ID W6ZAE2_COCMI Unreviewed; 473 AA.
AC W6ZAE2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ORFNames=COCMIDRAFT_23478 {ECO:0000313|EMBL:EUC48702.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC48702.1};
RN [1] {ECO:0000313|EMBL:EUC48702.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC48702.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KI963938; EUC48702.1; -; Genomic_DNA.
DR RefSeq; XP_007684699.1; XM_007686509.1.
DR AlphaFoldDB; W6ZAE2; -.
DR STRING; 930090.W6ZAE2; -.
DR GeneID; 19120442; -.
DR KEGG; bor:COCMIDRAFT_23478; -.
DR eggNOG; KOG2078; Eukaryota.
DR HOGENOM; CLU_022610_2_2_1; -.
DR OrthoDB; 276346at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
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 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 148..466
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 363
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
SQ SEQUENCE 473 AA; 53812 MW; 8B9BA6D13E69AC66 CRC64;
MSLQEATDDM FAPPVNRAMK VLDRSFFQKT IPTSAARIFN PKDISRCRKE LTAAKDTLPN
NRVDPIRADP DVDKAQKGVK CLLLRPEVIH TDRTTWSPKL RDLEQDGTLG VIPYQLHLDY
DYFTYSEITG AIIPPPESKH DDEIPQGFAL AGHVAHLNLR ERYWPYKYLI AAVLADKNPM
VKTVINKLDN VGTENAFRTF QYEVLYGPDD MNVELREQGC TFKFDFAKVY WNTRLHTEHE
RLCNLFKEGE AICDVMAGVG PFAIPSGKKK CFVWANDLNP ESYNSLVNNI KINKVGDFVR
PFNIDGGAFI RQASAHLLVL DPRHTIPIYP KTKFSRSNPQ ENKQPEPIKT LVRPRFFAHY
VMNLPASAIT FLPSFIGLYA NIPGLPAADI KKMLAPHTEQ KLPMIHVHCF STKSDDNVAE
IKGICEEISR QIEYEITPGM ADVYVHDVRD VAPKKRMFCA SFRLPEDVAF RDV
//
