TM10A_BOVIN
ID TM10A_BOVIN Reviewed; 338 AA.
AC Q3MHI8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; BC105223; AAI05224.1; -; mRNA.
DR RefSeq; NP_001030554.1; NM_001035477.2.
DR RefSeq; XP_005207767.1; XM_005207710.3.
DR RefSeq; XP_005207768.1; XM_005207711.3.
DR RefSeq; XP_010804261.1; XM_010805959.2.
DR AlphaFoldDB; Q3MHI8; -.
DR SMR; Q3MHI8; -.
DR STRING; 9913.ENSBTAP00000000230; -.
DR PaxDb; Q3MHI8; -.
DR PRIDE; Q3MHI8; -.
DR Ensembl; ENSBTAT00000000230; ENSBTAP00000000230; ENSBTAG00000000197.
DR GeneID; 616544; -.
DR KEGG; bta:616544; -.
DR CTD; 93587; -.
DR VEuPathDB; HostDB:ENSBTAG00000000197; -.
DR VGNC; VGNC:36366; TRMT10A.
DR eggNOG; KOG2967; Eukaryota.
DR GeneTree; ENSGT00530000063169; -.
DR HOGENOM; CLU_034384_7_0_1; -.
DR InParanoid; Q3MHI8; -.
DR OMA; FKKNDGW; -.
DR OrthoDB; 1396299at2759; -.
DR TreeFam; TF330972; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000000197; Expressed in semen and 105 other tissues.
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; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; ISS:UniProtKB.
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; 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..338
FT /note="tRNA methyltransferase 10 homolog A"
FT /id="PRO_0000311314"
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 296..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..80
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..328
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 MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBZ6"
SQ SEQUENCE 338 AA; 39573 MW; 7055B6CEF42A30DB CRC64;
MSSEMLPAFS ETCNVERQKN LSEDGEQNQK PGSSERFQPI SKRQMKKLMK QKQWEEQREL
RKQKRKEKRK RKQLERQCQP ESNSDGSDRK RIRRDVVHSP LRLIIDCSFD SLMVLKDIKK
LHKQIQRCYA ENRRALHPVQ FYLTSHGGQL KKNMDENDKG WVNWKDIHIK PEHYSEFIQK
EDLIYLTSDS PNILKELDES KAYVIGGLVD HNHHKGLTYK QASDHGIDHA QLPLGNFVKM
NSRKVLAVNH VFEIILEYLE TRDWQEAFFT ILPQRKGAVP TDQACESCSH DKKFARVEGG
LNSDSSEEEN RHELDSTHEE EKQDKENSTE STVNSVPH
