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A4T9V2 (SYFA_MYCGI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:Mflv_3533
OrganismMycobacterium gilvum (strain PYR-GCK) (Mycobacterium flavescens (strain ATCC 700033 / PYR-GCK)) [Complete proteome] [HAMAP]
Taxonomic identifier350054 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length347 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 By similarity 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 – 347347Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_1000078844

Sites

Metal binding2651Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A4T9V2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 9F7AB60DC8FC561B

FASTA34738,134
        10         20         30         40         50         60 
MAEQPVDLSD QALADAVSAV RRAFDGASTL EDLAKAKTEY LGDRSPIALA RQALGSLPKT 

        70         80         90        100        110        120 
ERADAGKRVN VARTEAQTAY DERLAVLRAE RDAAVLVAER IDVTLPSTRQ PVGARHPITI 

       130        140        150        160        170        180 
LAERVADTFV AMGWELAEGP EVETEQFNFD ALNFPPDHPA RSEQDTFQVA PDGSRQVLRT 

       190        200        210        220        230        240 
HTSPVQIRAL LERELPVYIV SIGRTFRTDE LDATHTPVFH QVEGLAVDKG LTMANLRGTL 

       250        260        270        280        290        300 
DAFARSEFGP QGRTRFRPHF FPFTEPSAEV DIWFPDKKGG PGWVEWGGCG MVNPNVLRAC 

       310        320        330        340 
GIDPEVYSGF AFGMGLERTL QFRNGIPDMR DMVEGDVRFS LPFGVGA 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PYR-GCK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000656 Genomic DNA. Translation: ABP46007.1.
RefSeqYP_001134795.1. NC_009338.1.

3D structure databases

ProteinModelPortalA4T9V2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4T9V2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000027282; EBMYCP00000026944; EBMYCG00000027277.
GeneID4974851.
GenomeReviewsGene locus Mflv_3533 in contig CP000656_GR.
KEGGmgi:Mflv_3533.
PATRIC18035230. VBIMycGil17082_3592.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
GeneTreeEBGT00050000016426.
HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBA4T9V2.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycMGIL350054:MFLV_3533-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_MYCGI
AccessionPrimary (citable) accession number: A4T9V2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 15, 2007
Last modified: January 25, 2012
This is version 40 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