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Reviewed, UniProtKB/Swiss-Prot O67298 (SYM_AQUAE)

Last modified November 3, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Methionyl-tRNA synthetase
    EC=6.1.1.10
Alternative name(s):
    Methionine--tRNA ligase
      Short name=MetRS
Gene names
Name: metG
Ordered Locus Names: aq_1257
OrganismAquifex aeolicus [Complete proteome] [HAMAP]
Taxonomic identifier63363 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

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Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation By similarity.

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP MF_01228

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. HAMAP MF_01228

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2A subfamily.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processmethionyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Methionyl-tRNA synthetase HAMAP MF_01228
PRO_0000139206

Regions

Motif14 – 2411"HIGH" region HAMAP MF_01228
Motif295 – 2995"KMSKS" region HAMAP MF_01228

Sites

Metal binding1291Zinc By similarity
Metal binding1321Zinc By similarity
Metal binding1471Zinc By similarity
Metal binding1501Zinc By similarity
Binding site2981ATP By similarity

Secondary structure

1 ....................................................................... 497
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O67298-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 846C68E72AFEB4F7

FASTA49758,931
        10         20         30         40         50         60 
MTLMKKFYVT TPIYYVNDVP HLGHAYTTIA ADTIARYYRL RDYDVFFLTG TDEHGLKIQK 

        70         80         90        100        110        120 
KAEELGISPK ELVDRNAERF KKLWEFLKIE YTKFIRTTDP YHVKFVQKVF EECYKRGDIY 

       130        140        150        160        170        180 
LGEYEGWYCV GCEEFKSEAE LAEDHTCPIH QKKCEYIKEP SYFFRLSKYQ DKLLELYEKN 

       190        200        210        220        230        240 
PEFIQPDYRR NEIISFVKQG LKDLSVTRPR SRVKWGIPVP FDPEHTIYVW FDALFNYISA 

       250        260        270        280        290        300 
LEDKVEIYWP ADLHLVGKDI LRFHTVYWPA FLMSLGYELP KKVFAHGWWT VEGKKMSKTL 

       310        320        330        340        350        360 
GNVVDPYEVV QEYGLDEVRY FLLREVPFGQ DGDFSKKAIL NRINGELANE IGNLYSRVVN 

       370        380        390        400        410        420 
MAHKFLGGEV SGARDEEYAK IAQESIKNYE NYMEKVNFYK AIEEILKFTS YLNKYVDEKQ 

       430        440        450        460        470        480 
PWALNKERKK EELQKVLYAL VDGLFVLTHL LYPITPNKMK EALQMLGEKE FLKELKPYSK 

       490 
NTYKLGERKI LFPKREG

« Hide

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References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Crystal structure of Aquifex aeolicus methionyl-tRNA synthetase complexed with tRNA(met)."
RIKEN structural genomics initiative (RSGI)
Submitted (SEP-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

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Cross-references

Sequence databases

AE000657 Genomic DNA. Translation: AAC07256.1.
PIRG70408.
RefSeqNP_213862.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2CSXX-ray2.70A/B1-497[»]
2CT8X-ray2.70A/B1-497[»]
ModBaseSearch...

Genome annotation databases

GeneID1192736.
GenomeReviewsGene locus aq_1257 in contig AE000657_GR.
KEGGaae:aq_1257.
NMPDRfig|224324.1.peg.877.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO67298.
OMANGELANE.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1257-MON.
BRENDA6.1.1.10. 189781.

Family and domain databases

HAMAPMF_01228.
[Tree]
InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR002304. Met-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR014758. tRNA-synt_met_N.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF09334. tRNA-synt_1g. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
TIGRFAMsTIGR00398. metG. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYM_AQUAE
AccessionPrimary (citable) accession number: O67298
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 64 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)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

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