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Q6G0Y4 (SYFA_BARQU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:BQ00770
OrganismBartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier283165 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length361 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 – 361361Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_0000231965

Sites

Metal binding2601Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G0Y4 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 713D6B314F10C9B6

FASTA36141,511
        10         20         30         40         50         60 
MNDIERLEKE ICLALEAASD EQTLETVRIA ALGKKGCISE KLKALGKMDV EERHKVGPVL 

        70         80         90        100        110        120 
NGLKNRVLEL WVQKRDLLRR QAMNKRLSRE TVDVTLPVRS SPLERGRIHP ISQVIEEIIA 

       130        140        150        160        170        180 
IYANMGFSLA EGPDIETDYY NFTALNFPEG HPAREMHDTF FFDVDKTGER KLLRTHTSPV 

       190        200        210        220        230        240 
QIRTMEKQKA PIRIIIPGKT YRMDSDATHS PMFHQVEGLV IDKTSTIAHM MWLHETFCKA 

       250        260        270        280        290        300 
FFEVPSVKMR FRPSFFPFTE PSMEVDIQCD RSGSKVKFGE GQDWLEILGC GMVHPYVLQN 

       310        320        330        340        350        360 
VGLDPDVYQG FAWGMGIDRI AMLKYGMPDL RAFFDADLRW LDHYGFRCFD MPAFFPGLRN 


E 

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References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX897700 Genomic DNA. Translation: CAF25584.1.
RefSeqYP_031802.1. NC_005955.1.

3D structure databases

ProteinModelPortalQ6G0Y4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2867409.
GenomeReviewsGene locus BQ00770 in contig BX897700_GR.
KEGGbqu:BQ00770.
NMPDRfig|283165.1.peg.72.
PATRIC31951287. VBIBarQui58630_0087.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBQ6G0Y4.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycBQUI283165:BQ00770-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_BARQU
AccessionPrimary (citable) accession number: Q6G0Y4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 52 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