Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q67QF3 (SYFA_SYMTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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 subunit

EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunit
Short name=PheRS
Gene names
Name:pheS
Synonyms:pheSA
Ordered Locus Names:STH1105
OrganismSymbiobacterium thermophilum (strain T / IAM 14863) [Complete proteome] [HAMAP]
Taxonomic identifier292459 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XVIII. Incertae SedisSymbiobacterium

Protein attributes

Sequence length343 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 – 343343Phenylalanine--tRNA ligase alpha subunit HAMAP-Rule MF_00281
PRO_0000126779

Sites

Metal binding2581Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q67QF3 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 920E073E177DCE5E

FASTA34337,988
        10         20         30         40         50         60 
MKDQLLKLRD EALAAIAAAA DVGAIQEMRV RYLGKKSELS QVLGGLGRLP TVEERKAMGA 

        70         80         90        100        110        120 
LGNEIKQAIT AALDAREAEL AAAALQARLA SERIDVTLPG APVRRGHLHI LNQVIHRIEE 

       130        140        150        160        170        180 
IFIAMGYEVA ESRQVETDWY NFEALNIPKG HPARDAQDSL FLSEEVLLRT HTSNTQIRYM 

       190        200        210        220        230        240 
LEVARGRTPV KIICPGRVFR RDFEDATHAM MFHQVEGLVI DKGITMASLK GALTEMARAL 

       250        260        270        280        290        300 
FGPDVGIRLR PSYFPFTEPS AEMDISCIFC GGKGCRTCKG SGWIEIGGSG MVHPNVLRAG 

       310        320        330        340 
GYDPEEVSGW AFGYGPERVA MLMYGIEDIR HFVNNDMRFL RQF 

« Hide

References

[1]"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism."
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.
Nucleic Acids Res. 32:4937-4944(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: T / IAM 14863.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006840 Genomic DNA. Translation: BAD40090.1.
RefSeqYP_074934.1. NC_006177.1.

3D structure databases

ProteinModelPortalQ67QF3.
SMRQ67QF3. Positions 83-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292459.STH1105.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD40090; BAD40090; STH1105.
GeneID2979552.
KEGGsth:STH1105.
PATRIC23780354. VBISymThe116959_1106.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
HOGENOMHOG000242675.
KOK01889.
OMAQIRTMEH.
OrthoDBEOG6WX4QN.

Enzyme and pathway databases

BioCycSTHE292459:GJMM-1166-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_SYMTH
AccessionPrimary (citable) accession number: Q67QF3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 67 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries