Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P23395 (SYM_THET8)

Last modified November 24, 2009. Version 82. 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

Hide | Top

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
Ordered Locus Names: TTHA1298
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Hide | Top

Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

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 MF_01228

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.

Sequence similarities

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

Contains 1 tRNA-binding domain.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 618618Methionyl-tRNA synthetase HAMAP MF_01228
PRO_0000139258

Regions

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

Sites

Metal binding1271Zinc HAMAP MF_01228
Metal binding1301Zinc HAMAP MF_01228
Metal binding1441Zinc HAMAP MF_01228
Metal binding1471Zinc HAMAP MF_01228
Binding site3001ATP By similarity

Experimental info

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

Secondary structure

1 ............................................................................. 618
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P23395-1 [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

Hide | Top

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: 1993699] [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].
[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: 10673435] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Hide | Top

Cross-references

Sequence databases

M64273 Genomic DNA. Translation: AAA27510.1.
AP008226 Genomic DNA. Translation: BAD71121.1.
RefSeqYP_144564.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1A8HX-ray2.00A1-500[»]
1WOYX-ray2.00A1-500[»]
2D54X-ray2.00A1-502[»]
2D5BX-ray1.80A1-500[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP23395.

Genome annotation databases

GeneID3169329.
GenomeReviewsGene locus TTHA1298 in contig AP008226_GR.
KEGGttj:TTHA1298.
NMPDRfig|300852.3.peg.1551.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP23395.
OMADWGIKVP

Enzyme and pathway databases

BioCycTTHE300852:TTHA1298-MON.

Family and domain databases

HAMAPMF_01228. Fused.
[Tree]
InterProIPR015413. aa-tRNA-synt_I.
IPR002304. Met-tRNA-synth_Ia.
IPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR014729. Rossmann-like_a/b/a_fold.
IPR014758. tRNA-synt_met_N.
IPR002547. tRNA_bd.
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. 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. False negative.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

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: November 24, 2009
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

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