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Q8E5U1 (SYFB_STRA3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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 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:gbs0888
OrganismStreptococcus agalactiae serotype III (strain NEM316) [Complete proteome] [HAMAP]
Taxonomic identifier211110 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length801 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 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 – 801801Phenylalanine--tRNA ligase beta subunit HAMAP-Rule MF_00283
PRO_0000126957

Regions

Domain39 – 153115tRNA-binding
Domain406 – 48176B5
Domain708 – 80194FDX-ACB

Sites

Metal binding4591Magnesium By similarity
Metal binding4651Magnesium; via carbonyl oxygen By similarity
Metal binding4681Magnesium By similarity
Metal binding4691Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8E5U1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D0E776E9D0084CEF

FASTA80187,622
        10         20         30         40         50         60 
MLVSYKWLKE LVDVDVTTAE LAEKMSTTGI EVEGVETPAE GLSKLVVGHI VSCEDVPDTH 

        70         80         90        100        110        120 
LHLCQVDTGD DELRQVVCGA PNVKTGINVI VAVPGARIAD NYKIKKGKIR GMESLGMICS 

       130        140        150        160        170        180 
LQELGLSESI IPKEFSDGIQ ILPEGAIPGD SIFSYLDLDD EIIELSITPN RADALSMRGV 

       190        200        210        220        230        240 
AHEVAAIYGK KVHFEEKNLI EEAERAADKI SVVIESDKVL SYSARIVKNV TVAPSPQWLQ 

       250        260        270        280        290        300 
NKLMNAGIRP INNVVDVTNY VLLTYGQPMH AFDFDKFDGT TIVARNAENG EKLITLDGEE 

       310        320        330        340        350        360 
RDLIADDLVI AVNDQPVALA GVMGGQSTEI GSSSKTVVLE AAVFNGTSIR KTSGRLNLRS 

       370        380        390        400        410        420 
ESSSRFEKGI NYDTVSEAMD FAAAMLQELA GGQVLSGQVT EGVLPTEPVE VSTTLGYVNT 

       430        440        450        460        470        480 
RLGTELTYTD IEEVFEKLGF AISGSEVKFT VLVPRRRWDI AIQADLVEEI ARIYGYEKLP 

       490        500        510        520        530        540 
TTLPEAGATA GELTSMQRLR RRVRTVAEGA GLSEIITYAL TTPEKAVQFS TQATNITELM 

       550        560        570        580        590        600 
WPMTVDRSAL RQNVVSGMLD TIAYNVARKN SNLAVYEIGK VFEQTGNPKE DLPTEVETFT 

       610        620        630        640        650        660 
FALTGLVEEK DFQTKAKPVD FFYAKGIVEA LFIKLKLDVT FVAQKGLASM HPGRTATILL 

       670        680        690        700        710        720 
DGKEIGFVGQ VHPQTAKQYD IPETYVAEIN LSTIESQMNQ ALIFEDITKY PSVSRDIALL 

       730        740        750        760        770        780 
LAESVSHHDI VSAIETSGVK RLTAIKLFDV YAGNNIAEGY KSMAYSLTFQ NPNDNLTDEE 

       790        800 
VAKYMEKITK SLVEKVNAEI R 

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References

[1]"Genome sequence of Streptococcus agalactiae, a pathogen causing invasive neonatal disease."
Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.
Mol. Microbiol. 45:1499-1513(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NEM316.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL766847 Genomic DNA. Translation: CAD46532.1.
RefSeqNP_735338.1. NC_004368.1.

3D structure databases

ProteinModelPortalQ8E5U1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211110.gbs0888.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD46532; CAD46532; CAD46532.
GeneID1029872.
KEGGsan:gbs0888.
PATRIC19637640. VBIStrAga3577_0912.

Organism-specific databases

GenoListgbs0888.
CMRSearch...

Phylogenomic databases

eggNOGCOG0072.
HOGENOMHOG000292087.
KOK01890.
OMAMKFSEQW.
OrthoDBEOG6CCH1J.
ProtClustDBPRK00629.

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_STRA3
AccessionPrimary (citable) accession number: Q8E5U1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 71 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries