A0A136IMB3 · A0A136IMB3_9PEZI
- ProteinQueuine tRNA-ribosyltransferase catalytic subunit 1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids433 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product.
Catalytic activity
- guanosine34 in tRNA + queuine = guanine + queuosine34 in tRNA
Cofactor
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 103 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 103-107 | substrate | ||||
Sequence: DSGGF | ||||||
Binding site | 157 | substrate | ||||
Sequence: D | ||||||
Binding site | 201 | substrate | ||||
Sequence: Q | ||||||
Binding site | 228 | substrate | ||||
Sequence: G | ||||||
Active site | 278 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 316 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 318 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 321 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 377 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | metal ion binding | |
Molecular Function | tRNA-guanosine(34) queuine transglycosylase activity | |
Biological Process | tRNA-guanine transglycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameQueuine tRNA-ribosyltransferase catalytic subunit 1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Xylariomycetidae > Xylariales > Microdochiaceae > Microdochium
Accessions
- Primary accessionA0A136IMB3
Proteomes
Subcellular Location
Interaction
Subunit
Heterodimer of a catalytic subunit and an accessory subunit.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-409 | tRNA-guanine15 transglycosylase-like | ||||
Sequence: RARASNLTLPHGPVQLPIFMPVATQASLKGLTPEQLEETGCRLCLNNTYHLGLKPGQDVLDAVGGAHKLQGWDHNILTDSGGFQMVSLLKLANITEDGVRFLSPHDGSPMLLTPEHSIDLQNSIGSDIIMQLDDVLVTTSPDAARMREAMLRSVRWLDRCVAAHRNPTTQNLFCIIQGGLDDEMRRECCAAMVQRDTPGIAIGGLSGGEAKSDFCRVVATCTEMLPELKPRYVMGIGYPEDLVVSVALGADMFDCVWPTRTARFGNAITRHGVLNLKNAVYADDFGPIEDGCGCICCRRPDSASSTSPSQTQSIPTTTTAEGGDSSGAINVTRAFVHHNTAKETAAAHLLTIHNVWHQLNLMREIRAAIIEDRYPAYLHQWFADF | ||||||
Region | 259-265 | RNA binding | ||||
Sequence: GIGYPED | ||||||
Region | 283-287 | RNA binding; important for wobble base 34 recognition | ||||
Sequence: TRTAR | ||||||
Region | 327-349 | Disordered | ||||
Sequence: ASSTSPSQTQSIPTTTTAEGGDS |
Sequence similarities
Belongs to the queuine tRNA-ribosyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length433
- Mass (Da)47,107
- Last updated2016-05-11 v1
- Checksum5783C6A5C4E5F044
Keywords
- Technical term