

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
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