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A1TR35 (SYFA_ACIAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. 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:Aave_2855
OrganismAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length350 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 – 350350Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000059231

Sites

Metal binding2711Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TR35 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 72C1C9E61876906E

FASTA35038,912
        10         20         30         40         50         60 
MNELDSLVDA ARRMFADAAT PTDLENAKAQ FLGKAGRVTE LLKGLAQLPV EEKKSRGAAV 

        70         80         90        100        110        120 
NVAKQAIEQA LNERRQALAD AELQAQLQAE ALDVTLPGRQ RGQGGLHPVS LTLERIEGIF 

       130        140        150        160        170        180 
GSMGFDVADG PEIESDWFNF TALNTPEDHP ARSMHDTFYV EGGTASAPLL LRTHTSPMQI 

       190        200        210        220        230        240 
RHAVQHVKKH RALLDAGQPM PEIRVIAPGR TYRVDSDATH SPMFHQCEGL WIGENVSFKD 

       250        260        270        280        290        300 
LKVVFTAFCR TFFESDDLVL RFRPSFFPFT EPSAEIDIQF QDGPLAGRWL EVAGSGQVHP 

       310        320        330        340        350 
NVVRNMGLDP EKYIGFAFGM GPDRLTMLRY GVNDLRLFFD GDIRFLSQFQ 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AAC00-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000512 Genomic DNA. Translation: ABM33423.1.
RefSeqYP_971197.1. NC_008752.1.

3D structure databases

ProteinModelPortalA1TR35.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TR35.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4668091.
GenomeReviewsGene locus Aave_2855 in contig CP000512_GR.
KEGGaav:Aave_2855.
NMPDRfig|397945.5.peg.2426.
PATRIC20680845. VBIAciCit38535_2901.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBA1TR35.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycAAVE397945:AAVE_2855-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_ACIAC
AccessionPrimary (citable) accession number: A1TR35
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: January 25, 2012
This is version 41 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