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Database: UniProt
Entry: A0A167CUU4_9ASCO
LinkDB: A0A167CUU4_9ASCO
Original site: A0A167CUU4_9ASCO 
ID   A0A167CUU4_9ASCO        Unreviewed;       467 AA.
AC   A0A167CUU4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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 {ECO:0000256|HAMAP-Rule:MF_03152};
GN   Name=TRM5 {ECO:0000256|HAMAP-Rule:MF_03152,
GN   ECO:0000313|EMBL:ANB12132.1};
GN   ORFNames=AWJ20_370 {ECO:0000313|EMBL:ANB12132.1};
OS   Sugiyamaella lignohabitans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Sugiyamaella.
OX   NCBI_TaxID=796027 {ECO:0000313|EMBL:ANB12132.1, ECO:0000313|Proteomes:UP000189580};
RN   [1] {ECO:0000313|EMBL:ANB12132.1, ECO:0000313|Proteomes:UP000189580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10342 {ECO:0000313|EMBL:ANB12132.1,
RC   ECO:0000313|Proteomes:UP000189580};
RA   Bellasio M., Peymann A., Valli M., Sipitzky M., Graf A., Sauer M., Marx H.,
RA   Mattanovich D.;
RT   "Complete genome sequence and transcriptome regulation of the pentose
RT   utilising yeast Sugiyamaella lignohabitans.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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   EMBL; CP014501; ANB12132.1; -; Genomic_DNA.
DR   RefSeq; XP_018734609.1; XM_018880728.1.
DR   AlphaFoldDB; A0A167CUU4; -.
DR   GeneID; 30035750; -.
DR   KEGG; slb:AWJ20_370; -.
DR   OrthoDB; 276346at2759; -.
DR   Proteomes; UP000189580; Chromosome a.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
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; 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:UP000189580};
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          150..462
FT                   /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51684"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT   BINDING         277..278
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT   BINDING         305..306
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT   BINDING         359
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
SQ   SEQUENCE   467 AA;  53124 MW;  D783791C36B8864E CRC64;
     MSASESVAKK QKTDRREWVR DFHPPVHRGM MELDKSAFTV KVPLVAALLK DQSFFASLVK
     NSRSDLLQLQ GISRIVEWEN NQKAILLRHD INSPDKVPQA VTPTTLDVLT KAEATYHPYT
     LNLDYDYWRA EDILESVLPE DLLNEVPTGF TVVGHIAHMN IREEYMPYRF LIGQVILDKN
     PLVETVVNKL DSIHAVYRTF DMEVLAGKEE FEVEQSESGC RFRFNFKAVY WNSRLHTEHA
     RLISQFNKGE AVCDVFAGVG PFAVPAGKKG VIVFANDLNP HSYESMVGNI KLNKVDRTVF
     PTNEDGREYI KKSSQMLVDF AAKNPVIEIP PKRVSRSKPE TSIPEKIPVP THFKHYVMNL
     PDSAIEFLDG FIGLYRDLSL RQAAFGTDTP TSQQMPIINV HCFHKHEPDE PEPEPAQIHE
     DLRARVSKNL SFQIALSELS FHKVRKVAPT KTMYCISFRL PLPVALA
//
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