ID A0A1R4AA99_BABMR Unreviewed; 403 AA.
AC A0A1R4AA99;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 homolog {ECO:0000256|HAMAP-Rule:MF_03152};
GN ORFNames=BMR1_02g01596 {ECO:0000313|EMBL:SJK85920.1};
OS Babesia microti (strain RI).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=1133968 {ECO:0000313|EMBL:SJK85920.1, ECO:0000313|Proteomes:UP000002899};
RN [1] {ECO:0000313|EMBL:SJK85920.1, ECO:0000313|Proteomes:UP000002899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RI {ECO:0000313|EMBL:SJK85920.1,
RC ECO:0000313|Proteomes:UP000002899};
RX PubMed=22833609; DOI=10.1093/nar/gks700;
RA Cornillot E., Hadj-Kaddour K., Dassouli A., Noel B., Ranwez V.,
RA Vacherie B., Augagneur Y., Bres V., Duclos A., Randazzo S., Carcy B.,
RA Debierre-Grockiego F., Delbecq S., Moubri-Menage K., Shams-Eldin H.,
RA Usmani-Brown S., Bringaud F., Wincker P., Vivares C.P., Schwarz R.T.,
RA Schetters T.P., Krause P.J., Gorenflot A., Berry V., Barbe V.,
RA Ben Mamoun C.;
RT "Sequencing of the smallest Apicomplexan genome from the human pathogen
RT Babesia microti.";
RL Nucleic Acids Res. 40:9102-9114(2012).
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; FO082872; SJK85920.1; -; Genomic_DNA.
DR RefSeq; XP_012648089.1; XM_012792635.1.
DR AlphaFoldDB; A0A1R4AA99; -.
DR GeneID; 24424106; -.
DR KEGG; bmic:BMR1_02g01596; -.
DR VEuPathDB; PiroplasmaDB:BMR1_02g01596; -.
DR OrthoDB; 276346at2759; -.
DR Proteomes; UP000002899; Chromosome II.
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 Reference proteome {ECO:0000313|Proteomes:UP000002899};
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 134..402
FT /note="SAM-dependent methyltransferase TRM5/TYW2-type"
FT /evidence="ECO:0000259|PROSITE:PS51684"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 261..262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 289..290
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
FT BINDING 325
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03152"
SQ SEQUENCE 403 AA; 46809 MW; 8A37E2E32A0B3D16 CRC64;
MSKYAVELPQ TSIFSGNSTI EQLEQYSNSV DAISLIIHHN ELIKLYKVND LQKYIINFPK
SKRMDKTRAP LMKIYFLPSI THDLSNWPKE AQKIIASVDH VIASDKLYYT YNDLSLSEAL
YLLAPNDNFQ SISFETIGHI AHLNLTENRI PIKHLIGKVI YDKNKHIKTV VNKVGKLNNT
FRTMELELIY GNKNYITTLT ENGIKFKVDY ENIYWNSRLE TERFRISQLL KPGDFVMDIF
AGLGAFAMYT ARKGCLTFAN DLNPIASQYI YENAQLNKVD HLIHSYNMDA REFINFILSN
KSILTYEINA KLNKGEPVTL HILMNLPEMA PEYLDSFHIL NQLPQVDVQF HTYLFCKNYE
DLSQIKEKAY QSLGFLPNAN FHEVRSVAPN KIMYCMEFSW QYS
//