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B7HF77 (SYFA_BACC4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. 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:BCB4264_A4672
OrganismBacillus cereus (strain B4264) [Complete proteome] [HAMAP]
Taxonomic identifier405532 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length344 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 By similarity 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 – 344344Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000119388

Sites

Metal binding2561Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
B7HF77 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: EB4175DBE7B38D1E

FASTA34438,990
        10         20         30         40         50         60 
MEARLKELKQ KALELIEEAK ELKGLNDVRV AYLGKKGPIT EVLRGMGKLS AEERPRMGAL 

        70         80         90        100        110        120 
VNEVREAIQT RLEDKISNLE KAVIEAKLAT ETIDVTLPGR PVETGCHHPL TAVVEQIEDV 

       130        140        150        160        170        180 
FIGMGYEVAE GTEVEKDYYN FEALNLPKDH PARDMQDTFY ITEETLLRTH TSSVQARTME 

       190        200        210        220        230        240 
NNKEKGPIKI ICPGKVYRRD DDDATHSHQF MQIEGLVIDK NIRMSDLKGT LQVFVKKMFG 

       250        260        270        280        290        300 
EDREIRLRPS FFPFTEPSVE MDISCMMCHG KGCGTCKGTG WIEILGAGMV HPNVLEMAGY 

       310        320        330        340 
DSKEYQGFAF GMGAERIAML KYGVDDIRHF YTNDVRFLQQ FKRA 

« Hide

References

[1]"Genome sequence of Bacillus cereus B4264."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B4264.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001176 Genomic DNA. Translation: ACK61871.1.
RefSeqYP_002369359.1. NC_011725.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB7HF77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000108183; EBBACP00000108049; EBBACG00000108176.
GeneID7100104.
GenomeReviewsGene locus BCB4264_A4672 in contig CP001176_GR.
KEGGbcb:BCB4264_A4672.
PATRIC18881241. VBIBacCer117876_4524.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002461.
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_BACC4
AccessionPrimary (citable) accession number: B7HF77
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 23 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