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Protein

Mitochondrial tRNA-specific 2-thiouridylase 1

Gene

Trmu

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base.By similarity

Catalytic activityi

A [protein]-S-sulfanyl-L-cysteine + 5-taurinomethyluridine(34) in tRNA + ATP + reduced acceptor = a [protein]-L-cysteine + 5-taurinomethyl-2-thiouridine(34) in tRNA + AMP + diphosphate + acceptor.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361ATP; via amide nitrogen and carbonyl oxygenBy similarity
Active sitei101 – 1011NucleophileBy similarity
Binding sitei126 – 1261ATP; via amide nitrogenBy similarity
Active sitei222 – 2221Cysteine persulfide intermediateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Enzyme and pathway databases

BRENDAi2.1.1.61. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial tRNA-specific 2-thiouridylase 1 (EC:2.8.1.14By similarity)
Gene namesi
Name:Trmu
Synonyms:Mtu1, Trmt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1919276. Trmu.

Subcellular locationi

  • Mitochondrion 1 Publication

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 417417Mitochondrial tRNA-specific 2-thiouridylase 1PRO_0000121709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi101 ↔ 222By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiQ9DAT5.
MaxQBiQ9DAT5.
PaxDbiQ9DAT5.
PRIDEiQ9DAT5.

PTM databases

PhosphoSiteiQ9DAT5.

Expressioni

Tissue specificityi

Widely expressed but most abundant in tissues with high metabolic rate including heart, liver and brain. Expression is low in spleen, testis, lung and skeletal muscle. Also expressed in inner ear.1 Publication

Gene expression databases

BgeeiQ9DAT5.
ExpressionAtlasiQ9DAT5. baseline and differential.
GenevisibleiQ9DAT5. MM.

Interactioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei127 – 1271Interaction with tRNABy similarity
Sitei267 – 2671Interaction with tRNABy similarity
Sitei367 – 3671Interaction with tRNABy similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023019.

Structurei

3D structure databases

ProteinModelPortaliQ9DAT5.
SMRiQ9DAT5. Positions 7-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 983Interaction with target base in tRNABy similarity
Regioni171 – 1733Interaction with tRNABy similarity
Regioni334 – 3352Interaction with tRNABy similarity

Sequence similaritiesi

Belongs to the MnmA/TRMU family.Curated

Phylogenomic databases

eggNOGiKOG2805. Eukaryota.
COG0482. LUCA.
GeneTreeiENSGT00390000014323.
HOGENOMiHOG000218046.
HOVERGENiHBG108157.
InParanoidiQ9DAT5.
KOiK00566.
OMAiAYRVCQI.
PhylomeDBiQ9DAT5.
TreeFamiTF105611.

Family and domain databases

Gene3Di2.30.30.280. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00144. tRNA_thiouridyl_MnmA.
InterProiIPR023382. Adenine_a_hdrlase_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004506. tRNA-specific_2-thiouridylase.
[Graphical view]
PANTHERiPTHR11933. PTHR11933. 1 hit.
TIGRFAMsiTIGR00420. trmU. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9DAT5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALRHVVCA LSGGVDSAVA ALLLRRRGYQ VTGVFMKNWD SLDEQGVCAA
60 70 80 90 100
DKDCEDAYKV CQILDIPFHQ VSYVKEYWND VFSDFLNEYE KGRTPNPDIN
110 120 130 140 150
CNKHIKFSCF YHYAVDNLGA DAVATGHYAR TSLEDEEVFE QKHTKKPDGL
160 170 180 190 200
FRNRFEVRNP VKLLQAADSF KDQTFFLSQV SQDALRRTIF PLGELTKDFV
210 220 230 240 250
KKIAAENSLH HVLQKRESMG ICFIGKRNLE HFLLQYLQPR PGKFVSIEDN
260 270 280 290 300
TVLGTHKGWF LYTLGQRAKI SGLREPWYVV EKDGTKGDVL VAPRVDHPAL
310 320 330 340 350
YRDLLRTNRV HWIAEEPPAA LVRDKMMECH FRFRHQMALV PCVLTLNQDG
360 370 380 390 400
TVWVTAVKAV RGLALGQFAV FYKGEECLGS GKILRLGPSA YTLQKGKNRT
410
RVAPEASSDS PGLHPTS
Length:417
Mass (Da):47,240
Last modified:June 1, 2001 - v1
Checksum:i8B4F0E6F461953CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY349617 mRNA. Translation: AAQ55218.1.
AK005541 mRNA. Translation: BAB24110.1.
AK043532 mRNA. Translation: BAC31570.1.
AK044059 mRNA. Translation: BAC31758.1.
BC061026 mRNA. Translation: AAH61026.1.
CCDSiCCDS27726.1.
RefSeqiNP_082339.1. NM_028063.2.
UniGeneiMm.158211.

Genome annotation databases

EnsembliENSMUST00000023019; ENSMUSP00000023019; ENSMUSG00000022386.
GeneIDi72026.
KEGGimmu:72026.
UCSCiuc007xdr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY349617 mRNA. Translation: AAQ55218.1.
AK005541 mRNA. Translation: BAB24110.1.
AK043532 mRNA. Translation: BAC31570.1.
AK044059 mRNA. Translation: BAC31758.1.
BC061026 mRNA. Translation: AAH61026.1.
CCDSiCCDS27726.1.
RefSeqiNP_082339.1. NM_028063.2.
UniGeneiMm.158211.

3D structure databases

ProteinModelPortaliQ9DAT5.
SMRiQ9DAT5. Positions 7-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000023019.

PTM databases

PhosphoSiteiQ9DAT5.

Proteomic databases

EPDiQ9DAT5.
MaxQBiQ9DAT5.
PaxDbiQ9DAT5.
PRIDEiQ9DAT5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023019; ENSMUSP00000023019; ENSMUSG00000022386.
GeneIDi72026.
KEGGimmu:72026.
UCSCiuc007xdr.1. mouse.

Organism-specific databases

CTDi55687.
MGIiMGI:1919276. Trmu.

Phylogenomic databases

eggNOGiKOG2805. Eukaryota.
COG0482. LUCA.
GeneTreeiENSGT00390000014323.
HOGENOMiHOG000218046.
HOVERGENiHBG108157.
InParanoidiQ9DAT5.
KOiK00566.
OMAiAYRVCQI.
PhylomeDBiQ9DAT5.
TreeFamiTF105611.

Enzyme and pathway databases

BRENDAi2.1.1.61. 3474.

Miscellaneous databases

PROiQ9DAT5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DAT5.
ExpressionAtlasiQ9DAT5. baseline and differential.
GenevisibleiQ9DAT5. MM.

Family and domain databases

Gene3Di2.30.30.280. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00144. tRNA_thiouridyl_MnmA.
InterProiIPR023382. Adenine_a_hdrlase_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR004506. tRNA-specific_2-thiouridylase.
[Graphical view]
PANTHERiPTHR11933. PTHR11933. 1 hit.
TIGRFAMsiTIGR00420. trmU. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of mouse TRMU gene encoding the mitochondrial 5-methylaminomethyl-2-thiouridylate-methyltransferase."
    Yan Q., Guan M.-X.
    Biochim. Biophys. Acta 1676:119-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "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: Brain cortex and Placenta.
  3. "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].
    Tissue: Liver.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Liver, Pancreas and Spleen.

Entry informationi

Entry nameiMTU1_MOUSE
AccessioniPrimary (citable) accession number: Q9DAT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

During the reaction, ATP is used to activate the C2 atom of U34 by adenylation. After this, the persulfide sulfur on the catalytic cysteine is transferred to the C2 atom of the wobble base (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards the activated C2 atom on U34. Subsequently, a transient disulfide bond is formed between the two active site cysteine residues (By similarity).By similarity

Caution

Was originally thought to be a 5-methylaminomethyl-2-methyltransferase involved in tRNA modification.1 Publication

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

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.