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 Q3APW3

[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_CHLCH
Primary accession number Q3APW3
Secondary accession numbers None
Integrated into Swiss-Prot on April 4, 2006
Sequence was last modified on November 22, 2005 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 20)
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: Cag_1711
From
Chlorobium chlorochromatii (strain CaD3) [TaxID: 340177] [HAMAP proteome]
Taxonomy Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobium/Pelodictyon group; Chlorobium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of Chlorobium chlorochromatii CaD3.";
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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
CP000108; ABB28962.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_380005.1; -.
3D structure databases
ModBase Q3APW3.
Enzyme and pathway databases
BioCyc CCHL340177:CAG_1711-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.
Graphical view of domain structure.
PANTHER PTHR11538; tRNA-synt_2d; 1.
Pfam 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 Q3APW3.
Genome annotation databases
GeneID 3746977; -.
GenomeReviews CP000108_GR; Cag_1711.
KEGG cch:Cag_1711; -.
Phylogenomic databases
HOGENOM Q3APW3; -.
Genome annotation databases
CMR Q3APW3; Cag_1711.
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   344  344     Phenylalanyl-tRNA synthetase alpha chain. PRO_0000231974
METAL   257   257        Magnesium (By similarity). 
Sequence information
Length: 344 AA [This is the length of the unprocessed precursor] Molecular weight: 38566 Da [This is the MW of the unprocessed precursor] CRC64: 3B356C51BE5EAF0C [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MEERILQAKQ EILEAPLTTL AELESFRLHF TVRKGLVAAL FGELKNVASA DKPRIGQLLN 

        70         80         90        100        110        120 
ELKQTAESRV SDAEAHLAAA QNSKQQPSLL DLTLPGRRSF CGSEHPVQKV LGDMKSIFNA 

       130        140        150        160        170        180 
MGFTIATGPE LEVGNYNFDM LNFAPDHPAR DMQDTFFVRT GSGNTPDVLL RTHTSPVQIR 

       190        200        210        220        230        240 
VMLDEKPPIR VICPGKVYRN EAISARSYCV FHQLEGLYID KNVSFADLKA TIYSFAQQMF 

       250        260        270        280        290        300 
GSDVKLRFRP SFFPFTEPSA EVDVTCYLCG GKGCRVCKKS GWLEILGCGM VHPNVLRNCG 

       310        320        330        340 
IDPEEWSGYA FGMGVDRTVL LRYKIDDIRL LFENDVRMLQ QFKA
Q3APW3 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!