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P27001 (SYFA_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 103. 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 subunit

EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunit
Short name=PheRS
Gene names
Name:pheS
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per tetramer.

Subunit structure

Tetramer of two alpha and two beta subunits.

Subcellular location

Cytoplasm HAMAP-Rule MF_00281.

Sequence similarities

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

Caution

The sequence shown here has been extracted from PDB entry 1B70.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Phenylalanine--tRNA ligase alpha subunit HAMAP-Rule MF_00281
PRO_0000126786

Sites

Metal binding2621Magnesium

Secondary structure

......................................................... 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27001 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: DEE0237F7CD9A461

FASTA35039,259
        10         20         30         40         50         60 
MLEEALAAIQ NARDLEELKA LKARYLGKKG LLTQEMKGLS ALPLEERRKR GQELNAIKAA 

        70         80         90        100        110        120 
LEAALEAREK ALEEAALKEA LERERVDVSL PGASLFSGGL HPITLMEREL VEIFRALGYQ 

       130        140        150        160        170        180 
AVEGPEVESE FFNFDALNIP EHHPARDMWD TFWLTGEGFR LEGPLGEEVE GRLLLRTHTS 

       190        200        210        220        230        240 
PMQVRYMVAH TPPFRIVVPG RVFRFEQTDA THEAVFHQLE GLVVGEGIAM AHLKGAIYEL 

       250        260        270        280        290        300 
AQALFGPDSK VRFQPVYFPF VEPGAQFAVW WPEGGKWLEL GGAGMVHPKV FQAVDAYRER 

       310        320        330        340        350 
LGLPPAYRGV TGFAFGLGVE RLAMLRYGIP DIRYFFGGRL KFLEQFKGVL 

« Hide

References

[1]"Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue."
Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.
J. Mol. Biol. 287:555-568(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B70X-ray2.70A1-350[»]
1B7YX-ray2.50A1-350[»]
2AKWX-ray2.80A85-350[»]
2ALYX-ray2.60A85-350[»]
2AMCX-ray2.70A85-350[»]
2IY5X-ray3.10A1-350[»]
3TEHX-ray2.85A1-350[»]
DisProtDP00053.
ProteinModelPortalP27001.
SMRP27001. Positions 6-350.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6104N.
MINTMINT-88286.
STRING262724.TTC1594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00281. Phe_tRNA_synth_alpha1.
InterProIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_ligase_II_N.
IPR022911. Phe_tRNA_ligase_alpha1_bac.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR010978. tRNA-bd_arm.
[Graphical view]
PfamPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMSSF46589. SSF46589. 1 hit.
TIGRFAMsTIGR00468. pheS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27001.

Entry information

Entry nameSYFA_THETH
AccessionPrimary (citable) accession number: P27001
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries