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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: 3 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)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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Phenylalanine--tRNA ligase alpha subunitPRO_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

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 3116Combined sources
Turni39 – 413Combined sources
Helixi42 – 443Combined sources
Helixi49 – 6113Combined sources
Helixi63 – 7311Combined sources
Helixi76 – 838Combined sources
Beta strandi88 – 903Combined sources
Helixi102 – 11514Combined sources
Turni116 – 1183Combined sources
Beta strandi126 – 1294Combined sources
Helixi130 – 1334Combined sources
Turni134 – 1385Combined sources
Beta strandi141 – 1433Combined sources
Turni144 – 1474Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi177 – 1793Combined sources
Helixi181 – 1899Combined sources
Beta strandi192 – 20312Combined sources
Beta strandi214 – 22512Combined sources
Helixi230 – 24415Combined sources
Beta strandi251 – 2555Combined sources
Beta strandi261 – 27111Combined sources
Turni272 – 2754Combined sources
Beta strandi276 – 28611Combined sources
Helixi288 – 30013Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi311 – 3188Combined sources
Helixi319 – 3268Combined sources
Helixi332 – 3343Combined sources
Turni335 – 3373Combined sources
Helixi340 – 3434Combined sources
Helixi344 – 3463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        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
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: November 26, 2014
This is version 106 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

External Data

Dasty 3