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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)DescriptionActionsGraphical viewLength
Binding sitei99SubstrateBy similarity1
Binding sitei189Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi221 – 223ATP1 Publication3
Nucleotide bindingi231 – 236ATP1 Publication6
Nucleotide bindingi305 – 306ATP1 Publication2
Nucleotide bindingi364 – 367ATP1 Publication4

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

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000729832 – 506Glycine--tRNA ligaseAdd BLAST505

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein dimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi300852.TTHA0543.

Structurei

Secondary structure

1506
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 15Combined sources10
Beta strandi18 – 21Combined sources4
Helixi24 – 26Combined sources3
Beta strandi33 – 35Combined sources3
Helixi37 – 54Combined sources18
Beta strandi59 – 65Combined sources7
Beta strandi68 – 71Combined sources4
Helixi74 – 77Combined sources4
Helixi80 – 83Combined sources4
Beta strandi85 – 90Combined sources6
Beta strandi164 – 167Combined sources4
Beta strandi169 – 173Combined sources5
Beta strandi175 – 177Combined sources3
Helixi180 – 182Combined sources3
Beta strandi183 – 186Combined sources4
Beta strandi188 – 190Combined sources3
Helixi191 – 196Combined sources6
Helixi198 – 205Combined sources8
Beta strandi209 – 221Combined sources13
Helixi229 – 231Combined sources3
Beta strandi234 – 245Combined sources12
Helixi247 – 249Combined sources3
Helixi250 – 267Combined sources18
Helixi272 – 274Combined sources3
Beta strandi275 – 279Combined sources5
Turni282 – 284Combined sources3
Beta strandi290 – 299Combined sources10
Beta strandi302 – 311Combined sources10
Helixi315 – 320Combined sources6
Turni324 – 328Combined sources5
Beta strandi348 – 350Combined sources3
Beta strandi357 – 364Combined sources8
Helixi365 – 376Combined sources12
Beta strandi377 – 381Combined sources5
Turni383 – 385Combined sources3
Beta strandi387 – 391Combined sources5
Helixi395 – 397Combined sources3
Beta strandi401 – 407Combined sources7
Helixi412 – 426Combined sources15
Turni427 – 429Combined sources3
Beta strandi433 – 435Combined sources3
Helixi441 – 450Combined sources10
Beta strandi454 – 459Combined sources6
Helixi461 – 464Combined sources4
Turni473 – 476Combined sources4
Beta strandi477 – 482Combined sources6
Turni483 – 485Combined sources3
Beta strandi488 – 492Combined sources5
Helixi493 – 504Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP56206.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni236 – 240Substrate binding5
Regioni360 – 364Substrate binding5

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)DescriptionActionsGraphical viewLength
Sequence conflicti2P → A (PubMed:7556056).Curated1
Sequence conflicti116 – 120YRAME → TGPWR in CAA10903 (PubMed:9490048).Curated5
Sequence conflicti171 – 182KTYVG…EDEAS → QDLRGPRGGRGL (PubMed:7556056).CuratedAdd BLAST12
Sequence conflicti171 – 182KTYVG…EDEAS → QDLRGPRGGRGL (PubMed:9490048).CuratedAdd BLAST12
Sequence conflicti192 – 200QGIFVNFKN → RASSSTSRT in CAA10903 (PubMed:9490048).Curated9
Sequence conflicti210P → G (PubMed:7556056).Curated1
Sequence conflicti210P → G (PubMed:9490048).Curated1
Sequence conflicti216 – 220IGKAF → SARPS in CAA10903 (PubMed:9490048).Curated5
Sequence conflicti267E → R in CAA10903 (PubMed:9490048).Curated1
Sequence conflicti284 – 285EL → SS (PubMed:7556056).Curated2
Sequence conflicti303 – 304LE → SL (PubMed:7556056).Curated2
Sequence conflicti311N → Q (PubMed:7556056).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ATIX-ray2.75A/B3-506[»]
1B76X-ray3.40A/B3-506[»]
1GGMX-ray3.40A/B3-506[»]
DisProtiDP00032.
ProteinModelPortaliP56206.
SMRiP56206.
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

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: November 2, 2016
This is version 117 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.