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UniProtKB - Q04214 (YM13B_YEAST)

Entry version 148 (18 Sep 2019)
Sequence version 2 (06 Mar 2007)
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Protein

Transposon Ty1-MR1 Gag-Pol polyprotein

Gene

TY1B-MR1

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 retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).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. Ty1 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 sitei461For protease activity; shared with dimeric partnerPROSITE-ProRule annotation1
<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 bindingi671Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi736Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi1346Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1427Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1428Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1610Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1652Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1685Magnesium; 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 Ty1-MR1 Gag-Pol polyprotein
Alternative name(s):
Gag-Pol-p199
TY1A-TY1B
Transposon Ty1 TYA-TYB polyprotein
p190
Cleaved into the following 4 chains:
Capsid protein
Short name:
CA
Alternative name(s):
Gag-p45
p54
Ty1 protease (EC:3.4.23.-)
Short name:
PR
Alternative name(s):
Pol-p20
p23
Integrase
Short name:
IN
Alternative name(s):
Pol-p71
p84
p90
Reverse transcriptase/ribonuclease H (EC:2.7.7.49, EC:2.7.7.7, EC:3.1.26.4)
Short name:
RT
Short name:
RT-RH
Alternative name(s):
Pol-p63
p60
<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:TY1B-MR1
Synonyms:YMRCTy1-3 POL
Ordered Locus Names:YMR045C
ORF Names:YM9532.10C
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YMR045C

Saccharomyces Genome Database

More...SGDi		S000004648 YMR045C

<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_00001995671 – 1755Transposon Ty1-MR1 Gag-Pol polyproteinAdd BLAST1755
ChainiPRO_00002791271 – 401Capsid proteinBy similarityAdd BLAST401
ChainiPRO_0000279128402 – 582Ty1 proteaseBy similarityAdd BLAST181
ChainiPRO_0000279129583 – 1217IntegraseBy similarityAdd BLAST635
ChainiPRO_00002791301218 – 1755Reverse 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 yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).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>Sitei401 – 402Cleavage; by Ty1 proteaseBy similarity2
Sitei582 – 583Cleavage; by Ty1 proteaseBy similarity2
Sitei1217 – 1218Cleavage; by Ty1 proteaseBy similarity2

Proteomic databases

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

More...PaxDbi		Q04214

PRoteomics IDEntifications database

More...PRIDEi		Q04214

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q04214

<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		35218, 11 interactors

Protein interaction database and analysis system

More...IntActi		Q04214, 4 interactors

Molecular INTeraction database

More...MINTi		Q04214

<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

3D structure databases

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

More...SMRi		Q04214

Database of comparative protein structure models

More...ModBasei		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>Domaini660 – 835Integrase catalyticPROSITE-ProRule annotationAdd BLAST176
Domaini1338 – 1476Reverse transcriptase Ty1/copia-typeAdd BLAST139
Domaini1610 – 1752RNase 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>Regioni299 – 401RNA-bindingBy similarityAdd BLAST103
Regioni583 – 640Integrase-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>Motifi1178 – 1212Bipartite 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		Q04214

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
IPR001969 Aspartic_peptidase_AS
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
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
PS00141 ASP_PROTEASE, 1 hit
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. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).By similarity
Isoform Transposon Ty1-MR1 Gag-Pol polyprotein (identifier: Q04214-1) [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
MESQQLSQHS PISHGSACAS VTSKEVQTTQ DPLDISASKT EECEKVSTQA 
        60         70         80         90        100
NSQQPTTPLS SAVPENHHHA SPQAAQVPLP QNGPYPQQRM MNTQQANISG 
       110        120        130        140        150
WPVYGHPSLM PYPPYQMSPM YAPPGAQSQF TQYPQYVGTH LNTPSPESGN 
       160        170        180        190        200
SFPDSSSAKS NMTSTNQHVR PPPILTSPND FLNWVKIYIK FLQNSNLGDI 
       210        220        230        240        250
IPTATRKAVR QMTDDELTFL CHTFQLFAPS QFLPPWVKDI LSVDYTDIMK 
       260        270        280        290        300
ILSKSINKMQ SDTQEVNDIT TLATLHYNGS TPADAFEAEV TNILDRLNNN 
       310        320        330        340        350
GIPINNKVAC QFIMRGLSGE YKFLRYARHR CIHMTVADLF SDIHSMYEEQ 
       360        370        380        390        400
QESKRNKSTH RRSPSDEKKD SRTYTNTTKP KSITRNSQKP NNSQSRTARA 
       410        420        430        440        450
HNVSTFNNSP GPDNDLIRGS TTEPIQLKNT HDLHLGQELT ESTVNHTNHS 
       460        470        480        490        500
DDKLPGHLLL DSGASRTLIR SAHHIHSASS NPDINVVDAQ KRNIPINAIG 
       510        520        530        540        550
DLQFHFQDNT KTSIKVLHTP NIAYDLLSLN ELAAVDITAC FTKNVLERSD 
       560        570        580        590        600
GTVLAPIVKY GDFYWVSKKY LLPSNISVPT INNVHTSEST RKYPYPFIHR 
       610        620        630        640        650
MLAHANAQTI RYSLKNNTIT YFNESDVDWS SAIDYQCPDC LIGKSTKHRH 
       660        670        680        690        700
IKGSRLKYQN SYEPFQYLHT DIFGPVHNLP KSAPSYFISF TDETTKFRWV 
       710        720        730        740        750
YPLHDRREDS ILDVFTTILA FIKNQFQASV LVIQMDRGSE YTNRTLHKFL 
       760        770        780        790        800
EKNGITPCYT TTADSRAHGV AERLNRTLLD DCRTQLQCSG LPNHLWFSAI 
       810        820        830        840        850
EFSTIVRNSL ASPKSKKSAR QHAGLAGLDI STLLPFGQPV IVNDHNPNSK 
       860        870        880        890        900
IHPRGIPGYA LHPSRNSYGY IIYLPSLKKT VDTTNYVILQ GKESRLDQFN 
       910        920        930        940        950
YDALTFDEDL NRLTASYHSF IASNEIQQSN DLNIESDHDF QSDIELHPEQ 
       960        970        980        990       1000
LRNVLSKAVS PTDSTPPSTH TEDSKRVSKT NIRAPREVDP NISESNILPS 
      1010       1020       1030       1040       1050
KKRSSTPQIS DIESTGSGGM HRLDVPLLAP MSQSNTHESS HASKSKDFRH 
      1060       1070       1080       1090       1100
SDSYSDNETN HTNVPISSTG GTNNKTVPQT SEQETEKRII HRSPSIDTSS 
      1110       1120       1130       1140       1150
SESNSLHHVV PIKTSDTCPK ENTEESIIAD LPLPDLPPEP PTELSDSFKE 
      1160       1170       1180       1190       1200
LPPINSRQTN SSLGGIGDSN AYTTINSKKR SLEDNETEIK VSRDTWNTKN 
      1210       1220       1230       1240       1250
MRSLEPPRSK KRIHLIAAVK AVKSIKPIRT TLRYDEAITY NKDIKEKEKY 
      1260       1270       1280       1290       1300
IEAYHKEVNQ LLKMKTWDTD KYYDRKEIDP KRVINSMFIF NRKRDGTHKA 
      1310       1320       1330       1340       1350
RFVARGDIQH PDTYDSGMQS NTVHHYALMT SLSLALDNNY YITQLDISSA 
      1360       1370       1380       1390       1400
YLYADIKEEL YIRPPPHLGM NDKLIRLKKS LYGLKQSGAN WYETIKSYLI 
      1410       1420       1430       1440       1450
KQCGMEEVRG WSCVFENSQV TICLFVDDMV LFSKNLNSNK RIIDKLKMQY 
      1460       1470       1480       1490       1500
DTKIINLGES DEEIQYDILG LEIKYQRGKY MKLGMENSLT EKIPKLNVPL 
      1510       1520       1530       1540       1550
NPKGRKLSAP GQPGLYIDQQ ELELEEDDYK MKVHEMQKLI GLASYVGYKF 
      1560       1570       1580       1590       1600
RFDLLYYINT LAQHILFPSK QVLDMTYELI QFIWNTRDKQ LIWHKSKPVK 
      1610       1620       1630       1640       1650
PTNKLVVISD ASYGNQPYYK SQIGNIYLLN GKVIGGKSTK ASLTCTSTTE 
      1660       1670       1680       1690       1700
AEIHAISESV PLLNNLSYLI QELDKKPITK GLLTDSKSTI SIIISNNEEK 
      1710       1720       1730       1740       1750
FRNRFFGTKA MRLRDEVSGN HLHVCYIETK KNIADVMTKP LPIKTFKLLT 

NKWIH
Note: Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YMR046C ORF.
Length:1,755
Mass (Da):198,899
Last modified:March 6, 2007 - v2
<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:i4B3B4D4AB68D3FBA
GO
Isoform Transposon Ty1-MR1 Gag polyprotein (identifier: Q04215-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry Q04215.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.
Length:440
Mass (Da):49,274
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 CAA88411 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
Z48502 Genomic DNA Translation: CAA88411.1 Sequence problems.
BK006946 Genomic DNA Translation: DAA09944.1

Protein sequence database of the Protein Information Resource

More...PIRi		S40969
S52894

NCBI Reference Sequences

More...RefSeqi		NP_013759.1, NM_001182542.2 [Q04214-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		855062

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YMR045C

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
Z48502 Genomic DNA Translation: CAA88411.1 Sequence problems.
BK006946 Genomic DNA Translation: DAA09944.1
PIRiS40969
S52894
RefSeqiNP_013759.1, NM_001182542.2 [Q04214-1]

3D structure databases

SMRiQ04214
ModBaseiSearch...

Protein-protein interaction databases

BioGridi35218, 11 interactors
IntActiQ04214, 4 interactors
MINTiQ04214

PTM databases

iPTMnetiQ04214

Proteomic databases

PaxDbiQ04214
PRIDEiQ04214

Genome annotation databases

GeneIDi855062
KEGGisce:YMR045C

Organism-specific databases

EuPathDBiFungiDB:YMR045C
SGDiS000004648 YMR045C

Phylogenomic databases

HOGENOMiHOG000280731
InParanoidiQ04214

Family and domain databases

Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
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
PF00665 rve, 1 hit
PF07727 RVT_2, 1 hit
PF01021 TYA, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS00141 ASP_PROTEASE, 1 hit
PS50994 INTEGRASE, 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 nameiYM13B_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: Q04214
Secondary accession number(s): D6VZM0
<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: November 1, 1997
Last sequence update: March 6, 2007
Last modified: September 18, 2019
This is version 148 of the entry and version 2 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 chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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