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Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

pheS

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 2 magnesium ions per tetramer.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi262Magnesium1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase alpha subunit (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunit
Short name:
PheRS
Gene namesi
Name:pheS
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001267861 – 350Phenylalanine--tRNA ligase alpha subunitAdd BLAST350

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.

Protein-protein interaction databases

DIPiDIP-6104N.
MINTiMINT-88286.
STRINGi262724.TTC1594.

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi102 – 115Combined sources14
Turni116 – 118Combined sources3
Beta strandi126 – 129Combined sources4
Helixi130 – 133Combined sources4
Turni134 – 138Combined sources5
Beta strandi141 – 143Combined sources3
Turni144 – 147Combined sources4
Beta strandi153 – 155Combined sources3
Beta strandi173 – 175Combined sources3
Beta strandi177 – 179Combined sources3
Helixi181 – 189Combined sources9
Beta strandi192 – 203Combined sources12
Beta strandi214 – 225Combined sources12
Helixi230 – 244Combined sources15
Beta strandi251 – 255Combined sources5
Beta strandi261 – 271Combined sources11
Turni272 – 275Combined sources4
Beta strandi276 – 286Combined sources11
Helixi288 – 300Combined sources13
Beta strandi311 – 318Combined sources8
Helixi319 – 326Combined sources8
Helixi332 – 334Combined sources3
Turni335 – 337Combined sources3
Helixi340 – 343Combined sources4
Helixi344 – 346Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B70X-ray2.70A1-350[»]
1B7YX-ray2.50A1-350[»]
2AKWX-ray2.80A85-350[»]
2ALYX-ray2.60A85-350[»]
2AMCX-ray2.70A85-350[»]
2IY5X-ray3.10A1-350[»]
3TEHX-ray2.85A1-350[»]
4TVAX-ray2.60A1-350[»]
DisProtiDP00053.
ProteinModelPortaliP27001.
SMRiP27001.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27001.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CSS. Bacteria.
COG0016. LUCA.

Family and domain databases

HAMAPiMF_00281. Phe_tRNA_synth_alpha1. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_ligase_II_N.
IPR022911. Phe_tRNA_ligase_alpha1_bac.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR010978. tRNA-bd_arm.
[Graphical view]
PfamiPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMiSSF46589. SSF46589. 1 hit.
TIGRFAMsiTIGR00468. pheS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27001-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEEALAAIQ NARDLEELKA LKARYLGKKG LLTQEMKGLS ALPLEERRKR
60 70 80 90 100
GQELNAIKAA LEAALEAREK ALEEAALKEA LERERVDVSL PGASLFSGGL
110 120 130 140 150
HPITLMEREL VEIFRALGYQ AVEGPEVESE FFNFDALNIP EHHPARDMWD
160 170 180 190 200
TFWLTGEGFR LEGPLGEEVE GRLLLRTHTS PMQVRYMVAH TPPFRIVVPG
210 220 230 240 250
RVFRFEQTDA THEAVFHQLE GLVVGEGIAM AHLKGAIYEL AQALFGPDSK
260 270 280 290 300
VRFQPVYFPF VEPGAQFAVW WPEGGKWLEL GGAGMVHPKV FQAVDAYRER
310 320 330 340 350
LGLPPAYRGV TGFAFGLGVE RLAMLRYGIP DIRYFFGGRL KFLEQFKGVL
Length:350
Mass (Da):39,259
Last modified:August 1, 1992 - v1
Checksum:iDEE0237F7CD9A461
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B70X-ray2.70A1-350[»]
1B7YX-ray2.50A1-350[»]
2AKWX-ray2.80A85-350[»]
2ALYX-ray2.60A85-350[»]
2AMCX-ray2.70A85-350[»]
2IY5X-ray3.10A1-350[»]
3TEHX-ray2.85A1-350[»]
4TVAX-ray2.60A1-350[»]
DisProtiDP00053.
ProteinModelPortaliP27001.
SMRiP27001.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6104N.
MINTiMINT-88286.
STRINGi262724.TTC1594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CSS. Bacteria.
COG0016. LUCA.

Miscellaneous databases

EvolutionaryTraceiP27001.

Family and domain databases

HAMAPiMF_00281. Phe_tRNA_synth_alpha1. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_ligase_II_N.
IPR022911. Phe_tRNA_ligase_alpha1_bac.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR010978. tRNA-bd_arm.
[Graphical view]
PfamiPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMiSSF46589. SSF46589. 1 hit.
TIGRFAMsiTIGR00468. pheS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYFA_THETH
AccessioniPrimary (citable) accession number: P27001
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 2, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.