TRM5_PEDHC
ID TRM5_PEDHC Reviewed; 463 AA.
AC E0VLV0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
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=PHUM294360;
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA;
RX PubMed=20566863; DOI=10.1073/pnas.1003379107;
RA Kirkness E.F., Haas B.J., Sun W., Braig H.R., Perotti M.A., Clark J.M.,
RA Lee S.H., Robertson H.M., Kennedy R.C., Elhaik E., Gerlach D.,
RA Kriventseva E.V., Elsik C.G., Graur D., Hill C.A., Veenstra J.A.,
RA Walenz B., Tubio J.M., Ribeiro J.M., Rozas J., Johnston J.S., Reese J.T.,
RA Popadic A., Tojo M., Raoult D., Reed D.L., Tomoyasu Y., Krause E.,
RA Mittapalli O., Margam V.M., Li H.M., Meyer J.M., Johnson R.M.,
RA Romero-Severson J., Vanzee J.P., Alvarez-Ponce D., Vieira F.G., Aguade M.,
RA Guirao-Rico S., Anzola J.M., Yoon K.S., Strycharz J.P., Unger M.F.,
RA Christley S., Lobo N.F., Seufferheld M.J., Wang N., Dasch G.A.,
RA Struchiner C.J., Madey G., Hannick L.I., Bidwell S., Joardar V., Caler E.,
RA Shao R., Barker S.C., Cameron S., Bruggner R.V., Regier A., Johnson J.,
RA Viswanathan L., Utterback T.R., Sutton G.G., Lawson D., Waterhouse R.M.,
RA Venter J.C., Strausberg R.L., Berenbaum M.R., Collins F.H., Zdobnov E.M.,
RA Pittendrigh B.R.;
RT "Genome sequences of the human body louse and its primary endosymbiont
RT provide insights into the permanent parasitic lifestyle.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12168-12173(2010).
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; DS235281; EEB14356.1; -; Genomic_DNA.
DR RefSeq; XP_002427094.1; XM_002427049.1.
DR AlphaFoldDB; E0VLV0; -.
DR SMR; E0VLV0; -.
DR STRING; 121225.PHUM294360-PA; -.
DR EnsemblMetazoa; PHUM294360-RA; PHUM294360-PA; PHUM294360.
DR GeneID; 8229727; -.
DR KEGG; phu:Phum_PHUM294360; -.
DR CTD; 8229727; -.
DR VEuPathDB; VectorBase:PHUM294360; -.
DR eggNOG; KOG2078; Eukaryota.
DR HOGENOM; CLU_022610_2_3_1; -.
DR InParanoid; E0VLV0; -.
DR OMA; PKKQMFC; -.
DR PhylomeDB; E0VLV0; -.
DR Proteomes; UP000009046; Unplaced.
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..463
FT /note="tRNA (guanine(37)-N1)-methyltransferase"
FT /id="PRO_0000414131"
FT BINDING 207
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 245..246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 274..275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT BINDING 305
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ SEQUENCE 463 AA; 54197 MW; D4282B842A07D7B7 CRC64;
MKVLDRSAFK KTINVYSIEI KPNQINNLNK CLKNYYFKNR RCKITEEKIS DNVKLFLNPA
LIKNFDDFSE NTKIELKNLG ITKDMFSNEI ITLDYDYWKL NEVLKAILPK DEPPLTSYSI
IGHIVHLNLK DHLIDYKYII AEVLKDKVSV AKTVVNKTNK IDNVYRNFEM EVLCGEPDFI
ASVIEYDTKF EFDFSKVYWN PRLSTEHNRI VNLVNHGDVL FDVFAGVGPF SIRAAKKNCL
VHANDLNPDS FKWLNHNINL NKKAKGWITT YNKDGSDFIL NDFKSNMLKI WSDSNFLGQI
HVVMNLPAKA LSFLKYFKGL FDEQDLKEIK KDHLEKHLPI IYCYFFAKKD ESLDEIFKTH
LEYKFDENEY EFNFVRNVSN GKNMHRVTFQ MPLSILMIDN SDISEPLPKR ISKSLKAKTK
AKEYTGNLKK IKETLNKNIS KIDSDFLKLQ NDISKKKEKP DDK
