ID M4X211_9PSED Unreviewed; 247 AA.
AC M4X211;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:AGI25601.1};
GN ORFNames=H681_18670 {ECO:0000313|EMBL:AGI25601.1};
OS Pseudomonas sp. ATCC 13867.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1294143 {ECO:0000313|EMBL:AGI25601.1, ECO:0000313|Proteomes:UP000012082};
RN [1] {ECO:0000313|EMBL:AGI25601.1, ECO:0000313|Proteomes:UP000012082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13867 {ECO:0000313|EMBL:AGI25601.1,
RC ECO:0000313|Proteomes:UP000012082};
RX PubMed=23723394;
RA Ainala S.K., Somasundar A., Park S.;
RT "Complete genome sequence of Pseudomonas denitrificans ATCC 13867.";
RL Genome Announc. 1:E00257-E00213(2013).
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; CP004143; AGI25601.1; -; Genomic_DNA.
DR RefSeq; WP_015478453.1; NC_020829.1.
DR AlphaFoldDB; M4X211; -.
DR STRING; 1294143.H681_18670; -.
DR KEGG; pdr:H681_18670; -.
DR PATRIC; fig|1294143.3.peg.3791; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_6; -.
DR OrthoDB; 9807416at2; -.
DR Proteomes; UP000012082; Chromosome.
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; IPR000953; Chromo/chromo_shadow_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; PF01746; tRNA_m1G_MT; 1.
DR PIRSF; PIRSF000386; tRNA_mtase; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
DR PROSITE; PS50013; CHROMO_2; 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};
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 BINDING 113
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 133..138
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 247 AA; 27885 MW; B899FAAB350FB532 CRC64;
MWIGVISIFP EMFRAISDYG ITSRAVKQEL IRLQCFNPRS NTEDRHQTVD DRPFGGGPGM
VMKIKPLEGA LGDARQAAGG PAKVIYLSPQ GRKLTQAAVK ELANEERLIL IAGRYEGIDE
RFIEEHVDEE WSVGDYVLSG GELPAMVLID AVTRLLPGAL GHVDSAEEDS FTDGLLDCPH
YTRPEVYADK RVPEVLLSGN HEHIRRWRLQ QSLGRTWERR ADLLDCRSLS GEEKKLLEEY
IRQRNDS
//