ID I4AK24_BERLS Unreviewed; 228 AA.
AC I4AK24;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 OrderedLocusNames=Fleli_1919 {ECO:0000313|EMBL:AFM04309.1};
OS Bernardetia litoralis (strain ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB
OS 1366 / Fx l1 / Sio-4) (Flexibacter litoralis).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Bernardetiaceae;
OC Bernardetia.
OX NCBI_TaxID=880071 {ECO:0000313|EMBL:AFM04309.1, ECO:0000313|Proteomes:UP000006054};
RN [1] {ECO:0000313|Proteomes:UP000006054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23117 / DSM 6794 / NBRC 15988 / NCIMB 1366 / Sio-4
RC {ECO:0000313|Proteomes:UP000006054};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Lang E., Kopitz M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Flexibacter litoralis DSM 6794.";
RL Submitted (JUN-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}.
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DR EMBL; CP003345; AFM04309.1; -; Genomic_DNA.
DR RefSeq; WP_014797760.1; NC_018018.1.
DR AlphaFoldDB; I4AK24; -.
DR STRING; 880071.Fleli_1919; -.
DR KEGG; fli:Fleli_1919; -.
DR PATRIC; fig|880071.3.peg.1902; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_10; -.
DR OrthoDB; 9807416at2; -.
DR Proteomes; UP000006054; 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 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:UP000006054};
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 228 AA; 25777 MW; B718949AE03FEE84 CRC64;
MRIDIITCLP QLIESFIGHS ILQRAQANNL VTLTLHDLKK YSQDKHGRID DYAFGGGAGM
VMTPVPLATC IEELLSENKY DEIIYMTPDG VTFNQSMANT YSLKENIMII CGHYKGIDER
IRQKYVTKEI SVGDFVVSGG EIPAALIADA IIRLVPRVMN DETSALTDSF QDDLLAPPVY
TRPANWEGME VPEILLSGHA AKIEDWRLQQ AMERTKKRRP DLWKKYSE
//