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Protein

Glycine--tRNA ligase

Gene

glyQS

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of glycine to tRNA(Gly).By similarity

Catalytic activityi

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei99 – 991SubstrateBy similarity
Binding sitei189 – 1891Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi221 – 2233ATP1 Publication
Nucleotide bindingi231 – 2366ATP1 Publication
Nucleotide bindingi305 – 3062ATP1 Publication
Nucleotide bindingi364 – 3674ATP1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • glycine-tRNA ligase activity Source: UniProtKB
  • protein dimerization activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-568-MONOMER.
BRENDAi6.1.1.14. 2305.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine--tRNA ligase (EC:6.1.1.14)
Alternative name(s):
Glycyl-tRNA synthetase
Short name:
GlyRS
Gene namesi
Name:glyQS
Synonyms:glyS
Ordered Locus Names:TTHA0543
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 506505Glycine--tRNA ligasePRO_0000072983Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi300852.TTHA0543.

Structurei

Secondary structure

1
506
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1510Combined sources
Beta strandi18 – 214Combined sources
Helixi24 – 263Combined sources
Beta strandi33 – 353Combined sources
Helixi37 – 5418Combined sources
Beta strandi59 – 657Combined sources
Beta strandi68 – 714Combined sources
Helixi74 – 774Combined sources
Helixi80 – 834Combined sources
Beta strandi85 – 906Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi175 – 1773Combined sources
Helixi180 – 1823Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi188 – 1903Combined sources
Helixi191 – 1966Combined sources
Helixi198 – 2058Combined sources
Beta strandi209 – 22113Combined sources
Helixi229 – 2313Combined sources
Beta strandi234 – 24512Combined sources
Helixi247 – 2493Combined sources
Helixi250 – 26718Combined sources
Helixi272 – 2743Combined sources
Beta strandi275 – 2795Combined sources
Turni282 – 2843Combined sources
Beta strandi290 – 29910Combined sources
Beta strandi302 – 31110Combined sources
Helixi315 – 3206Combined sources
Turni324 – 3285Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi357 – 3648Combined sources
Helixi365 – 37612Combined sources
Beta strandi377 – 3815Combined sources
Turni383 – 3853Combined sources
Beta strandi387 – 3915Combined sources
Helixi395 – 3973Combined sources
Beta strandi401 – 4077Combined sources
Helixi412 – 42615Combined sources
Turni427 – 4293Combined sources
Beta strandi433 – 4353Combined sources
Helixi441 – 45010Combined sources
Beta strandi454 – 4596Combined sources
Helixi461 – 4644Combined sources
Turni473 – 4764Combined sources
Beta strandi477 – 4826Combined sources
Turni483 – 4853Combined sources
Beta strandi488 – 4925Combined sources
Helixi493 – 50412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATIX-ray2.75A/B3-506[»]
1B76X-ray3.40A/B3-506[»]
1GGMX-ray3.40A/B3-506[»]
DisProtiDP00032.
ProteinModelPortaliP56206.
SMRiP56206. Positions 2-506.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56206.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 2405Substrate binding
Regioni360 – 3645Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D9H. Bacteria.
COG0423. LUCA.
HOGENOMiHOG000242016.
KOiK01880.
OMAiERFGWVE.
PhylomeDBiP56206.

Family and domain databases

CDDicd00774. GlyRS-like_core. 1 hit.
Gene3Di3.40.50.800. 1 hit.
HAMAPiMF_00253_B. Gly_tRNA_synth_B. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR022961. Gly_tRNA_ligase_bac.
IPR033731. GlyRS-like_core.
IPR002315. tRNA-synt_gly.
[Graphical view]
PANTHERiPTHR10745. PTHR10745. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSiPR01043. TRNASYNTHGLY.
SUPFAMiSSF52954. SSF52954. 1 hit.
TIGRFAMsiTIGR00389. glyS_dimeric. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56206-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPASSLDELV ALCKRRGFIF QSSEIYGGLQ GVYDYGPLGV ELKNNLKQAW
60 70 80 90 100
WRRNVYERDD MEGLDASVLT HRLVLHYSGH EATFADPMVD NRITKKRYRL
110 120 130 140 150
DHLLKEQPEE VLKRLYRAME VEEENLHALV QAMMQAPERA GGAMTAAGVL
160 170 180 190 200
DPASGEPGDW TPPRYFNMMF KTYVGPVEDE ASLAYLRPET AQGIFVNFKN
210 220 230 240 250
VLDATSRKLP FGIAQIGKAF RNEITPRNFI FRVREFEQME IEYFVRPGED
260 270 280 290 300
EYWHRYWVEE RLKWWQEMGL SRENLVPYQQ PPEELAHYAK ATVDILYRFP
310 320 330 340 350
HGLEELEGIA NRTDFDLGSH TKDQEALGIT ARVLRNEHST QRLAYRDPET
360 370 380 390 400
GKWFVPYVIE PSAGVDRGVL ALLAEAFTRE ELPNGEERIV LKLKPQLAPI
410 420 430 440 450
KVAVIPLVKN RPEITEYAKR LKARLLALGL GRVLYEDTGN IGKAYRRHDE
460 470 480 490 500
VGTPFAVTVD YDTIGQSKDG TTRLKDTVTV RDRDTMEQIR LHVDELEGFL

RERLRW
Length:506
Mass (Da):58,387
Last modified:January 23, 2007 - v3
Checksum:iC0794381A539FD89
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21P → A (PubMed:7556056).Curated
Sequence conflicti116 – 1205YRAME → TGPWR in CAA10903 (PubMed:9490048).Curated
Sequence conflicti171 – 18212KTYVG…EDEAS → QDLRGPRGGRGL (PubMed:7556056).CuratedAdd
BLAST
Sequence conflicti171 – 18212KTYVG…EDEAS → QDLRGPRGGRGL (PubMed:9490048).CuratedAdd
BLAST
Sequence conflicti192 – 2009QGIFVNFKN → RASSSTSRT in CAA10903 (PubMed:9490048).Curated
Sequence conflicti210 – 2101P → G (PubMed:7556056).Curated
Sequence conflicti210 – 2101P → G (PubMed:9490048).Curated
Sequence conflicti216 – 2205IGKAF → SARPS in CAA10903 (PubMed:9490048).Curated
Sequence conflicti267 – 2671E → R in CAA10903 (PubMed:9490048).Curated
Sequence conflicti284 – 2852EL → SS (PubMed:7556056).Curated
Sequence conflicti303 – 3042LE → SL (PubMed:7556056).Curated
Sequence conflicti311 – 3111N → Q (PubMed:7556056).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ222643 Genomic DNA. Translation: CAA10903.1.
AP008226 Genomic DNA. Translation: BAD70366.1.
RefSeqiWP_011228014.1. NC_006461.1.
YP_143809.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70366; BAD70366; BAD70366.
GeneIDi3169948.
KEGGittj:TTHA0543.
PATRICi23956063. VBITheThe93045_0542.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ222643 Genomic DNA. Translation: CAA10903.1.
AP008226 Genomic DNA. Translation: BAD70366.1.
RefSeqiWP_011228014.1. NC_006461.1.
YP_143809.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATIX-ray2.75A/B3-506[»]
1B76X-ray3.40A/B3-506[»]
1GGMX-ray3.40A/B3-506[»]
DisProtiDP00032.
ProteinModelPortaliP56206.
SMRiP56206. Positions 2-506.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0543.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70366; BAD70366; BAD70366.
GeneIDi3169948.
KEGGittj:TTHA0543.
PATRICi23956063. VBITheThe93045_0542.

Phylogenomic databases

eggNOGiENOG4105D9H. Bacteria.
COG0423. LUCA.
HOGENOMiHOG000242016.
KOiK01880.
OMAiERFGWVE.
PhylomeDBiP56206.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-568-MONOMER.
BRENDAi6.1.1.14. 2305.

Miscellaneous databases

EvolutionaryTraceiP56206.

Family and domain databases

CDDicd00774. GlyRS-like_core. 1 hit.
Gene3Di3.40.50.800. 1 hit.
HAMAPiMF_00253_B. Gly_tRNA_synth_B. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR022961. Gly_tRNA_ligase_bac.
IPR033731. GlyRS-like_core.
IPR002315. tRNA-synt_gly.
[Graphical view]
PANTHERiPTHR10745. PTHR10745. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSiPR01043. TRNASYNTHGLY.
SUPFAMiSSF52954. SSF52954. 1 hit.
TIGRFAMsiTIGR00389. glyS_dimeric. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYG_THET8
AccessioniPrimary (citable) accession number: P56206
Secondary accession number(s): O50551, Q5SKV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 115 of the entry and version 3 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.