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Q2FGF8 (SYG_STAA3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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
Ordered Locus Names:SAUSA300_1525
OrganismStaphylococcus aureus (strain USA300) [Complete proteome] [HAMAP]
Taxonomic identifier367830 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the attachment of glycine to tRNA(Gly) By similarity. HAMAP-Rule MF_00253

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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 termComplete 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 sequence or structural similarity. Source: UniProtKB

protein dimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Glycine--tRNA ligase HAMAP-Rule MF_00253
PRO_1000047384

Regions

Nucleotide binding206 – 2083ATP By similarity
Nucleotide binding216 – 2216ATP By similarity
Nucleotide binding290 – 2912ATP By similarity
Nucleotide binding334 – 3374ATP By similarity
Region221 – 2255Substrate binding By similarity
Region330 – 3345Substrate binding By similarity

Sites

Binding site981Substrate By similarity
Binding site1741Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FGF8 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: F873C180BC51C467

FASTA46353,620
        10         20         30         40         50         60 
MAKDMDTIVS LAKHRGFVFP GSDIYGGLSN TWDYGPLGVE LKNNVKKAWW QKFITQSPFN 

        70         80         90        100        110        120 
VGIDAAILMN PKVWEASGHL NNFNDPMIDN KDSKIRYRAD KLIEDYMQDV KGDENFIADG 

       130        140        150        160        170        180 
LSFEQMKKII DDEGIVCPVS KTANWTEIRQ FNLMFKTFQG VTEDSTNEIF LRPETAQGIF 

       190        200        210        220        230        240 
VNYKNVQRSM RKKLPFGIGQ IGKSFRNEIT PGNFIFRTRE FEQMELEFFC KPGEEIEWQN 

       250        260        270        280        290        300 
YWKTFASDWL TSLNMSSENM RLRDHDEDEL SHYSNATTDI EYKFPFGWGE LWGIASRTDF 

       310        320        330        340        350        360 
DLRKHAEHSG EDFRYHDPET NEKYIPYCIE PSLGADRVTL AFLCDAYDEE GVEGSKDART 

       370        380        390        400        410        420 
VLHFHPALAP YKAAILPLSK KLSGEAIKIF EQLSSKFSID FDESQSIGKR YRRQDEIGTP 

       430        440        450        460 
YCVTFDFDSL EDNQVTVRDR DSMEQVRMPI SELEAFLTEK TKF 

« Hide

References

[1]"Complete genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus."
Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., Perdreau-Remington F.
Lancet 367:731-739(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USA300.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000255 Genomic DNA. Translation: ABD22244.1.
RefSeqYP_494220.1. NC_007793.1.

3D structure databases

HSSPHSSP built from PDB template 2G4C based on UniProtKB Q9UHN1.
ProteinModelPortalQ2FGF8.
SMRQ2FGF8. Positions 2-463.
ModBaseSearch...

Protein-protein interaction databases

STRING451515.SAUSA300_1525.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD22244; ABD22244; SAUSA300_1525.
GeneID3913901.
KEGGsaa:SAUSA300_1525.
PATRIC19592475. VBIStaAur129981_1666.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0423.
HOGENOMHOG000242016.
KOK01880.
OMADLSYFDQ.
ProtClustDBPRK04173.

Enzyme and pathway databases

BioCycSAUR451515:GH3C-1578-MONOMER.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
HAMAPMF_00253_B. Gly_tRNA_synth_B.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR022961. Gly_tRNA_ligase_bac.
IPR002315. tRNA-synt_gly.
[Graphical view]
PANTHERPTHR10745. PTHR10745. 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_STAA3
AccessionPrimary (citable) accession number: Q2FGF8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 21, 2006
Last modified: May 1, 2013
This is version 53 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families