TRM5_BOVIN
ID TRM5_BOVIN Reviewed; 497 AA.
AC Q3MHN8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000255|HAMAP-Rule:MF_03152};
GN Name=TRMT5 {ECO:0000255|HAMAP-Rule:MF_03152};
GN Synonyms=TRM5 {ECO:0000255|HAMAP-Rule:MF_03152};
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in mitochondrial tRNA methylation (By similarity).
CC Specifically methylates the N1 position of guanosine-37 in various
CC tRNAs. Methylation is not dependent on the nature of the nucleoside 5'
CC of the target nucleoside. This is the first step in the biosynthesis of
CC wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and
CC required for accurate decoding. {ECO:0000250|UniProtKB:Q32P41,
CC ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03152};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000305}.
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DR EMBL; BC105167; AAI05168.1; -; mRNA.
DR RefSeq; NP_001029737.1; NM_001034565.2.
DR AlphaFoldDB; Q3MHN8; -.
DR SMR; Q3MHN8; -.
DR STRING; 9913.ENSBTAP00000015658; -.
DR PaxDb; Q3MHN8; -.
DR PRIDE; Q3MHN8; -.
DR Ensembl; ENSBTAT00000015658; ENSBTAP00000015658; ENSBTAG00000011796.
DR GeneID; 528221; -.
DR KEGG; bta:528221; -.
DR CTD; 57570; -.
DR VEuPathDB; HostDB:ENSBTAG00000011796; -.
DR VGNC; VGNC:36373; TRMT5.
DR eggNOG; KOG2078; Eukaryota.
DR GeneTree; ENSGT00940000153304; -.
DR HOGENOM; CLU_022610_2_3_1; -.
DR InParanoid; Q3MHN8; -.
DR OrthoDB; 788980at2759; -.
DR TreeFam; TF315073; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000011796; Expressed in prostate gland and 105 other tissues.
DR ExpressionAtlas; Q3MHN8; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_03152; TRM5; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..497
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000256512"
FT REGION 478..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 325..326
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 353..354
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 386
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 497 AA; 56954 MW; D52FC94A36D0DE8C CRC64;
MRSLLKQFAF SRRLLKVESC RITESASLIL LPWASLIQKL NRVPVIFLLD QRKRFSTMPE
IETNHRDSEL FSPPSEVRGM TELDRTAFKK TVTIPVLKVR KEVVNKLMRS LKRAALQRPG
IKRVIEDPED GEGRLIMLDP YKMFTVDSFE KEELSILKQL NVNPQISKYN LDLTYENFKS
EEILRAVLPE GQDVTSGFSR VGHIAHLNLR DHQLPYKHLI GQVMIDKNPG ITSAVNKINN
IDNTYRNFEM EVLSGEENMM TKVRENNYTY EFDFSKVYWN PRLSTEHSRI TELLKPGDVL
FDVFAGVGPF AIPAAKKKCT VFANDLNPES HKWLLHNCKL NKVDQKVKVF NLDGRDFLQG
PVREELMQQL GPLSKERKHS VHIVMNLPAK AIEFLSAFKA LLEGQPCGSE LLPIVHCYSF
SKDANPAKDV QQRAATVLGI SLEAYSSVHL VRNVAPNKEM LCITFRIPAA ILYKNQTVNR
DNHEGPPLKR QRTDKDF
