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A9M9V4 (SYFA_BRUC2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:BCAN_A2166
OrganismBrucella canis (strain ATCC 23365 / NCTC 10854) [Complete proteome] [HAMAP]
Taxonomic identifier483179 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length369 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 – 369369Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000078827

Sites

Metal binding2691Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A9M9V4 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 0DB5F54B59E8E544

FASTA36941,672
        10         20         30         40         50         60 
MNDLEQLERQ ILEDIAAAVD EQGIEAVRVA ALGKKGTVSE KLKTLGGMSP EERQMQGPAI 

        70         80         90        100        110        120 
NGLKNRVTEA LSERRTELRK AAVAARLERE KVDVTLPVRE SAASRGRIHP ISQVIDEITA 

       130        140        150        160        170        180 
IFADMGFSIA EGPDIETDYY NFTALNFPEG HPAREMHDTF FFNPDEKSER KLLRTHTSPV 

       190        200        210        220        230        240 
QVHTMEKFAA MRDKEGRDEL IRIVIPGKTY RMDSDATHSP MFHQVEGLVV DKSANVANMK 

       250        260        270        280        290        300 
WVLEEFCKAF FEVPSVKMRM RPSFFPFTEP SVEVDIQCDR SGPHVKFGEG NDWLEILGCG 

       310        320        330        340        350        360 
MVHPNVLRMS GYDPEVYQGF AWGMGIDRIA MLKYGMPDLR AFFDADVRWI EHYGFRPLDI 


PTLFGGLSA 

« Hide

References

[1]"Brucella canis ATCC 23365 whole genome shotgun sequencing project."
Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. expand/collapse author list , Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C., Munk C., Brettin T.S.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23365 / NCTC 10854.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000872 Genomic DNA. Translation: ABX63149.1.
RefSeqYP_001593920.1. NC_010103.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA9M9V4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5784235.
GenomeReviewsGene locus BCAN_A2166 in contig CP000872_GR.
KEGGbcs:BCAN_A2166.
PATRIC17833068. VBIBruCan25663_2160.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284353.
OMAFRASYFP.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycBCAN483179:BCAN_A2166-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_BRUC2
AccessionPrimary (citable) accession number: A9M9V4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 30 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