TRM5_POLPP
ID TRM5_POLPP Reviewed; 426 AA.
AC D3BT31;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 35.
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};
GN Name=trmt5; ORFNames=PPL_11323;
OS Polysphondylium pallidum (strain ATCC 26659 / Pp 5 / PN500) (Heterostelium
OS pallidum).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC Acytosteliaceae; Heterostelium.
OX NCBI_TaxID=670386;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26659 / Pp 5 / PN500;
RX PubMed=21757610; DOI=10.1101/gr.121137.111;
RA Heidel A.J., Lawal H.M., Felder M., Schilde C., Helps N.R., Tunggal B.,
RA Rivero F., John U., Schleicher M., Eichinger L., Platzer M., Noegel A.A.,
RA Schaap P., Gloeckner G.;
RT "Phylogeny-wide analysis of social amoeba genomes highlights ancient
RT origins for complex intercellular communication.";
RL Genome Res. 21:1882-1891(2011).
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: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; ADBJ01000056; EFA75248.1; -; Genomic_DNA.
DR AlphaFoldDB; D3BT31; -.
DR SMR; D3BT31; -.
DR STRING; 670386.D3BT31; -.
DR InParanoid; D3BT31; -.
DR OMA; PKKQMFC; -.
DR OrthoDB; 788980at2759; -.
DR Proteomes; UP000001396; 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)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..426
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000414134"
FT REGION 374..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 242..243
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 269..270
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 292
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 426 AA; 48106 MW; 4C79BA888DAF1800 CRC64;
MSSLLLNKEI FSKSISIVGL KVNKTLLKTL AQEFKGYLLI RDRVKHIVDD SDSKDKKLVL
LSESIENGNV GAYGVNKQLP DNLQSFLKTH SIEVVKHQVQ LNYNNFSYEE VMKELIPTGL
PIPHAFEKIG HIAHLNLKEE LLPYKNMIGQ VILDKKGPQI RTVLNKVGKI DTVFRTFNFE
LLAGDNDLLA QVVYWNSRLQ FEHSNLIQTF KSHDIVVDMF AGVGPFAVPA SKLVKCKVYA
NDLNPNSVKY MRENATRNKA STIEISNLDA RDFVRELVSR DPPVAFTQAI MNLPSTSIEF
LDVFREIFLN PEKAPPIPAP TIHCYTFTPV SETAGGDLKE LTIKNVEAII KHPLPADTTV
YEVRDVSPNK RMMRISFKMP TLKKRKDTEN NDDQENNNNS SNNNNNNKID YNEAVSSGGE
GKKIKH
