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Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

pheS

Organism
Rickettsia bellii (strain RML369-C)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi258 – 2581MagnesiumUniRule annotation

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

Enzyme and pathway databases

BioCyciRBEL336407:GJCY-673-MONOMER.

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:RBE_0654
OrganismiRickettsia bellii (strain RML369-C)
Taxonomic identifieri336407 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group
ProteomesiUP000001951 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Phenylalanine--tRNA ligase alpha subunitPRO_0000278010Add
BLAST

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ1RIS9.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiCOG0016.
HOGENOMiHOG000242675.
KOiK01889.
OMAiMGKELNS.
OrthoDBiEOG6WX4QN.

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.

Q1RIS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDNIETILRL AEEKILLVQS LKVLQEYKVE FLGKNGIVTN ELKKLGSLSE
60 70 80 90 100
QDRKEFGLKI NKLKEEIQNI IKAKEEILEE EELNLKLSSD KIDLSLPARR
110 120 130 140 150
YKQGSIHPIT QCMEELIQVF AKFGFSIEDG PNIENDFHNF TALNFEDDHP
160 170 180 190 200
ARQMHDTFYL KGQENDKPML LRTHTSTVQI RAMKNGKPPF RFIAPGRTYR
210 220 230 240 250
SDSDMTHTPM FHQIEGLVID KDINMGHLKY VITEFIRCFF ENSNIELRFR
260 270 280 290 300
PSFFPFTEPS AEVDIRMSKT DKWLEVLGCG MVHPNVLKNV GIDNSQYQGF
310 320 330 340
AFGLGVERFA MLKYNIKDLR QFFEGDMRWL KHYSFSSFDI PNLAGGLTK
Length:349
Mass (Da):40,516
Last modified:May 16, 2006 - v1
Checksum:iD473EEEE2C2EFFB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000087 Genomic DNA. Translation: ABE04735.1.
RefSeqiWP_011477323.1. NC_007940.1.
YP_537824.1. NC_007940.1.

Genome annotation databases

EnsemblBacteriaiABE04735; ABE04735; RBE_0654.
KEGGirbe:RBE_0654.
PATRICi17882766. VBIRicBel102610_0750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000087 Genomic DNA. Translation: ABE04735.1.
RefSeqiWP_011477323.1. NC_007940.1.
YP_537824.1. NC_007940.1.

3D structure databases

ProteinModelPortaliQ1RIS9.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE04735; ABE04735; RBE_0654.
KEGGirbe:RBE_0654.
PATRICi17882766. VBIRicBel102610_0750.

Phylogenomic databases

eggNOGiCOG0016.
HOGENOMiHOG000242675.
KOiK01889.
OMAiMGKELNS.
OrthoDBiEOG6WX4QN.

Enzyme and pathway databases

BioCyciRBEL336407:GJCY-673-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
    Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
    PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RML369-C.

Entry informationi

Entry nameiSYFA_RICBR
AccessioniPrimary (citable) accession number: Q1RIS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 16, 2006
Last modified: June 24, 2015
This is version 65 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

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Rickettsia bellii strain RML369-C
    Rickettsia bellii (strain RML369-C): entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.