ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9PL83

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name SYFA_CHLMU
Primary accession number Q9PL83
Secondary accession numbers None
Integrated into Swiss-Prot on December 8, 2000
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 56)
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: TC_0224
From
Chlamydia muridarum [TaxID: 83560] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(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
AE002160; AAF39096.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F81727; F81727.
RefSeq NP_296603.1; -.
3D structure databases
HSSP P27001; 1JJC. [HSSP ENTRY / PDB]
ModBase Q9PL83.
Enzyme and pathway databases
BioCyc CMUR243161:TC_0224-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 Q9PL83.
Genome annotation databases
GeneID 1246392; -.
GenomeReviews AE002160_GR; TC_0224.
KEGG cmu:TC0224; -.
TIGR TC_0224; -.
Phylogenomic databases
HOGENOM Q9PL83; -.
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   341  341     Phenylalanyl-tRNA synthetase alpha chain. PRO_0000126686
METAL   256   256        Magnesium (By similarity). 
Sequence information
Length: 341 AA [This is the length of the unprocessed precursor] Molecular weight: 38781 Da [This is the MW of the unprocessed precursor] CRC64: 62426ADD147EFB89 [This is a checksum on the sequence] 
        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
Q9PL83 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!