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Q5PBV2 (SYFA_ANAMM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:AM055
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length351 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 – 351351Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_0000231960

Sites

Metal binding2661Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PBV2 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 00020A4FF87B5D4D

FASTA35139,649
        10         20         30         40         50         60 
MGMLVPLISK ISDLSEEAKA CVAACSSVEE LDEVRGRYIG RAGALTALLR QISTIQDMDE 

        70         80         90        100        110        120 
RKAVGSAANA ACAALKLAIQ DRESQLAREQ LHSRLASERI DVTLPARPRT CGKIHPISGV 

       130        140        150        160        170        180 
IREISSILSE LGFAVVHGPE LEDEFHVFDA LNTPEHHPAR AENDTFYMTK RLNGRRVVLR 

       190        200        210        220        230        240 
THTSSMQIRA MESNPNPPIK IISPGRVYRN DWDATHSPVF HQVEGLFVDK HVTMGHLKYC 

       250        260        270        280        290        300 
INYFLSRFFA RKVETRMRAS FFPFTEPSAE IDVKDRHQKW VEVLGCGMVH PAVLENVNID 

       310        320        330        340        350 
PEKYRGFAFG MGVERMAMLK YGITDLRNFY SNKLEWLNHY GFCFTDILGR A 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86227.1.
RefSeqYP_153482.1. NC_004842.2.

3D structure databases

ProteinModelPortalQ5PBV2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5PBV2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3171485.
GenomeReviewsGene locus AM055 in contig CP000030_GR.
KEGGama:AM055.
PATRIC20946227. VBIAnaMar46146_0053.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBQ5PBV2.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycAMAR234826:AM055-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_ANAMM
AccessionPrimary (citable) accession number: Q5PBV2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 49 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