A0A9X3DBN0 · A0A9X3DBN0_9SPHI
- ProteinGlutamine--tRNA ligase
- GeneglnS
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids551 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- tRNA(Gln) + L-glutamine + ATP = L-glutaminyl-tRNA(Gln) + AMP + diphosphate
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 33-35 | ATP (UniProtKB | ChEBI) | ||||
Sequence: EPN | ||||||
Binding site | 39-45 | ATP (UniProtKB | ChEBI) | ||||
Sequence: HIGHAKA | ||||||
Binding site | 65 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 209 | L-glutamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 228 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 257-258 | ATP (UniProtKB | ChEBI) | ||||
Sequence: RL | ||||||
Binding site | 265-267 | ATP (UniProtKB | ChEBI) | ||||
Sequence: MSK |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | glutamine-tRNA ligase activity | |
Biological Process | glutaminyl-tRNA aminoacylation | |
Biological Process | glutamyl-tRNA aminoacylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamine--tRNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Sphingobacteriia > Sphingobacteriales > Sphingobacteriaceae > Pedobacter
Accessions
- Primary accessionA0A9X3DBN0
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-333 | Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic | ||||
Sequence: LVTRFPPEPNGYLHIGHAKAICLNFGLTQKYGGYTNLRFDDTNPVTEKTEYVNSQQEDIKWLGFNWKNELYASDYFDELYSFAVKLIEKGLAYVDESSADEIAALKGTPTEPGQDSPYRNRSVEENLNIFTRMKNGEFADGAYILRAKIDMASPNMLMRDPIIYRIKHAEHHRTGNKWCIYPMYDFAHGQSDSIENITHSICTLEYVSHRELYDWFIEQLEIFPSKQYEFARLNLTSTVMSKRKLLQLVNENLVSGWDDPRMPTISGLRRRGFTPKSVREFCERIGIAKRENLIELSLLEFCIREDLN | ||||||
Motif | 32-42 | 'HIGH' region | ||||
Sequence: PEPNGYLHIGH | ||||||
Motif | 264-268 | 'KMSKS' region | ||||
Sequence: VMSKR | ||||||
Domain | 336-435 | Glutamyl/glutaminyl-tRNA synthetase class Ib anti-codon binding | ||||
Sequence: ANRVMAVLDPIKLIITNYEKGTEDLIGENNPEAEDGGGTRVIPFSNELWIEREDFMEVPAKKWFRLAPGAMVRLKFAYIVKCEDFVKDENGNVTEIHCTY | ||||||
Domain | 453-527 | tRNA synthetases class I (E and Q) anti-codon binding | ||||
Sequence: TIHWVSAQHAKTAEIRLYDRLFSSETPDAEEGDFKDYLNPESLTILPNAYIEPALTDADLDSRYQFIRKGYFCLD |
Sequence similarities
Belongs to the class-I aminoacyl-tRNA synthetase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length551
- Mass (Da)63,491
- Last updated2023-11-08 v1
- ChecksumA7B83C53CBDDC7C0