ACL_RS04480
  | Uniprot: A9NGN9
Description: alanine--tRNA ligase EC number: 6.1.1.7 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). {ECO:0000255|HAMAP-Rule:MF_00036}. Cofactor: COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00036}; ; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00036} Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain. {ECO:0000255|HAMAP-Rule:MF_00036}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: METAL 535 535 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.; METAL 539 539 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.; METAL 637 637 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}.; METAL 641 641 Zinc. {ECO:0000255|HAMAP-Rule:MF_00036}. Nucleotide binding: Site: Gene names (primary): alaS Gene names (synonym): Mass: 96,289 Subunit structure [CC]: Gene ontology (GO): cytoplasm [GO:0005737]; alanine-tRNA ligase activity [GO:0004813]; ATP binding [GO:0005524]; tRNA binding [GO:0000049]; zinc ion binding [GO:0008270]; alanyl-tRNA aminoacylation [GO:0006419] Gene ontology IDs: GO:0000049; GO:0004813; GO:0005524; GO:0005737; GO:0006419; GO:0008270 Chain: CHAIN 1 851 Alanine--tRNA ligase. /FTId=PRO_0000347467. Signal peptide: Domain [CC]: DOMAIN: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_00036}. Sequence similarities: SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. {ECO:0000255|HAMAP-Rule:MF_00036}. Protein families: Class-II aminoacyl-tRNA synthetase family Coiled coil: Domain [FT]: Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NGN9 MEROPS: EnsemblBacteria KO: ABX81519 UniPathway: K01872 CDD: Gene3D: HAMAP: InterPro: MF_00036_B PANTHER: IPR002318;IPR018162;IPR018165;IPR018164;IPR023033;IPR003156;IPR018163;IPR009000;IPR012947 PIRSF: PRINTS: PROSITE: PR00980 Pfam: PS50860 ProDom: PF02272;PF01411;PF07973 SMART: SUPFAM: SM00863 TIGRFAMs: SSF101353;SSF50447;SSF55186 |
934988-937544(-) >nucleotide sequence AAAATCAGGTTTACCACCACCACGACCATCAAGTACTTTGTTTAACTCATTAATGACGTT TCTTGCTTCATTTACTGATGATTTTACTAAGTAACTTGCCTTGTCTTCAGAGATGTTTAA TAAGACAACAGTATCTGCCTTTATTTTATCATATAAGACATCAATGAGTGGTTTTAATGA TGACTGTGGTAAGTTATCACTATAAATATAGGTAGTTGGTTCAATTGTTTTAGGTATAAA TGTATCTGCTTGTAAAATAATTTGATCAATTAATTTAGCTTCAAGTTGTTTTTCAACAAC TTTAGATTCATTTGAAATATATTGATTATAAAGTCTTAGATTGATGATATCTTGATAAGA TCCAGTTAATTCTGGTAATGGTTTTAAATTATGATTTTCATCAAGCGATTTAATTTTTTC AATATGTTGATGAATCATATCAAGTAAATTTTGAACTATTTTTTTAACTTGTGATAATAC TTGACCAGTAATAGCTTCAAATCTATAAGTACCTGAACCAATAGATTCTACAGAAGTAAT CATAAAGTTTTTGATGTCTGATGTGTTTTTAACATGTGTACCACCACAAAACTCCATACT CCAAGATCCTACATCAACTACTCTAACAATATCACCATATTTTTCACCAAATTGCATCGC TGCACCTAATTTTTTAGCTTCATCAATTGGTAAGACGTGTGTTACTACATCAATTTGTTC TTTTATTTTTTGTTGAACGATTTTCTCTACTGTTAAAATTTCTTCATCTTTGATAGTTTC ATAATGGTTAATATCAAACGTTAGTTTTAAATCACCATTATAAGAACCTTGTTGTTTCAC GTGACTTCCTAACGTATCTTTTAAGGCTTGATTAAGTAAGTGTGTCGCTGTATGATTTTT CATTGTGTGATGGCGTTTGTCCTGATTGACAATACATAATACTTCATCACCTTCAGTAAA TGCATCTGTTTCAATTAAGTGTAGATGTTGACCATGTGGTAATTTAATGACATCTCTAAC AACTAGACCATTAATTGATCCTGTGTCTGATATTTGACCACCACTATTTGCATAAAATGG TGTTTTATCTAATACGATACCTTGATCAAATACTTTGATGACTTTACTTTCTGTTTGAAG GTAGTCATAACCTACAAATTCACTAGGTACATCAAAGTTTAATAAAGCCTCATCTTGACC CTTCATAGAGTGTGTTACTTTTCTAGCATCTCTACTTCTTGATTTTTGAACTTCAAGTGC TTCATTAAATCCTTTAATATCTACAGTGATACCATGTTCTTCTGCATATTCAATTGTTAA TTCTATTGGGAAGCCATAAGTATCATAAAGTTTAAATGCATCCTCACCACTTAACTTACC ATCTTTAATGGATTGAAGTAAGTGTTTTTCACCATCTAGGATGGTTGAAAAGAATTTTTC TTCTTCTTTTAAAATAATTTTCTTAACAATGACTGCAGTTTCTATTAAGTTTGTGTAGAA GTTTGACATCATATCAACGACTGTATCTACAAGTAAATGTAAGAATGGTGCATCAAAACC AATAGATTTACCATACTTCACCGCACGGCGTAGGATACGACGTAATACATAACCTCTACC TTCGTTTGAAAGGTTCGCACCATCAGAGATTGCAAATACTAACGTTTTAATGTGGTCAGA GATCACTTTGAATGCCATTTGTCCATCGTATTTTACACCACTTAAAGACTCTACTTTAAG AATCACTGGATAGTGTAGGTCTGTTTCAAAGTTTGTCTTAGTACCTTGTAGTACACAAGC AAATCTTTCTAAACCAGCACCGGTATCAATATTCTTATTTGGTAGTTCTTTATATTCAGA TCTCTTGAGTTTAGGATCTGCATTATATTGTGAGAAAACAATATTCCAAATTTCAATAAA CCGCTCATTTTCAATATCATCACGAATAAGTTCAGGACCTCTTAAATCATAAGATGTGCC TCTATCAAAAAAGATTTCAGTATCCGGACCCGATGGACCAGCTCCAATTTCCCAGAAGTT ACCTTCAACAGGGATTAAATGATCTTCTTTGACACCTAACTTTAACCAAGTATTTTTAGC TTCCACATCGGTTGGATAATATGTCATATAAAGTTTATCTAATGGTATATCAAAGTATTT TGGACTTGTTAAAAGTTCGAATCCAAATTCAATTGCTTCTTTTTTAAAGTAATCACCAAT ACTAAAATTCCCCATCATCTCAAAAAATGTATGGTGTCTTGCAGTTTTTCCAACATTATC AATATCATTTGTTCTAATACTTTTTTGGATGTTTGTAATACGTTTTGATTTCGGTGTTTC TGTACCATCAAAATATTTCTTTAATGGAGCTACACCCGCATTAATCCATAAAAGTGTAGG GTCATCTACAGGAATTAATGATGCAGAGGGTTCAATAATATGCCCCTTATCTTTAAAAAA GTTTAACCAAGTTTGTCTGATTTGTTCACTTGTCAT >protein sequence TNIQKSIRTNDIDNVGKTARHHTFFEMMGNFSIGDYFKKEAIEFGFELLTSPKYFDIPLD KLYMTYYPTDVEAKNTWLKLGVKEDHLIPVEGNFWEIGAGPSGPDTEIFFDRGTSYDLRG PELIRDDIENERFIEIWNIVFSQYNADPKLKRSEYKELPNKNIDTGAGLERFACVLQGTK TNFETDLHYPVILKVESLSGVKYDGQMAFKVISDHIKTLVFAISDGANLSNEGRGYVLRR ILRRAVKYGKSIGFDAPFLHLLVDTVVDMMSNFYTNLIETAVIVKKIILKEEEKFFSTIL DGEKHLLQSIKDGKLSGEDAFKLYDTYGFPIELTIEYAEEHGITVDIKGFNEALEVQKSR SRDARKVTHSMKGQDEALLNFDVPSEFVGYDYLQTESKVIKVFDQGIVLDKTPFYANSGG QISDTGSINGLVVRDVIKLPHGQHLHLIETDAFTEGDEVLCIVNQDKRHHTMKNHTATHL LNQALKDTLGSHVKQQGSYNGDLKLTFDINHYETIKDEEILTVEKIVQQKIKEQIDVVTH VLPIDEAKKLGAAMQFGEKYGDIVRVVDVGSWSMEFCGGTHVKNTSDIKNFMITSVESIG SGTYRFEAITGQVLSQVKKIVQNLLDMIHQHIEKIKSLDENHNLKPLPELTGSYQDIINL RLYNQYISNESKVVEKQLEAKLIDQIILQADTFIPKTIEPTTYIYSDNLPQSSLKPLIDV LYDKIKADTVVLLNISEDKASYLVKSSVNEARNVINELNKVLDGRGGGKPDFAQGGTQAL DKVQMFLKGKN |
© Fisunov Lab of Proteomics, 2016.