Skip Header

Contribute Send feedback
Read comments (?) or add your own

A6U0V5 (SYFA_STAA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:
Phenylalanine--tRNA ligase alpha chain

EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha chain
Short name=PheRS
Gene names
Name:pheS
Ordered Locus Names:SaurJH1_1219
OrganismStaphylococcus aureus (strain JH1) [Complete proteome] [HAMAP]
Taxonomic identifier359787 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00281

Cofactor

Binds 2 magnesium ions per tetramer By similarity. HAMAP MF_00281

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm By similarity HAMAP MF_00281.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 1 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphenylalanyl-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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000078851

Sites

Metal binding2581Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A6U0V5 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 01FD437729B8FDF7

FASTA35240,121
        10         20         30         40         50         60 
MSEQQTMSEL KQQALVDINE ANDERALQEV KVKYLGKKGS VSGLMKLMKD LPNEEKPAFG 

        70         80         90        100        110        120 
QKVNELRQTI QNELDERQQM LVKEKLNKQL AEETIDVSLP GRHIEIGSKH PLTRTIEEIE 

       130        140        150        160        170        180 
DLFLGLGYEI VNGYEVEQDH YNFEMLNLPK SHPARDMQDS FYITDEILLR THTSPVQART 

       190        200        210        220        230        240 
MESRHGQGPV KIICPGKVYR RDSDDATHSH QFTQIEGLVV DKNVKMSDLK GTLELLAKKL 

       250        260        270        280        290        300 
FGADREIRLR PSYFPFTEPS VEVDVSCFKC KGKGCNVCKH TGWIEILGAG MVHPNVLEMA 

       310        320        330        340        350 
GFDSSEYSGF AFGMGPDRIA MLKYGIEDIR HFYTNDVRFL DQFKAVEDRG DM 

« Hide

References

[1]"Complete sequence of chromosome of Staphylococcus aureus subsp. aureus JH1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Tomasz A., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000736 Genomic DNA. Translation: ABR52073.1.
RefSeqYP_001316360.1. NC_009632.1.

3D structure databases

ProteinModelPortalA6U0V5.
SMRA6U0V5. Positions 84-351.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6U0V5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000014036; EBSTAP00000013539; EBSTAG00000014035.
GeneID5316636.
GenomeReviewsGene locus SaurJH1_1219 in contig CP000736_GR.
KEGGsah:SaurJH1_1219.
PATRIC19534285. VBIStaAur98826_1253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
GeneTreeEBGT00050000024011.
HOGENOMHBG284353.
OMAFRASYFP.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycSAUR359787:SAURJH1_1219-MONOMER.

Family and domain databases

HAMAPMF_00281. Phe_tRNA_synth_alpha1.
[Tree]
InterProIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_synth_II_N.
IPR022911. Phe_tRNA_synth_alpha1_bac.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR010978. tRNA-bd_arm.
[Graphical view]
KOK01889.
PfamPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMSSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00468. PheS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBA6U0V5.

Entry information

Entry nameSYFA_STAA2
AccessionPrimary (citable) accession number: A6U0V5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 37 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