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Protein

Queuine tRNA-ribosyltransferase catalytic subunit 1

Gene

Qtrt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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). 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.UniRule annotation

Catalytic activityi

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

Cofactori

Zn2+UniRule annotation

Pathwayi: tRNA-queuosine biosynthesis

This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway tRNA-queuosine biosynthesis and in tRNA modification.

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

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Queuosine biosynthesis, tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00392.

Names & Taxonomyi

Protein namesi
Recommended name:
Queuine tRNA-ribosyltransferase catalytic subunit 1UniRule annotation (EC:2.4.2.29UniRule annotationBy similarity)
Alternative name(s):
Guanine insertion enzymeUniRule annotation
tRNA-guanine transglycosylaseUniRule annotation
Gene namesi
Name:Qtrt1UniRule annotation
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620996. Qtrt1.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Mitochondrion outer membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation

  • Note: Weakly associates with mitochondria, possibly via QTRT2.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4395.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00003839462 – 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

PaxDbiQ4QR99.
PRIDEiQ4QR99.

Expressioni

Gene expression databases

BgeeiENSRNOG00000007158.
GenevisibleiQ4QR99. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010030.

Structurei

3D structure databases

ProteinModelPortaliQ4QR99.
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.
HOGENOMiHOG000223473.
InParanoidiQ4QR99.
KOiK00773.
OrthoDBiEOG091G09KJ.
PhylomeDBiQ4QR99.
TreeFamiTF300732.

Family and domain databases

Gene3Di3.20.20.105. 1 hit.
HAMAPiMF_00168. Q_tRNA_Tgt. 1 hit.
InterProiIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view]
PfamiPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMiSSF51713. SSF51713. 1 hit.
TIGRFAMsiTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q4QR99-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAVGSPGSL ESAPRIMRLV AECSRSRARA GELRLPHGTV ATPVFMPVGT
60 70 80 90 100
QATMKGITAE QLDSLGCRIC LGNTYHLGLR PGPELIQKAH GLHGFMNWPH
110 120 130 140 150
NLLTDSGGFQ MVSLISLSEV TEEGVRFRSP YDGEETLLSP ERSVEIQNAL
160 170 180 190 200
GSDIIMQLDD VVSSTVTGPR VEEAMHRSVR WLDRCIAAHK RQDKQNLFAI
210 220 230 240 250
IQGGLNADLR TTCLKEMTKR DVPGFAIGGL SGGESKEQFW KMVALSTSML
260 270 280 290 300
PKDKPRYLMG VGYATDLVVC VALGCDMFDC VYPTRTARFG SALVPTGNLQ
310 320 330 340 350
LKKQQYAKDF SPINPECPCA TCQTHSRAFL HTLLHSDNTA ALHHLTVHNI
360 370 380 390 400
AYQLQLLSAA RSSILEQRFP DFVRNFMRTM YGDHSLCPAW AIEALASVGI

TLT
Length:403
Mass (Da):44,187
Last modified:July 19, 2005 - v1
Checksum:iA60C00474906A9F8
GO
Isoform 2 (identifier: Q4QR99-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     354-403: LQLLSAARSSILEQRFPDFVRNFMRTMYGDHSLCPAWAIEALASVGITLT → VTWMDMVWGREGLGSQGRVG

Note: No experimental confirmation available.
Show »
Length:373
Mass (Da):40,810
Checksum:iF5F6ABB52E96EEDA
GO

Sequence cautioni

The sequence BAA93552 differs from that shown. Reason: Frameshift at position 1.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_038056354 – 403LQLLS…GITLT → VTWMDMVWGREGLGSQGRVG in isoform 2. 1 PublicationAdd BLAST50

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034634 mRNA. Translation: BAA93552.1. Frameshift.
BC097321 mRNA. Translation: AAH97321.1.
RefSeqiNP_071586.2. NM_022250.2. [Q4QR99-1]
UniGeneiRn.53858.

Genome annotation databases

GeneIDi64016.
KEGGirno:64016.
UCSCiRGD:620996. rat. [Q4QR99-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB034634 mRNA. Translation: BAA93552.1. Frameshift.
BC097321 mRNA. Translation: AAH97321.1.
RefSeqiNP_071586.2. NM_022250.2. [Q4QR99-1]
UniGeneiRn.53858.

3D structure databases

ProteinModelPortaliQ4QR99.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010030.

Chemistry databases

ChEMBLiCHEMBL4395.

Proteomic databases

PaxDbiQ4QR99.
PRIDEiQ4QR99.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64016.
KEGGirno:64016.
UCSCiRGD:620996. rat. [Q4QR99-1]

Organism-specific databases

CTDi81890.
RGDi620996. Qtrt1.

Phylogenomic databases

eggNOGiKOG3908. Eukaryota.
COG0343. LUCA.
HOGENOMiHOG000223473.
InParanoidiQ4QR99.
KOiK00773.
OrthoDBiEOG091G09KJ.
PhylomeDBiQ4QR99.
TreeFamiTF300732.

Enzyme and pathway databases

UniPathwayiUPA00392.

Miscellaneous databases

PROiQ4QR99.

Gene expression databases

BgeeiENSRNOG00000007158.
GenevisibleiQ4QR99. RN.

Family and domain databases

Gene3Di3.20.20.105. 1 hit.
HAMAPiMF_00168. Q_tRNA_Tgt. 1 hit.
InterProiIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view]
PfamiPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMiSSF51713. SSF51713. 1 hit.
TIGRFAMsiTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTGT_RAT
AccessioniPrimary (citable) accession number: Q4QR99
Secondary accession number(s): Q9JMA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 19, 2005
Last modified: November 30, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.