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P23395

- SYM_THET8

UniProt

P23395 - SYM_THET8

Protein

Methionine--tRNA ligase

Gene

metG

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi127 – 1271Zinc
    Metal bindingi130 – 1301Zinc
    Metal bindingi144 – 1441Zinc
    Metal bindingi147 – 1471Zinc
    Binding sitei300 – 3001ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-KW
    3. methionine-tRNA ligase activity Source: UniProtKB-HAMAP
    4. tRNA binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. methionyl-tRNA aminoacylation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-1332-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methionine--tRNA ligase (EC:6.1.1.10)
    Alternative name(s):
    Methionyl-tRNA synthetase
    Short name:
    MetRS
    Gene namesi
    Name:metG
    Synonyms:metS
    Ordered Locus Names:TTHA1298
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 618618Methionine--tRNA ligasePRO_0000139258Add
    BLAST

    Proteomic databases

    PRIDEiP23395.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi300852.TTHA1298.

    Structurei

    Secondary structure

    1
    618
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi20 – 3819
    Beta strandi42 – 509
    Helixi54 – 6310
    Helixi67 – 8418
    Beta strandi90 – 945
    Helixi98 – 11316
    Beta strandi117 – 12711
    Turni128 – 1314
    Beta strandi132 – 1343
    Turni136 – 1383
    Turni145 – 1473
    Beta strandi152 – 16110
    Helixi163 – 1664
    Helixi167 – 1759
    Beta strandi180 – 1834
    Helixi184 – 19411
    Beta strandi204 – 2063
    Turni207 – 2093
    Beta strandi219 – 2246
    Helixi226 – 2316
    Helixi233 – 2364
    Turni237 – 2426
    Helixi244 – 2496
    Helixi250 – 2523
    Beta strandi253 – 2586
    Helixi259 – 2613
    Helixi262 – 2665
    Helixi268 – 2769
    Beta strandi282 – 2876
    Turni300 – 3023
    Helixi308 – 3158
    Helixi317 – 32711
    Helixi338 – 34811
    Helixi349 – 3535
    Helixi354 – 36714
    Helixi379 – 3868
    Helixi387 – 39610
    Helixi400 – 42122
    Helixi423 – 4264
    Turni427 – 4293
    Helixi431 – 45222
    Turni453 – 4553
    Helixi457 – 46610
    Helixi475 – 4795
    Beta strandi480 – 4823

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A8HX-ray2.00A1-500[»]
    1WOYX-ray2.00A1-500[»]
    2D54X-ray2.00A1-502[»]
    2D5BX-ray1.80A1-500[»]
    3VU8X-ray2.20A1-502[»]
    ProteinModelPortaliP23395.
    SMRiP23395. Positions 1-500, 512-615.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23395.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini518 – 618101tRNA-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi12 – 2211"HIGH" regionAdd
    BLAST
    Motifi297 – 3015"KMSKS" region

    Sequence similaritiesi

    Contains 1 tRNA-binding domain.Curated

    Phylogenomic databases

    eggNOGiCOG0143.
    HOGENOMiHOG000200401.
    KOiK01874.
    OMAiHPEFVQP.
    OrthoDBiEOG6CVV9B.
    PhylomeDBiP23395.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    2.40.50.140. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPiMF_01228. Met_tRNA_synth_type2.
    InterProiIPR004495. 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]
    PfamiPF09334. tRNA-synt_1g. 1 hit.
    PF01588. tRNA_bind. 1 hit.
    [Graphical view]
    PRINTSiPR01041. TRNASYNTHMET.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00398. metG. 1 hit.
    TIGR00399. metG_C_term. 1 hit.
    PROSITEiPS50886. TRBD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23395-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKVFYVTTP IYYVNAEPHL GHAYTTVVAD FLARWHRLDG YRTFFLTGTD    50
    EHGETVYRAA QAAGEDPKAF VDRVSGRFKR AWDLLGIAYD DFIRTTEERH 100
    KKVVQLVLKK VYEAGDIYYG EYEGLYCVSC ERFYTEKELV EGLCPIHGRP 150
    VERRKEGNYF FRMEKYRPWL QEYIQENPDL IRPEGYRNEV LAMLAEPIGD 200
    LSISRPKSRV PWGIPLPWDE NHVTYVWFDA LLNYVSALDY PEGEAYRTFW 250
    PHAWHLIGKD ILKPHAVFWP TMLKAAGIPM YRHLNVGGFL LGPDGRKMSK 300
    TLGNVVDPFA LLEKYGRDAL RYYLLREIPY GQDTPVSEEA LRTRYEADLA 350
    DDLGNLVQRT RAMLFRFAEG RIPEPVAGEE LAEGTGLAGR LRPLVRELKF 400
    HVALEEAMAY VKALNRYINE KKPWELFKKE PEEARAVLYR VVEGLRIASI 450
    LLTPAMPDKM AELRRALGLK EEVRLEEAER WGLAEPRPIP EEAPVLFPKK 500
    EAKVEAKPKE EAWIGIEDFA KVELRVAEVL AAEKHPNADR LLVLRLSLGN 550
    EERTVVSGIA KWYRPEELVG KKVVLVANLK PAKLRGIESQ GMILAAQEGE 600
    ALALVTVEGE VPPGAVVK 618
    Length:618
    Mass (Da):70,693
    Last modified:March 29, 2005 - v2
    Checksum:i920A449052C62558
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti615 – 6184AVVK → RW in AAA27510. (PubMed:1993699)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64273 Genomic DNA. Translation: AAA27510.1.
    AP008226 Genomic DNA. Translation: BAD71121.1.
    RefSeqiYP_144564.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD71121; BAD71121; BAD71121.
    GeneIDi3169329.
    KEGGittj:TTHA1298.
    PATRICi23957557. VBITheThe93045_1276.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64273 Genomic DNA. Translation: AAA27510.1 .
    AP008226 Genomic DNA. Translation: BAD71121.1 .
    RefSeqi YP_144564.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A8H X-ray 2.00 A 1-500 [» ]
    1WOY X-ray 2.00 A 1-500 [» ]
    2D54 X-ray 2.00 A 1-502 [» ]
    2D5B X-ray 1.80 A 1-500 [» ]
    3VU8 X-ray 2.20 A 1-502 [» ]
    ProteinModelPortali P23395.
    SMRi P23395. Positions 1-500, 512-615.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA1298.

    Chemistry

    ChEMBLi CHEMBL1641341.

    Proteomic databases

    PRIDEi P23395.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD71121 ; BAD71121 ; BAD71121 .
    GeneIDi 3169329.
    KEGGi ttj:TTHA1298.
    PATRICi 23957557. VBITheThe93045_1276.

    Phylogenomic databases

    eggNOGi COG0143.
    HOGENOMi HOG000200401.
    KOi K01874.
    OMAi HPEFVQP.
    OrthoDBi EOG6CVV9B.
    PhylomeDBi P23395.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-1332-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P23395.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    2.40.50.140. 1 hit.
    3.40.50.620. 2 hits.
    HAMAPi MF_01228. Met_tRNA_synth_type2.
    InterProi IPR004495. 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 ]
    Pfami PF09334. tRNA-synt_1g. 1 hit.
    PF01588. tRNA_bind. 1 hit.
    [Graphical view ]
    PRINTSi PR01041. TRNASYNTHMET.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00398. metG. 1 hit.
    TIGR00399. metG_C_term. 1 hit.
    PROSITEi PS50886. TRBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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).

    Entry informationi

    Entry nameiSYM_THET8
    AccessioniPrimary (citable) accession number: P23395
    Secondary accession number(s): Q5SIR6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3