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Q6F872 (SYFA_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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:ACIAD3042
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length330 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 – 330330Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_0000126654

Sites

Metal binding2551Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6F872 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: A538F98CD0A91A64

FASTA33037,153
        10         20         30         40         50         60 
MRVTMSLEAL TTEALAAIAA AQDLAALDQV RVLFTGKKSQ LAEQSKALGK MDPEQRKVQG 

        70         80         90        100        110        120 
AAIHAVREAI NAALTERQTA LQQAALQQKL ASETIDITLP GRGQHMGSIH PVTQVQERIC 

       130        140        150        160        170        180 
QFFTKAGFSV ATGPEVEDDY HNFEALNIPG HHPARAMHDT FYFDVNHLLR THTSGVQIRT 

       190        200        210        220        230        240 
METTQPPIRI VCPGRVYRCD SDQTHSPMFH QIEGLYVAEN TSFAELKGLL INLLNEFFEK 

       250        260        270        280        290        300 
DLKVRFRPSY FPFTEPSAEV DIMDERGRWL EVLGCGMVHP NVLRAAGIDP EKYKGFAFGL 

       310        320        330 
GVERFAMLRY GINDLRMFYQ NDVRFLRQFA 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG69743.1.
RefSeqYP_047565.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ6F872.
SMRQ6F872. Positions 85-330.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6F872.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2880188.
GenomeReviewsGene locus ACIAD3042 in contig CR543861_GR.
KEGGaci:ACIAD3042.
NMPDRfig|62977.3.peg.2758.
PATRIC20743587. VBIAciSp98416_2717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBQ6F872.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycASP62977:ACIAD3042-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_ACIAD
AccessionPrimary (citable) accession number: Q6F872
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 54 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