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Q2YQV4 (SYFB_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 beta subunit

EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name=PheRS
Gene names
Name:pheT
Ordered Locus Names:BAB1_2127
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length804 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP-Rule MF_00283

Cofactor

Binds 2 magnesium ions per tetramer By similarity. HAMAP-Rule MF_00283

Subunit structure

Tetramer of two alpha and two beta subunits By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00283.

Sequence similarities

Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.

Contains 1 B5 domain.

Contains 1 FDX-ACB domain.

Contains 1 tRNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processphenylalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA processing

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 804804Phenylalanine--tRNA ligase beta subunit HAMAP-Rule MF_00283
PRO_0000232048

Regions

Domain38 – 148111tRNA-binding
Domain401 – 47676B5
Domain710 – 80394FDX-ACB

Sites

Metal binding4541Magnesium By similarity
Metal binding4601Magnesium; via carbonyl oxygen By similarity
Metal binding4631Magnesium By similarity
Metal binding4641Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YQV4 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: EABC1EC1A8230AA8

FASTA80485,838
        10         20         30         40         50         60 
MKFTLSWLKD HLETDATLDE IVEKLTDIGL EVESVDDRAA FRAFTIARVL TATRHPDADK 

        70         80         90        100        110        120 
LQVLSVDTGD GKPVQVVCGA PNARAGLVGV LGRPGDYVPG LDVTLSVGKI RGVESFGMMC 

       130        140        150        160        170        180 
SERELELSDE HNGIIDLAEN APVGTSFAAY MGLDDPIIEI GLTPNRADCT GIRGIARDLA 

       190        200        210        220        230        240 
AAGLGTLKNT LPDAVKGEGE TPVKVILDQD AGNPFCTGFA LRMVKGVKNG PSPKWMQQRL 

       250        260        270        280        290        300 
KAIGLRPINA LVDITNYVTF DQGRPLHVFD AAKVKGNLTV RTARDGETIL ALDQREYKLN 

       310        320        330        340        350        360 
AGMYVIADEN GPESIAGIMG GEHSGCDENT VDVLIESALW DPRMIASTGR ELGIVTDARY 

       370        380        390        400        410        420 
RFERGVDPEM MVPGAEIATK LVLELCGGQP TVLDVVGYKP HTARVIDFPV TEVKRLTGLD 

       430        440        450        460        470        480 
VSYEDAFDIL KRLGFGVEGD GKTIRATVPS WRGDVEGKAD LVEEVMRIHG INRIDPQPLP 

       490        500        510        520        530        540 
SHGAVNGRIL TTLQIRTRHA RRMLASRGMM EAVTYSFISE AQAKAFGGGK PELKLANPIA 

       550        560        570        580        590        600 
ADMSDMRPSL LPGLLAAAQR NADRGFDDIA LFEVSGIYEG DTPDKQRRVA GGVRRGTAKV 

       610        620        630        640        650        660 
EGAGRFWAGN AAPVGVFDAK ADALAALEAA GAPVDRIQIE AGGPEWLHPG RSGTLKLGPK 

       670        680        690        700        710        720 
VVLGTFGEFH PDTLEALDVS GALCGFEVYL DAIPEPKAKS ARTKPALSLS LFQSLKRDYA 

       730        740        750        760        770        780 
FVVDAAVEAG NVVKAVSSAD KKLIVGVQVF DIFTGASLGE GKKSIAVEVL LQPQDRTLTD 

       790        800 
EDLEALSKQI VASVAKQTGG VLRG 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ12083.1.
RefSeqYP_415448.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YQV4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_2127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ12083; CAJ12083; BAB1_2127.
GeneID3788852.
KEGGbmf:BAB1_2127.
PATRIC17847353. VBIBruMel86222_2212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0073.
HOGENOMHOG000292085.
KOK01890.
OMARTSCDET.
OrthoDBEOG6CCH1J.

Enzyme and pathway databases

BioCycBABO359391:GKDV-2181-MONOMER.
BMEL359391:GJOQ-2181-MONOMER.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.30.56.20. 1 hit.
3.30.70.380. 1 hit.
3.50.40.10. 1 hit.
HAMAPMF_00283. Phe_tRNA_synth_beta1.
InterProIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR012340. NA-bd_OB-fold.
IPR004532. Phe-tRNA-ligase_IIc_bsu.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005121. PheS_beta_Fdx_antiC-bd.
IPR002547. tRNA-bd_dom.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
PF03147. FDX-ACB. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
SMARTSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
SM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMSSF46955. SSF46955. 1 hit.
SSF50249. SSF50249. 1 hit.
SSF54991. SSF54991. 1 hit.
SSF56037. SSF56037. 1 hit.
TIGRFAMsTIGR00472. pheT_bact. 1 hit.
PROSITEPS51483. B5. 1 hit.
PS51447. FDX_ACB. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYFB_BRUA2
AccessionPrimary (citable) accession number: Q2YQV4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries