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Q2T087 (SYM_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionine--tRNA ligase
EC=6.1.1.10
Alternative name(s):
Methionyl-tRNA synthetase
Short name=MetRS
Gene names
Name:metG
Ordered Locus Names:BTH_I0856
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length718 AA.
Sequence statusComplete.
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. HAMAP MF_00098

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP MF_00098

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00098

Subunit structure

Homodimer By similarity. HAMAP MF_00098

Subcellular location

Cytoplasm By similarity HAMAP MF_00098.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 1 subfamily.

Contains 1 tRNA-binding domain.

Sequence caution

The sequence ABC38961.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 718718Methionine--tRNA ligase HAMAP MF_00098
PRO_0000331797

Regions

Domain612 – 718107tRNA-binding
Motif27 – 3711"HIGH" region HAMAP MF_00098
Motif348 – 3525"KMSKS" region HAMAP MF_00098

Sites

Metal binding1581Zinc By similarity
Metal binding1611Zinc By similarity
Metal binding1711Zinc By similarity
Metal binding1741Zinc By similarity
Binding site3511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2T087 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 4DC90AD0ECA7ED19

FASTA71879,413
        10         20         30         40         50         60 
MSASDLHPVQ AGAPQGRRQI LVTSALPYAN GQIHIGHLVE YIQTDIWART MRMHGHEIYY 

        70         80         90        100        110        120 
IGADDTHGTP VMLRAEQEGV SPKQLIERVW REHKRDFDSF GVSFDNFYTT DSDENRVLSE 

       130        140        150        160        170        180 
KIYLALKEAG FIAEREIEQA YDPVKQMFLP DRFIKGECPK CHAKDQYGDS CEVCGTTYQP 

       190        200        210        220        230        240 
TDLVNPYSVV SGATPVRKTS THHFFRLSDP RCEAFLREWV SGLAQPEATN KMREWLGDAG 

       250        260        270        280        290        300 
EAKLADWDIS RDAPYFGFEI PGAPGKYFYV WLDAPVGYYA SFKNLCERRG LDFDAWISKD 

       310        320        330        340        350        360 
STTEQYHFIG KDILYFHTLF WPAMLEFSGH RTPTNVFAHG FLTVDGAKMS KSRGTFITAQ 

       370        380        390        400        410        420 
SYIDAGLNPE WLRYYFAAKL NATMEDIDLN LEDFQARVNS DLVGKYVNIA SRAAGFLIKR 

       430        440        450        460        470        480 
FDGRVQASAT NHPLLVTLRD AIPQIAAHYE AREYGRALRQ TMELADAVNG YVDTAKPWEL 

       490        500        510        520        530        540 
AKDPANAVAL HETCTVSLEA FRLLSLALKP VLPRVAEGVE AFLGIAPLTW ADANKPLSSE 

       550        560        570        580        590        600 
QPIRAYQHLM TRVDPKQIDA LLAANRSSLQ GAAAADAAGA TNGNGAKAAK SAKAANAASA 

       610        620        630        640        650        660 
DDEASPFISI DDFAKIDLRI AKIVACQAVE GSDKLLQLTL DVGEEKTRNV FSGIKSAYQP 

       670        680        690        700        710 
EQLVGKLTVM VANLAPRKMK FGLSEGMVLA ASAADEKAEP GLYILEPHSG AKPGMRVK

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References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000086 Genomic DNA. Translation: ABC38961.1. Different initiation.
RefSeqYP_441412.3. NC_007651.1.

3D structure databases

ProteinModelPortalQ2T087.
SMRQ2T087. Positions 18-566.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2T087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3848452.
GenomeReviewsGene locus BTH_I0856 in contig CP000086_GR.
KEGGbte:BTH_I0856.
PATRIC19304524. VBIBurTha36512_3578.
TIGRBTH_I0856.

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHBG721667.
ProtClustDBPRK00133.

Enzyme and pathway databases

BioCycBTHA271848:BTH_I0856-MONOMER.

Family and domain databases

HAMAPMF_00098. Met_tRNA_synth_type1.
[Tree]
InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR014758. Met-tRNA_synth.
IPR023458. Met-tRNA_synth_1.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR009080. tRNAsynth_1a_anticodon-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. 2 hits.
KOK01874.
PfamPF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.
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_BURTA
AccessionPrimary (citable) accession number: Q2T087
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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