ACL_RS01225
  | Uniprot: A9NEU5
Description: phenylalanine--tRNA ligase subunit alpha EC number: 6.1.1.20 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). {ECO:0000255|HAMAP-Rule:MF_00281}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00281}; ; Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP-Rule:MF_00281} Enzyme regulation: Function [CC]: Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: METAL 255 255 Magnesium. {ECO:0000255|HAMAP-Rule:MF_00281}. Nucleotide binding: Site: Gene names (primary): pheS Gene names (synonym): Mass: 38,573 Subunit structure [CC]: SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000255|HAMAP-Rule:MF_00281}. Gene ontology (GO): cytoplasm [GO:0005737]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049]; phenylalanyl-tRNA aminoacylation [GO:0006432] Gene ontology IDs: GO:0000049; GO:0000287; GO:0004826; GO:0005524; GO:0005737; GO:0006432 Chain: CHAIN 1 337 Phenylalanine--tRNA ligase alpha subunit. /FTId=PRO_1000078824. Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00281}. Protein families: Class-II aminoacyl-tRNA synthetase family, Phe-tRNA synthetase alpha subunit type 1 subfamily Coiled coil: Domain [FT]: Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NEU5 MEROPS: EnsemblBacteria KO: ABX80875 UniPathway: K01889 CDD: Gene3D: HAMAP: InterPro: MF_00281 PANTHER: IPR006195;IPR004529;IPR004188;IPR022911;IPR002319;IPR010978 PIRSF: PRINTS: PROSITE: Pfam: PS50862 ProDom: PF02912;PF01409 SMART: SUPFAM: TIGRFAMs: SSF46589 |
248034-249048(+) >nucleotide sequence ACATTAAATGATTTAGAAGCATTAAGAGTTGAGTATCTAGGAAAAAATGGTATTTTAACA TCTCAAATGTCTCTAATTAGAACTTTACCAAATGAAGAAAAACCTAAGTTTGGTCAATGG ATCAATGATGCAAAGGTTGCAATAGAACAAGTAATTAGTGATCAAAAAAACATATTACTT ACAATAGCAATGAATGAACAATTAAAAAAAGAAACACTTGATGTTACAATGCCAGGGTTA AACTTTAAAAAAGGTAGCTTACACCCATTAACATTAGTGACTCAAGATTTAGAAGATTAC TTTATTGGTTTAGGCTATAAAGTTGCTGAAGGTCCAGAACTAGAGTTAGATAAATATAAC TTTGAAATGATGAATCTAGCAAGTGATCACCCTGCTAGAGAAATGCATGATTCTTTTTAT GTAACTCAAAATACATTACTAAGAACACATACATCTCCAATTCAAGCACGCTATATGGAA AAATCAAAGGGGCAACCAATCGCAATTATTGCTCCAGGTAAAACCTATAGAAGAGATCCA GATGATCGTACGCACTCACACCAATTTATGCAATGTGAAGGTTTAGTCATTGATAAGGAT GTGACATTTGCACACCTTAAAGAAACGCTACTTGGTATGGCACGTCATATCTTTGGTGAA GAAAGAACGATTCGTTTAAGACCATCTTACTTCCCATTTACTGAACCATCTGTTGAAGTC GATGTATCTTATGTGGACAGTGATGGTAAAACAGAGTGGATCGAAGTTTTAGGTGCTGGT ATGGTACACCCAAATGTGTTAACTATGGGTGGATATGATCCTAAAGTATACCGTGGGTTT GCTTTTGGGATTGGACTTGAACGTATTGCCATCTTAAAATATAAAATCGATGACATTCGT CAATTTTATACTAATGATCTACGCTTCTTAAATCAATTTAAAGGAGTCTTATAA >protein sequence INDAKVAIEQVISDQKNILLTIAMNEQLKKETLDVTMPGLNFKKGSLHPLTLVTQDLEDY FIGLGYKVAEGPELELDKYNFEMMNLASDHPAREMHDSFYVTQNTLLRTHTSPIQARYME KSKGQPIAIIAPGKTYRRDPDDRTHSHQFMQCEGLVIDKDVTFAHLKETLLGMARHIFGE ERTIRLRPSYFPFTEPSVEVDVSYVDSDGKTEWIEVLGAGMVHPNVLTMGGYDPKVYRGF AFGIGLERIAILKYKIDDIRQFYTNDLRFLNQFKGVL |
© Fisunov Lab of Proteomics, 2016.