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B0VV85 (SYFA_ACIBS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:ABSDF2908
OrganismAcinetobacter baumannii (strain SDF) [Complete proteome] [HAMAP]
Taxonomic identifier509170 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

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 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 – 330330Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000114839

Sites

Metal binding2551Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
B0VV85 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: A9D6199D2AC06CAD

FASTA33037,158
        10         20         30         40         50         60 
MRVTMSLEAL TTEALAAIAA AQDLVALDQV RVQFTGKKSQ LAEQSKALGK MDPEERKVQG 

        70         80         90        100        110        120 
AAIHAVRETI NNALTERQTA LQQAALAQKL ASETIDITLP GRGQRVGTVH PVTQVQERIC 

       130        140        150        160        170        180 
QFFTKAGFTV ATGPEVEDDY HNFEALNIPG HHPARAMHDT FYFDANHLLR THTSGVQIRT 

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

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

       310        320        330 
GVERFAMLRY GINDLRMFYQ NDVRFLRQFA 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SDF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU468230 Genomic DNA. Translation: CAP02198.1.
RefSeqYP_001708068.1. NC_010400.1.

3D structure databases

ProteinModelPortalB0VV85.
SMRB0VV85. Positions 85-330.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0VV85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5987136.
GenomeReviewsGene locus ABSDF2908 in contig CU468230_GR.
KEGGabm:ABSDF2908.
PATRIC20736533. VBIAciBau88365_2753.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284353.
OMAFRASYFP.
ProtClustDBPRK00488.

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_ACIBS
AccessionPrimary (citable) accession number: B0VV85
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 31 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