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Q6NHH2 (SYFA_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:DIP1165
OrganismCorynebacterium diphtheriae [Complete proteome] [HAMAP]
Taxonomic identifier1717 [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_0000126694

Sites

Metal binding2691Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NHH2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: CAE1BEECB271397F

FASTA35138,851
        10         20         30         40         50         60 
MSEQPDYPAV ELTEEGLAQA ADAAIRAFGV ASNLDELNIA RRDHLGDAAP IPQARRSLGT 

        70         80         90        100        110        120 
LPKDQRKDAG RLVNMARGRL EKHFAQVKEV LEAKHLEEML KAERVDVTVP TTRHQTGALH 

       130        140        150        160        170        180 
PITTLSEKIA DIFVAMGYEV ADGPEIEAEY FNFDSLNFIP DHPARTLQDT FHVGEPGSSQ 

       190        200        210        220        230        240 
VLRTHTSPVQ MRTMLSREVP IYVVCPGRVF RTDELDATHT PVFHQVEGLA VDKGLTMAHL 

       250        260        270        280        290        300 
RGTLDHLAKT LFGPETKTRM RANYFPFTEP SAEVDVWFPN KKGGAGWIEW GGCGMVNPNV 

       310        320        330        340        350 
LKAAGIDPEV YSGFAFGMGL ERTLQFRNGL TDMRDMVEGD VRFTLPFGVQ A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248357 Genomic DNA. Translation: CAE49685.1.
RefSeqNP_939522.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NHH2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2648565.
GenomeReviewsGene locus DIP1165 in contig BX248353_GR.
KEGGcdi:DIP1165.
NMPDRfig|257309.1.peg.1113.
PATRIC21483517. VBICorDip47633_1147.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBQ6NHH2.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycCDIP257309:DIP1165-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_CORDI
AccessionPrimary (citable) accession number: Q6NHH2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 53 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