A0A014KTF7 · A0A014KTF7_MYCMC
- ProteinAlanine--tRNA ligase
- GenealaS
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids896 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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.
Catalytic activity
- ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | alanine-tRNA ligase activity | |
Molecular Function | ATP binding | |
Molecular Function | tRNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | alanyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAlanine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Mycoplasmatota > Mollicutes > Mycoplasmataceae > Mycoplasma
Accessions
- Primary accessionA0A014KTF7
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-720 | Alanyl-transfer RNA synthetases family profile | ||||
Sequence: LSTNQIRKIWLDFFISKDHYFLETVSLIPVDDPSLLWINSGVATLKPYFDGRKTPPSPRLTNSQKAIRTNDIENVGVTARHHTMFEMLGNFSIGDYFKKEAIELAWELLTDKKYFDIDKNKLYITVFNEDTEAYNIWKDIIKIDEDHIFRLSRKTNFWDVGQGPCGPNTEIFYDRGEIWDPNKIGPRLISDDIENDRYIEVWNIVFSQFNNDGNDNYTELPRKNIDTGAGLERFASIFQNTPTNFETDIFYPTIKKVEQLTNDQFKYSIDNYFNPNKKQTRINTAFKVIADHIRATVFAISDGVFPGNKDRGYIIRRLIRRSCVFGNELGIKQAFLYKLVDSVIESMKEFYPYLIDKKTLVEQTIKDEEEKFLKTLSKGYDLLENIIKTKNTVSDKDALLLFESYGFPIEQTIEISELSNVTVDVEGFKKLLEQTKQATRNARKDLKAWDKQNELFTKLKVESEFTGWSETSRDNAKVIYMFTDQKQVESITDQEVFVILDKTPFYAEKGGQAADSGIIFNDQMKGFVIDVQQGPMHQNIHRIKVQGTLKVNDLINCRVDEEKRIYTMKNHSGTHMIHYALREVLGTSVMQSGSYNDENGLRMDFTYHRLPTNQELLKAQNLVLEKIKNKVDRQTYFCSLEESVNKHQALAFFTEKYDQIVRVIKFGDFSSELCGGTHVNNTSEIEDFIITGIESKGSGLYRIKCLTSFKTVNEYLN | ||||||
Coiled coil | 727-843 | |||||
Sequence: KDQAEIIIDKYNKNKDLLKNDQLENIYLQIKNITINKDNLLVIKDLLDKLKEINKDYDKKVNDLITANKLLKYKDLTPSLNKDNVNEIKLETTDLNIKDLKQLADDLRNKYDDLIVI |
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.
Sequence similarities
Belongs to the class-II aminoacyl-tRNA synthetase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length896
- Mass (Da)103,846
- Last updated2014-06-11 v1
- ChecksumF4421F73754D29AD
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JFAE01000018 EMBL· GenBank· DDBJ | EXU60241.1 EMBL· GenBank· DDBJ | Genomic DNA |