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P56206 (SYG_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine--tRNA ligase
EC=6.1.1.14
Alternative name(s):
Glycyl-tRNA synthetase
Short name=GlyRS
Gene names
Name:glyQS
Synonyms:glyS
Ordered Locus Names:TTHA0543
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

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)

Function

Catalyzes the attachment of glycine to tRNA(Gly) By similarity. HAMAP MF_00253_B

Catalytic activity

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). HAMAP MF_00253_B

Subunit structure

Homodimer. Ref.1

Subcellular location

Cytoplasm HAMAP MF_00253_B.

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
Reference proteome
Gene Ontology (GO)
   Biological processglycyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycine-tRNA ligase activity

Inferred from direct assay Ref.4. Source: UniProtKB

protein dimerization activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP MF_00253_B
Chain2 – 506505Glycine--tRNA ligase HAMAP MF_00253_B
PRO_0000072983

Regions

Nucleotide binding221 – 2233ATP HAMAP MF_00253_B
Nucleotide binding231 – 2366ATP HAMAP MF_00253_B
Nucleotide binding305 – 3062ATP HAMAP MF_00253_B
Nucleotide binding364 – 3674ATP HAMAP MF_00253_B
Region236 – 2405Substrate binding HAMAP MF_00253_B
Region360 – 3645Substrate binding HAMAP MF_00253_B

Sites

Binding site991Substrate By similarity
Binding site1891Substrate

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

1 .................................................................................... 506
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56206 [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), SUBUNIT.
[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].
Strain: HB8 / ATCC 27634 / DSM 579.
[4]"Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine."
Arnez J.G., Dock-Bregeon A.-C., Moras D.
J. Mol. Biol. 286:1449-1459(1999) [PubMed: 10064708] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 3-506 IN COMPLEX WITH ATP AND SUBSTRATE ANALOG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ222643 Genomic DNA. Translation: CAA10903.1.
AP008226 Genomic DNA. Translation: BAD70366.1.
RefSeqYP_143809.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATIX-ray2.75A/B3-506[»]
1B76X-ray3.40A/B3-506[»]
1GGMX-ray3.40A/B3-506[»]
ProteinModelPortalP56206.
SMRP56206. Positions 2-506.
DisProtDP00032.
ModBaseSearch...

Protein-protein interaction databases

STRINGP56206.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3169948.
GenomeReviewsGene locus TTHA0543 in contig AP008226_GR.
KEGGttj:TTHA0543.
NMPDRfig|300852.3.peg.700.
PATRIC23956063. VBITheThe93045_0542.

Phylogenomic databases

eggNOGCOG0423.
HOGENOMHBG319978.
OMAGSEWGEL.
ProtClustDBPRK04173.

Enzyme and pathway databases

BioCycTTHE300852:TTHA0543-MONOMER.
BRENDA6.1.1.14. 6341.

Family and domain databases

HAMAPMF_00253_B. Gly_tRNA_synth_B.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR022961. Gly_tRNA_synth_bac.
IPR002315. tRNA-synt_gly.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
KOK01880.
PANTHERPTHR10745. tRNA-synt_gly. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR01043. TRNASYNTHGLY.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
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: January 25, 2012
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents