TRMB_AQUAE
ID TRMB_AQUAE Reviewed; 297 AA.
AC O66479;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=aq_065;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP PROTEIN SEQUENCE OF 204-214, AND ROLE OF C-TERMINAL REGION.
RX PubMed=17150909; DOI=10.1093/nass/nrl122;
RA Tomikawa C., Hori H.;
RT "The core domain of Aquifex aeolicus tRNA (m7G46) methyltransferase has the
RT methyl-transfer activity to tRNA.";
RL Nucleic Acids Symp. Ser. 50:245-246(2006).
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 -!- DOMAIN: The C-terminal region is probably involved in protein
CC stability.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_01057}.
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DR EMBL; AE000657; AAC06452.1; -; Genomic_DNA.
DR PIR; D70306; D70306.
DR RefSeq; NP_213039.1; NC_000918.1.
DR RefSeq; WP_010879977.1; NC_000918.1.
DR AlphaFoldDB; O66479; -.
DR SMR; O66479; -.
DR STRING; 224324.aq_065; -.
DR PRIDE; O66479; -.
DR EnsemblBacteria; AAC06452; AAC06452; aq_065.
DR KEGG; aae:aq_065; -.
DR PATRIC; fig|224324.8.peg.56; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_077150_0_0_0; -.
DR InParanoid; O66479; -.
DR OMA; PWPKAGH; -.
DR OrthoDB; 1025521at2; -.
DR BRENDA; 2.1.1.33; 396.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..297
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171286"
FT ACT_SITE 97
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 47
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 165..168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 297 AA; 35639 MW; 8CF24B95B3FD1599 CRC64;
MLCYVNYKRV KRPVEIPNLE VEIGFGRGDF IVKLAKENPD KNFFGIEISQ ISIEKLMKRV
GKKGLKNVYC TNVDAYWGFY FLFRDNYVEN IYMNYPDPWF KKRHHKRRLT KPERLYMFAK
KLKLGGEIRI RTDNYEFLEF TKESAKVLDC FEVEEGTLNV KEPLTKYEQK WLSMGKTLYK
LILRKVKEPK FVEHPEVEEV RELFPVKVKV ESVDPKKIES REIKLDEEVY FKTFKVWQRD
KDFLVECLLS EKGYLQKFFI QIKRKEDGYV IDVSPYSEVL RTRNLQRSIQ TVAQLLS
