ID H1D1D8_9FIRM Unreviewed; 248 AA.
AC H1D1D8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000256|ARBA:ARBA00014679, ECO:0000256|HAMAP-Rule:MF_00605};
DE EC=2.1.1.228 {ECO:0000256|ARBA:ARBA00012807, ECO:0000256|HAMAP-Rule:MF_00605};
DE AltName: Full=M1G-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00605};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|HAMAP-Rule:MF_00605};
GN Name=trmD {ECO:0000256|HAMAP-Rule:MF_00605};
GN ORFNames=HMPREF9453_01426 {ECO:0000313|EMBL:EHO62645.1};
OS Dialister succinatiphilus YIT 11850.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Dialister.
OX NCBI_TaxID=742743 {ECO:0000313|EMBL:EHO62645.1, ECO:0000313|Proteomes:UP000003277};
RN [1] {ECO:0000313|EMBL:EHO62645.1, ECO:0000313|Proteomes:UP000003277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11850 {ECO:0000313|EMBL:EHO62645.1,
RC ECO:0000313|Proteomes:UP000003277};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Dunbar C., Gearin G.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Lui A.,
RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dialister succinatiphilus YIT 11850.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC {ECO:0000256|ARBA:ARBA00002634, ECO:0000256|HAMAP-Rule:MF_00605,
CC ECO:0000256|RuleBase:RU003464}.
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|ARBA:ARBA00001189, ECO:0000256|HAMAP-
CC Rule:MF_00605, ECO:0000256|RuleBase:RU003464};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00605, ECO:0000256|RuleBase:RU003464}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00605, ECO:0000256|RuleBase:RU003464}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC {ECO:0000256|ARBA:ARBA00007630, ECO:0000256|HAMAP-Rule:MF_00605,
CC ECO:0000256|RuleBase:RU003464}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHO62645.1}.
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DR EMBL; ADLT01000048; EHO62645.1; -; Genomic_DNA.
DR RefSeq; WP_008859920.1; NZ_JH591188.1.
DR AlphaFoldDB; H1D1D8; -.
DR STRING; 742743.HMPREF9453_01426; -.
DR PATRIC; fig|742743.3.peg.1450; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_9; -.
DR OrthoDB; 9807416at2; -.
DR Proteomes; UP000003277; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052906; F:tRNA (guanine(37)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR CDD; cd18080; TrmD-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR Gene3D; 1.10.1270.20; tRNA(m1g37)methyltransferase, domain 2; 1.
DR HAMAP; MF_00605; TrmD; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR InterPro; IPR002649; tRNA_m1G_MeTrfase_TrmD.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR NCBIfam; TIGR00088; trmD; 1.
DR PANTHER; PTHR46417; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR46417:SF1; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PIRSF; PIRSF000386; tRNA_mtase; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00605};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00605}; Reference proteome {ECO:0000313|Proteomes:UP000003277};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00605};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00605};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_00605}.
FT DOMAIN 23..222
FT /note="tRNA methyltransferase TRMD/TRM10-type"
FT /evidence="ECO:0000259|Pfam:PF01746"
FT BINDING 114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00605,
FT ECO:0000256|PIRSR:PIRSR000386-1"
FT BINDING 134..139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00605,
FT ECO:0000256|PIRSR:PIRSR000386-1"
SQ SEQUENCE 248 AA; 28010 MW; 22F05B04271C6853 CRC64;
MKIDILSLFP EFVEAFFHQS MIKRALEAGL IEMAVTNPRD FTKSRHRQVD DTIYGGGAGM
LMMCQPLFDA CHHVLPEKGP RDRVIFLSPA GKTFNQDKAK ELQRDYDHLV LICGHYEGVD
HRVEEHLADE LISIGDYVLT GGELGAMVIS DAVARMVPGV LGDAGSAASD SFYEPILEYP
QYTKPAEYNG WKVPDVLLSG HHANIARWRR KEALRRTMAY RPDLLEGQEL SKEDRKLMAE
IKEELIHS
//
