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Q9PL83 (SYFA_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenylalanine--tRNA ligase alpha chain

EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha chain
Short name=PheRS
Gene names
Name:pheS
Ordered Locus Names:TC_0224
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). HAMAP MF_00281

Cofactor

Binds 2 magnesium ions per tetramer By similarity. HAMAP MF_00281

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm HAMAP MF_00281.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphenylalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Phenylalanine--tRNA ligase alpha chain HAMAP MF_00281
PRO_0000126686

Sites

Metal binding2561Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PL83 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 62426ADD147EFB89

FASTA34138,781
        10         20         30         40         50         60 
MTIQEELEAV KQQFSCDLSL VHSSKDLFDL KVKYLGKKGI FRGFADQLRE CPVEQKATIG 

        70         80         90        100        110        120 
ASINACKQYI EEVLLEKSQV ILAKEEAEEF LKEKVDVSLP GEDAPLGGKH IIKKVLDDVV 

       130        140        150        160        170        180 
DIFVRFGFCV REAPNIESEK NNFSLLNFEE DHPARQMQDT FYLDPVTVLR THTSNVQSRE 

       190        200        210        220        230        240 
LARNKPPVRV VAPGECFRNE DISARSHVTF HQVEAFHVDR DVSFSDLTSM LSGFYHIFFG 

       250        260        270        280        290        300 
RKVELRYRHS YFPFVEPGIE VDISCECRGA GCSLCKHSGW LEVAGAGMIH PNVLRQANID 

       310        320        330        340 
PEEYSGYALG MGIERLAMLK YGISDIRLFS ENDLRFLRQF S 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39096.1.
PIRF81727.
RefSeqNP_296603.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PL83.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1246392.
GenomeReviewsGene locus TC_0224 in contig AE002160_GR.
KEGGcmu:TC0224.
PATRIC20371832. VBIChlMur19118_0244.
TIGRTC_0224.

Phylogenomic databases

HOGENOMHBG284353.
OMAFRASYFP.
PhylomeDBQ9PL83.
ProtClustDBPRK00488.

Enzyme and pathway databases

BioCycCMUR243161:TC_0224-MONOMER.

Family and domain databases

HAMAPMF_00281. Phe_tRNA_synth_alpha1.
[Tree]
InterProIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR004188. Phe-tRNA_synth_II_N.
IPR022911. Phe_tRNA_synth_alpha1_bac.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR010978. tRNA-bd_arm.
[Graphical view]
KOK01889.
PfamPF02912. Phe_tRNA-synt_N. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
SUPFAMSSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00468. PheS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYFA_CHLMU
AccessionPrimary (citable) accession number: Q9PL83
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families