TRMB_CAUVC
ID TRMB_CAUVC Reviewed; 226 AA.
AC P58088;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
GN Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057}; OrderedLocusNames=CC_0049;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01057};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01057}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_01057}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK22037.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005673; AAK22037.1; ALT_INIT; Genomic_DNA.
DR PIR; A87255; A87255.
DR RefSeq; NP_418869.1; NC_002696.2.
DR RefSeq; WP_012639863.1; NC_002696.2.
DR AlphaFoldDB; P58088; -.
DR SMR; P58088; -.
DR STRING; 190650.CC_0049; -.
DR PRIDE; P58088; -.
DR EnsemblBacteria; AAK22037; AAK22037; CC_0049.
DR KEGG; ccr:CC_0049; -.
DR PATRIC; fig|190650.5.peg.47; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_050910_0_3_5; -.
DR OMA; PDPWHKS; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; PTHR23417; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00091; TIGR00091; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..226
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171313"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..144
FT /note="Interaction with RNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT ACT_SITE 133
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 206..209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 226 AA; 25322 MW; 6575F723126A1032 CRC64;
MTTPQQPHGP LRSFGRLKSR PVKPRQQALL DTLLPEIAVP TGPFQPLDLM PEAKAVWLEI
GFGGGEHMAS QAGRNPETLV IGAEPFVNGV ASAVRHVEEQ ALKNVRIHEG DARDVVDWLP
DACLDRVFIM FPDPWHKARH NKRRLIQPEF VAKLARVMKP GAALRFATDW ADYAEWTTER
VLADPSFRFA DEAADRNAIP ADHVTTRYEE KKLGDCAPVF LDFTRG
