Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A3MJU2 (SYFA_BURM7)

Last modified February 9, 2010. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phenylalanyl-tRNA synthetase alpha chain
    EC=6.1.1.20
Alternative name(s):
    Phenylalanine--tRNA ligase alpha chain
      Short name=PheRS
Gene names
Name: pheS
Ordered Locus Names: BMA10247_0967
OrganismBurkholderia mallei (strain NCTC 10247) [Complete proteome] [HAMAP]
Taxonomic identifier320389 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length337 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. HAMAP MF_00281

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Phenylalanyl-tRNA synthetase alpha chain HAMAP MF_00281
PRO_1000006805

Sites

Metal binding2581Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MJU2-1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 5343093C696E0F5E

FASTA33737,996
        10         20         30         40         50         60 
MDLDQIVADA QQSFEGAADI TTLENEKARF LGKSGALTEL LKGLGKLDPE TRKTEGARIN 

        70         80         90        100        110        120 
VAKQQVEAAL NARRQALADA LLNQRLAAEA IDVTLPGRGA GAGSLHPVMR TWERVEQIFR 

       130        140        150        160        170        180 
SIGFDVADGP EIETDWYNFT ALNSPENHPA RSMQDTFYVD GKDADGRPLL LRTHTSPMQV 

       190        200        210        220        230        240 
RYARMNRPPI KVIAPGRTYR VDSDATHSPM FNQVEGLWID ENVSFADLKG AYTDFLKKFF 

       250        260        270        280        290        300 
ERDDILVRFR PSYFPFTEPS AEIDMMFEHG KNAGKWLEIS GSGQVHPTVI RNMGLDPERY 

       310        320        330 
IGFAFGSGLE RLTMLRYGVQ DLRLFFENDL RFLRQFA 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000548 Genomic DNA. Translation: ABO06722.1.
RefSeqYP_001080528.2.

3D structure databases

SMRA3MJU2. Positions 82-337.
ModBaseSearch...

Genome annotation databases

GeneID4894419.
GenomeReviewsGene locus BMA10247_0967 in contig CP000548_GR.
KEGGbmn:BMA10247_0967.
TIGRBMA10247_0967.

Phylogenomic databases

HOGENOMHBG284353.
OMAFRASYFP.

Family and domain databases

HAMAPMF_00281. Phe_tRNA_synth_alpha1.
[Tree]
InterProIPR006195. aa-tRNA-synth_II_cons-dom.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_synth_II_N.
IPR002319. Phenylalanyl-tRNA_Synthase_acu.
IPR010978. tRNA_bd_arm.
[Graphical view]
PANTHERPTHR11538. tRNA-synt_2d. 1 hit.
PfamPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
TIGRFAMsTIGR00468. pheS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYFA_BURM7
AccessionPrimary (citable) accession number: A3MJU2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: February 9, 2010
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents