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Entry version 155 (31 Jul 2019)
Sequence version 1 (01 Jun 1994)
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Protein

Dual-specificity RNA methyltransferase RlmN

Gene

rlmN

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

Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation.3 Publications

Miscellaneous

Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue. In details, the methyl group from one SAM molecule is initially transferred to Cys-355 in a typical SN2 displacement. Then a 5'-dA radical formed from a second molecule of SAM abstracts a hydrogen from the methyl group of mCys-355, and the resulting Cys-appended methyl radical attacks the substrate adenine ring. Methyl transfer to C2 thus results in a covalent adduct between the substrate and Cys-355, which is resolved by formation of a disulfide bond between Cys-355 and a second conserved Cys residue (Cys-118).

<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

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei105Proton acceptorSequence analysis1
<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 bindingi125Iron-sulfur (4Fe-4S-S-AdoMet)1
Metal bindingi129Iron-sulfur (4Fe-4S-S-AdoMet)1
Metal bindingi132Iron-sulfur (4Fe-4S-S-AdoMet)1
<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 sitei211S-adenosyl-L-methionine1
Binding sitei312S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen1
Active sitei355S-methylcysteine intermediate2 Publications1

<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

  • rRNA base methylation Source: EcoCyc
  • response to antibiotic Source: UniProtKB-KW
  • tRNA methylation Source: UniProtKB

<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 functionMethyltransferase, Transferase
Biological processAntibiotic resistance, rRNA processing, tRNA processing
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG12401-MONOMER
ECOL316407:JW2501-MONOMER
MetaCyc:EG12401-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.1.1.192 2165

<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:
Dual-specificity RNA methyltransferase RlmN (EC:2.1.1.1924 Publications)
Alternative name(s):
23S rRNA (adenine(2503)-C(2))-methyltransferase
23S rRNA m2A2503 methyltransferase
Ribosomal RNA large subunit methyltransferase N
tRNA (adenine(37)-C(2))-methyltransferase
tRNA m2A37 methyltransferase
<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:rlmN
Synonyms:yfgB
Ordered Locus Names:b2517, JW2501
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG12401 rlmN

<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

<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

Cells lacking this gene lack nucleoside m2A in both rRNA and tRNAs. Inactivation of rlmN produces an error-prone phenotype since it increases the misreading of a UAG stop codon, and thus decreases translational accuracy. Also leads to increased susceptibility to tiamulin, hygromycin A and sparsomycin.2 Publications

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>Mutagenesisi118C → A: No change in iron-sulfur cluster content. No effect on methylation of Cys-355. 1 Publication1
Mutagenesisi125 – 132CALECKFC → AALEAKFA: Loss of iron-sulfur cluster binding. No methylation of Cys-355. 1 Publication8
Mutagenesisi355C → A: No change in iron-sulfur cluster content. 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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001719191 – 384Dual-specificity RNA methyltransferase RlmNAdd BLAST384

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi118 ↔ 355(transient)Curated

Keywords - PTMi

Disulfide bond

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P36979

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

More...
PaxDbi
P36979

PRoteomics IDEntifications database

More...
PRIDEi
P36979

<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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<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
4261302, 67 interactors

Database of interacting proteins

More...
DIPi
DIP-12035N

Protein interaction database and analysis system

More...
IntActi
P36979, 95 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2517

<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

1384
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
P36979

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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>Regioni179 – 180S-adenosyl-L-methionine binding2
Regioni233 – 235S-adenosyl-L-methionine binding3

<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 radical SAM superfamily. RlmN family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C55 Bacteria
COG0820 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000217992

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P36979

KEGG Orthology (KO)

More...
KOi
K06941

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P36979

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01849 RNA_methyltr_RlmN, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785 Aldolase_TIM
IPR040072 Methyltransferase_A
IPR027492 RNA_MTrfase_RlmN
IPR004383 rRNA_lsu_MTrfase_RlmN/Cfr
IPR007197 rSAM

The PANTHER Classification System

More...
PANTHERi
PTHR30544 PTHR30544, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04055 Radical_SAM, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF006004 CHP00048, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDF00275 adenosine_C2_methyltransferase, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00048 rRNA_mod_RlmN, 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.

P36979-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSEQLVTPEN VTTKDGKINL LDLNRQQMRE FFKDLGEKPF RADQVMKWMY
60 70 80 90 100
HYCCDNFDEM TDINKVLRGK LKEVAEIRAP EVVEEQRSSD GTIKWAIAVG
110 120 130 140 150
DQRVETVYIP EDDRATLCVS SQVGCALECK FCSTAQQGFN RNLRVSEIIG
160 170 180 190 200
QVWRAAKIVG AAKVTGQRPI TNVVMMGMGE PLLNLNNVVP AMEIMLDDFG
210 220 230 240 250
FGLSKRRVTL STSGVVPALD KLGDMIDVAL AISLHAPNDE IRDEIVPINK
260 270 280 290 300
KYNIETFLAA VRRYLEKSNA NQGRVTIEYV MLDHVNDGTE HAHQLAELLK
310 320 330 340 350
DTPCKINLIP WNPFPGAPYG RSSNSRIDRF SKVLMSYGFT TIVRKTRGDD
360 370 380
IDAACGQLAG DVIDRTKRTL RKRMQGEAID IKAV
Length:384
Mass (Da):43,086
Last modified:June 1, 1994 - 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:i92C1BDCC840FCE7B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U02965 Genomic DNA Translation: AAA21359.1
U00096 Genomic DNA Translation: AAC75570.1
AP009048 Genomic DNA Translation: BAA16404.1

Protein sequence database of the Protein Information Resource

More...
PIRi
D65028

NCBI Reference Sequences

More...
RefSeqi
NP_417012.1, NC_000913.3
WP_000003317.1, NZ_STEB01000011.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75570; AAC75570; b2517
BAA16404; BAA16404; BAA16404

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946249

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2501
eco:b2517

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.4219

<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
U02965 Genomic DNA Translation: AAA21359.1
U00096 Genomic DNA Translation: AAC75570.1
AP009048 Genomic DNA Translation: BAA16404.1
PIRiD65028
RefSeqiNP_417012.1, NC_000913.3
WP_000003317.1, NZ_STEB01000011.1

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
3RF9X-ray2.20A/B1-384[»]
3RFAX-ray2.05A/B1-384[»]
5HR6X-ray2.88A/B1-384[»]
5HR7X-ray2.40A/B1-384[»]
SMRiP36979
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4261302, 67 interactors
DIPiDIP-12035N
IntActiP36979, 95 interactors
STRINGi511145.b2517

Proteomic databases

jPOSTiP36979
PaxDbiP36979
PRIDEiP36979

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75570; AAC75570; b2517
BAA16404; BAA16404; BAA16404
GeneIDi946249
KEGGiecj:JW2501
eco:b2517
PATRICifig|1411691.4.peg.4219

Organism-specific databases

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

More...
EchoBASEi
EB2301
EcoGeneiEG12401 rlmN

Phylogenomic databases

eggNOGiENOG4105C55 Bacteria
COG0820 LUCA
HOGENOMiHOG000217992
InParanoidiP36979
KOiK06941
PhylomeDBiP36979

Enzyme and pathway databases

BioCyciEcoCyc:EG12401-MONOMER
ECOL316407:JW2501-MONOMER
MetaCyc:EG12401-MONOMER
BRENDAi2.1.1.192 2165

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P36979

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_01849 RNA_methyltr_RlmN, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR040072 Methyltransferase_A
IPR027492 RNA_MTrfase_RlmN
IPR004383 rRNA_lsu_MTrfase_RlmN/Cfr
IPR007197 rSAM
PANTHERiPTHR30544 PTHR30544, 1 hit
PfamiView protein in Pfam
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF006004 CHP00048, 1 hit
SFLDiSFLDF00275 adenosine_C2_methyltransferase, 1 hit
TIGRFAMsiTIGR00048 rRNA_mod_RlmN, 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 nameiRLMN_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: P36979
<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: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 31, 2019
This is version 155 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  4. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
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