TRM52_PHATC
ID TRM52_PHATC Reviewed; 587 AA.
AC B7G5J1;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03152};
DE EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=M1G-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA [GM37] methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_03152};
DE AltName: Full=tRNA methyltransferase 5 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03152};
GN ORFNames=PHATRDRAFT_47967;
OS Phaeodactylum tricornutum (strain CCAP 1055/1).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC Phaeodactylum.
OX NCBI_TaxID=556484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCAP 1055/1;
RX PubMed=18923393; DOI=10.1038/nature07410;
RA Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA Grigoriev I.V.;
RT "The Phaeodactylum genome reveals the evolutionary history of diatom
RT genomes.";
RL Nature 456:239-244(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=CCAP 1055/1;
RG Diatom Consortium;
RA Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA Rokhsar D., Bowler C.;
RL Submitted (AUG-2008) 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: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; CM000617; EEC46325.1; -; Genomic_DNA.
DR RefSeq; XP_002182424.1; XM_002182388.1.
DR AlphaFoldDB; B7G5J1; -.
DR SMR; B7G5J1; -.
DR STRING; 556484.B7G5J1; -.
DR GeneID; 7203207; -.
DR KEGG; pti:PHATRDRAFT_47967; -.
DR eggNOG; KOG2078; Eukaryota.
DR HOGENOM; CLU_022610_2_3_1; -.
DR InParanoid; B7G5J1; -.
DR OrthoDB; 788980at2759; -.
DR Proteomes; UP000000759; Chromosome 15.
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..587
FT /note="tRNA (guanine(37)-N1)-methyltransferase 2"
FT /id="PRO_0000414154"
FT REGION 446..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 360
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 430..431
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 478
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 587 AA; 66387 MW; 0506CF5F3A44CCF5 CRC64;
MTTRVTGNER RGRQLLLRFS GFLSAALTVM ALITATRALA PVVAYIAPQR VRSHFMRRAF
ASGNCRSRRF SVLRSTVGTE TRNENNITTP YHSPLPTSRY VYQSSRTLSS RNPALPLEST
LMHSNANELT DVELKNLVAH WRDHPVLNPM VTFRSWVVPI KGKMIQAILN SKSLQPYLAS
RHELLQEMHV RLKIVRDYTD STDGTEKLIL LHPDTPPLSE LPADVQQLLR NCQIHENGPV
MPTKFTYKDF TASYILSQLL PIAVHPPPTA FETIGHVAHL NLKERHWPYR FLIGQVLLET
LPLIESVINK VGEVSGPYRT YDFGLLAGRN DTRVKLTESG VQLQFDLADV YWCSRLSEER
QRLLRTFQPG QIIADPFCGV GALCLLAASL PQRNCTIWAN DWNPKAVEYL RENARRNHVS
DRIERLQCGD AYDFLMDMGL QQHQKASTRS RKEDVTNKDG NHVTPTEPMR LPDHVVMNYP
VEAPKFLGAL RWWPVPPSSR RGSTTRDGGI GSVIVPRVHV YTFARADPTT DRDAEEVAVD
LVAANLLPLG NTIHCRTEMN EDYDCDIQVH PVRDVAPGKV VLCGDFR
