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P27002 (SYFB_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 108. 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
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length785 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Subunit structure

Tetramer of two alpha and two beta subunits.

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.

Caution

The sequence shown here has been extracted from PDB entry 1B70.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
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 – 785785Phenylalanine--tRNA ligase beta subunit HAMAP-Rule MF_00283
PRO_0000126978

Regions

Domain39 – 147109tRNA-binding
Domain399 – 47476B5
Domain688 – 78093FDX-ACB

Sites

Metal binding4521Magnesium
Metal binding4581Magnesium; via carbonyl oxygen
Metal binding4611Magnesium
Metal binding4621Magnesium

Secondary structure

......................................................................................................................................... 785
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27002 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: BDC51952DE8E0F00

FASTA78586,611
        10         20         30         40         50         60 
MRVPFSWLKA YVPELESPEV LEERLAGLGF ETDRIERVFP IPRGVVFARV LEAHPIPGTR 

        70         80         90        100        110        120 
LKRLVLDAGR TVEVVSGAEN ARKGIGVALA LPGTELPGLG QKVGERVIQG VRSFGMALSP 

       130        140        150        160        170        180 
RELGVGEYGG GLLEFPEDAL PPGTPLSEAW PEEVVLDLEV TPNRPDALGL LGLARDLHAL 

       190        200        210        220        230        240 
GYALVEPEAA LKAEALPLPF ALKVEDPEGA PHFTLGYAFG LRVAPSPLWM QRALFAAGMR 

       250        260        270        280        290        300 
PINNVVDVTN YVMLERAQPM HAFDLRFVGE GIAVRRAREG ERLKTLDGVE RTLHPEDLVI 

       310        320        330        340        350        360 
AGWRGEESFP LGLAGVMGGA ESEVREDTEA IALEVACFDP VSIRKTARRH GLRTEASHRF 

       370        380        390        400        410        420 
ERGVDPLGQV PAQRRALSLL QALAGARVAE ALLEAGSPKP PEAIPFRPEY ANRLLGTSYP 

       430        440        450        460        470        480 
EAEQIAILKR LGCRVEGEGP TYRVTPPSHR LDLRLEEDLV EEVARIQGYE TIPLALPAFF 

       490        500        510        520        530        540 
PAPDNRGVEA PYRKEQRLRE VLSGLGFQEV YTYSFMDPED ARRFRLDPPR LLLLNPLAPE 

       550        560        570        580        590        600 
KAALRTHLFP GLVRVLKENL DLDRPERALL FEVGRVFRER EETHLAGLLF GEGVGLPWAK 

       610        620        630        640        650        660 
ERLSGYFLLK GYLEALFARL GLAFRVEAQA FPFLHPGVSG RVLVEGEEVG FLGALHPEIA 

       670        680        690        700        710        720 
QELELPPVHL FELRLPLPDK PLAFQDPSRH PAAFRDLAVV VPAPTPYGEV EALVREAAGP 

       730        740        750        760        770        780 
YLESLALFDL YQGPPLPEGH KSLAFHLRFR HPKRTLRDEE VEEAVSRVAE ALRARGFGLR 


GLDTP 

« Hide

References

[1]"Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue."
Reshetnikova L., Moor N., Lavrik O., Vassylyev D.G.
J. Mol. Biol. 287:555-568(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B70X-ray2.70B1-785[»]
1B7YX-ray2.50B1-785[»]
2AKWX-ray2.80B1-785[»]
2ALYX-ray2.60B1-785[»]
2AMCX-ray2.70B1-785[»]
2IY5X-ray3.10B1-785[»]
3TEHX-ray2.85B1-785[»]
ProteinModelPortalP27002.
SMRP27002. Positions 1-785.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6105N.
MINTMINT-88295.
STRING262724.TTC1595.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
IPR002319. Phenylalanyl-tRNA_Synthase.
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.
PF01409. tRNA-synt_2d. 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. 3 hits.
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...

Other

EvolutionaryTraceP27002.

Entry information

Entry nameSYFB_THETH
AccessionPrimary (citable) accession number: P27002
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 1, 1992
Last modified: February 19, 2014
This is version 108 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries