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Q1RIS9 (SYFA_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:RBE_0654
OrganismRickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]
Taxonomic identifier336407 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group

Protein attributes

Sequence length349 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 – 349349Phenylalanine--tRNA ligase alpha subunit HAMAP-Rule MF_00281
PRO_0000278010

Sites

Metal binding2581Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1RIS9 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: D473EEEE2C2EFFB0

FASTA34940,516
        10         20         30         40         50         60 
MDNIETILRL AEEKILLVQS LKVLQEYKVE FLGKNGIVTN ELKKLGSLSE QDRKEFGLKI 

        70         80         90        100        110        120 
NKLKEEIQNI IKAKEEILEE EELNLKLSSD KIDLSLPARR YKQGSIHPIT QCMEELIQVF 

       130        140        150        160        170        180 
AKFGFSIEDG PNIENDFHNF TALNFEDDHP ARQMHDTFYL KGQENDKPML LRTHTSTVQI 

       190        200        210        220        230        240 
RAMKNGKPPF RFIAPGRTYR SDSDMTHTPM FHQIEGLVID KDINMGHLKY VITEFIRCFF 

       250        260        270        280        290        300 
ENSNIELRFR PSFFPFTEPS AEVDIRMSKT DKWLEVLGCG MVHPNVLKNV GIDNSQYQGF 

       310        320        330        340 
AFGLGVERFA MLKYNIKDLR QFFEGDMRWL KHYSFSSFDI PNLAGGLTK 

« Hide

References

[1]"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000087 Genomic DNA. Translation: ABE04735.1.
RefSeqYP_537824.1. NC_007940.1.

3D structure databases

ProteinModelPortalQ1RIS9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336407.RBE_0654.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE04735; ABE04735; RBE_0654.
GeneID3996325.
KEGGrbe:RBE_0654.
PATRIC17882766. VBIRicBel102610_0750.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
HOGENOMHOG000242675.
KOK01889.
OMAMGKELNS.
OrthoDBEOG6WX4QN.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycRBEL336407:GJCY-673-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_RICBR
AccessionPrimary (citable) accession number: Q1RIS9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 55 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

Rickettsia bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries