ID A0A2K4ZDN1_9FIRM Unreviewed; 489 AA.
AC A0A2K4ZDN1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|ARBA:ARBA00029736, ECO:0000256|HAMAP-Rule:MF_00605};
DE AltName: Full=tRNA [GM37] methyltransferase {ECO:0000256|ARBA:ARBA00033392, ECO:0000256|HAMAP-Rule:MF_00605};
GN Name=trmD {ECO:0000256|HAMAP-Rule:MF_00605,
GN ECO:0000313|EMBL:SOY28560.1};
GN ORFNames=AMURIS_01270 {ECO:0000313|EMBL:SOY28560.1};
OS Acetatifactor muris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetatifactor.
OX NCBI_TaxID=879566 {ECO:0000313|EMBL:SOY28560.1, ECO:0000313|Proteomes:UP000236311};
RN [1] {ECO:0000313|EMBL:SOY28560.1, ECO:0000313|Proteomes:UP000236311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP69 {ECO:0000313|EMBL:SOY28560.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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 -!- 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};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00605}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00605}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC {ECO:0000256|ARBA:ARBA00007630, ECO:0000256|HAMAP-Rule:MF_00605}.
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DR EMBL; OFSM01000005; SOY28560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4ZDN1; -.
DR OrthoDB; 9807416at2; -.
DR Proteomes; UP000236311; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; cd04301; NAT_SF; 1.
DR CDD; cd18080; TrmD-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 1.10.1270.20; tRNA(m1g37)methyltransferase, domain 2; 1.
DR HAMAP; MF_00605; TrmD; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR013653; FR47.
DR InterPro; IPR000182; GNAT_dom.
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; PF08445; FR47; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
DR PROSITE; PS51186; GNAT; 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:UP000236311};
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 357..489
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00605"
FT BINDING 131..136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00605"
SQ SEQUENCE 489 AA; 55466 MW; B2F3B249D1537B41 CRC64;
MRFHVLTLFP EMIEQGLGQG ILGKAAARQL FTLNVVNIRD YTQERHGKVD DYPYGGGAGM
LMQAQPVYDA FEAVTAGRKV RTIYVTPQGE PFTQRKAREL SEEEELLFLC GHYEGIDERV
LEEIVTDSIS IGDYVLTGGE LPAMVMIDAI ARLLPGVLGN DSSAEEESFH CDLLEYPQYS
RPEIWHGQKV PEVLLSGDHR KTAAWRLEQS VSRTAERRPD LYEKYRRKQE MIKRLSSEKR
NNIHMMESLA AGRGEILYAA DVGTSGEWDI LVYDGESRIC MMMAADGTAG KALAEKIPAD
ARWIVTSQPF MKEILERREF PDSGRTFPGD IKGKFHEISP CVQMLYTPRE TLSVRYREIR
RLTEKDIAYV CLHYPEREGG GEGYIRERIR SGALYGAFAG ERLIGFAGVH RGGSLGMLYV
EEARRRSGIG QSLEAYMVNR MLDRGRTPYL YVDERDAAMY RLQEKLGFYK AGKSFLWLKK
VLANSMALC
//
