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 159 (16 Oct 2019)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial

Gene

QRI7

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

Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t6A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.UniRule annotation3 Publications

Miscellaneous

Present with 1400 molecules/cell in log phase SD medium.1 Publication

<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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

a divalent metal cationUniRule annotation2 PublicationsNote: Binds 1 divalent metal cation per subunit.UniRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bindingi145Divalent metal cationUniRule annotation1 Publication1
Metal bindingi149Divalent metal cationUniRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei203SubstrateUniRule annotation1 Publication1
Binding sitei217Substrate; via amide nitrogenUniRule annotation1 Publication1
Binding sitei221SubstrateUniRule annotation1 Publication1
Binding sitei360SubstrateUniRule annotation1 Publication1
Metal bindingi361Divalent metal cationUniRule annotation1 Publication1

<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 functionAcyltransferase, Transferase
Biological processtRNA processing
LigandMetal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YDL104C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.6.99.4 984

<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:
tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrialUniRule annotation (EC:2.3.1.234UniRule annotation1 Publication)
Alternative name(s):
N6-L-threonylcarbamoyladenine synthaseUniRule annotation
Short name:
t(6)A synthaseUniRule annotation
t(6)A37 threonylcarbamoyladenosine biosynthesis protein QRI7UniRule annotation
tRNA threonylcarbamoyladenosine biosynthesis protein QRI7UniRule annotation
<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:QRI7
Ordered Locus Names:YDL104C
ORF Names:D2366
<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:YDL104C

Saccharomyces Genome Database

More...
SGDi
S000002262 QRI7

<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

Mitochondrion

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of QRI7 leads to the formation of mitochondria with abnormal morphology and no DNA.1 Publication

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>Mutagenesisi39E → A: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi43D → A: Severely impairs t(6)A37 formation. No effect on dimer formation. 1 Publication1
Mutagenesisi44D → A: Severely impairs t(6)A37 formation. No effect on dimer formation. 1 Publication1
Mutagenesisi77I → E: Severely impairs t(6)A37 formation. No effect on dimer formation. 1 Publication1
Mutagenesisi104R → A: Reduces enzyme activity by 35%. Partially impairs dimer formation. 1 Publication1
Mutagenesisi130K → A: Severely impairs t(6)A37 formation. Partially impairs dimer formation. 1 Publication1
Mutagenesisi134V → R: Severely impairs t(6)A37 formation. Prevents dimerization. 1 Publication1
Mutagenesisi145H → A: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi149H → A: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi172S → K: Severely impairs t(6)A37 formation. 1 Publication1
Mutagenesisi207R → A: Severely impairs t(6)A37 formation. No effect on dimer formation. 1 Publication1
Mutagenesisi258S → A: Severely impairs t(6)A37 formation. No effect on dimer formation. 1 Publication1
Mutagenesisi361D → A: Severely impairs t(6)A37 formation. 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 ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 30MitochondrionUniRule annotationAdd BLAST30
<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_000009698831 – 407tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrialUniRule annotationAdd BLAST377

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P43122

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

More...
PaxDbi
P43122

PRoteomics IDEntifications database

More...
PRIDEi
P43122

<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

Homodimer.

UniRule annotation2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31958, 176 interactors

Database of interacting proteins

More...
DIPi
DIP-5028N

Protein interaction database and analysis system

More...
IntActi
P43122, 1 interactor

STRING: functional protein association networks

More...
STRINGi
4932.YDL104C

<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

1407
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
P43122

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

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>Regioni170 – 174Substrate bindingUniRule annotation1 Publication5
Regioni328 – 329Substrate bindingUniRule annotation1 Publication2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the KAE1 / TsaD family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000109570

KEGG Orthology (KO)

More...
KOi
K01409

Identification of Orthologs from Complete Genome Data

More...
OMAi
VPRLKMK

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01445 TsaD, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000905 Gcp-like_dom
IPR017861 KAE1/TsaD
IPR017860 Peptidase_M22_CS
IPR022450 TsaD

The PANTHER Classification System

More...
PANTHERi
PTHR11735 PTHR11735, 1 hit
PTHR11735:SF6 PTHR11735:SF6, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00814 Peptidase_M22, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00789 OSIALOPTASE

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00329 gcp_kae1, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01016 GLYCOPROTEASE, 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>Sequencei

<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.

P43122-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MISIKGTGRF LLDNYRIWQR RAFNRPIQLR KGYKVLAIET SCDDTCVSVL
60 70 80 90 100
DRFSKSAAPN VLANLKDTLD SIDEGGIIPT KAHIHHQARI GPLTERALIE
110 120 130 140 150
SNAREGIDLI CVTRGPGMPG SLSGGLDFAK GLAVAWNKPL IGVHHMLGHL
160 170 180 190 200
LIPRMGTNGK VPQFPFVSLL VSGGHTTFVL SRAIDDHEIL CDTIDIAVGD
210 220 230 240 250
SLDKCGRELG FKGTMIAREM EKFINQDIND QDFALKLEMP SPLKNSASKR
260 270 280 290 300
NMLSFSFSAF ITALRTNLTK LGKTEIQELP EREIRSIAYQ VQESVFDHII
310 320 330 340 350
NKLKHVLKSQ PEKFKNVREF VCSGGVSSNQ RLRTKLETEL GTLNSTSFFN
360 370 380 390 400
FYYPPMDLCS DNSIMIGWAG IEIWESLRLV SDLDICPIRQ WPLNDLLSVD

GWRTDQL
Length:407
Mass (Da):45,543
Last modified:November 1, 1995 - 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:i328A21F239D6DB25
GO

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
X79380 Genomic DNA Translation: CAA55926.1
X95644 Genomic DNA Translation: CAA64909.1
Z74152 Genomic DNA Translation: CAA98671.1
BK006938 Genomic DNA Translation: DAA11756.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S50740

NCBI Reference Sequences

More...
RefSeqi
NP_010179.1, NM_001180163.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDL104C_mRNA; YDL104C; YDL104C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851454

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDL104C

<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
X79380 Genomic DNA Translation: CAA55926.1
X95644 Genomic DNA Translation: CAA64909.1
Z74152 Genomic DNA Translation: CAA98671.1
BK006938 Genomic DNA Translation: DAA11756.1
PIRiS50740
RefSeqiNP_010179.1, NM_001180163.1

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
3WUHX-ray2.94A/B30-407[»]
4K25X-ray2.88A30-407[»]
SMRiP43122
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31958, 176 interactors
DIPiDIP-5028N
IntActiP43122, 1 interactor
STRINGi4932.YDL104C

Proteomic databases

MaxQBiP43122
PaxDbiP43122
PRIDEiP43122

Genome annotation databases

EnsemblFungiiYDL104C_mRNA; YDL104C; YDL104C
GeneIDi851454
KEGGisce:YDL104C

Organism-specific databases

EuPathDBiFungiDB:YDL104C
SGDiS000002262 QRI7

Phylogenomic databases

HOGENOMiHOG000109570
KOiK01409
OMAiVPRLKMK

Enzyme and pathway databases

BioCyciYEAST:YDL104C-MONOMER
BRENDAi2.6.99.4 984

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P43122

Family and domain databases

HAMAPiMF_01445 TsaD, 1 hit
InterProiView protein in InterPro
IPR000905 Gcp-like_dom
IPR017861 KAE1/TsaD
IPR017860 Peptidase_M22_CS
IPR022450 TsaD
PANTHERiPTHR11735 PTHR11735, 1 hit
PTHR11735:SF6 PTHR11735:SF6, 1 hit
PfamiView protein in Pfam
PF00814 Peptidase_M22, 1 hit
PRINTSiPR00789 OSIALOPTASE
TIGRFAMsiTIGR00329 gcp_kae1, 1 hit
PROSITEiView protein in PROSITE
PS01016 GLYCOPROTEASE, 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 nameiQRI7_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: P43122
Secondary accession number(s): D6VRP6
<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, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2019
This is version 159 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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