TRM5_PLAKH
ID TRM5_PLAKH Reviewed; 698 AA.
AC B3L2G0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 ORFNames=PKH_071150;
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H;
RX PubMed=18843368; DOI=10.1038/nature07306;
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R.D., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M.A., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clark T.G., Galinski M.R., Hall N., Harper D., Harris D.,
RA Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S., Marti M.,
RA Moule S., Meyer I.M., Ormond D., Peters N., Sanders M., Sanders S.,
RA Sargeant T.J., Simmonds M., Smith F., Squares R., Thurston S., Tivey A.R.,
RA Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F.,
RA Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I.,
RA Barrell B.G., Berriman M.;
RT "The genome of the simian and human malaria parasite Plasmodium knowlesi.";
RL Nature 455:799-803(2008).
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; AM910989; CAQ39186.1; -; Genomic_DNA.
DR RefSeq; XP_002258414.1; XM_002258378.1.
DR AlphaFoldDB; B3L2G0; -.
DR SMR; B3L2G0; -.
DR STRING; 5850.PKH_071150; -.
DR EnsemblProtists; CAQ39186; CAQ39186; PKH_071150.
DR GeneID; 7320142; -.
DR KEGG; pkn:PKNH_0712200; -.
DR VEuPathDB; PlasmoDB:PKNH_0712200; -.
DR HOGENOM; CLU_395119_0_0_1; -.
DR InParanoid; B3L2G0; -.
DR OMA; GYDNMNT; -.
DR PhylomeDB; B3L2G0; -.
DR Proteomes; UP000031513; Chromosome 7.
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; -; 2.
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..698
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000414144"
FT REGION 233..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 432..433
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 459..460
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 603
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 698 AA; 80681 MW; 253859B1821CEC3E CRC64;
MFYGFLLLYP LLSLCLEHVI SLSKKGKPTL GFVIMRNAVD IKTLSDVKDR VKNEKRTHCL
VVNKYKVNDV LKNKEAKFYF LNVFRFPSVL KLREYEGNLM ETGQYNGEVL RFIHSYVERL
GGGGTHVGGK ADSKADGKVN HDVSDQVVAQ QTDQQMDQQM DQQTDQQMDQ QMDQKRDAAL
EDCRLIPLNA RFNKALQELM QREGKEIMEG LDMHLEEGDA GNVTVEGVAM EDDSTAHDSV
QRNEGKTPKG PLDGQWPPLE ELFRIIKKEG IQISIIQLQF GYDNMNTSEI LRKIFPTESE
VIHKYEMIGH IAHLNFCERF ENYKKVIAEI ILDKNKSIKT VINKMDTLKN LHRTFNIELL
AGEKNYLTTL KENDIKVKLN YELIYWNSKL KKERDRIYDL VENNSIIVDL FAGVGIFSLH
LSKKKCLCFS NDINSHAYNF MNVNIKLNKR KSILTYNLDA RAFVQMLLGL DIFSSDKTTL
SMQLSEQNWK NISLDFINSP DQNNVDTGKR KKRESDRVGH VDDDITANAT IDKKKKLRHA
DTNDPLEERP LGLAATHHGE ENIQSVERTN NDSEKTKEDA PRDVTHQVDI NLGIYGDIHV
LMNLPQTAFE FLDIFRELLD TYSTDQKDFQ GKCRRDQMRN VFIHCYFFSK PELFYEDAER
NIRMQLGGLP REMKITEIRK VSPSKLMYVA EFNLKDVF
