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Reviewed, UniProtKB/Swiss-Prot P56206 (SYG_THET8)

Last modified June 16, 2009. Version 68. 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

Names and origin

Protein namesRecommended name:
    Glycyl-tRNA synthetase
    EC=6.1.1.14
Alternative name(s):
    Glycine--tRNA ligase
      Short name=GlyRS
Gene names
Name: glyQS
Synonyms: glyS
Ordered Locus Names: TTHA0543
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). HAMAP MF_00253

Subunit structure

Homodimer. HAMAP MF_00253

Subcellular location

Cytoplasm. HAMAP MF_00253

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processglycyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glycine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP MF_00253
Chain2 – 506505Glycyl-tRNA synthetase HAMAP MF_00253
PRO_0000072983

Experimental info

Sequence conflict21P → A Ref.1
Sequence conflict116 – 1205YRAME → TGPWR in CAA10903. Ref.2
Sequence conflict171 – 18212KTYVG…EDEAS → QDLRGPRGGRGL Ref.1
Sequence conflict171 – 18212KTYVG…EDEAS → QDLRGPRGGRGL Ref.2
Sequence conflict192 – 2009QGIFVNFKN → RASSSTSRT in CAA10903. Ref.2
Sequence conflict2101P → G Ref.1
Sequence conflict2101P → G Ref.2
Sequence conflict216 – 2205IGKAF → SARPS in CAA10903. Ref.2
Sequence conflict2671E → R in CAA10903. Ref.2
Sequence conflict284 – 2852EL → SS Ref.1
Sequence conflict303 – 3042LE → SL Ref.1
Sequence conflict3111N → Q Ref.1

Secondary structure

.................................................................................... 506
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56206-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C0794381A539FD89

FASTA50658,387
        10         20         30         40         50         60 
MPASSLDELV ALCKRRGFIF QSSEIYGGLQ GVYDYGPLGV ELKNNLKQAW WRRNVYERDD 

        70         80         90        100        110        120 
MEGLDASVLT HRLVLHYSGH EATFADPMVD NRITKKRYRL DHLLKEQPEE VLKRLYRAME 

       130        140        150        160        170        180 
VEEENLHALV QAMMQAPERA GGAMTAAGVL DPASGEPGDW TPPRYFNMMF KTYVGPVEDE 

       190        200        210        220        230        240 
ASLAYLRPET AQGIFVNFKN VLDATSRKLP FGIAQIGKAF RNEITPRNFI FRVREFEQME 

       250        260        270        280        290        300 
IEYFVRPGED EYWHRYWVEE RLKWWQEMGL SRENLVPYQQ PPEELAHYAK ATVDILYRFP 

       310        320        330        340        350        360 
HGLEELEGIA NRTDFDLGSH TKDQEALGIT ARVLRNEHST QRLAYRDPET GKWFVPYVIE 

       370        380        390        400        410        420 
PSAGVDRGVL ALLAEAFTRE ELPNGEERIV LKLKPQLAPI KVAVIPLVKN RPEITEYAKR 

       430        440        450        460        470        480 
LKARLLALGL GRVLYEDTGN IGKAYRRHDE VGTPFAVTVD YDTIGQSKDG TTRLKDTVTV 

       490        500 
RDRDTMEQIR LHVDELEGFL RERLRW 

« Hide

References

« Hide 'large scale' references
[1]"Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus."
Logan D.T., Mazauric M.-H., Kern D., Moras D.
EMBO J. 14:4156-4167(1995) [PubMed: 7556056] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
[2]"Glycyl-tRNA synthetase from Thermus thermophilus -- wide structural divergence with other prokaryotic glycyl-tRNA synthetases and functional inter-relation with prokaryotic and eukaryotic glycylation systems."
Mazauric M.-H., Keith G., Logan D., Kreutzer R., Giege R., Kern D.
Eur. J. Biochem. 251:744-757(1998) [PubMed: 9490048] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ222643 Genomic DNA. Translation: CAA10903.1.
AP008226 Genomic DNA. Translation: BAD70366.1.
RefSeqYP_143809.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1ATIX-ray2.75A/B3-506[»]
1B76X-ray3.40A/B3-506[»]
1GGMX-ray3.40A/B3-506[»]
DisProtDP00032.
ModBaseSearch...

Genome annotation databases

GeneID3169948.
GenomeReviewsGene locus TTHA0543 in contig AP008226_GR.
KEGGttj:TTHA0543.
NMPDRfig|300852.3.peg.700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP56206.
OMAP56206. GIHSRTD.

Enzyme and pathway databases

BioCycTTHE300852:TTHA0543-MON.
BRENDA6.1.1.14. 245.

Family and domain databases

HAMAPMF_00253.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR002315. tRNA-synt_gly.
IPR018160. tRNA-synth_gly_a2dimer_C.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
PANTHERPTHR10745. tRNA-synt_gly. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01043. TRNASYNTHGLY.
TIGRFAMsTIGR00389. glyS_dimeric. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYG_THET8
AccessionPrimary (citable) accession number: P56206
Secondary accession number(s): O50551, Q5SKV0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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