TM10A_RAT
ID TM10A_RAT Reviewed; 335 AA.
AC Q4KLI2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-24 AND SER-331, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=24204302; DOI=10.1371/journal.pgen.1003888;
RA Igoillo-Esteve M., Genin A., Lambert N., Desir J., Pirson I.,
RA Abdulkarim B., Simonis N., Drielsma A., Marselli L., Marchetti P.,
RA Vanderhaeghen P., Eizirik D.L., Wuyts W., Julier C., Chakera A.J.,
RA Ellard S., Hattersley A.T., Abramowicz M., Cnop M.;
RT "tRNA methyltransferase homolog gene TRMT10A mutation in young onset
RT diabetes and primary microcephaly in humans.";
RL PLoS Genet. 9:E1003888-E1003888(2013).
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 -!- TISSUE SPECIFICITY: Ubiquitously expressed. Is more abundant in brain
CC and pancreatic islets compared to other tissues (at protein level).
CC {ECO:0000269|PubMed:24204302}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
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DR EMBL; BC099190; AAH99190.1; -; mRNA.
DR RefSeq; NP_001037697.1; NM_001044232.1.
DR RefSeq; XP_006233431.1; XM_006233369.3.
DR AlphaFoldDB; Q4KLI2; -.
DR SMR; Q4KLI2; -.
DR STRING; 10116.ENSRNOP00000014694; -.
DR iPTMnet; Q4KLI2; -.
DR PhosphoSitePlus; Q4KLI2; -.
DR PaxDb; Q4KLI2; -.
DR PRIDE; Q4KLI2; -.
DR GeneID; 295496; -.
DR KEGG; rno:295496; -.
DR CTD; 93587; -.
DR RGD; 1594565; Trmt10a.
DR VEuPathDB; HostDB:ENSRNOG00000011025; -.
DR eggNOG; KOG2967; Eukaryota.
DR HOGENOM; CLU_034384_7_0_1; -.
DR InParanoid; Q4KLI2; -.
DR PhylomeDB; Q4KLI2; -.
DR PRO; PR:Q4KLI2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011025; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q4KLI2; baseline and differential.
DR Genevisible; Q4KLI2; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; ISO:RGD.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0010960; P:magnesium ion homeostasis; ISO:RGD.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; ISO:RGD.
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 1: Evidence at protein level;
KW Coiled coil; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..335
FT /note="tRNA methyltransferase 10 homolog A"
FT /id="PRO_0000311317"
FT DOMAIN 88..279
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 279..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..84
FT /evidence="ECO:0000255"
FT COMPBIAS 20..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 COMPBIAS 317..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 335 AA; 38424 MW; 738170C7C86BF615 CRC64;
MSSEVLPASI EPPNVEGKPG ASDSEEERQK QRVDAEAQPI SKRQLKKLMK QRLWEEQREQ
RKEKRKEKRK RKKLERRCQL ESNSDGNDRK RIRRHVAPSN LRLIIDCSFD DLMVLKDIKK
LHKQIQRCYA ENRRASHPVQ FYLTSHGGQL KKNMDENDQG WVNWKDIHIK SEHYSELIKK
EDLVYLTSDS PNVLKDLDES KAYVIGGLVD HNHHKGLTFK QASSYGIKHA QLPLAEFVKM
NSRKVLAVNH VFEIILEFLE TGDWQEAFFT ILPPRKGAVP AHKACESSPQ DHQALPGGWD
SAIEGEHGRD DPGSPHKEQQ GQQSSSVSAV SPDPQ
