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Database: UniProt
Entry: H2MLW7_ORYLA
LinkDB: H2MLW7_ORYLA
Original site: H2MLW7_ORYLA 
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
//
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