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Q65GD2 (SYFA_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:BLi03016, BL00340
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

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 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_0000231962

Sites

Metal binding2561Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65GD2 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 91FF113F0C3FD99E

FASTA34438,798
        10         20         30         40         50         60 
MQEELKRLEK EAVEKVEAAG SLKEVNDVRV AYLGKKGPIT EVLRGMGKLS AEERPKMGAL 

        70         80         90        100        110        120 
ANEVREKIAA AIAEKNARLE EEEVKRKLKE QTIDVTLPGS PVKTGARHPL TIVIEEIEDL 

       130        140        150        160        170        180 
FISMGYSVEE GPEVETDYYN FEALNLPKEH PARDMQDSFY ITEDTLMRTQ TSPVQTRTME 

       190        200        210        220        230        240 
KHKGKGPVKI ICPGKVYRRD NDDATHSHQF MQIEGLCVDR DISMSDLKGT LETVAKKMFG 

       250        260        270        280        290        300 
EEREIRLRPS FFPFTEPSVE VDVSCFKCGG KGCSVCKQTG WIEILGAGMV HPNVLEMAGF 

       310        320        330        340 
DSKQYQGFAF GMGVERIAML KYGIDDIRHF YTNDVRFLSQ FKQA 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU24524.1.
AE017333 Genomic DNA. Translation: AAU41882.1.
RefSeqYP_080162.1. NC_006270.3.
YP_092575.1. NC_006322.1.

3D structure databases

ProteinModelPortalQ65GD2.
SMRQ65GD2. Positions 82-342.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65GD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000054761; EBBACP00000053292; EBBACG00000054752.
EBBACT00000059050; EBBACP00000057483; EBBACG00000059041.
GeneID3028881.
3098552.
GenomeReviewsGene locus BLi03016 in contig AE017333_GR.
Gene locus BL00340 in contig CP000002_GR.
KEGGbld:BLi03016.
bli:BL00340.
NMPDRfig|279010.5.peg.3364.
PATRIC18951758. VBIBacLic203714_3079.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
GeneTreeEBGT00050000002461.
HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBQ65GD2.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI03016-MONOMER.
BLIC279010:BL00340-MONOMER.

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_BACLD
AccessionPrimary (citable) accession number: Q65GD2
Secondary accession number(s): Q62RT6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 57 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