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P27001

- SYFA_THETH

UniProt

P27001 - SYFA_THETH

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Protein
Phenylalanine--tRNA ligase alpha subunit
Gene
pheS
Organism
Thermus thermophilus
Status
Reviewed - 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).UniRule annotation

Cofactori

Binds 2 magnesium ions per tetramer.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi262 – 2621Magnesium

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. magnesium ion binding Source: UniProtKB-HAMAP
  3. phenylalanine-tRNA ligase activity Source: UniProtKB-HAMAP
  4. tRNA binding Source: InterPro

GO - Biological processi

  1. phenylalanyl-tRNA aminoacylation Source: UniProtKB-HAMAP
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

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Phenylalanine--tRNA ligase alpha subunitUniRule annotation
PRO_0000126786Add
BLAST

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 3116
Turni39 – 413
Helixi42 – 443
Helixi49 – 6113
Helixi63 – 7311
Helixi76 – 838
Beta strandi88 – 903
Helixi102 – 11514
Turni116 – 1183
Beta strandi126 – 1294
Helixi130 – 1334
Turni134 – 1385
Beta strandi141 – 1433
Turni144 – 1474
Beta strandi153 – 1553
Beta strandi173 – 1753
Beta strandi177 – 1793
Helixi181 – 1899
Beta strandi192 – 20312
Beta strandi214 – 22512
Helixi230 – 24415
Beta strandi251 – 2555
Beta strandi261 – 27111
Turni272 – 2754
Beta strandi276 – 28611
Helixi288 – 30013
Beta strandi307 – 3093
Beta strandi311 – 3188
Helixi319 – 3268
Helixi332 – 3343
Turni335 – 3373
Helixi340 – 3434
Helixi344 – 3463

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
DisProtiDP00053.
ProteinModelPortaliP27001.
SMRiP27001. Positions 6-350.

Miscellaneous databases

EvolutionaryTraceiP27001.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

HAMAPiMF_00281. Phe_tRNA_synth_alpha1.
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

MLEEALAAIQ NARDLEELKA LKARYLGKKG LLTQEMKGLS ALPLEERRKR    50
GQELNAIKAA LEAALEAREK ALEEAALKEA LERERVDVSL PGASLFSGGL 100
HPITLMEREL VEIFRALGYQ AVEGPEVESE FFNFDALNIP EHHPARDMWD 150
TFWLTGEGFR LEGPLGEEVE GRLLLRTHTS PMQVRYMVAH TPPFRIVVPG 200
RVFRFEQTDA THEAVFHQLE GLVVGEGIAM AHLKGAIYEL AQALFGPDSK 250
VRFQPVYFPF VEPGAQFAVW WPEGGKWLEL GGAGMVHPKV FQAVDAYRER 300
LGLPPAYRGV TGFAFGLGVE RLAMLRYGIP DIRYFFGGRL KFLEQFKGVL 350
Length:350
Mass (Da):39,259
Last modified:August 1, 1992 - v1
Checksum:iDEE0237F7CD9A461
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B70 X-ray 2.70 A 1-350 [» ]
1B7Y X-ray 2.50 A 1-350 [» ]
2AKW X-ray 2.80 A 85-350 [» ]
2ALY X-ray 2.60 A 85-350 [» ]
2AMC X-ray 2.70 A 85-350 [» ]
2IY5 X-ray 3.10 A 1-350 [» ]
3TEH X-ray 2.85 A 1-350 [» ]
DisProti DP00053.
ProteinModelPortali P27001.
SMRi P27001. Positions 6-350.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6104N.
MINTi MINT-88286.
STRINGi 262724.TTC1594.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P27001.

Family and domain databases

HAMAPi MF_00281. Phe_tRNA_synth_alpha1.
InterProi IPR006195. 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 ]
Pfami PF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view ]
SUPFAMi SSF46589. SSF46589. 1 hit.
TIGRFAMsi TIGR00468. pheS. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

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: February 19, 2014
This is version 103 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.

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

External Data

Dasty 3

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