Skip Header

Contribute Send feedback
Read comments (?) or add your own

A1A1X6 (SYFA_BIFAA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:BAD_0928
OrganismBifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a) [Complete proteome] [HAMAP]
Taxonomic identifier367928 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeBifidobacterialesBifidobacteriaceaeBifidobacterium

Protein attributes

Sequence length355 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 – 355355Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000006801

Sites

Metal binding2731Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A1A1X6 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: F7E21EEEE4C666BC

FASTA35538,936
        10         20         30         40         50         60 
MAEGAVFDAQ AVTDAVAEGI AKIENASTME ELKAIKTQYA GAESAMTQAS KAIGALPKDQ 

        70         80         90        100        110        120 
KKDAGKLMGK LRADFGRAFG TKEKQVKAEE EARELAAETV DMTLPVNRKP LGARHPLPKL 

       130        140        150        160        170        180 
MEDVEDFFIS MGWQISDGPE VETEWYDFDA LNFGPDHPAR QMQDTFYVKG NQAKDAAGFV 

       190        200        210        220        230        240 
GSNMVLRTQT SSDQVRGLIT RGVPLYIACP GRVFRTDELD ATHTPVFHQV EALAVDKHLT 

       250        260        270        280        290        300 
MADLKGVLDK LAVAMFGPEA KTRLRPSYFP FTEPSAELDL WFPDKKGGAG WLEWGGCGMV 

       310        320        330        340        350 
NPNVLKSAGL DPEVYTGFAF GVGVERTLLL RHDINDMHDL VEGDVRFSEQ FVMGE 

« Hide

References

[1]"Bifidobacterium adolescentis complete genome sequence."
Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S., Tanaka K., Watanabe K.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15703 / DSM 20083 / NCTC 11814 / E194a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009256 Genomic DNA. Translation: BAF39709.1.
RefSeqYP_909791.1. NC_008618.1.

3D structure databases

ProteinModelPortalA1A1X6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1A1X6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4556529.
GenomeReviewsGene locus BAD_0928 in contig AP009256_GR.
KEGGbad:BAD_0928.
NMPDRfig|1680.3.peg.1199.
PATRIC21101283. VBIBifAdo27973_1005.

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_BIFAA
AccessionPrimary (citable) accession number: A1A1X6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 40 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