TRM5_MACFA
ID TRM5_MACFA Reviewed; 509 AA.
AC Q95KJ2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 73.
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};
DE Flags: Precursor;
GN Name=TRMT5 {ECO:0000255|HAMAP-Rule:MF_03152};
GN Synonyms=TRM5 {ECO:0000255|HAMAP-Rule:MF_03152}; ORFNames=QtrA-10686;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (APR-2001) 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; AB060834; BAB46864.1; -; mRNA.
DR RefSeq; NP_001306556.1; NM_001319627.1.
DR AlphaFoldDB; Q95KJ2; -.
DR SMR; Q95KJ2; -.
DR STRING; 9541.XP_005561487.1; -.
DR GeneID; 102130005; -.
DR CTD; 57570; -.
DR eggNOG; KOG2078; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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:0070901; P:mitochondrial tRNA methylation; ISS:UniProtKB.
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; Transit peptide; tRNA processing.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT CHAIN 58..509
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000256514"
FT REGION 478..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 289
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 327..328
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 355..356
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 387
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 509 AA; 58106 MW; F16A7D71C22F108F CRC64;
MVLWILWRPF GFSRRLLKLE RHSITESKSL IPLAWTSLTQ TLSESPGIFL LGQRKRFSTM
PEIETHEGDS ELFSPPSDVR GMTKLDRTAF KKTVNIPVLK VRKEIVSRLM RSLRRAALQR
PGIKRVIEDP EDKESRLILL DPYKIFTHDS FEKAGLSVLE QLNVSPQISK YNLELTYENF
KSEEILRAVL PEGQDVTSGF SRVGHIAHLN LRDHQLPFKQ LIGQVMIDKN PGITSAVNKI
NNIDNMYRNF HMEVLSGEQN MMTKVRENKY TYEFDFSKVY WNPRLSTEHS RITELLKAGD
VLFDVFAGVG PFAIPVAKKN CTVFANDLNP ESHKWLLHNC KLNKVDQKVK IFNLDGKDFL
QGPVKEELIQ LLSLSKERKP SVHIVMNLPA KAIEFLSAFK WLLDGQPCSN EFLPIVHCYS
FSKDANPAKD VRQRAGAVLG ISLEACSSVH LVRNVAPNKE MLCITFQIPA AVLYKNQTKN
PENHEDPPLK RQRTAEAFSD EKTQIASNT
