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Q4JW06 (SYFA_CORJK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:jk0839
OrganismCorynebacterium jeikeium (strain K411) [Complete proteome] [HAMAP]
Taxonomic identifier306537 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

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_0000231976

Sites

Metal binding2691Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JW06 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 82837D6BE07338F2

FASTA35138,866
        10         20         30         40         50         60 
MTDSADTPQV ELSEQGLNAA ADAAEKAFAE AANLEELAAA RREHLGDDAP IPAARRSLGS 

        70         80         90        100        110        120 
LPKDQRKDAG RLVNMARGRV EKRFAQVKAE LERKRNEEVL RAERIDVTEP TTRGQRGAQH 

       130        140        150        160        170        180 
PITILSEQIA DIFVGMGWEI ADGPEVEAEY FNFDSLNFIP DHPARTLQDT FHIAPEGSGQ 

       190        200        210        220        230        240 
VLRTHTSPVQ MRTMLSRDLP IYIACPGRVF RTDELDATHT PVFHQVEGLA VDKGLTMAHL 

       250        260        270        280        290        300 
KGTLDHLAKT LFGEEAKTRI RPNYFPFTEP SAEVDVWFAD KKGGAGWIEW GGCGMVNPNV 

       310        320        330        340        350 
LIAAGVDPEE YSGFAFGMGI ERTLQFRNGL PDMRDMVEGD VRFTLPFGVR R 

« Hide

References

[1]"Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora."
Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., Puehler A.
J. Bacteriol. 187:4671-4682(2005) [PubMed: 15968079] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K411.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR931997 Genomic DNA. Translation: CAI37001.1.
RefSeqYP_250619.1. NC_007164.1.

3D structure databases

ProteinModelPortalQ4JW06.
SMRQ4JW06. Positions 99-347.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4JW06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3432398.
GenomeReviewsGene locus jk0839 in contig CR931997_GR.
KEGGcjk:jk0839.
NMPDRfig|306537.3.peg.2031.
PATRIC21512578. VBICorJei31838_0850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
HOGENOMHBG284353.
OMAFRASYFP.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycCJEI306537:JK0839-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_CORJK
AccessionPrimary (citable) accession number: Q4JW06
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 2, 2005
Last modified: January 25, 2012
This is version 47 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