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Protein

Queuine tRNA-ribosyltransferase

Gene

Qtrt1

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

Functioni

Interacts with QTRTD1 to form an active queuine tRNA-ribosyltransferase. This enzyme exchanges queuine for the guanine at the wobble position of tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).1 Publication

Catalytic activityi

Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi: tRNA-queuosine biosynthesis

This protein is involved in the pathway tRNA-queuosine biosynthesis, which is part of tRNA modification.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061SubstrateBy similarity
Active sitei279 – 2791NucleophileBy similarity
Metal bindingi317 – 3171ZincBy similarity
Metal bindingi319 – 3191ZincBy similarity
Metal bindingi322 – 3221ZincBy similarity
Metal bindingi348 – 3481ZincBy similarity

GO - Molecular functioni

GO - Biological processi

  • queuosine biosynthetic process Source: UniProtKB
  • tRNA modification Source: InterPro
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 (EC:2.4.2.29)
Alternative name(s):
Guanine insertion enzyme
tRNA-guanine transglycosylase
Gene namesi
Name:Qtrt1
Synonyms:Tgt, Tgut
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1931441. Qtrt1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 403402Queuine tRNA-ribosyltransferasePRO_0000135566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JMA2.
MaxQBiQ9JMA2.
PaxDbiQ9JMA2.
PeptideAtlasiQ9JMA2.
PRIDEiQ9JMA2.

PTM databases

iPTMnetiQ9JMA2.
PhosphoSiteiQ9JMA2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9JMA2.
CleanExiMM_QTRT1.
GenevisibleiQ9JMA2. MM.

Interactioni

Subunit structurei

Interacts with QTRTD1.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000002902.

Structurei

3D structure databases

ProteinModelPortaliQ9JMA2.
SMRiQ9JMA2. Positions 14-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3908. Eukaryota.
COG0343. LUCA.
GeneTreeiENSGT00530000063679.
HOGENOMiHOG000223473.
HOVERGENiHBG101131.
InParanoidiQ9JMA2.
KOiK00773.
OMAiTPRFMPV.
OrthoDBiEOG7W41BR.
PhylomeDBiQ9JMA2.
TreeFamiTF300732.

Family and domain databases

Gene3Di3.20.20.105. 1 hit.
HAMAPiMF_00168. Q_tRNA_Tgt.
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.

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

The sequence BAB27717.1 differs from that shown. Reason: Frameshift at position 6. Curated
The sequence BAB27717.1 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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9JMA2.
SMRiQ9JMA2. Positions 14-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000002902.

PTM databases

iPTMnetiQ9JMA2.
PhosphoSiteiQ9JMA2.

Proteomic databases

EPDiQ9JMA2.
MaxQBiQ9JMA2.
PaxDbiQ9JMA2.
PeptideAtlasiQ9JMA2.
PRIDEiQ9JMA2.

Protocols and materials databases

DNASUi60507.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi81890.
MGIiMGI:1931441. Qtrt1.

Phylogenomic databases

eggNOGiKOG3908. Eukaryota.
COG0343. LUCA.
GeneTreeiENSGT00530000063679.
HOGENOMiHOG000223473.
HOVERGENiHBG101131.
InParanoidiQ9JMA2.
KOiK00773.
OMAiTPRFMPV.
OrthoDBiEOG7W41BR.
PhylomeDBiQ9JMA2.
TreeFamiTF300732.

Enzyme and pathway databases

UniPathwayiUPA00392.

Miscellaneous databases

PROiQ9JMA2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JMA2.
CleanExiMM_QTRT1.
GenevisibleiQ9JMA2. MM.

Family and domain databases

Gene3Di3.20.20.105. 1 hit.
HAMAPiMF_00168. Q_tRNA_Tgt.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  3. "Another gene for tRNA-guanine transglycosylase in mammals."
    Morishita T., Hidaka T.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-403.
    Tissue: Brain.
  4. "Queuosine formation in eukaryotic tRNA occurs via a mitochondria-localized heteromeric transglycosylase."
    Boland C., Hayes P., Santa-Maria I., Nishimura S., Kelly V.P.
    J. Biol. Chem. 284:18218-18227(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH QTRTD1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Spleen and Testis.

Entry informationi

Entry nameiTGT_MOUSE
AccessioniPrimary (citable) accession number: Q9JMA2
Secondary accession number(s): Q80VS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 16, 2009
Last modified: July 6, 2016
This is version 107 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.