ID Q9RSB4_DEIRA Unreviewed; 230 AA.
AC Q9RSB4;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=tRNA (guanosine(18)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060};
DE EC=2.1.1.34 {ECO:0000256|HAMAP-Rule:MF_02060};
DE AltName: Full=tRNA [Gm18] methyltransferase {ECO:0000256|HAMAP-Rule:MF_02060};
GN Name=trmH {ECO:0000256|HAMAP-Rule:MF_02060};
GN OrderedLocusNames=DR_2211 {ECO:0000313|EMBL:AAF11758.1};
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF11758.1, ECO:0000313|Proteomes:UP000002524};
RN [1] {ECO:0000313|EMBL:AAF11758.1, ECO:0000313|Proteomes:UP000002524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
CC -!- FUNCTION: Catalyzes the 2'-O methylation of guanosine at position 18 in
CC tRNA. {ECO:0000256|HAMAP-Rule:MF_02060}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:20077, Rhea:RHEA-COMP:10190, Rhea:RHEA-COMP:10192,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.34;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02060};
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000256|HAMAP-
CC Rule:MF_02060}.
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DR EMBL; AE000513; AAF11758.1; -; Genomic_DNA.
DR PIR; C75301; C75301.
DR RefSeq; NP_295933.1; NC_001263.1.
DR RefSeq; WP_010888841.1; NZ_JMLF01000004.1.
DR AlphaFoldDB; Q9RSB4; -.
DR STRING; 243230.DR_2211; -.
DR PaxDb; 243230-DR_2211; -.
DR EnsemblBacteria; AAF11758; AAF11758; DR_2211.
DR GeneID; 69518460; -.
DR KEGG; dra:DR_2211; -.
DR PATRIC; fig|243230.17.peg.2438; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_4_2_0; -.
DR InParanoid; Q9RSB4; -.
DR OrthoDB; 9794400at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0141100; F:tRNA (guanine(18)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002938; P:tRNA guanine ribose methylation; IBA:GO_Central.
DR CDD; cd18092; SpoU-like_TrmH; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_02060; tRNA_methyltr_TrmH; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR022724; rRNA_MeTrfase_SpoU_C.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR033671; TrmH.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR43453; RRNA METHYLASE-LIKE; 1.
DR PANTHER; PTHR43453:SF1; SPOU_METHYLASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12105; SpoU_methylas_C; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_02060}; Reference proteome {ECO:0000313|Proteomes:UP000002524};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_02060};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_02060};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02060};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_02060};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_02060}.
FT DOMAIN 22..166
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
FT DOMAIN 171..223
FT /note="RNA methyltransferase SpoU/TrmH type C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12105"
FT BINDING 104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT BINDING 127..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02060"
SQ SEQUENCE 230 AA; 25348 MW; D6EBECD303D56A92 CRC64;
MAPTPERYAK IRRVLSKRQP TLTVLMDEVN KPHNLSAIIR TCDAVGVPEA HAVPPKHGTL
ASFEGHTYEA TSGSAHKWVK VHPHADAVSA VRELQAQGFQ VLATHLSQRS VDYREPDYTK
PTCVLLGAEK WGVSDEAAEA ADANIVIPMF GMVQSLNVSV AAATILFEAQ RQRLAAGMYE
EPQLSPEELH RLSFEWGYPD LAPGYRERGE AYPALGEEGE LLREPVSRPE
//
