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P59056 (SYFA_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. 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
Ordered Locus Names:BUsg_121
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 Potential.

Subunit structure

Tetramer of two alpha and two beta subunits By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00281.

Sequence similarities

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

Caution

Lacks the conserved glutamate residue that binds magnesium.

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: 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 – 329329Phenylalanine--tRNA ligase alpha subunit HAMAP-Rule MF_00281
PRO_0000126677

Sequences

Sequence LengthMass (Da)Tools
P59056 [UniParc].

Last modified October 25, 2002. Version 1.
Checksum: BD51678030D4E6D4

FASTA32938,862
        10         20         30         40         50         60 
MLILQKLFDS VKIEIKNSHT IDKLDHIRIK YLGKKGIFSN LIKDLKNFSL EERKKYFIIF 

        70         80         90        100        110        120 
NEIKKKTINQ INKKKIELNK IILDKQIEKE KIDVSLPGRR IKNGVIHPIN HTITYIKNFF 

       130        140        150        160        170        180 
SKLGFESISG FEIEDEYHNF DALNIPKDHP ARNIHDTFWF DENRLLRTQT SSMQIRIMKK 

       190        200        210        220        230        240 
EKPPIRLIFP GKVYRNDYDS THTPMFHQVE GLIVEKNINF SNLKWIIYNF LRNFFHKDIA 

       250        260        270        280        290        300 
IRFRPSYFPF TTPSAEVDVV TNNGKLLEVL GCGMVHPSVL KNVNIDSNFY SACAFGIGIE 

       310        320 
RITMLRYGIS DLRSFFENDI RFIKQFKHI 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67689.1.
RefSeqNP_660478.1. NC_004061.1.

3D structure databases

ProteinModelPortalP59056.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg121.

Proteomic databases

PRIDEP59056.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67689; AAM67689; BUsg_121.
GeneID1005938.
KEGGbas:BUsg121.
PATRIC21247023. VBIBucAph100086_0125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
KOK01889.
OMAFEALNTP.
OrthoDBEOG6WX4QN.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-131-MONOMER.

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...

Entry information

Entry nameSYFA_BUCAP
AccessionPrimary (citable) accession number: P59056
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: October 25, 2002
Last modified: February 19, 2014
This is version 78 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries