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A5E8L7 (SYFA_BRASB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:BBta_0214
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length360 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 – 360360Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000006802

Sites

Metal binding2601Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A5E8L7 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: E77CA7D9E19620FD

FASTA36039,880
        10         20         30         40         50         60 
MSDLASLETS ILDQIAAAGD EAALEAVRVA ALGKKGSISA LLATLGKMSP DERKTQGAAI 

        70         80         90        100        110        120 
NLAKDKVTQA LAARRDVLKA AALDARLAAE TIDVTLPLQD SPAETGRIHP LSQVMDELTT 

       130        140        150        160        170        180 
IFADMGFSIA EGPDVETDDY NFTKLNFPEG HPAREMHDTF FFNPKPDGSR MLLRTHTSPV 

       190        200        210        220        230        240 
QVRTMLTQKP PIRVICPGRT YRIDSDATHT PQFHQVEGLV IDKGSHLGHL KWILHEFCKA 

       250        260        270        280        290        300 
FFEVDHINMK FRPSFFPFTE PSLEVDIQCR RDKGEIRFGE GEDWLEILGC GMVHPNVLRA 

       310        320        330        340        350        360 
CGIDPDEYQG FAWGMGIDRI AMLKYGMSDL RQLFEGDVRW LSHYGFKPLE VPTLAGGLST 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000494 Genomic DNA. Translation: ABQ32511.1.
RefSeqYP_001236417.1. NC_009485.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5E8L7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5151147.
GenomeReviewsGene locus BBta_0214 in contig CP000494_GR.
KEGGbbt:BBta_0214.
PATRIC21201430. VBIBraSp29847_0419.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
HOGENOMHBG284353.
OMAFRASYFP.
ProtClustDBPRK00488.

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...

Entry information

Entry nameSYFA_BRASB
AccessionPrimary (citable) accession number: A5E8L7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 34 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