TRM5_MOUSE
ID TRM5_MOUSE Reviewed; 501 AA.
AC Q9D0C4; Q5DTY1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000255|HAMAP-Rule:MF_03152};
GN Name=Trmt5; Synonyms=Kiaa1393, Trm5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-501 (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in mitochondrial tRNA methylation (By similarity).
CC Specifically methylates the N1 position of guanosine-37 in various
CC tRNAs. Methylation is not dependent on the nature of the nucleoside 5'
CC of the target nucleoside. This is the first step in the biosynthesis of
CC wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and
CC required for accurate decoding. {ECO:0000250|UniProtKB:Q32P41,
CC ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03152};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D0C4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D0C4-2; Sequence=VSP_021355;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000305}.
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DR EMBL; AK011576; BAB27710.1; -; mRNA.
DR EMBL; BC012521; AAH12521.1; -; mRNA.
DR EMBL; AK220389; BAD90443.1; -; mRNA.
DR CCDS; CCDS36474.1; -. [Q9D0C4-1]
DR RefSeq; NP_083856.1; NM_029580.3. [Q9D0C4-1]
DR AlphaFoldDB; Q9D0C4; -.
DR SMR; Q9D0C4; -.
DR BioGRID; 218076; 1.
DR STRING; 10090.ENSMUSP00000112121; -.
DR iPTMnet; Q9D0C4; -.
DR PhosphoSitePlus; Q9D0C4; -.
DR EPD; Q9D0C4; -.
DR MaxQB; Q9D0C4; -.
DR PaxDb; Q9D0C4; -.
DR PeptideAtlas; Q9D0C4; -.
DR PRIDE; Q9D0C4; -.
DR ProteomicsDB; 258982; -. [Q9D0C4-1]
DR ProteomicsDB; 258983; -. [Q9D0C4-2]
DR Antibodypedia; 85; 73 antibodies from 20 providers.
DR DNASU; 76357; -.
DR Ensembl; ENSMUST00000116420; ENSMUSP00000112121; ENSMUSG00000034442. [Q9D0C4-1]
DR GeneID; 76357; -.
DR KEGG; mmu:76357; -.
DR UCSC; uc007nwf.1; mouse. [Q9D0C4-2]
DR UCSC; uc007nwg.1; mouse. [Q9D0C4-1]
DR CTD; 57570; -.
DR MGI; MGI:1923607; Trmt5.
DR VEuPathDB; HostDB:ENSMUSG00000034442; -.
DR eggNOG; KOG2078; Eukaryota.
DR GeneTree; ENSGT00940000153304; -.
DR HOGENOM; CLU_022610_2_3_1; -.
DR InParanoid; Q9D0C4; -.
DR OMA; PKKQMFC; -.
DR OrthoDB; 788980at2759; -.
DR PhylomeDB; Q9D0C4; -.
DR TreeFam; TF315073; -.
DR BioGRID-ORCS; 76357; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Trmt5; mouse.
DR PRO; PR:Q9D0C4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9D0C4; protein.
DR Bgee; ENSMUSG00000034442; Expressed in spermatocyte and 230 other tissues.
DR ExpressionAtlas; Q9D0C4; baseline and differential.
DR Genevisible; Q9D0C4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03152; TRM5; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Methyltransferase; Mitochondrion; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..501
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000256515"
FT REGION 474..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 320..321
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 348..349
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 380
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT VAR_SEQ 475..501
FT /note="QNDQEPPLKRQKTGDPFSGEPQIASDS -> REFFTMKCGVYYP (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_021355"
FT CONFLICT 334
FT /note="K -> Q (in Ref. 3; BAD90443)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 56794 MW; 55816182B08766C0 CRC64;
MRIVWKLFGF SRRLLQVEWC HPSESILLFT LVPRLRKAPS VFLLGQRQGL STMPEIEASV
RDSELFSPPS DVRGMRELDR TAFKKTVSIP VLKARKEVVN RLMRALRRVA LQRPGIKRVI
EDPKDEDSRL IMLDPYRMLT ADSFDKAELG VLKELDVSPQ LSQYNLELTY ENFKSEEILK
AVLPEGQDVT SGFSRVGHIA HLNLRDHQLP FKHLIGQVMV DKNPGITSAV NKTSNIDNTY
RNFQMEVLCG EENMLTKVRE NNYTYEFDFS KVYWNPRLST EHGRITELLN PGDVLFDVFA
GVGPFAIPAA RKNCTVFAND LNPESHKWLL HNCKLNKVDQ KVKVFNMDGK DFIQGPVREE
LMLRLGLSAE AKPSVHIVMN LPAKAIEFLS VFRSLLDGQP CSTELLPTVH CYCFSKDSDP
AKDVRQQAEA VLGVSLETSS SVHLVRNVAP NKEMLCITFQ IPTATLYRNQ SLSLQNDQEP
PLKRQKTGDP FSGEPQIASD S
