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Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

pheS

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed-Annotation score: 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).UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 2 magnesium ions per tetramer.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi258MagnesiumUniRule annotation1

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 subunitUniRule annotation (EC:6.1.1.20UniRule annotation)
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha subunitUniRule annotation
Short name:
PheRSUniRule annotation
Gene namesi
Name:pheSUniRule annotation
Ordered Locus Names:SH1823
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000543 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002320281 – 352Phenylalanine--tRNA ligase alpha subunitAdd BLAST352

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.UniRule annotation

Protein-protein interaction databases

STRINGi279808.SH1823.

Structurei

Secondary structure

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi85 – 89Combined sources5
Turni90 – 93Combined sources4
Helixi111 – 124Combined sources14
Turni125 – 127Combined sources3
Beta strandi135 – 138Combined sources4
Helixi139 – 142Combined sources4
Helixi144 – 146Combined sources3
Helixi153 – 155Combined sources3
Turni157 – 159Combined sources3
Beta strandi162 – 169Combined sources8
Beta strandi171 – 173Combined sources3
Helixi174 – 183Combined sources10
Turni184 – 186Combined sources3
Beta strandi190 – 199Combined sources10
Beta strandi210 – 223Combined sources14
Helixi226 – 241Combined sources16
Beta strandi247 – 251Combined sources5
Beta strandi257 – 266Combined sources10
Beta strandi268 – 270Combined sources3
Beta strandi271 – 273Combined sources3
Turni276 – 280Combined sources5
Beta strandi281 – 292Combined sources12
Helixi294 – 298Combined sources5
Turni299 – 301Combined sources3
Turni304 – 306Combined sources3
Beta strandi308 – 314Combined sources7
Helixi316 – 324Combined sources9
Helixi331 – 334Combined sources4
Helixi337 – 340Combined sources4
Helixi341 – 343Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RHQX-ray2.20A84-351[»]
2RHSX-ray2.20A/C84-351[»]
ProteinModelPortaliQ4L5E3.
SMRiQ4L5E3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4L5E3.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CSS. Bacteria.
COG0016. LUCA.
HOGENOMiHOG000242675.
KOiK01889.
OMAiEYHPARD.
OrthoDBiPOG091H00QY.

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.

Q4L5E3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQNDSMAEL KQQALVDINE AQNERELQDV KVKYLGKKGS VSGLMKNMKD
60 70 80 90 100
LPNEEKPAYG QKVNELRQTI QKELDEKQEL LKNEKLNQQL AEETIDVTLP
110 120 130 140 150
SRQISIGSKH PLTRTVEEIE DLFLGLGYEI VDGYEVEQDY YNFEALNLPK
160 170 180 190 200
SHPARDMQDS FYITDEILMR THTSPVQART MEKRNGQGPV KIICPGKVYR
210 220 230 240 250
RDSDDATHSH QFTQIEGLVV DKNIKMSDLK GTLELVAKKL FGADREIRLR
260 270 280 290 300
PSYFPFTEPS VEVDVSCFKC KGKGCNVCKH TGWIEILGAG MVHPNVLEMA
310 320 330 340 350
GFDSNEYSGF AFGMGPDRIA MLKYGIEDIR YFYTNDVRFL EQFKAVEDRG

EA
Length:352
Mass (Da):40,138
Last modified:August 2, 2005 - v1
Checksum:iB3C516F1D4A223E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05132.1.
RefSeqiWP_011276100.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE05132; BAE05132; SH1823.
GeneIDi24247946.
KEGGisha:SH1823.
PATRICi19619751. VBIStaHae67511_1798.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE05132.1.
RefSeqiWP_011276100.1. NC_007168.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RHQX-ray2.20A84-351[»]
2RHSX-ray2.20A/C84-351[»]
ProteinModelPortaliQ4L5E3.
SMRiQ4L5E3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279808.SH1823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE05132; BAE05132; SH1823.
GeneIDi24247946.
KEGGisha:SH1823.
PATRICi19619751. VBIStaHae67511_1798.

Phylogenomic databases

eggNOGiENOG4105CSS. Bacteria.
COG0016. LUCA.
HOGENOMiHOG000242675.
KOiK01889.
OMAiEYHPARD.
OrthoDBiPOG091H00QY.

Miscellaneous databases

EvolutionaryTraceiQ4L5E3.

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_STAHJ
AccessioniPrimary (citable) accession number: Q4L5E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 2, 2005
Last modified: November 2, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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.