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Entry version 181 (13 Nov 2019)
Sequence version 3 (15 Jul 1998)
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Protein

tRNA modification GTPase MnmE

Gene

mnmE

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

Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm5s2U34.

<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

K+Note: Binds 1 potassium ion per subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

GTPase activity is strongly activated by potassium ions.

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=511 µM for GTP2 Publications
  2. KM=346 µM for XTP2 Publications
  1. Vmax=193 nmol/min/mg enzyme with GTP as substrate2 Publications
  2. Vmax=100 nmol/min/mg enzyme with XTP as substrate2 Publications

pH dependencei

Optimum pH is 7.5-9.5.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section 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 sitei23FormyltetrahydrofolateUniRule annotation1
Binding sitei80FormyltetrahydrofolateUniRule annotation1
Binding sitei120FormyltetrahydrofolateUniRule annotation1
<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 bindingi226Potassium1
Metal bindingi230Magnesium1
Metal bindingi245Potassium; via carbonyl oxygen1
Metal bindingi247Potassium; via carbonyl oxygen1
Metal bindingi250Potassium1
Metal bindingi251Magnesium1
Binding sitei454FormyltetrahydrofolateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi226 – 231GTP6
Nucleotide bindingi245 – 251GTP7
Nucleotide bindingi270 – 273GTP4
Nucleotide bindingi335 – 338GTP4
Nucleotide bindingi358 – 360GTP3

<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 functionHydrolase
Biological processtRNA processing
LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10997-MONOMER
ECOL316407:JW3684-MONOMER
MetaCyc:EG10997-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_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
tRNA modification GTPase MnmEUniRule annotation (EC:3.6.-.-UniRule annotation)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:mnmEUniRule annotation
Synonyms:thdFUniRule annotation, trmEUniRule annotation
Ordered Locus Names:b3706, JW3684
<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

<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_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>Mutagenesisi224R → A: 1.5-fold decrease in GTPase activity and almost no change in affinity. 1 Publication1
Mutagenesisi226N → A: 100-fold decrease in GTPase activity. 5-fold decrease of affinity for GTP. 1 Publication1
Mutagenesisi226N → K: 70-fold decrease in GTPase activity. 2-fold decrease of affinity for GTP. 1 Publication1
Mutagenesisi228G → A: Loss of GTP binding and hydrolase activity. Completely impairs tRNA modifying function. 1 Publication1
Mutagenesisi249G → A: 22-fold decrease in GTPase activity and 7-fold increase of affinity. 1 Publication1
Mutagenesisi250T → A: 4-fold decrease in GTPase activity and 1.5-fold increase of affinity. 1 Publication1
Mutagenesisi250T → S: 1.8-fold decrease in GTPase activity and 1.5-fold increase of affinity. 1 Publication1
Mutagenesisi251T → A: 92-fold decrease in GTPase activity and 59-fold increase of affinity. 1 Publication1
Mutagenesisi251T → S: 4-fold decrease in GTPase activity and 1.2-fold decrease of affinity. 1 Publication1
Mutagenesisi252R → A: 7-fold decrease in GTPase activity and 6-fold increase of affinity. 1 Publication1
Mutagenesisi252R → K: 2-fold decrease in GTPase activity and no change in affinity. 1 Publication1
Mutagenesisi253D → A: 9-fold decrease in GTPase activity and 13-fold increase of affinity. 1 Publication1
Mutagenesisi255L → D: 1.5-fold decrease in affinity for GTP. 1 Publication1
Mutagenesisi256R → A: 2-fold decrease in GTPase activity and almost no change in affinity. 1 Publication1
Mutagenesisi270D → A: Does not affect GTP binding, but impairs hydrolase activity. Completely impairs tRNA modifying function. 1 Publication1
Mutagenesisi275R → A: 6-fold decrease in GTPase activity and 1.9-fold increase of affinity. 1 Publication1
Mutagenesisi282E → A: 1900-fold decrease in GTPase activity. 1 Publication1
Mutagenesisi282E → Q: 370-fold decrease in GTPase activity. 1 Publication1
Mutagenesisi288R → A: 1.7-fold decrease in GTPase activity and 1.5-fold increase of affinity. 1 Publication1
Mutagenesisi338D → N: Strong decrease in GTP binding. Does not affect hydrolase activity, but has 10-fold higher affinity for XTP than for GTP. Partially impairs tRNA modifying function. 1 Publication1
Mutagenesisi451C → S: No change in GTP binding and hydrolase activity. Does not affect association to the cell inner membrane. Completely impairs tRNA modifying function. 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_00001888741 – 454tRNA modification GTPase MnmEAdd BLAST454

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P25522

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

More...
PaxDbi
P25522

PRoteomics IDEntifications database

More...
PRIDEi
P25522

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Heterotetramer of two MnmE and two MnmG subunits.

UniRule annotation1 Publication

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261522, 160 interactors
852524, 3 interactors

Database of interacting proteins

More...
DIPi
DIP-11033N

Protein interaction database and analysis system

More...
IntActi
P25522, 24 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b3706

<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

1454
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
P25522

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
P25522

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini216 – 377TrmE-type GAdd BLAST162

<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 TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C1H Bacteria
COG0486 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000200714

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25522

KEGG Orthology (KO)

More...
KOi
K03650

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P25522

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04164 trmE, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.120.430, 1 hit
3.30.1360.120, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00379 GTPase_MnmE, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031168 G_TrmE
IPR018948 GTP-bd_TrmE_N
IPR006073 GTP_binding_domain
IPR004520 GTPase_MnmE
IPR027368 MnmE_dom2
IPR025867 MnmE_helical
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR027266 TrmE/GcvT_dom1

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01926 MMR_HSR1, 1 hit
PF12631 MnmE_helical, 1 hit
PF10396 TrmE_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00450 mnmE_trmE_thdF, 1 hit
TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51709 G_TRME, 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.

P25522-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDNDTIVAQ ATPPGRGGVG ILRISGFKAR EVAETVLGKL PKPRYADYLP
60 70 80 90 100
FKDADGSVLD QGIALWFPGP NSFTGEDVLE LQGHGGPVIL DLLLKRILTI
110 120 130 140 150
PGLRIARPGE FSERAFLNDK LDLAQAEAIA DLIDASSEQA ARSALNSLQG
160 170 180 190 200
AFSARVNHLV EALTHLRIYV EAAIDFPDEE IDFLSDGKIE AQLNDVIADL
210 220 230 240 250
DAVRAEARQG SLLREGMKVV IAGRPNAGKS SLLNALAGRE AAIVTDIAGT
260 270 280 290 300
TRDVLREHIH IDGMPLHIID TAGLREASDE VERIGIERAW QEIEQADRVL
310 320 330 340 350
FMVDGTTTDA VDPAEIWPEF IARLPAKLPI TVVRNKADIT GETLGMSEVN
360 370 380 390 400
GHALIRLSAR TGEGVDVLRN HLKQSMGFDT NMEGGFLARR RHLQALEQAA
410 420 430 440 450
EHLQQGKAQL LGAWAGELLA EELRLAQQNL SEITGEFTSD DLLGRIFSSF

CIGK
Length:454
Mass (Da):49,231
Last modified:July 15, 1998 - v3
<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:i032211797805D2FE
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB19981 differs from that shown.Curated

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
S57109 Genomic DNA Translation: AAB19981.1 Sequence problems.
L10328 Genomic DNA Translation: AAA62057.1
U00096 Genomic DNA Translation: AAC76729.1
AP009048 Genomic DNA Translation: BAE77587.1

Protein sequence database of the Protein Information Resource

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PIRi
A38160
C65173

NCBI Reference Sequences

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RefSeqi
NP_418162.1, NC_000913.3
WP_001282346.1, NZ_SSZK01000035.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76729; AAC76729; b3706
BAE77587; BAE77587; BAE77587

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
948222

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW3684
eco:b3706

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2997

<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
S57109 Genomic DNA Translation: AAB19981.1 Sequence problems.
L10328 Genomic DNA Translation: AAA62057.1
U00096 Genomic DNA Translation: AAC76729.1
AP009048 Genomic DNA Translation: BAE77587.1
PIRiA38160
C65173
RefSeqiNP_418162.1, NC_000913.3
WP_001282346.1, NZ_SSZK01000035.1

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
1RFLNMR-A210-377[»]
2GJ8X-ray1.70A/B/C/D216-384[»]
2GJ9X-ray2.00A/B/C/D216-384[»]
2GJAX-ray1.85A/B216-384[»]
SMRiP25522
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4261522, 160 interactors
852524, 3 interactors
DIPiDIP-11033N
IntActiP25522, 24 interactors
STRINGi511145.b3706

Proteomic databases

jPOSTiP25522
PaxDbiP25522
PRIDEiP25522

Genome annotation databases

EnsemblBacteriaiAAC76729; AAC76729; b3706
BAE77587; BAE77587; BAE77587
GeneIDi948222
KEGGiecj:JW3684
eco:b3706
PATRICifig|1411691.4.peg.2997

Organism-specific databases

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

More...
EchoBASEi
EB0990

Phylogenomic databases

eggNOGiENOG4105C1H Bacteria
COG0486 LUCA
HOGENOMiHOG000200714
InParanoidiP25522
KOiK03650
PhylomeDBiP25522

Enzyme and pathway databases

BioCyciEcoCyc:EG10997-MONOMER
ECOL316407:JW3684-MONOMER
MetaCyc:EG10997-MONOMER

Miscellaneous databases

EvolutionaryTraceiP25522

Protein Ontology

More...
PROi
PR:P25522

Family and domain databases

CDDicd04164 trmE, 1 hit
Gene3Di1.20.120.430, 1 hit
3.30.1360.120, 1 hit
HAMAPiMF_00379 GTPase_MnmE, 1 hit
InterProiView protein in InterPro
IPR031168 G_TrmE
IPR018948 GTP-bd_TrmE_N
IPR006073 GTP_binding_domain
IPR004520 GTPase_MnmE
IPR027368 MnmE_dom2
IPR025867 MnmE_helical
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR027266 TrmE/GcvT_dom1
PfamiView protein in Pfam
PF01926 MMR_HSR1, 1 hit
PF12631 MnmE_helical, 1 hit
PF10396 TrmE_N, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00450 mnmE_trmE_thdF, 1 hit
TIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51709 G_TRME, 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 nameiMNME_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: P25522
Secondary accession number(s): Q2M819
<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: May 1, 1992
Last sequence update: July 15, 1998
Last modified: November 13, 2019
This is version 181 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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