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Entry version 98 (02 Jun 2021)
Sequence version 1 (05 Jul 2004)
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Protein

tRNA-5-methyluridine(54) 2-sulfurtransferase

Gene

ttuA

Organism
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
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

Catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m5s2U or s2T) (PubMed:16547008, PubMed:28439027).

This modification allows thermal stabilization of tRNAs in thermophilic microorganisms, and is required for cell growth at high temperatures (PubMed:16547008).

TtuA transfers the S atom from the thiocarboxylated C-terminus of TtuB to tRNA (PubMed:28439027).

2 Publications

Miscellaneous

The thiolation reaction consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by thiocarboxylated TtuB for the adenyl group. However, it is not clear if the S-transfer mechanism is direct or indirect.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Enzymatic activity may be regulated by TtuB conjugation.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tRNA modification

This protein is involved in tRNA modification.1 Publication
View all proteins of this organism that are known to be involved in tRNA modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi3Zinc 1Combined sources1 Publication1
Metal bindingi6Zinc 1Combined sources1 Publication1
Metal bindingi22Zinc 1Combined sources1 Publication1
Metal bindingi25Zinc 1; via pros nitrogenCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei59ATPCombined sources1 Publication1
Binding sitei79ATP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Metal bindingi130Iron-sulfur (4Fe-4S)Combined sources1 Publication1
Metal bindingi133Iron-sulfur (4Fe-4S)Combined sources1 Publication1
Binding sitei156ATP; via amide nitrogenCombined sources1 Publication1
Binding sitei161ATPCombined sources1 Publication1
Metal bindingi222Iron-sulfur (4Fe-4S)Combined sources1 Publication1
Metal bindingi274Zinc 2Combined sources1 Publication1
Metal bindingi277Zinc 2Combined sources1 Publication1
Metal bindingi286Zinc 2Combined sources1 Publication1
Metal bindingi289Zinc 2Combined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi53 – 55ATPCombined sources1 Publication3

<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 functionRNA-binding, Transferase, tRNA-binding
Biological processtRNA processing
Ligand4Fe-4S, ATP-binding, Iron, Iron-sulfur, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-20129

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.8.1.15, 2305

<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%5Fand%5Ftaxonomy%5Fsection">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-5-methyluridine(54) 2-sulfurtransferase1 Publication (EC:2.8.1.151 Publication1 Publication)
Alternative name(s):
2-thiouridine synthetase TtuA1 Publication
tRNA two-thiouridine-synthesizing protein A1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ttuA1 Publication
Ordered Locus Names:TT_C0106Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiThermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri262724 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000592 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

<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

Disruption of this gene completely abolishes the presence of m5s2U in tRNAs, although its precursor, 5-methyluridine (ribothymidine) is present; other nucleoside modifications remain unchanged. These deletion mutants exhibit a temperature-sensitive phenotype, they are unable to grow above 80 degrees Celsius.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi58K → A: About 40% decrease in catalytic activity. 1 Publication1
Mutagenesisi59D → A: Complete loss of catalytic activity. 1 Publication1
Mutagenesisi130C → S: Decrease in Fe content, and about 90% decrease in catalytic activity. 2 Publications1
Mutagenesisi133C → S: Decrease in Fe content, and almost complete loss of catalytic activity. 2 Publications1
Mutagenesisi157H → A: Slight decrease in catalytic activity. 1 Publication1
Mutagenesisi158N → A: Slight decrease in catalytic activity. 1 Publication1
Mutagenesisi161D → A: Complete loss of catalytic activity. 1 Publication1
Mutagenesisi203E → A: About 80% decrease in catalytic activity. 1 Publication1
Mutagenesisi222C → S: Decrease in Fe content, and almost complete loss of catalytic activity. 2 Publications1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004423631 – 321tRNA-5-methyluridine(54) 2-sulfurtransferaseAdd BLAST321

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in TtuB)1 Publication
Cross-linki226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in TtuB)1 Publication
Cross-linki229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in TtuB)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Conjugated to TtuB via covalent linkages involving Lys-137, Lys-226 and Lys-229.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q72LF3

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:28439027). Is able to form a heterocomplex with TtuB (PubMed:16547008, PubMed:28439027).

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
262724.TT_C0106

<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

1321
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
Q72LF3

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

<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 TtcA family. TtuA subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0037, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_026481_1_1_0

Identification of Orthologs from Complete Genome Data

More...
OMAi
PCKACVL

Database of Orthologous Groups

More...
OrthoDBi
1051352at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.620, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000541, Ncs6/Tuc1/Ctu1
IPR014729, Rossmann-like_a/b/a_fold
IPR011063, TilS/TtcA_N
IPR035107, tRNA_thiolation_TtcA_Ctu1

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01171, ATP_bind_3, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF004976, ATPase_YdaO, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00269, TIGR00269, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q72LF3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVCKVCGQKA QVEMRSRGLA LCREHYLDWF VKETERAIRR HRMLLPGERV
60 70 80 90 100
LVAVSGGKDS LALWDVLSRL GYQAVGLHIE LGIGEYSKRS LEVTQAFARE
110 120 130 140 150
RGLELLVVDL KEAYGFGVPE LARLSGRVAC SACGLSKRYI INQVAVEEGF
160 170 180 190 200
RVVATGHNLD DEAAVLFGNL LNPQEETLSR QGPVLPEKPG LAARVKPFYR
210 220 230 240 250
FSEREVLSYT LLRGIRYLHE ECPNAKGAKS LLYKEALNLV ERSMPGAKLR
260 270 280 290 300
FLDGFLEKIR PRLDVGEEVA LRECERCGYP TTGAVCAFCR MWDAVYRRAK
310 320
KRKLLPEEVS FRPRVKPLRA G
Length:321
Mass (Da):36,194
Last modified:July 5, 2004 - 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:i2DB12E870BFA5314
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
AE017221 Genomic DNA Translation: AAS80454.1

NCBI Reference Sequences

More...
RefSeqi
WP_011172563.1, NC_005835.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAS80454; AAS80454; TT_C0106

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
tth:TT_C0106

<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
AE017221 Genomic DNA Translation: AAS80454.1
RefSeqiWP_011172563.1, NC_005835.1

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
5B4EX-ray2.70A1-321[»]
5B4FX-ray2.75A1-321[»]
5GHAX-ray2.50A/B/C/D1-321[»]
SMRiQ72LF3
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi262724.TT_C0106

Proteomic databases

PRIDEiQ72LF3

Genome annotation databases

EnsemblBacteriaiAAS80454; AAS80454; TT_C0106
KEGGitth:TT_C0106

Phylogenomic databases

eggNOGiCOG0037, Bacteria
HOGENOMiCLU_026481_1_1_0
OMAiPCKACVL
OrthoDBi1051352at2

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-20129
BRENDAi2.8.1.15, 2305

Family and domain databases

Gene3Di3.40.50.620, 1 hit
InterProiView protein in InterPro
IPR000541, Ncs6/Tuc1/Ctu1
IPR014729, Rossmann-like_a/b/a_fold
IPR011063, TilS/TtcA_N
IPR035107, tRNA_thiolation_TtcA_Ctu1
PfamiView protein in Pfam
PF01171, ATP_bind_3, 1 hit
PIRSFiPIRSF004976, ATPase_YdaO, 1 hit
TIGRFAMsiTIGR00269, TIGR00269, 1 hit

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 nameiTTUA_THET2
<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: Q72LF3
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2017
Last sequence update: July 5, 2004
Last modified: June 2, 2021
This is version 98 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 programProkaryotic 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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