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P23395 (SYM_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:metS
Ordered Locus Names:TTHA1298
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. HAMAP-Rule MF_01228

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_01228.

Sequence similarities

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

Contains 1 tRNA-binding domain.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 618618Methionine--tRNA ligase HAMAP-Rule MF_01228
PRO_0000139258

Regions

Domain518 – 618101tRNA-binding
Motif12 – 2211"HIGH" region HAMAP-Rule MF_01228
Motif297 – 3015"KMSKS" region HAMAP-Rule MF_01228

Sites

Metal binding1271Zinc
Metal binding1301Zinc
Metal binding1441Zinc
Metal binding1471Zinc
Binding site3001ATP By similarity

Experimental info

Sequence conflict615 – 6184AVVK → RW in AAA27510. Ref.1

Secondary structure

............................................................................. 618
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23395 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 920A449052C62558

FASTA61870,693
        10         20         30         40         50         60 
MEKVFYVTTP IYYVNAEPHL GHAYTTVVAD FLARWHRLDG YRTFFLTGTD EHGETVYRAA 

        70         80         90        100        110        120 
QAAGEDPKAF VDRVSGRFKR AWDLLGIAYD DFIRTTEERH KKVVQLVLKK VYEAGDIYYG 

       130        140        150        160        170        180 
EYEGLYCVSC ERFYTEKELV EGLCPIHGRP VERRKEGNYF FRMEKYRPWL QEYIQENPDL 

       190        200        210        220        230        240 
IRPEGYRNEV LAMLAEPIGD LSISRPKSRV PWGIPLPWDE NHVTYVWFDA LLNYVSALDY 

       250        260        270        280        290        300 
PEGEAYRTFW PHAWHLIGKD ILKPHAVFWP TMLKAAGIPM YRHLNVGGFL LGPDGRKMSK 

       310        320        330        340        350        360 
TLGNVVDPFA LLEKYGRDAL RYYLLREIPY GQDTPVSEEA LRTRYEADLA DDLGNLVQRT 

       370        380        390        400        410        420 
RAMLFRFAEG RIPEPVAGEE LAEGTGLAGR LRPLVRELKF HVALEEAMAY VKALNRYINE 

       430        440        450        460        470        480 
KKPWELFKKE PEEARAVLYR VVEGLRIASI LLTPAMPDKM AELRRALGLK EEVRLEEAER 

       490        500        510        520        530        540 
WGLAEPRPIP EEAPVLFPKK EAKVEAKPKE EAWIGIEDFA KVELRVAEVL AAEKHPNADR 

       550        560        570        580        590        600 
LLVLRLSLGN EERTVVSGIA KWYRPEELVG KKVVLVANLK PAKLRGIESQ GMILAAQEGE 

       610 
ALALVTVEGE VPPGAVVK 

« Hide

References

« Hide 'large scale' references
[1]"Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus thermophilus HB8. Molecular cloning, primary-structure analysis, expression in Escherichia coli, and site-directed mutagenesis."
Nureki O., Muramatsu T., Suzuki K., Kohda D., Matsuzawa H., Ohta T., Miyazawa T., Yokoyama S.
J. Biol. Chem. 266:3268-3277(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"The 2.0-A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules."
Sugiura I., Nureki O., Ugaji-Yoshikawa Y., Kuwabara S., Shimada A., Tateno M., Lorber B., Giege R., Moras D., Yokoyama S., Konno M.
Structure 8:197-208(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64273 Genomic DNA. Translation: AAA27510.1.
AP008226 Genomic DNA. Translation: BAD71121.1.
RefSeqYP_144564.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8HX-ray2.00A1-500[»]
1WOYX-ray2.00A1-500[»]
2D54X-ray2.00A1-502[»]
2D5BX-ray1.80A1-500[»]
3VU8X-ray2.20A1-502[»]
ProteinModelPortalP23395.
SMRP23395. Positions 1-500, 512-615.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1298.

Chemistry

ChEMBLCHEMBL1641341.

Proteomic databases

PRIDEP23395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71121; BAD71121; BAD71121.
GeneID3169329.
KEGGttj:TTHA1298.
PATRIC23957557. VBITheThe93045_1276.

Phylogenomic databases

eggNOGCOG0143.
HOGENOMHOG000200401.
KOK01874.
OMAHPEFVQP.
OrthoDBEOG6CVV9B.
PhylomeDBP23395.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1332-MONOMER.

Family and domain databases

Gene3D1.10.730.10. 1 hit.
2.40.50.140. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_01228. Met_tRNA_synth_type2.
InterProIPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR014758. Met-tRNA_synth.
IPR023457. Met-tRNA_synth_2.
IPR015413. Methionyl/Leucyl_tRNA_Synth.
IPR012340. NA-bd_OB-fold.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PfamPF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
SUPFAMSSF47323. SSF47323. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00398. metG. 1 hit.
TIGR00399. metG_C_term. 1 hit.
PROSITEPS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23395.

Entry information

Entry nameSYM_THET8
AccessionPrimary (citable) accession number: P23395
Secondary accession number(s): Q5SIR6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries