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Reviewed, UniProtKB/Swiss-Prot P23920 (SYM_BACST)

Last modified June 16, 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:
    Methionyl-tRNA synthetase
    EC=6.1.1.10
Alternative name(s):
    Methionine--tRNA ligase
      Short name=MetRS
Gene names
Name: metG
Synonyms: metS
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length649 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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. HAMAP MF_01228

Subunit structure

Homodimer. HAMAP MF_01228

Subcellular location

Cytoplasm. HAMAP MF_01228

Sequence similarities

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

Contains 1 tRNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 649649Methionyl-tRNA synthetase HAMAP MF_01228
PRO_0000139210

Regions

Domain555 – 64793tRNA-binding
Motif13 – 2311"HIGH" region HAMAP MF_01228
Motif298 – 3025"KMSKS" region HAMAP MF_01228

Sites

Metal binding1281Zinc By similarity
Metal binding1311Zinc By similarity
Metal binding1451Zinc By similarity
Metal binding1481Zinc By similarity
Binding site3011ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P23920-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: BDF5DCCA79B21A89

FASTA64974,354
        10         20         30         40         50         60 
MEKKTFYLTT PIYYPSDKLH IGHAYTTVAG DAMARYKRLR GYDVMYLTGT DEHGQKIQRK 

        70         80         90        100        110        120 
AQEKGVTPQQ YVDDIVAGIQ ELWRKLDISY DDFIRTTQER HKKIVEKIFA RLVEQGDIYL 

       130        140        150        160        170        180 
GEYEGWYCTP CESFYTERQL VDGNCPDCGR PVEKVKEESY FFRMSKYVDR LLQYYEENPD 

       190        200        210        220        230        240 
FIQPESRKNE MINNFIKPGL EDLAVSRTTF DWGIKVPGDP KHVIYVWIDA LANYITALGY 

       250        260        270        280        290        300 
GTDNDEKFRK YWPADVHLVG KEIVRFHTIY WPIMLMALGL PLPKKVFGHG WLLMKDGKMS 

       310        320        330        340        350        360 
KSKGNVVDPV MIIDRYGLDA LRYYLLREVP FGSDGVFTPE GFIERINYDL ANDLGNLLHR 

       370        380        390        400        410        420 
TVAMIEKYFG GAIPPYRGPK TPFDRDLSET AREVVRQYEE AMERMEFSVA LSAVWQLIGR 

       430        440        450        460        470        480 
TNKYIDETQP WVLAKEESKR EELASVMAHL AESLRYTAVL LQPFLTRTPE RIFTQLGISD 

       490        500        510        520        530        540 
RSLKEWDSLY DFGLIPEGTN VQKGEPLFPR LDIGVEVEYI KAHMQGGKPA EAAKEEKQAA 

       550        560        570        580        590        600 
RAEEISIDDF AKVDLRVAEV VQPERMKNAD KLLKLQLDLG GEKRQVISGI AEFYKPEELI 

       610        620        630        640 
GKKVICVANL KPAKLRGEWS EGMILAGGSG GGFSLATVDQ HVPNGTKIK 

« Hide

References

[1]"Methionyl-tRNA synthetase from Bacillus stearothermophilus: structural and functional identities with the Escherichia coli enzyme."
Mechulam Y., Schmitt E., Panvert M., Schmitter J.-M., Lapadat-Tapolsky M., Meinnel T., Dessen P., Blanquet S., Fayat G.
Nucleic Acids Res. 19:3673-3681(1991) [PubMed: 1852609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 1518.

Cross-references

Sequence databases

X57925 Genomic DNA. Translation: CAA40999.1.
PIRS16682.

3D structure databases

HSSPHSSP built from PDB template 1MKH based on UniProtKB Q9V011.
ModBaseSearch...

Enzyme and pathway databases

BRENDA6.1.1.10. 266715.

Family and domain databases

HAMAPMF_01228. Fused.
[Tree]
InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR002304. Met-tRNA-synth_Ia.
IPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR014758. tRNA-synt_met_N.
IPR002547. tRNA_bd.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
TIGRFAMsTIGR00398. metG. 1 hit.
TIGR00399. metG_C_term. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYM_BACST
AccessionPrimary (citable) accession number: P23920
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: June 16, 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

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