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 A9NEU5


[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_ACHLI
Primary accession number A9NEU5
Secondary accession numbers None
Integrated into Swiss-Prot on May 20, 2008
Sequence was last modified on February 5, 2008 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 9)
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: ACL_0249
From
Acholeplasma laidlawii (strain PG-8A) [TaxID: 441768] [HAMAP proteome]
Taxonomy Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae; Acholeplasma.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.A., Kostrjukova E.S., Selezneva O.V., Vtyurin N.N., Rogov S.I., Alekseev D.G., Ladygina V.G., Titova G.A., Karpov V.A., Govorun V.M.;
"Acholeplasma laidlawii complete genome.";
Submitted (NOV-2007) 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
CP000896; ABX80875.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001620251.1; -.
3D structure databases
ModBase A9NEU5.
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).
BLOCKS A9NEU5.
ProtoNet A9NEU5.
Genome annotation databases
GeneID 5804105; -.
GenomeReviews CP000896_GR; ACL_0249.
KEGG acl:ACL_0249; -.
CMR A9NEU5; ACL_0249.
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   337  337     Phenylalanyl-tRNA synthetase alpha chain. PRO_1000078824
METAL   255   255        Magnesium (By similarity). 
Sequence information
Length: 337 AA [This is the length of the unprocessed precursor] Molecular weight: 38573 Da [This is the MW of the unprocessed precursor] CRC64: 853E6B5A2F804E64 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKEKIDSIVK SLNDKIHPDL TLNDLEALRV EYLGKNGILT SQMSLIRTLP NEEKPKFGQW 

        70         80         90        100        110        120 
INDAKVAIEQ VISDQKNILL TIAMNEQLKK ETLDVTMPGL NFKKGSLHPL TLVTQDLEDY 

       130        140        150        160        170        180 
FIGLGYKVAE GPELELDKYN FEMMNLASDH PAREMHDSFY VTQNTLLRTH TSPIQARYME 

       190        200        210        220        230        240 
KSKGQPIAII APGKTYRRDP DDRTHSHQFM QCEGLVIDKD VTFAHLKETL LGMARHIFGE 

       250        260        270        280        290        300 
ERTIRLRPSY FPFTEPSVEV DVSYVDSDGK TEWIEVLGAG MVHPNVLTMG GYDPKVYRGF 

       310        320        330 
AFGIGLERIA ILKYKIDDIR QFYTNDLRFL NQFKGVL 

A9NEU5 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!