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 124 (07 Apr 2021)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Ribosome-associated inhibitor A

Gene

raiA

Organism
Escherichia coli (strain K12)
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

During stationary phase prevents 70S dimer formation, probably in order to regulate translation efficiency during transition between the exponential and the stationary phases (PubMed:16324148). During environmental stress such as cold shock or excessive cell density at stationary phase, stabilizes the 70S ribosome against dissociation, inhibits translation elongation and increases translation accuracy (PubMed:11375931, PubMed:15219834). When normal growth conditions are restored, is quickly released from the ribosome (PubMed:11375931). Has been suggested to inhibit translation elongation by blocking the A-site (aminoacyl-tRNA site) (PubMed:11375931). Has also been suggested to inhibit translation initiation by blocking the A-site and P-site (peptidyl-tRNA site) of the ribosome (PubMed:15502846, PubMed:23420694). At 15 degrees Celsius binds 30S subunits and stimulates their association with 50S subunits into idle 70S ribosomes (PubMed:23420694). Crystallization with T.thermophilus 70S ribosomes shows it binds in the channel between the head and body of the 30S subunit, where mRNA, tRNAs, initiation factors IF1 and IF3 and elongation factor G would bind; this protein's extended tail follows the mRNA channel and probably prevents RMF binding, which would prevent ribosome dimerization (PubMed:22605777). This protein also stabilizes the 30S head relative to the rest of the ribosome, which may also prevent dimerization (PubMed:22605777). Counteracts miscoding (translation errors) particularly efficiently at magnesium concentrations close to those observed in vivo but less efficiently at higher concentrations (PubMed:15219834). Counteraction of miscoding was shown to be stronger than inhibition of translation, suggesting that the former activity could be the main function of this protein in vivo (PubMed:15219834).8 Publications

<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, rRNA-binding
Biological processStress response, Translation regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG11151-MONOMER

<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:
Ribosome-associated inhibitor A1 Publication
Alternative name(s):
Protein Y1 Publication
Short name:
pY1 Publication
Ribosome associated factor Y1 Publication
Spot Y1 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:raiA1 Publication
Synonyms:yfiACurated
Ordered Locus Names:b2597, JW2578
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 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

<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

Non-essential gene, increased formation of inactive 100S ribosomes in stationary phase, which persist longer than in wild-type. Double hpr-yfiA deletion mutants form 90S ribosomes (PubMed:16324148). A quadruple yfiA-hpf-rmf-sra knockout strain is significantly outcompeted by wild-type after 4 days growth (PubMed:17277072). No visible effect on viability or growth rate at 37 or 10 degrees Celsius, slight effect on bulk translation and timing of expression of some cold-shock proteins (PubMed:23420694).3 Publications

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved4 Publications
<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_00001692612 – 113Ribosome-associated inhibitor AAdd BLAST112

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei66N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AD49

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

More...
PaxDbi
P0AD49

PRoteomics IDEntifications database

More...
PRIDEi
P0AD49

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0AD49

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0AD49

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

During stationary phase (at protein level) (PubMed:11168583, PubMed:11375931). Also by cold stress, remains ribosome-associated for the 4 hours tested, then disappears when cells are warmed (at protein level) (PubMed:11375931, PubMed:23420694).3 Publications

<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

Associates mainly with 70S ribosomes (PubMed:11168583, PubMed:11375931). Localized at the surface of the 30S ribosomal subunit, at the interface with the 50S subunit (PubMed:10535924, PubMed:15502846, PubMed:22605777). Binds across the channel in the 30S subunit where tRNAs and mRNA interact during protein biosynthesis (PubMed:15502846, PubMed:22605777). Can also associate with 100S ribosomes, which are inactive dimers of 70S ribosomes (PubMed:11168583). Contacts modifed methylated residues of 16S rRNA (in complex with T.thermophilus ribosome, 2/3 residues are also modified in E.coli) (PubMed:25775268).

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261618, 36 interactors
851463, 2 interactors

Database of interacting proteins

More...
DIPi
DIP-36014N

Protein interaction database and analysis system

More...
IntActi
P0AD49, 7 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2597

<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

1113
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P0AD49

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

More...
SMRi
P0AD49

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
P0AD49

<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>Regioni23 – 26Interaction with 16S rRNA1 Publication4
Regioni83 – 91Interaction with 16S rRNA1 Publication9

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG1544, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_071472_3_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AD49

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AD49

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00552, RaiA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.160.100, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036567, RHF-like
IPR003489, RHF/RaiA

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02482, Ribosomal_S30AE, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF69754, SSF69754, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00741, yfiA, 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.

<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 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.

P0AD49-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTMNITSKQM EITPAIRQHV ADRLAKLEKW QTHLINPHII LSKEPQGFVA
60 70 80 90 100
DATINTPNGV LVASGKHEDM YTAINELINK LERQLNKLQH KGEARRAATS
110
VKDANFVEEV EEE
Length:113
Mass (Da):12,785
Last modified:January 23, 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:i562901F819836A87
GO

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 12640 Da. Determined by MALDI. 1 Publication

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
M10431 Genomic DNA Translation: AAA24328.1
Z70523 Genomic DNA Translation: CAA94436.1
U00096 Genomic DNA Translation: AAC75646.1
AP009048 Genomic DNA Translation: BAA16481.1
M58024 Genomic DNA Translation: AAA62782.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A30275, Q5ECPA

NCBI Reference Sequences

More...
RefSeqi
NP_417088.1, NC_000913.3
WP_000178456.1, NZ_STEB01000040.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75646; AAC75646; b2597
BAA16481; BAA16481; BAA16481

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
58463062
947129

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2578
eco:b2597

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4141

<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
M10431 Genomic DNA Translation: AAA24328.1
Z70523 Genomic DNA Translation: CAA94436.1
U00096 Genomic DNA Translation: AAC75646.1
AP009048 Genomic DNA Translation: BAA16481.1
M58024 Genomic DNA Translation: AAA62782.1
PIRiA30275, Q5ECPA
RefSeqiNP_417088.1, NC_000913.3
WP_000178456.1, NZ_STEB01000040.1

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
1L4SNMR-A2-113[»]
1N3GNMR-A1-113[»]
4V4GX-ray11.50a2-91[»]
4V8IX-ray2.70AY/CY1-113[»]
4Y4OX-ray2.301y/2y1-113[»]
5FDUX-ray2.901x/2x2-98[»]
5FDVX-ray2.801x/2x2-98[»]
5V8IX-ray3.251y/2y1-113[»]
6CFKX-ray2.701y/2y1-113[»]
6FKRX-ray3.201z/2z2-98[»]
6XHXX-ray2.551y/2y1-113[»]
BMRBiP0AD49
SMRiP0AD49
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261618, 36 interactors
851463, 2 interactors
DIPiDIP-36014N
IntActiP0AD49, 7 interactors
STRINGi511145.b2597

PTM databases

iPTMnetiP0AD49

2D gel databases

SWISS-2DPAGEiP0AD49

Proteomic databases

jPOSTiP0AD49
PaxDbiP0AD49
PRIDEiP0AD49

Genome annotation databases

EnsemblBacteriaiAAC75646; AAC75646; b2597
BAA16481; BAA16481; BAA16481
GeneIDi58463062
947129
KEGGiecj:JW2578
eco:b2597
PATRICifig|1411691.4.peg.4141

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB1140

Phylogenomic databases

eggNOGiCOG1544, Bacteria
HOGENOMiCLU_071472_3_0_6
InParanoidiP0AD49
PhylomeDBiP0AD49

Enzyme and pathway databases

BioCyciEcoCyc:EG11151-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0AD49

Protein Ontology

More...
PROi
PR:P0AD49

Family and domain databases

CDDicd00552, RaiA, 1 hit
Gene3Di3.30.160.100, 1 hit
InterProiView protein in InterPro
IPR036567, RHF-like
IPR003489, RHF/RaiA
PfamiView protein in Pfam
PF02482, Ribosomal_S30AE, 1 hit
SUPFAMiSSF69754, SSF69754, 1 hit
TIGRFAMsiTIGR00741, yfiA, 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 nameiYFIA_ECOLI
<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: P0AD49
Secondary accession number(s): P11285
<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, 2005
Last sequence update: January 23, 2007
Last modified: April 7, 2021
This is version 124 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 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, Direct protein sequencing, Reference proteome

Documents

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