B2RAR3 · B2RAR3_HUMAN

  • Protein
    Queuine tRNA-ribosyltransferase catalytic subunit 1
  • Gene
    QTRT1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

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

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site105Proton acceptor
Binding site105-109substrate
Binding site159substrate
Binding site202substrate
Binding site229substrate
Active site279Nucleophile
Binding site317Zn2+ (UniProtKB | ChEBI)
Binding site319Zn2+ (UniProtKB | ChEBI)
Binding site322Zn2+ (UniProtKB | ChEBI)
Binding site348Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrial outer membrane
Molecular Functionmetal ion binding
Molecular FunctiontRNA-guanosine(34) queuine transglycosylase activity
Biological ProcesstRNA-guanine transglycosylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Queuine tRNA-ribosyltransferase catalytic subunit 1
  • EC number
  • Alternative names
    • Guanine insertion enzyme
    • tRNA-guanine transglycosylase

Gene names

    • Name
      QTRT1

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    B2RAR3

Subcellular Location

Cytoplasm
Mitochondrion outer membrane
; Peripheral membrane protein
Note: Weakly associates with mitochondria, possibly via QTRT2.

Keywords

PTM/Processing

Proteomic databases

Interaction

Subunit

Heterodimer of a catalytic subunit QTRT1 and an accessory subunit QTRT2.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain27-380tRNA-guanine15 transglycosylase-like
Region260-266RNA binding
Region284-288RNA binding; important for wobble base 34 recognition

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    403
  • Mass (Da)
    43,990
  • Last updated
    2008-07-01 v1
  • Checksum
    1CCDDC17BF47A106
MAGAATQASLESAPRIMRLVAECSRSRARAGELWLPHGTVATPVFMPVGTQATMKGITTEQLDALGCRICLGNTYHLGLRPGPELIQKANGLHGFMNWPHNLLTDSGGFQMVSLVSLSEVTEEGVRFRSPYDGNETLLSPEKSVQIQNALGSDIIMQLDDVVSSTVTGPRVEEAMYRSIRWLDRCIAAHQRPDKQNLFAIIQGGLDADLRATCLEEMTKRDVPGFAIGGLSGGESKSQFWRMVALSTSRLPKDKPRYLMGVGYATDLVVCVALGCDMFDCVFPTRTARFGSALVPTGNLQLRKKVFEKDFGPIDPECTCPTCQKHSRAFLHALLHSDNTAALHHLTVHNIAYQLQLMSAVRTSIVEKRFPGFVRDFMGAMYGDPTLCPTWATDALASVGITLG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK314308
EMBL· GenBank· DDBJ
BAG36960.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp