Skip Header

Contribute Send feedback
Read comments (?) or add your own

A1TAB5 (SYFA_MYCVP) 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:Mvan_3317
OrganismMycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP]
Taxonomic identifier350058 [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 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_1000006863

Sites

Metal binding2651Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TAB5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 4D290A29FE765B0B

FASTA34738,055
        10         20         30         40         50         60 
MAEQPVDLSD EALAQAVSAA SRAFDQASTL DELAKAKTEH LGDRSPIALA RQALGSLPKT 

        70         80         90        100        110        120 
DRADAGKRVN VARTQAQAGY DDRLAALRAE RDAEVLVAER IDVTLPSTRQ PVGARHPITI 

       130        140        150        160        170        180 
LAENVADTFV AMGWELAEGP EVETEQFNFD ALNFPPDHPA RSEQDTFHIA PDGSRQVLRT 

       190        200        210        220        230        240 
HTSPVQVRTL LERELPVYVI SIGRTFRTDE LDATHTPVFH QVEGLAVDKG LTMAHLRGTL 

       250        260        270        280        290        300 
DAFARAQFGP QGRTRFRPHF FPFTEPSAEV DIWFPNKKGG PGWVEWGGCG MVNPNVLRAC 

       310        320        330        340 
GIDPEVYSGF AFGMGLERTL QFRNGIPDMR DMVEGDVRFS LPFGVGA 

« Hide

References

[1]"Complete sequence of Mycobacterium vanbaalenii PYR-1."
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., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000511 Genomic DNA. Translation: ABM14115.1.
RefSeqYP_954121.1. NC_008726.1.

3D structure databases

ProteinModelPortalA1TAB5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TAB5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000081835; EBMYCP00000079788; EBMYCG00000081830.
GeneID4644514.
GenomeReviewsGene locus Mvan_3317 in contig CP000511_GR.
KEGGmva:Mvan_3317.
PATRIC18184921. VBIMycVan31953_3378.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0016.
GeneTreeEBGT00050000016426.
HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBA1TAB5.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycMVAN350058:MVAN_3317-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_MYCVP
AccessionPrimary (citable) accession number: A1TAB5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 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