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A5U306 (SYFA_MYCTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:MRA_1660
OrganismMycobacterium tuberculosis (strain ATCC 25177 / H37Ra) [Complete proteome] [HAMAP]
Taxonomic identifier419947 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length341 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 – 341341Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000006862

Sites

Metal binding2591Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A5U306 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: C4C31DD8CAEE449B

FASTA34137,371
        10         20         30         40         50         60 
MLSPEALTTA VDAAQQAIAL ADTLDVLARV KTEHLGDRSP LALARQALAV LPKEQRAEAG 

        70         80         90        100        110        120 
KRVNAARNAA QRSYDERLAT LRAERDAAVL VAEGIDVTLP STRVPAGARH PIIMLAEHVA 

       130        140        150        160        170        180 
DTFIAMGWEL AEGPEVETEQ FNFDALNFPA DHPARGEQDT FYIAPEDSRQ LLRTHTSPVQ 

       190        200        210        220        230        240 
IRTLLARELP VYIISIGRTF RTDELDATHT PIFHQVEGLA VDRGLSMAHL RGTLDAFARA 

       250        260        270        280        290        300 
EFGPSARTRI RPHFFPFTEP SAEVDVWFAN KIGGAAWVEW GGCGMVHPNV LRATGIDPDL 

       310        320        330        340 
YSGFAFGMGL ERTLQFRNGI PDMRDMVEGD VRFSLPFGVG A 

« Hide

References

[1]"Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25177 / H37Ra.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000611 Genomic DNA. Translation: ABQ73406.1.
RefSeqYP_001282968.1. NC_009525.1.

3D structure databases

ProteinModelPortalA5U306.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5U306.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000067582; EBMYCP00000065692; EBMYCG00000067577.
GeneID5215195.
GenomeReviewsGene locus MRA_1660 in contig CP000611_GR.
KEGGmra:MRA_1660.
PATRIC18143283. VBIMycTub106795_1843.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
GeneTreeEBGT00050000016426.
HOGENOMHBG284353.
OMAFRASYFP.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycMTUB419947:MRA_1660-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_MYCTA
AccessionPrimary (citable) accession number: A5U306
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: January 25, 2012
This is version 37 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