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

Gene

SPAC1687.19c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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:24911101). 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 annotation1 Publication

Catalytic activityi

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

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 annotation1 Publication
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 sitei98Proton acceptorUniRule annotation1
Binding sitei152SubstrateUniRule annotation1
Binding sitei195SubstrateUniRule annotation1
Binding sitei222Substrate; via amide nitrogenUniRule annotation1
Active sitei272NucleophileUniRule annotation1
Metal bindingi310ZincUniRule annotation1
Metal bindingi312ZincUniRule annotation1
Metal bindingi315ZincUniRule annotation1
Metal bindingi347Zinc; via pros nitrogenUniRule annotation1

GO - Molecular functioni

GO - Biological processi

  • queuosine biosynthetic process Source: GO_Central
  • tRNA modification Source: PomBase
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 subunitUniRule annotation (EC:2.4.2.29UniRule annotation)
Alternative name(s):
Guanine insertion enzymeUniRule annotation
tRNA-guanine transglycosylaseUniRule annotation
Gene namesi
ORF Names:SPAC1687.19c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1687.19c.
PomBaseiSPAC1687.19c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Lacks queuosine in tRNA(Asp).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001355691 – 404Queuine tRNA-ribosyltransferase catalytic subunitAdd BLAST404

Proteomic databases

MaxQBiO94460.
PRIDEiO94460.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi278609. 3 interactors.
MINTiMINT-4684371.

Structurei

3D structure databases

ProteinModelPortaliO94460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 102Substrate bindingUniRule annotation5
Regioni253 – 259RNA bindingUniRule annotation7
Regioni277 – 281RNA binding; important for wobble base 34 recognitionUniRule annotation5

Sequence similaritiesi

Belongs to the queuine tRNA-ribosyltransferase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000223473.
InParanoidiO94460.
KOiK00773.
OMAiGIDLFDC.
OrthoDBiEOG092C34JM.
PhylomeDBiO94460.

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.

Sequencei

Sequence statusi: Complete.

O94460-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSFPALQF KVVARCSTTR ARVTDIQLPH GLVESPVFMP VGTQASLKGV
60 70 80 90 100
LPEQLDALGC KIMLNNTYHL GLKPGQEVLD TVGGAHRFQS WNKNILTDSG
110 120 130 140 150
GFQMVSLLKL ATITEDGVTF LSPRDGTPML LTPEHSISLQ NSIGSDIMMQ
160 170 180 190 200
LDDVVHTLTE SKRMEEAMYR SIRWLDRCIQ AHKRPETQNL FCIIQGGLDK
210 220 230 240 250
RLREICCREM VKRNTPGIAV GGLSGGEEKH AFCETVYTCT SILPDNKPRY
260 270 280 290 300
LMGVGYAEDL VVCVALGMDM FDCVYPTRTA RFGNALTRKG VINLRNQKFR
310 320 330 340 350
NDIGPLEEGC SCPCCKTELE GGWGITRAYF NSLVSKETVG ANLMTIHNVH
360 370 380 390 400
FQLQLMRDMR ESIIKDEFPS FVKNFFHEWN HGDKSNYPSW AVDALRMVNI

DLLA
Length:404
Mass (Da):45,176
Last modified:May 1, 1999 - v1
Checksum:iD192781D8854D4C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA22613.1.
PIRiT37762.
RefSeqiNP_593138.1. NM_001018534.2.

Genome annotation databases

EnsemblFungiiSPAC1687.19c.1; SPAC1687.19c.1:pep; SPAC1687.19c.
GeneIDi2542133.
KEGGispo:SPAC1687.19c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA22613.1.
PIRiT37762.
RefSeqiNP_593138.1. NM_001018534.2.

3D structure databases

ProteinModelPortaliO94460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278609. 3 interactors.
MINTiMINT-4684371.

Proteomic databases

MaxQBiO94460.
PRIDEiO94460.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1687.19c.1; SPAC1687.19c.1:pep; SPAC1687.19c.
GeneIDi2542133.
KEGGispo:SPAC1687.19c.

Organism-specific databases

EuPathDBiFungiDB:SPAC1687.19c.
PomBaseiSPAC1687.19c.

Phylogenomic databases

HOGENOMiHOG000223473.
InParanoidiO94460.
KOiK00773.
OMAiGIDLFDC.
OrthoDBiEOG092C34JM.
PhylomeDBiO94460.

Enzyme and pathway databases

UniPathwayiUPA00392.

Miscellaneous databases

PROiO94460.

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_SCHPO
AccessioniPrimary (citable) accession number: O94460
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. 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.