ID A0A1L7CTI5_9CORY Unreviewed; 417 AA.
AC A0A1L7CTI5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ORFNames=CFRA_07540 {ECO:0000313|EMBL:APT89137.1};
OS Corynebacterium frankenforstense DSM 45800.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1437875 {ECO:0000313|EMBL:APT89137.1, ECO:0000313|Proteomes:UP000185434};
RN [1] {ECO:0000313|EMBL:APT89137.1, ECO:0000313|Proteomes:UP000185434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST18 {ECO:0000313|EMBL:APT89137.1,
RC ECO:0000313|Proteomes:UP000185434};
RA Ruckert C., Albersmeier A., Winkler A., Lipski A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium frankenforstense ST18(T) (=DSM
RT 45800(T)), isolated from raw cow milk.";
RL Submitted (AUG-2014) 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; CP009247; APT89137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7CTI5; -.
DR STRING; 1437875.CFRA_07540; -.
DR KEGG; cfk:CFRA_07540; -.
DR OrthoDB; 9807416at2; -.
DR Proteomes; UP000185434; 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; 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 PANTHER; PTHR46417; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR46417:SF1; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 2.
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:UP000185434};
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 22..75
FT /note="tRNA methyltransferase TRMD/TRM10-type"
FT /evidence="ECO:0000259|Pfam:PF01746"
FT DOMAIN 112..256
FT /note="tRNA methyltransferase TRMD/TRM10-type"
FT /evidence="ECO:0000259|Pfam:PF01746"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00605"
FT BINDING 168..173
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00605"
SQ SEQUENCE 417 AA; 44960 MW; 0FC66B6C72621413 CRC64;
MRLDVITIFP DYLDPLRHAL LGKAIEQGRL SVGVHDLRDW APGVHQSVDD SPYGGGPGMV
MKPEVWGPAL DDVAAGRAGQ ELASAEPHRD AARHDELNGV APQAYPGENA DLPLLIVPTP
AGRPFTQADA RAWSAEDHIV FACGRYEGID QRVIDDAAAR YRVREVSIGD YVLIGGEVAA
LVIAEAVVRL IPGVLGNRRS HEEDSFSDGL LEGPCYTKPR SWRGLDVPEV LFSGDHARVD
RWHRERSLER TWRRRPELLD AVELTAADRD FLAGLAEADA EAAAPAEGDA SRAVHCSLQL
LIPPVEWPAI AEAMPDKLAA AGVTGAQVWA AETDFTCEPD NMLVTEYAQR EGHPPIAEVL
HRVTVTGTTG LELREVTRAV VAALPEGAYW YGSSYEGAAD PEAGDAGSAA CAWQAED
//
