ID K1LRZ4_9FLAO Unreviewed; 224 AA.
AC K1LRZ4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=HMPREF9699_00075 {ECO:0000313|EMBL:EKB59710.1};
OS Bergeyella zoohelcum ATCC 43767.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Bergeyella.
OX NCBI_TaxID=883096 {ECO:0000313|EMBL:EKB59710.1, ECO:0000313|Proteomes:UP000006085};
RN [1] {ECO:0000313|EMBL:EKB59710.1, ECO:0000313|Proteomes:UP000006085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43767 {ECO:0000313|EMBL:EKB59710.1,
RC ECO:0000313|Proteomes:UP000006085};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bergeyella zoohelcum ATCC 43767.";
RL Submitted (JUL-2012) 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:EKB59710.1}.
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DR EMBL; AGYA01000003; EKB59710.1; -; Genomic_DNA.
DR RefSeq; WP_002661429.1; NZ_JH932293.1.
DR AlphaFoldDB; K1LRZ4; -.
DR STRING; 883096.HMPREF9699_00075; -.
DR PATRIC; fig|883096.3.peg.74; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_10; -.
DR OrthoDB; 9807416at2; -.
DR Proteomes; UP000006085; 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:UP000006085};
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..220
FT /note="tRNA methyltransferase TRMD/TRM10-type"
FT /evidence="ECO:0000259|Pfam:PF01746"
FT BINDING 112
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 132..137
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 224 AA; 25246 MW; 05B93A738DC10027 CRC64;
MRIDIISVLP ELMESPFQAS ILRRAVQKGL VEVHFHQLRD WSVGKHRQVD DEPYGGGAGM
VMMVEPLDKC ITELKSQRNY DEIIYLTPDG ITLSQKIANT LSIKENLLLV CGHYKGIDQR
VRDLHITMEI SIGDFVLTGG ELAACVLADS VIRLLPGVLN DEQSALTDSF QDNLLSPPIY
TRPEEYKGLK VPSILLSGNT PKIEEWRHSE ALRITEERRP DLLD
//
