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Reviewed, UniProtKB/Swiss-Prot Q9WYA4 (MNME_THEMA)

Last modified November 3, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    tRNA modification GTPase mnmE
    EC=3.6.5.-
Gene names
Name: mnmE
Synonyms: trmE
Ordered Locus Names: TM_0267
OrganismThermotoga maritima [Complete proteome] [HAMAP]
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. HAMAP MF_00379

Cofactor

Binds 1 potassium ion per subunit By similarity.

Subunit structure

Homodimer. Heterotetramer of two mnmE and two mnmG subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the era/mnmE GTP-binding protein family. MnmE subfamily.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
Potassium
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processtRNA modification

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionGTP binding

Inferred from electronic annotation. Source: HAMAP

GTPase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

potassium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450tRNA modification GTPase mnmE HAMAP MF_00379
PRO_0000188939

Regions

Nucleotide binding221 – 2266GTP By similarity
Nucleotide binding240 – 2467GTP By similarity
Nucleotide binding265 – 2684GTP By similarity
Nucleotide binding326 – 3294GTP By similarity
Nucleotide binding353 – 3553GTP By similarity

Sites

Metal binding2211Potassium By similarity
Metal binding2251Magnesium By similarity
Metal binding2401Potassium; via carbonyl oxygen By similarity
Metal binding2421Potassium; via carbonyl oxygen By similarity
Metal binding2451Potassium By similarity
Metal binding2461Magnesium By similarity
Binding site201Formyltetrahydrofolate HAMAP MF_00379
Binding site781Formyltetrahydrofolate HAMAP MF_00379
Binding site1171Formyltetrahydrofolate HAMAP MF_00379
Binding site4501Formyltetrahydrofolate HAMAP MF_00379

Secondary structure

.................................................................. 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WYA4-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 8DAD2D1EB8500CC0

FASTA45050,682
        10         20         30         40         50         60 
MDTIVAVATP PGKGAIAILR LSGPDSWKIV QKHLRTRSKI VPRKAIHGWI HENGEDVDEV 

        70         80         90        100        110        120 
VVVFYKSPKS YTGEDMVEVM CHGGPLVVKK LLDLFLKSGA RMAEPGEFTK RAFLNGKMDL 

       130        140        150        160        170        180 
TSAEAVRDLI EAKSETSLKL SLRNLKGGLR DFVDSLRREL IEVLAEIRVE LDYPDEIETN 

       190        200        210        220        230        240 
TGEVVTRLER IKEKLTEELK KADAGILLNR GLRMVIVGKP NVGKSTLLNR LLNEDRAIVT 

       250        260        270        280        290        300 
DIPGTTRDVI SEEIVIRGIL FRIVDTAGVR SETNDLVERL GIERTLQEIE KADIVLFVLD 

       310        320        330        340        350        360 
ASSPLDEEDR KILERIKNKR YLVVINKVDV VEKINEEEIK NKLGTDRHMV KISALKGEGL 

       370        380        390        400        410        420 
EKLEESIYRE TQEIFERGSD SLITNLRQKQ LLENVKGHLE DAIKSLKEGM PVDMASIDLE 

       430        440        450 
RALNLLDEVT GRSFREDLLD TIFSNFCVGK 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed: 10360571] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Characterization of GTPase activity of TrmE, a member of a novel GTPase superfamily, from Thermotoga maritima."
Yamanaka K., Hwang J., Inouye M.
J. Bacteriol. 182:7078-7082(2000) [PubMed: 11092873] [Abstract]
Cited for: CHARACTERIZATION.
[3]"The structure of the TrmE GTP-binding protein and its implications for tRNA modification."
Scrima A., Vetter I.R., Armengod M.-E., Wittinghofer A.
EMBO J. 24:23-33(2005) [PubMed: 15616586] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FORMYLTETRAHYDROFOLATE; GTP-BINDING, SUBUNIT.

Cross-references

Sequence databases

AE000512 Genomic DNA. Translation: AAD35356.1.
PIRA72397.
RefSeqNP_228080.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1XZPX-ray2.30A1-450[»]
B1-118[»]
1XZQX-ray2.90A1-450[»]
B1-117[»]
ModBaseSearch...

Genome annotation databases

GeneID897178.
GenomeReviewsGene locus TM_0267 in contig AE000512_GR.
KEGGtma:TM0267.
NMPDRfig|243274.1.peg.264.
TIGRTM_0267.

Phylogenomic databases

HOGENOMQ9WYA4.
OMAKGPNSFT.

Enzyme and pathway databases

BioCycTMAR243274:TM_0267-MON.

Family and domain databases

HAMAPMF_00379.
[Tree]
InterProIPR006073. GTP1_OBG.
IPR018948. GTP_bd_TrmE_N.
IPR002917. MMR_HSR1_GTP_bd.
IPR005225. Small_GTP_bd.
IPR004520. ThdF.
[Graphical view]
Gene3DG3DSA:3.30.1360.120. GTP_bd_TrmE_N. 1 hit.
PfamPF01926. MMR_HSR1. 1 hit.
PF10396. TrmE_N. 1 hit.
[Graphical view]
PRINTSPR00326. GTP1OBG.
TIGRFAMsTIGR00450. mnmE_trmE_thdF. 1 hit.
TIGR00231. small_GTP. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMNME_THEMA
AccessionPrimary (citable) accession number: Q9WYA4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1999
Last modified: November 3, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents