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P68850 (SYFA_STAAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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

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:MW1021
OrganismStaphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]
Taxonomic identifier196620 [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 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_0000126765

Sites

Metal binding2581Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
P68850 [UniParc].

Last modified December 21, 2004. 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]"Genome and virulence determinants of high virulence community-acquired MRSA."
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.
Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MW2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000033 Genomic DNA. Translation: BAB94886.1.
RefSeqNP_645838.1. NC_003923.1.

3D structure databases

ProteinModelPortalP68850.
SMRP68850. Positions 84-351.
ModBaseSearch...

Protein-protein interaction databases

STRINGP68850.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000027038; EBSTAP00000026077; EBSTAG00000027037.
GeneID1003133.
GenomeReviewsGene locus MW1021 in contig BA000033_GR.
KEGGsam:MW1021.
PATRIC19568622. VBIStaAur44266_1070.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
GeneTreeEBGT00050000024011.
HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBP68850.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycSAUR196620:MW1021-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

BindingDBP68850.

Entry information

Entry nameSYFA_STAAW
AccessionPrimary (citable) accession number: P68850
Secondary accession number(s): Q99QR1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: December 21, 2004
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families