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Entry version 136 (26 Feb 2020)
Sequence version 1 (01 May 2000)
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Protein

Threonine--tRNA ligase

Gene

thrS

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Status
Reviewed-Annotation score:

Annotation score:4 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 attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (Probable). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain (PubMed:16902403, PubMed:21098258). Deacylates correctly charged glycyl-tRNA(Gly), but neither glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA(Thr) adenine 76 has been replaced by hydrogen) nor the 2'-fluoro tRNA derivative do so, strongly suggesting the editing function is tRNA catalyzed (PubMed:26113036).3 Publications

<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

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

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 bindingi298ZincUniRule annotation1
Metal bindingi350Zinc; via tele nitrogenUniRule annotation1
Metal bindingi474Zinc; via pros nitrogenUniRule 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 functionAminoacyl-tRNA synthetase, Ligase, RNA-binding, tRNA-binding
Biological processProtein biosynthesis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
PABY272844:G1GT8-1473-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.1.1.3 5242

<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:
Threonine--tRNA ligaseUniRule annotation (EC:6.1.1.3UniRule annotation)
Alternative name(s):
Threonyl-tRNA synthetaseUniRule annotation
Short name:
ThrRSUniRule annotation
<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:thrSUniRule annotation
Ordered Locus Names:PYRAB13430
ORF Names:PAB1490
<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>OrganismiPyrococcus abyssi (strain GE5 / Orsay)
<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 identifieri272844 [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 lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
<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
  • UP000000810 <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
  • UP000009139 Componenti: Chromosome

<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

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%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>Mutagenesisi83H → A: Isolated domain has decreased to no deacylation of mischarged L-seryl-tRNA(Thr). Deacylates correctly charged glycyl-tRNA(Gly). 2 Publications1
Mutagenesisi120Y → A: Isolated domain has nearly wild-type deacylation of mischarged L-seryl-tRNA(Thr), no longer binds L-Ser or L-Cys. No activity on threonyl-tRNA(Thr). Same results; when associated with A-134. 2 Publications1
Mutagenesisi121K → M: Isolated domain has nearly wild-type deacylation of mischarged L-seryl-tRNA(Thr). Later shown not to deacylate L-seryl-tRNA(Thr), no activity on L-threonyl-tRNA(Thr). 2 Publications1
Mutagenesisi121K → S: Isolated domain does not deacylate mischarged L-seryl-tRNA(Thr). 1 Publication1
Mutagenesisi134E → A: Isolated domain has nearly wild-type deacylation of mischarged L-seryl-tRNA(Thr). No activity on L-threonyl-tRNA(Thr). Same results; when associated with A-120. 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_00001011071 – 625Threonine--tRNA ligaseAdd BLAST625

<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.

UniRule annotation

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
272844.PAB1490

<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

1625
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
Q9UZ14

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9UZ14

<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>Regioni1 – 143Editing domainUniRule annotation4 PublicationsAdd BLAST143
Regioni206 – 505CatalyticUniRule annotationAdd BLAST300

<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 N-terminal domain (about residues 1-143) is an archaea-specific tRNA-editing domain (PubMed:16902403) that has a highly similar structure to Dtd (D-aminoacyl-tRNA deacylase); the domain binds L-serine and L-cysteine and most D-amino acids but not L-threonine (PubMed:15908961, PubMed:16902403). Editing of incorrectly charged L-seryl-tRNA(Thr) by this domain is tRNA catalyzed (PubMed:16902403, PubMed:21098258, PubMed:26113036).4 Publications

<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 class-II aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
arCOG00401 Archaea
COG0441 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_029833_0_0_2

KEGG Orthology (KO)

More...
KOi
K01868

Identification of Orthologs from Complete Genome Data

More...
OMAi
SCKGHPL

Database of Orthologous Groups

More...
OrthoDBi
11656at2157

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00771 ThrRS_core, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.800, 1 hit
3.50.80.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00184 Thr_tRNA_synth, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002314 aa-tRNA-synt_IIb
IPR006195 aa-tRNA-synth_II
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR023509 DTD-like_sf
IPR002320 Thr-tRNA-ligase_IIa
IPR015011 Threonyl-tRNA_syn_edit_dom_arc
IPR033728 ThrRS_core

The PANTHER Classification System

More...
PANTHERi
PTHR11451 PTHR11451, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03129 HGTP_anticodon, 1 hit
PF00587 tRNA-synt_2b, 1 hit
PF08915 tRNA-Thr_ED, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01047 TRNASYNTHTHR

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00418 thrS, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50862 AA_TRNA_LIGASE_II, 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.

Q9UZ14-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRVLLIHSDY IEYEVKDKAL KNPEPISEDM KRGRMEEVLV AFISVEKVDE
60 70 80 90 100
KNPEEVSLKA IEEISKVAEQ VKAENVFVYP FAHLSSELAK PSVAMDILNR
110 120 130 140 150
VYQGLKERGF NVGKAPFGYY KAFKISCKGH PLAELSRTIV PEEARVEEVP
160 170 180 190 200
EALRKEEEEL VSYWYILTPE GELIEVDKFD FTGYENLRKF VNYEIAKNRI
210 220 230 240 250
AEKEPPHVKL MLEHELVDYE PGSDPGNLRY YPKGRLIKSL LEQYVTEKVI
260 270 280 290 300
EYGAMEVETP IMYDFEHPAL EKYLNRFPAR QYIVLSGDKR YFLRFAACFG
310 320 330 340 350
QFMIKKDAII SYRNLPLRMY ELTRYSFRRE KRGELSGLRR LRAFTMPDMH
360 370 380 390 400
TLAKDIEQAK EEFKKQFKLS MEVLEGVGLT PEDYEVAIRF TEDFWKEHKD
410 420 430 440 450
FIVELVKLIG KPVLIEMWKQ RFFYFILKFE FNFVDNLDKA AALSTVQIDV
460 470 480 490 500
ENAERFGITY YDENGEEKYP LILHCSPSGA IERVMYAILE KQAKLMNEGK
510 520 530 540 550
KPMFPLWLSP IQVRVIPVSE EYLDYALYVA GKLEGAKIRV DVDDEDERLN
560 570 580 590 600
KKIRRAEKEW IPYIVVVGAR EKENGTITVR RREDGKQYET RIEELIKEIK
610 620
EKTEGFPYKP RPLPLLLSKR PKFRG
Length:625
Mass (Da):73,372
Last modified:May 1, 2000 - 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:iAF8E48AAE789124F
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
AJ248287 Genomic DNA Translation: CAB50248.1
HE613800 Genomic DNA Translation: CCE70785.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C75044

NCBI Reference Sequences

More...
RefSeqi
WP_010868458.1, NC_000868.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB50248; CAB50248; PAB1490

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1496731

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
pab:PAB1490

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|272844.11.peg.1427

<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
AJ248287 Genomic DNA Translation: CAB50248.1
HE613800 Genomic DNA Translation: CCE70785.1
PIRiC75044
RefSeqiWP_010868458.1, NC_000868.1

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
1Y2QX-ray1.95A1-143[»]
2HKZX-ray2.10A1-143[»]
2HL0X-ray1.86A1-143[»]
2HL1X-ray2.25A/B1-147[»]
2HL2X-ray2.60A/B1-143[»]
3PD2X-ray1.86A/B1-147[»]
3PD3X-ray1.86A/B1-147[»]
3PD4X-ray2.40A/B1-147[»]
3PD5X-ray2.29A/B1-147[»]
4RRQX-ray1.79A/B1-147[»]
4RRRX-ray1.86A/B1-147[»]
4S02X-ray1.95A1-143[»]
4S03X-ray2.05A1-143[»]
4S0IX-ray2.36A1-143[»]
4S0JX-ray2.10A1-143[»]
4S0KX-ray2.10A1-143[»]
4S0LX-ray2.50A1-143[»]
SMRiQ9UZ14
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi272844.PAB1490

Genome annotation databases

EnsemblBacteriaiCAB50248; CAB50248; PAB1490
GeneIDi1496731
KEGGipab:PAB1490
PATRICifig|272844.11.peg.1427

Phylogenomic databases

eggNOGiarCOG00401 Archaea
COG0441 LUCA
HOGENOMiCLU_029833_0_0_2
KOiK01868
OMAiSCKGHPL
OrthoDBi11656at2157

Enzyme and pathway databases

BioCyciPABY272844:G1GT8-1473-MONOMER
BRENDAi6.1.1.3 5242

Miscellaneous databases

EvolutionaryTraceiQ9UZ14

Family and domain databases

CDDicd00771 ThrRS_core, 1 hit
Gene3Di3.40.50.800, 1 hit
3.50.80.10, 1 hit
HAMAPiMF_00184 Thr_tRNA_synth, 1 hit
InterProiView protein in InterPro
IPR002314 aa-tRNA-synt_IIb
IPR006195 aa-tRNA-synth_II
IPR004154 Anticodon-bd
IPR036621 Anticodon-bd_dom_sf
IPR023509 DTD-like_sf
IPR002320 Thr-tRNA-ligase_IIa
IPR015011 Threonyl-tRNA_syn_edit_dom_arc
IPR033728 ThrRS_core
PANTHERiPTHR11451 PTHR11451, 1 hit
PfamiView protein in Pfam
PF03129 HGTP_anticodon, 1 hit
PF00587 tRNA-synt_2b, 1 hit
PF08915 tRNA-Thr_ED, 1 hit
PRINTSiPR01047 TRNASYNTHTHR
TIGRFAMsiTIGR00418 thrS, 1 hit
PROSITEiView protein in PROSITE
PS50862 AA_TRNA_LIGASE_II, 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 nameiSYT_PYRAB
<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: Q9UZ14
Secondary accession number(s): G8ZHE8
<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: June 20, 2001
Last sequence update: May 1, 2000
Last modified: February 26, 2020
This is version 136 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
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