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UniProtKB/Swiss-Prot entry Q9PP34

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SYFA_CAMJE
Primary accession number Q9PP34
Secondary accession number Q0PA01
Integrated into Swiss-Prot on December 8, 2000
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 52)
Name and origin of the protein
Protein name Phenylalanyl-tRNA synthetase alpha chain
Synonyms EC 6.1.1.20
Phenylalanine--tRNA ligase alpha chain
PheRS
Gene name
Name: pheS
OrderedLocusNames: Cj0897
From
Campylobacter jejuni [TaxID: 197] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL111168; CAL35018.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A81363; A81363.
3D structure databases
HSSP P27001; 1JJC. [HSSP ENTRY / PDB]
ModBase Q9PP34.
Protein-protein interaction databases
IntAct Q9PP34; -.
Enzyme and pathway databases
BioCyc CJEJ192222:CJ0897C-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0004826; Molecular function: phenylalanine-tRNA ligase activity (inferred from electronic annotation from HAMAP).
GO:0006432; Biological process: phenylalanyl-tRNA aminoacylation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00281; -; 1.
PBIL [Tree]
InterPro IPR006195; aa-tRNA-synth_II.
IPR002319; Phe-tRNA-synth_IIc.
IPR004529; Phe-tRNA-synth_IIc_asu.
IPR004188; Phe-tRNA_synth_II_N.
Graphical view of domain structure.
PANTHER PTHR11538; tRNA-synt_2d; 1.
Pfam PF02912; Phe_tRNA-synt_N; 1.
PF01409; tRNA-synt_2d; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00468; pheS; 1.
PROSITE PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9PP34.
Genome annotation databases
GenomeReviews AL111168_GR; Cj0897.
CMR Q9PP34; Cj0897.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   330  330     Phenylalanyl-tRNA synthetase alpha chain. PRO_0000126681
METAL   246   246        Magnesium (By similarity). 
Sequence information
Length: 330 AA [This is the length of the unprocessed precursor] Molecular weight: 37987 Da [This is the MW of the unprocessed precursor] CRC64: 02013BD56B6AEAF2 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MQNFIEQIQK CENLNDLEAI RISVLGKKGI LTEGFTKLKE LEDEAKKEFA AKLNAQKEIF 

        70         80         90        100        110        120 
NEAYLAKFKD LENLALEERM KQDALNFNYF DESITTGALH PVMSTMDKII EYFIALNFSI 

       130        140        150        160        170        180 
EKGPLIEDDF HNFEALNLPK SHPARDMQDT FYFDDKRLLR TQTSPVQIRT MLAQKPPIRM 

       190        200        210        220        230        240 
IAPGAVFRRD FDITHTPMFH QVEGLVVEEG QKVSFANLKS VLEDFLRYMF GDVKVRFRPS 

       250        260        270        280        290        300 
FFPFTEPSAE VDISCVFCKG KGCRVCKHTG WLEVLGCGIV DPNVYNFVGY ENVSGYAFGL 

       310        320        330 
GVERFAMLLH QIPDLRSLFE GDLRLLEQFR
Q9PP34 in FASTA format

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