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Protein

tRNA (guanine(37)-N1)-methyltransferase

Gene

Trmt5

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

Functioni

Involved in mitochondrial tRNA methylation (By similarity). Specifically methylates the N1 position of guanosine-37 in various tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.UniRule annotationBy similarity

Catalytic activityi

S-adenosyl-L-methionine + guanine(37) in tRNA = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei282 – 2821S-adenosyl-L-methionineUniRule annotation
Binding sitei380 – 3801S-adenosyl-L-methionineUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine(37)-N1)-methyltransferaseUniRule annotation (EC:2.1.1.228UniRule annotation)
Alternative name(s):
M1G-methyltransferaseUniRule annotation
tRNA [GM37] methyltransferaseUniRule annotation
tRNA methyltransferase 5 homologUniRule annotation
Gene namesi
Name:Trmt5
Synonyms:Kiaa1393, Trm5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1923607. Trmt5.

Subcellular locationi

  • Mitochondrion matrix UniRule annotation
  • Nucleus UniRule annotation
  • Cytoplasm UniRule annotation

  • Note: Predominantly in the mitochondria and in the nucleus.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501tRNA (guanine(37)-N1)-methyltransferasePRO_0000256515Add
BLAST

Proteomic databases

EPDiQ9D0C4.
MaxQBiQ9D0C4.
PaxDbiQ9D0C4.
PRIDEiQ9D0C4.

PTM databases

iPTMnetiQ9D0C4.
PhosphoSiteiQ9D0C4.

Expressioni

Gene expression databases

BgeeiQ9D0C4.
GenevisibleiQ9D0C4. MM.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

IntActiQ9D0C4. 1 interaction.
MINTiMINT-4126392.
STRINGi10090.ENSMUSP00000112121.

Structurei

3D structure databases

ProteinModelPortaliQ9D0C4.
SMRiQ9D0C4. Positions 177-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni320 – 3212S-adenosyl-L-methionine bindingUniRule annotation
Regioni348 – 3492S-adenosyl-L-methionine bindingUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2078. Eukaryota.
COG2520. LUCA.
GeneTreeiENSGT00390000008208.
HOGENOMiHOG000195270.
HOVERGENiHBG094093.
InParanoidiQ9D0C4.
KOiK15429.
OMAiFIQGPVR.
OrthoDBiEOG7VDXP0.
PhylomeDBiQ9D0C4.
TreeFamiTF315073.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_03152. TRM5.
InterProiIPR030382. MeTrfase_TRM5/TYW2.
IPR029063. SAM-dependent_MTases.
IPR025792. tRNA_Gua_MeTrfase_euk.
[Graphical view]
PfamiPF02475. Met_10. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51684. SAM_MT_TRM5_TYW2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9D0C4-1) [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
MRIVWKLFGF SRRLLQVEWC HPSESILLFT LVPRLRKAPS VFLLGQRQGL
60 70 80 90 100
STMPEIEASV RDSELFSPPS DVRGMRELDR TAFKKTVSIP VLKARKEVVN
110 120 130 140 150
RLMRALRRVA LQRPGIKRVI EDPKDEDSRL IMLDPYRMLT ADSFDKAELG
160 170 180 190 200
VLKELDVSPQ LSQYNLELTY ENFKSEEILK AVLPEGQDVT SGFSRVGHIA
210 220 230 240 250
HLNLRDHQLP FKHLIGQVMV DKNPGITSAV NKTSNIDNTY RNFQMEVLCG
260 270 280 290 300
EENMLTKVRE NNYTYEFDFS KVYWNPRLST EHGRITELLN PGDVLFDVFA
310 320 330 340 350
GVGPFAIPAA RKNCTVFAND LNPESHKWLL HNCKLNKVDQ KVKVFNMDGK
360 370 380 390 400
DFIQGPVREE LMLRLGLSAE AKPSVHIVMN LPAKAIEFLS VFRSLLDGQP
410 420 430 440 450
CSTELLPTVH CYCFSKDSDP AKDVRQQAEA VLGVSLETSS SVHLVRNVAP
460 470 480 490 500
NKEMLCITFQ IPTATLYRNQ SLSLQNDQEP PLKRQKTGDP FSGEPQIASD

S
Length:501
Mass (Da):56,794
Last modified:June 1, 2001 - v1
Checksum:i55816182B08766C0
GO
Isoform 2 (identifier: Q9D0C4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     475-501: QNDQEPPLKRQKTGDPFSGEPQIASDS → REFFTMKCGVYYP

Show »
Length:487
Mass (Da):55,465
Checksum:i1165769DA919820F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti334 – 3341K → Q in BAD90443 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei475 – 50127QNDQE…IASDS → REFFTMKCGVYYP in isoform 2. 1 PublicationVSP_021355Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011576 mRNA. Translation: BAB27710.1.
BC012521 mRNA. Translation: AAH12521.1.
AK220389 mRNA. Translation: BAD90443.1.
CCDSiCCDS36474.1. [Q9D0C4-1]
RefSeqiNP_083856.1. NM_029580.3. [Q9D0C4-1]
UniGeneiMm.311344.

Genome annotation databases

EnsembliENSMUST00000116420; ENSMUSP00000112121; ENSMUSG00000034442. [Q9D0C4-1]
GeneIDi76357.
KEGGimmu:76357.
UCSCiuc007nwf.1. mouse. [Q9D0C4-2]
uc007nwg.1. mouse. [Q9D0C4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011576 mRNA. Translation: BAB27710.1.
BC012521 mRNA. Translation: AAH12521.1.
AK220389 mRNA. Translation: BAD90443.1.
CCDSiCCDS36474.1. [Q9D0C4-1]
RefSeqiNP_083856.1. NM_029580.3. [Q9D0C4-1]
UniGeneiMm.311344.

3D structure databases

ProteinModelPortaliQ9D0C4.
SMRiQ9D0C4. Positions 177-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D0C4. 1 interaction.
MINTiMINT-4126392.
STRINGi10090.ENSMUSP00000112121.

PTM databases

iPTMnetiQ9D0C4.
PhosphoSiteiQ9D0C4.

Proteomic databases

EPDiQ9D0C4.
MaxQBiQ9D0C4.
PaxDbiQ9D0C4.
PRIDEiQ9D0C4.

Protocols and materials databases

DNASUi76357.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000116420; ENSMUSP00000112121; ENSMUSG00000034442. [Q9D0C4-1]
GeneIDi76357.
KEGGimmu:76357.
UCSCiuc007nwf.1. mouse. [Q9D0C4-2]
uc007nwg.1. mouse. [Q9D0C4-1]

Organism-specific databases

CTDi57570.
MGIiMGI:1923607. Trmt5.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG2078. Eukaryota.
COG2520. LUCA.
GeneTreeiENSGT00390000008208.
HOGENOMiHOG000195270.
HOVERGENiHBG094093.
InParanoidiQ9D0C4.
KOiK15429.
OMAiFIQGPVR.
OrthoDBiEOG7VDXP0.
PhylomeDBiQ9D0C4.
TreeFamiTF315073.

Miscellaneous databases

ChiTaRSiTrmt5. mouse.
PROiQ9D0C4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0C4.
GenevisibleiQ9D0C4. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_03152. TRM5.
InterProiIPR030382. MeTrfase_TRM5/TYW2.
IPR029063. SAM-dependent_MTases.
IPR025792. tRNA_Gua_MeTrfase_euk.
[Graphical view]
PfamiPF02475. Met_10. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51684. SAM_MT_TRM5_TYW2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] (ISOFORM 1).
    Strain: C57BL/6J.
  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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-501 (ISOFORM 2).
    Tissue: Fetal brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen and Testis.

Entry informationi

Entry nameiTRM5_MOUSE
AccessioniPrimary (citable) accession number: Q9D0C4
Secondary accession number(s): Q5DTY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 105 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. 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.