TM10B_MOUSE
ID TM10B_MOUSE Reviewed; 318 AA.
AC Q9D075; A2AKB5; A2AKB6; Q8VCR1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=tRNA methyltransferase 10 homolog B;
DE EC=2.1.1.221 {ECO:0000250|UniProtKB:Q6PF06};
DE AltName: Full=RNA (guanine-9-)-methyltransferase domain-containing protein 3;
DE AltName: Full=tRNA (guanine(9)-N(1))-methyltransferase TRMT10B;
GN Name=Trmt10b; Synonyms=Rg9mtd3;
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].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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:Q6PF06}.
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:Q6PF06};
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=CAM26862.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAM26863.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK011746; BAB27815.1; -; mRNA.
DR EMBL; AK030465; BAC26974.1; -; mRNA.
DR EMBL; AL772285; CAM26862.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772285; CAM26863.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL772285; CAM26864.1; -; Genomic_DNA.
DR EMBL; BC019428; AAH19428.1; -; mRNA.
DR CCDS; CCDS18135.1; -.
DR RefSeq; NP_081542.2; NM_027266.4.
DR RefSeq; XP_006538305.1; XM_006538242.3.
DR RefSeq; XP_006538306.1; XM_006538243.3.
DR RefSeq; XP_006538307.1; XM_006538244.3.
DR AlphaFoldDB; Q9D075; -.
DR SMR; Q9D075; -.
DR STRING; 10090.ENSMUSP00000041052; -.
DR iPTMnet; Q9D075; -.
DR PhosphoSitePlus; Q9D075; -.
DR PaxDb; Q9D075; -.
DR PRIDE; Q9D075; -.
DR ProteomicsDB; 258900; -.
DR Antibodypedia; 5730; 111 antibodies from 18 providers.
DR DNASU; 69934; -.
DR Ensembl; ENSMUST00000044673; ENSMUSP00000041052; ENSMUSG00000035601.
DR GeneID; 69934; -.
DR KEGG; mmu:69934; -.
DR UCSC; uc008ssj.1; mouse.
DR CTD; 158234; -.
DR MGI; MGI:1917184; Trmt10b.
DR VEuPathDB; HostDB:ENSMUSG00000035601; -.
DR eggNOG; KOG2967; Eukaryota.
DR GeneTree; ENSGT00530000063169; -.
DR InParanoid; Q9D075; -.
DR OMA; ALQAWFP; -.
DR OrthoDB; 1396299at2759; -.
DR PhylomeDB; Q9D075; -.
DR TreeFam; TF330972; -.
DR BioGRID-ORCS; 69934; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Trmt10b; mouse.
DR PRO; PR:Q9D075; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D075; protein.
DR Bgee; ENSMUSG00000035601; Expressed in animal zygote and 250 other tissues.
DR ExpressionAtlas; Q9D075; baseline and differential.
DR Genevisible; Q9D075; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISO:MGI.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..318
FT /note="tRNA methyltransferase 10 homolog B"
FT /id="PRO_0000311322"
FT DOMAIN 114..311
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 72..93
FT /evidence="ECO:0000255"
FT COMPBIAS 72..88
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 157..158
FT /note="NK -> KQ (in Ref. 1; BAB27815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 36377 MW; B3C58B5932C041B1 CRC64;
MDCKSEESAQ RTDSQAFQEP DGLPEAGGED GLSESFQLLQ VDVEYERPEE TSPANSAVWS
SKNMQRKQRH WERIVSSKKS KRKQERERRK AKRAEDPGNG TCPQHSKRFL KALTKEKLLE
AKHSGPRLCV DLSMTQHMSK KELSRLAGQI RRLYGSNKKA SRPFWICLTG FSTASPLYEE
CLRMNDGFSA YLLDVTEEDC FSLFPLETLV YLTPDSEHSL EDIDQSTVYV IGGLVDESIQ
KKVTFQKARE YSVKTARLPI QEYMIKRQNE KNYHSEILAI NQVFDILSTY FETRNWPEAL
KKGVSPGKGY VLQNSAEG
