Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Queuine tRNA-ribosyltransferase catalytic subunit 1

Gene

Qtrt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 GUN 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) (PubMed:19414587). 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 (By similarity).UniRule annotation1 Publication

Catalytic activityi

Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine.UniRule annotation1 Publication

Cofactori

Zn2+UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei105Proton acceptorUniRule annotation1
Binding sitei159SubstrateUniRule annotation1
Binding sitei202SubstrateUniRule annotation1
Binding sitei229Substrate; via amide nitrogenUniRule annotation1
Active sitei279NucleophileUniRule annotation1
Metal bindingi317ZincUniRule annotation1
Metal bindingi319ZincUniRule annotation1
Metal bindingi322ZincUniRule annotation1
Metal bindingi348Zinc; via pros nitrogenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • tRNA-guanine transglycosylation Source: UniProtKB

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processtRNA processing
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Queuine tRNA-ribosyltransferase catalytic subunit 1UniRule annotation (EC:2.4.2.29UniRule annotation1 Publication)
Alternative name(s):
Guanine insertion enzymeUniRule annotation
tRNA-guanine transglycosylaseUniRule annotation
Gene namesi
Name:Qtrt1UniRule annotation
Synonyms:Tgt, Tgut
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1931441. Qtrt1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001355662 – 403Queuine tRNA-ribosyltransferase catalytic subunit 1Add BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei139PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JMA2.
MaxQBiQ9JMA2.
PaxDbiQ9JMA2.
PeptideAtlasiQ9JMA2.
PRIDEiQ9JMA2.

PTM databases

iPTMnetiQ9JMA2.
PhosphoSitePlusiQ9JMA2.

Expressioni

Tissue specificityi

Expressed in brain, heart, kidney, liver, ling, skeletal muscle, spleen and testis.1 Publication

Gene expression databases

BgeeiENSMUSG00000002825.
CleanExiMM_QTRT1.
ExpressionAtlasiQ9JMA2. baseline and differential.
GenevisibleiQ9JMA2. MM.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit QTRT1 and an accessory subunit QTRT2.UniRule annotation1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000002902.

Structurei

3D structure databases

ProteinModelPortaliQ9JMA2.
SMRiQ9JMA2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni105 – 109Substrate bindingUniRule annotation5
Regioni260 – 266RNA bindingUniRule annotation7
Regioni284 – 288RNA binding; important for wobble base 34 recognitionUniRule annotation5

Sequence similaritiesi

Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3908. Eukaryota.
COG0343. LUCA.
GeneTreeiENSGT00530000063679.
HOGENOMiHOG000223473.
HOVERGENiHBG101131.
InParanoidiQ9JMA2.
KOiK00773.
OMAiTYHLFLR.
OrthoDBiEOG091G09KJ.
PhylomeDBiQ9JMA2.
TreeFamiTF300732.

Family and domain databases

Gene3Di3.20.20.105. 1 hit.
HAMAPiMF_00168. Q_tRNA_Tgt. 1 hit.
InterProiView protein in InterPro
IPR004803. TGT.
IPR036511. TGT-like_sf.
IPR002616. tRNA_ribo_trans-like.
PfamiView protein in Pfam
PF01702. TGT. 1 hit.
SUPFAMiSSF51713. SSF51713. 1 hit.
TIGRFAMsiTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JMA2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVGSPGSL ESAPRIMRLV AECSRSGARA GELRLPHGTV ATPVFMPVGT
60 70 80 90 100
QATMKGITTE QLDSLGCRIC LGNTYHLGLR PGPELIRKAQ GLHGFMNWPH
110 120 130 140 150
NLLTDSGGFQ MVSLFSLSEV TEEGVHFRSP YDGEETLLSP ERSVEIQNAL
160 170 180 190 200
GSDIIMQLDH VVSSTVTGPL VEEAMHRSVR WLDRCIAAHK HPDKQNLFAI
210 220 230 240 250
IQGGLNADLR TTCLKEMTKR DVPGFAIGGL SGGESKAQFW KMVALSTSML
260 270 280 290 300
PKDKPRYLMG VGYATDLVVC VALGCDMFDC VYPTRTARFG SALVPTGNLQ
310 320 330 340 350
LKKKQYAKDF SPINPECPCP TCQTHSRAFL HALLHSDNTT ALHHLTVHNI
360 370 380 390 400
AYQLQLLSAV RSSILEQRFP DFVRNFMRTM YGDHSLCPAW AVEALASVGI

MLT
Length:403
Mass (Da):44,093
Last modified:June 16, 2009 - v2
Checksum:iDC514C9E384314AD
GO

Sequence cautioni

Q9JMA2: The sequence BAB27717 differs from that shown. Reason: Frameshift at position 6.Curated
Q9JMA2: The sequence BAB27717 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011586 mRNA. Translation: BAB27717.1. Sequence problems.
BC044811 mRNA. Translation: AAH44811.1.
AB034632 mRNA. Translation: BAA93550.1.
CCDSiCCDS52735.1.
RefSeqiNP_068688.2. NM_021888.2.
UniGeneiMm.436579.

Genome annotation databases

EnsembliENSMUST00000002902; ENSMUSP00000002902; ENSMUSG00000002825.
GeneIDi60507.
KEGGimmu:60507.
UCSCiuc009oli.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiTGT_MOUSE
AccessioniPrimary (citable) accession number: Q9JMA2
Secondary accession number(s): Q80VS3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 16, 2009
Last modified: October 25, 2017
This is version 118 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families