TRMB_STRPN
ID TRMB_STRPN Reviewed; 211 AA.
AC P67506; Q8DQV7; Q97S62;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=SP_0550;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS).
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of the conserved methyltransferase from Streptococcus
RT pneumoniae TIGR4.";
RL Submitted (APR-2005) to the PDB data bank.
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}.
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DR EMBL; AE005672; AAK74707.1; -; Genomic_DNA.
DR PIR; B95064; B95064.
DR RefSeq; WP_001266083.1; NZ_AKVY01000001.1.
DR PDB; 1YZH; X-ray; 2.02 A; A/B=1-211.
DR PDBsum; 1YZH; -.
DR AlphaFoldDB; P67506; -.
DR SMR; P67506; -.
DR STRING; 170187.SP_0550; -.
DR EnsemblBacteria; AAK74707; AAK74707; SP_0550.
DR GeneID; 60233560; -.
DR GeneID; 66805716; -.
DR KEGG; spn:SP_0550; -.
DR eggNOG; COG0220; Bacteria.
DR OMA; WRGAKTA; -.
DR PhylomeDB; P67506; -.
DR BioCyc; SPNE170187:G1FZB-571-MON; -.
DR UniPathway; UPA00989; -.
DR EvolutionaryTrace; P67506; -.
DR Proteomes; UP000000585; 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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..211
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171403"
FT REGION 124..129
FT /note="Interaction with RNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT ACT_SITE 118
FT /evidence="ECO:0000250|UniProtKB:Q12009"
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 191..194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:1YZH"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1YZH"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:1YZH"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:1YZH"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:1YZH"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1YZH"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:1YZH"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:1YZH"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:1YZH"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:1YZH"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:1YZH"
SQ SEQUENCE 211 AA; 24379 MW; E6155B8C5E9C4485 CRC64;
MRVRNRKGAT ELLEANPQYV VLNPLEAKAK WRDLFGNDNP IHVEVGSGKG AFVSGMAKQN
PDINYIGIDI QKSVLSYALD KVLEVGVPNI KLLWVDGSDL TDYFEDGEID RLYLNFSDPW
PKKRHEKRRL TYKTFLDTFK RILPENGEIH FKTDNRGLFE YSLVSFSQYG MKLNGVWLDL
HASDFEGNVM TEYEQKFSNK GQVIYRVEAE F
