TRM2B_MOUSE
ID TRM2B_MOUSE Reviewed; 493 AA.
AC Q8BQJ6; Q8CE55;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=tRNA (uracil-5-)-methyltransferase homolog B;
DE EC=2.1.1.35 {ECO:0000269|PubMed:31736397};
DE AltName: Full=TRM2 homolog B {ECO:0000305};
DE AltName: Full=rRNA (uracil-5-)-methyltransferase TRMT2B {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:31736397};
DE Flags: Precursor;
GN Name=Trmt2b {ECO:0000303|PubMed:31736397, ECO:0000312|MGI:MGI:2442530};
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=Skin;
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=C57BL/6J;
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31736397; DOI=10.1080/15476286.2019.1694733;
RA Laptev I., Shvetsova E., Levitskii S., Serebryakova M., Rubtsova M.,
RA Bogdanov A., Kamenski P., Sergiev P., Dontsova O.;
RT "Mouse Trmt2B protein is a dual specific mitochondrial metyltransferase
RT responsible for m5U formation in both tRNA and rRNA.";
RL RNA Biol. 17:441-450(2020).
CC -!- FUNCTION: Mitochondrial S-adenosyl-L-methionine-dependent
CC methyltransferase that catalyzes the formation of 5-methyl-uridine in
CC tRNAs and 12S rRNA (PubMed:31736397). Catalyzes the methylation of
CC uridine at position 54 (m5U54) in all tRNAs (PubMed:31736397).
CC Specifically methylates the uridine in position 425 of 12S rRNA
CC (m5U425) (PubMed:31736397). Does not affect RNA stability or
CC mitochondrial translation (By similarity).
CC {ECO:0000250|UniProtKB:Q96GJ1, ECO:0000269|PubMed:31736397}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(54) in tRNA = 5-
CC methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42712, Rhea:RHEA-COMP:10167, Rhea:RHEA-COMP:10193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447; EC=2.1.1.35;
CC Evidence={ECO:0000269|PubMed:31736397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42713;
CC Evidence={ECO:0000269|PubMed:31736397};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in 12S rRNA + S-adenosyl-L-methionine = a 5-
CC methyluridine in 12S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:69859, Rhea:RHEA-COMP:17791, Rhea:RHEA-COMP:17792,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74447;
CC Evidence={ECO:0000269|PubMed:31736397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69860;
CC Evidence={ECO:0000269|PubMed:31736397};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q96GJ1}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01024}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK028999; BAC26233.1; -; mRNA.
DR EMBL; AK049523; BAC33793.1; -; mRNA.
DR EMBL; AL672215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056937; AAH56937.1; -; mRNA.
DR CCDS; CCDS41121.1; -.
DR RefSeq; NP_001161466.1; NM_001167994.1.
DR RefSeq; NP_766128.2; NM_172540.2.
DR AlphaFoldDB; Q8BQJ6; -.
DR SMR; Q8BQJ6; -.
DR STRING; 10090.ENSMUSP00000084820; -.
DR iPTMnet; Q8BQJ6; -.
DR PhosphoSitePlus; Q8BQJ6; -.
DR EPD; Q8BQJ6; -.
DR PaxDb; Q8BQJ6; -.
DR PRIDE; Q8BQJ6; -.
DR ProteomicsDB; 258849; -.
DR Antibodypedia; 28575; 163 antibodies from 24 providers.
DR DNASU; 215201; -.
DR Ensembl; ENSMUST00000087541; ENSMUSP00000084820; ENSMUSG00000067369.
DR Ensembl; ENSMUST00000113252; ENSMUSP00000108878; ENSMUSG00000067369.
DR GeneID; 215201; -.
DR KEGG; mmu:215201; -.
DR UCSC; uc009ufq.2; mouse.
DR CTD; 79979; -.
DR MGI; MGI:2442530; Trmt2b.
DR VEuPathDB; HostDB:ENSMUSG00000067369; -.
DR eggNOG; KOG2187; Eukaryota.
DR GeneTree; ENSGT00530000063723; -.
DR HOGENOM; CLU_014689_4_0_1; -.
DR InParanoid; Q8BQJ6; -.
DR OMA; VLNCEFI; -.
DR OrthoDB; 248059at2759; -.
DR PhylomeDB; Q8BQJ6; -.
DR TreeFam; TF352239; -.
DR BioGRID-ORCS; 215201; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Trmt2b; mouse.
DR PRO; PR:Q8BQJ6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BQJ6; protein.
DR Bgee; ENSMUSG00000067369; Expressed in myocardium of ventricle and 213 other tissues.
DR ExpressionAtlas; Q8BQJ6; baseline and differential.
DR Genevisible; Q8BQJ6; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0070041; F:rRNA (uridine-C5-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030697; F:S-adenosylmethionine-dependent tRNA (m5U54) methyltransferase activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025714; Methyltranfer_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR045850; TRM2_euk.
DR InterPro; IPR025823; tRNA_(uracil-5-)_MeTrfase_met.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR PANTHER; PTHR45904; PTHR45904; 1.
DR Pfam; PF13847; Methyltransf_31; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..14
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 15..493
FT /note="tRNA (uracil-5-)-methyltransferase homolog B"
FT /id="PRO_0000311933"
FT ACT_SITE 440
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT ACT_SITE 486
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P23003"
FT BINDING 312
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 362
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT BINDING 412
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01024"
FT CONFLICT 151
FT /note="R -> K (in Ref. 1; BAC26233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 55476 MW; 81FF48C6A9F0314E CRC64;
MHNPRLFLSR AGFFSKPGLL PWDTGRPPDL SQSLLGRAYK GSFTSVIAKK HPSRQKYQKK
QRHCRDDSWQ ERLADVVTPL WRLSYEAQLK VKFEAQKKLL QSLESHLKVL HGVSDTVAAH
QSEGLRCLLH PIIPSPTTTG YRNKSTFSVY RSPDGNPKTV GYYLGTWKDG NVVCLPCNHL
KNIPEKHSQV AQYYEVFLRQ SSVEPCLLFH EGGHWRELVV RTNRQGHTMA IVTFHPQGLS
EEEVCVQKVT LKDFFTKGPG AICELTSLYF QESTMTRCSH QQSPYQLLFG EPHIFEDLLG
LKIRISPDAF FQINTAGAEM LYRIIGELSG VNSESLLLDI CCGTGVIGLS VAQRASQVHG
IELVEQAVED ARWTAAFNGV TNCEFHAGRA ETILPQLLKS QKDEKLTVAV VNPARAGLHY
RVVRAIRNCR TIHTLVFVSC KPHGESTRNF IELCCPPNSA KQLLGDPFVL REAVPVDLFP
HTPHCELVLL FTR
