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Q57AE0 (SYFA_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:BruAb1_2097
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length369 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 By similarity. HAMAP-Rule MF_00281

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.

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 – 369369Phenylalanine--tRNA ligase alpha subunit HAMAP-Rule MF_00281
PRO_0000231967

Sites

Metal binding2691Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57AE0 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: BC2B822DB0270926

FASTA36941,598
        10         20         30         40         50         60 
MSDLEQLERQ ILEDIAAAVD EQGIEAVRVA ALGKKGTVSE KLKTLGGMSP EERQMQGPAI 

        70         80         90        100        110        120 
NGLKNRVTEA LSERRTELRK AAVAARLERE KVDVTLPVRE SAASRGRIHP ISQVIDEITA 

       130        140        150        160        170        180 
IFADMGFSIA EGPDIETDYY NFTALNFPEG HPAREMHDTF FFNPDEKGER KLLRTHTSPV 

       190        200        210        220        230        240 
QVHTMEKFAA MRDKEGRDEP IRIVIPGKTY RMDSDATHSP MFHQVEGLVV DKSANVANMK 

       250        260        270        280        290        300 
WVLEEFCKAF FEVPSVKMRM RPSFFPFTEP SVEVDIQCDR SGPHVKFGEG NDWLEILGCG 

       310        320        330        340        350        360 
MVHPNVLRMS GYDPEVYQGF AWGMGIDRIA MLKYGMPDLR AFFDADVRWI EHYGFRPLDI 


PTLFGGLSA 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017223 Genomic DNA. Translation: AAX75394.1.
RefSeqYP_222755.1. NC_006932.1.

3D structure databases

ProteinModelPortalQ57AE0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb1_2097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX75394; AAX75394; BruAb1_2097.
GeneID3341112.
KEGGbmb:BruAb1_2097.
PATRIC17826055. VBIBruAbo15061_2215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
HOGENOMHOG000242675.
KOK01889.
OMAFEALNTP.
OrthoDBEOG6WX4QN.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycBABO262698:GJC2-2147-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_BRUAB
AccessionPrimary (citable) accession number: Q57AE0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: May 10, 2005
Last modified: February 19, 2014
This is version 57 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

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries