ID H2MLW7_ORYLA Unreviewed; 471 AA.
AC H2MLW7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE EC=2.1.1.228 {ECO:0000256|HAMAP-Rule:MF_03152};
DE AltName: Full=M1G-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA methyltransferase 5 homolog {ECO:0000256|HAMAP-Rule:MF_03152};
GN Name=TRMT5 {ECO:0000256|HAMAP-Rule:MF_03152};
GN Synonyms=TRM5 {ECO:0000256|HAMAP-Rule:MF_03152}, trmt5
GN {ECO:0000313|Ensembl:ENSORLP00000019703.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000019703.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000019703.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019703.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000019703.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019703.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 in
CC various cytoplasmic and mitochondrial tRNAs. Methylation is not
CC dependent on the nature of the nucleoside 5' of the target nucleoside.
CC This is the first step in the biosynthesis of wybutosine (yW), a
CC modified base adjacent to the anticodon of tRNAs and required for
CC accurate decoding. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03152};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03152}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC Rule:MF_03152}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03152}. Cytoplasm
CC {ECO:0000256|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC mitochondria and in the nucleus. {ECO:0000256|HAMAP-Rule:MF_03152}.
CC -!- SIMILARITY: Belongs to the TRM5 / TYW2 family. {ECO:0000256|HAMAP-
CC Rule:MF_03152}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000256|ARBA:ARBA00009775}.
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DR RefSeq; XP_004082329.1; XM_004082281.2.
DR AlphaFoldDB; H2MLW7; -.
DR STRING; 8090.ENSORLP00000019703; -.
DR Ensembl; ENSORLT00000019704.2; ENSORLP00000019703.2; ENSORLG00000015734.2.
DR GeneID; 101175279; -.
DR KEGG; ola:101175279; -.
DR CTD; 57570; -.
DR eggNOG; KOG2078; Eukaryota.
DR GeneTree; ENSGT00940000153304; -.
DR HOGENOM; CLU_022610_2_3_1; -.
DR InParanoid; H2MLW7; -.
DR OrthoDB; 276346at2759; -.
DR TreeFam; TF315073; -.
DR Proteomes; UP000001038; Chromosome 22.
DR Bgee; ENSORLG00000015734; Expressed in gastrula and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0052906; F:tRNA (guanine(37)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0070901; P:mitochondrial tRNA methylation; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.300.110; Met-10+ protein-like domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 PANTHER; PTHR23245:SF36; TRNA (GUANINE(37)-N1)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23245; TRNA METHYLTRANSFERASE; 1.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03152};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03152};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03152};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03152};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03152};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03152};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03152}.
FT DOMAIN 174..440
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
FT REGION 451..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 301..302
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 329..330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 357
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
SQ SEQUENCE 471 AA; 52905 MW; D07BAEAB0A1829E2 CRC64;
MRILCRIFAS AQIHCKIPGI VQPSHFHSAS ACSGLTVKSV MEHKLYRPPP EVRGMTSLDK
DAFTQTITVP ALRVPTVVIN KVMKSLKKAT IQRPGVSRVV QDKEGNSDFR LILLDPNRMA
SSSCFSDAEA EALRSFSVSD ELHNFELKLT YDNLKTEEVL EAVLPEGQDV TSGFSRVGHI
AHMNLRDHQL LYKNLIGQVI MDKTPGITCV VNKTNTIDST YRNFKMEVLA GEENMVAKVK
ENGVTYEFDF SRVYWNPRLS TEHERVVQLV KRGDTMFDVF AGVGPFTIPA ARRGANIFAN
DLNPESYRWL QHNSRLNKVE SRVRTFNLDG REFIRGPLKQ ELPALVKGGA GVHVVMNLPA
LALEFLDAFR GLLKNEPPCD LNLPTVYCYG FSKDEDPGAD MVKRASSSLG FPLENKSTVH
FVRNVAPNKD MMCIRFTLPK EVLFCKNDEL QEPSEEPASK KQKCEESNHS K
//