TM10A_MOUSE
ID TM10A_MOUSE Reviewed; 328 AA.
AC Q8C1Z8; Q4KMM8; Q5CZW9; Q8VDF5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=tRNA methyltransferase 10 homolog A;
DE EC=2.1.1.221 {ECO:0000250|UniProtKB:Q8TBZ6};
DE AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 2;
DE AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase TRMT10A;
GN Name=Trmt10a; Synonyms=Rg9mtd2;
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].
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].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Blastocyst, Head, and 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).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent guanine N(1)-
CC methyltransferase that catalyzes the formation of N(1)-methylguanine at
CC position 9 (m1G9) in tRNAs. Probably not able to catalyze formation of
CC N(1)-methyladenine at position 9 (m1A9) in tRNAs.
CC {ECO:0000250|UniProtKB:Q8TBZ6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000250|UniProtKB:Q8TBZ6};
CC -!- SUBUNIT: Interacts with tRNA. {ECO:0000250|UniProtKB:Q8TBZ6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TBZ6}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q8TBZ6}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22121.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=AAH90650.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH98478.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC41020.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK089967; BAC41020.1; ALT_INIT; mRNA.
DR EMBL; BC022121; AAH22121.1; ALT_INIT; mRNA.
DR EMBL; BC090650; AAH90650.1; ALT_INIT; mRNA.
DR EMBL; BC098478; AAH98478.1; ALT_INIT; mRNA.
DR RefSeq; NP_001335125.1; NM_001348196.1.
DR RefSeq; NP_001335126.1; NM_001348197.1.
DR RefSeq; NP_780598.2; NM_175389.5.
DR RefSeq; XP_006500906.1; XM_006500843.3.
DR RefSeq; XP_006500907.1; XM_006500844.1.
DR RefSeq; XP_006500909.1; XM_006500846.3.
DR RefSeq; XP_006500910.1; XM_006500847.3.
DR RefSeq; XP_011238285.1; XM_011239983.2.
DR AlphaFoldDB; Q8C1Z8; -.
DR SMR; Q8C1Z8; -.
DR IntAct; Q8C1Z8; 1.
DR STRING; 10090.ENSMUSP00000042082; -.
DR iPTMnet; Q8C1Z8; -.
DR PhosphoSitePlus; Q8C1Z8; -.
DR EPD; Q8C1Z8; -.
DR jPOST; Q8C1Z8; -.
DR MaxQB; Q8C1Z8; -.
DR PaxDb; Q8C1Z8; -.
DR PRIDE; Q8C1Z8; -.
DR ProteomicsDB; 258899; -.
DR DNASU; 108943; -.
DR GeneID; 108943; -.
DR KEGG; mmu:108943; -.
DR CTD; 93587; -.
DR MGI; MGI:1920421; Trmt10a.
DR eggNOG; KOG2967; Eukaryota.
DR InParanoid; Q8C1Z8; -.
DR OrthoDB; 1396299at2759; -.
DR PhylomeDB; Q8C1Z8; -.
DR TreeFam; TF330972; -.
DR BioGRID-ORCS; 108943; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Trmt10a; mouse.
DR PRO; PR:Q8C1Z8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C1Z8; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; ISO:MGI.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0010960; P:magnesium ion homeostasis; IMP:MGI.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; ISO:MGI.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR016653; TRM10/TRM10A.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR PANTHER; PTHR13563:SF13; PTHR13563:SF13; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PIRSF; PIRSF016323; tRNA_m1G_mtfrase_met; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..328
FT /note="tRNA methyltransferase 10 homolog A"
FT /id="PRO_0000311316"
FT DOMAIN 88..278
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 43..83
FT /evidence="ECO:0000255"
FT COMPBIAS 18..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KLI2"
FT CONFLICT 13
FT /note="P -> T (in Ref. 2; AAH90650/AAH98478)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="N -> D (in Ref. 2; AAH98478)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="S -> N (in Ref. 2; AAH22121/AAH90650/AAH98478)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="E -> K (in Ref. 2; AAH22121)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="R -> K (in Ref. 2; AAH22121)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="S -> R (in Ref. 2; AAH22121)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="D -> V (in Ref. 2; AAH90650/AAH98478)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="P -> L (in Ref. 2; AAH22121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 37966 MW; F800131ECE737FA7 CRC64;
MSSEMLPASI ESPNVEEKLG TSDGEEERQE PRVDAGAEPI SKRQLKKLMK QKQWEEQREQ
RKEKRKEKRK RKKLERRQLE SNSDGNDRKR VRRDVARSSL RLVIDCSFDD LMVLKDIKKL
HKQIQRCYAE NRRASHPVQF YLTSHGGQLK KNMDENDQGW VNWKDIHIKS EHYSELIKKE
DLVYLTSDSP NVLKDLDESK AYVIGGLVDH SHHKGLTFKQ ATSYGIEHAQ LPLADFVKMN
SRKVLAVNHV FEIILEFLET RDWQEAFFTI LPQRKGAVPA HKACESSPQD HQSLPEGWDS
ASEGESCRDN PDSPQKDEQG QQSSPVLQ
