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P23395

- SYM_THET8

UniProt

P23395 - SYM_THET8

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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

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
Complete GO annotation...

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-HAMAP
Complete GO annotation...

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

        10         20         30         40         50
MEKVFYVTTP IYYVNAEPHL GHAYTTVVAD FLARWHRLDG YRTFFLTGTD
60 70 80 90 100
EHGETVYRAA QAAGEDPKAF VDRVSGRFKR AWDLLGIAYD DFIRTTEERH
110 120 130 140 150
KKVVQLVLKK VYEAGDIYYG EYEGLYCVSC ERFYTEKELV EGLCPIHGRP
160 170 180 190 200
VERRKEGNYF FRMEKYRPWL QEYIQENPDL IRPEGYRNEV LAMLAEPIGD
210 220 230 240 250
LSISRPKSRV PWGIPLPWDE NHVTYVWFDA LLNYVSALDY PEGEAYRTFW
260 270 280 290 300
PHAWHLIGKD ILKPHAVFWP TMLKAAGIPM YRHLNVGGFL LGPDGRKMSK
310 320 330 340 350
TLGNVVDPFA LLEKYGRDAL RYYLLREIPY GQDTPVSEEA LRTRYEADLA
360 370 380 390 400
DDLGNLVQRT RAMLFRFAEG RIPEPVAGEE LAEGTGLAGR LRPLVRELKF
410 420 430 440 450
HVALEEAMAY VKALNRYINE KKPWELFKKE PEEARAVLYR VVEGLRIASI
460 470 480 490 500
LLTPAMPDKM AELRRALGLK EEVRLEEAER WGLAEPRPIP EEAPVLFPKK
510 520 530 540 550
EAKVEAKPKE EAWIGIEDFA KVELRVAEVL AAEKHPNADR LLVLRLSLGN
560 570 580 590 600
EERTVVSGIA KWYRPEELVG KKVVLVANLK PAKLRGIESQ GMILAAQEGE
610
ALALVTVEGE VPPGAVVK
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.
RefSeqiWP_011228577.1. NC_006461.1.
YP_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 WP_011228577.1. NC_006461.1.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 121 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