GCW_92036
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Uniprot: A0A0F6CLY4
Description: Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain EC number: 6.1.1.20 Annotation score: 2 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:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS00089465}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00281}; ; Note=Binds 2 magnesium ions per tetramer. {ECO:0000256|HAMAP-Rule:MF_00281} Enzyme regulation: Function [CC]: Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: METAL 252 252 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00281}. Nucleotide binding: Site: Gene names (primary): pheS Gene names (synonym): Mass: 39,438 Subunit structure [CC]: SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS00089470}. 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: 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:0000256|HAMAP-Rule:MF_00281, ECO:0000256|SAAS:SAAS00541523}. Protein families: Class-II aminoacyl-tRNA synthetase family, Phe-tRNA synthetase alpha subunit type 1 subfamily Coiled coil: Domain [FT]: DOMAIN 185 315 AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:PS50862}. Motif: Region: EMBL: CP006916 ProteinModelPortal: MEROPS: EnsemblBacteria KO: AHV85436 UniPathway: K01889 CDD: Gene3D: HAMAP: InterPro: MF_00281 PANTHER: IPR006195;IPR004529;IPR022911;IPR002319 PIRSF: PRINTS: PROSITE: Pfam: PS50862 ProDom: PF01409 SMART: SUPFAM: TIGRFAMs: In one protein complex with GCW_92037 480204-481221(+) >nucleotide sequence CAAAAAGAACTGATTGTAACTAAAAACATCTTTGTTAAAAAACACGTCACCCCACTATTT CAACAACTACGTGAGTTAGAAGAATTAGCAGTTAAAAAAGCATTTGGAAAAGAATTAAAC TTCTTACAAGAAGCGATTCAAGAGTTATTTGAAGAAAAAAACCAACAGTTAGTAATCAAC TTAGATCAGAATCAAAAACCAGCTTATGATCTAATGATTCCAGCTTTAGATCTAGTTGAT GGTTCAATTCATCCCTTAAATTTAGTGGTAAATCAGATCGTTGATTTTTTTAAGAAGTTT AACTTTACGATCGTCAATTACCCAGAATTAGTGACAACCAAACATTGTTTTGATGATCTA AATATCCCTTTAGATCATCCTGGTAGATCTAAAACAGACACGTTTTATGTAAGTGATAAG CAATTATTACGAACACACTGTACAGCAGGAACGATCGAAGCGATTGCTGCTATGAATAAA CATAAAGATATTCGTGTGATTAGCTTTGGTAATGTTTATCGTAATGACACCGATGATGCA ACTCACTCACACCAGTTTATGCAAATGGACTTTATGTGGGTTAATAAGGATCTATCTTTA TCAAACCTTAAGTGGTTTGTTACCAAATTCATCGAACATATGTTTGGTAATGATCTTAAA ACTCGGTTTAGACTTTCACACTTTCCGTTTACTGAACCAAGTTTTGAAGTCGATGTTGAA TGTTGAAACTGTCAAAGCGGTTGTTTTTTATGTAAAAAAACCAGATGGATCGAGATCATG GGTTCAGGAATCTTACACCCTAAAGTGTTAGAAGCTGCACATATTGATCCTGAAAAGATG GTGGGGATTGCTGCTGGAATTGGGATTGAAAGAATCGCGATGCTAAAAAATAATATCACT GACATTAGGGATTTTTATTTTAATGACTTTCGGTTTATCAAGCAATTTTATGAGTAG >protein sequence FLQEAIQELFEEKNQQLVINLDQNQKPAYDLMIPALDLVDGSIHPLNLVVNQIVDFFKKF NFTIVNYPELVTTKHCFDDLNIPLDHPGRSKTDTFYVSDKQLLRTHCTAGTIEAIAAMNK HKDIRVISFGNVYRNDTDDATHSHQFMQMDFMWVNKDLSLSNLKWFVTKFIEHMFGNDLK TRFRLSHFPFTEPSFEVDVECWNCQSGCFLCKKTRWIEIMGSGILHPKVLEAAHIDPEKM VGIAAGIGIERIAMLKNNITDIRDFYFNDFRFIKQFYE |
© Fisunov Lab of Proteomics, 2016.