TRMN_THET2
ID TRMN_THET2 Reviewed; 335 AA.
AC Q72IH5;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=tRNA (guanine(6)-N2)-methyltransferase {ECO:0000305};
DE EC=2.1.1.256 {ECO:0000269|PubMed:22337946, ECO:0000269|PubMed:22362751};
DE AltName: Full=tRNA:m2G6 methyltransferase {ECO:0000303|PubMed:22362751};
GN Name=trmN {ECO:0000303|PubMed:22337946};
GN OrderedLocusNames=TT_C1157 {ECO:0000312|EMBL:AAS81499.1};
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [2]
RP SUBUNIT, SUBCELLULAR LOCATION, AND CRYSTALLIZATION.
RX PubMed=22102250; DOI=10.1107/s1744309111036347;
RA Fislage M., Roovers M., Muennich S., Droogmans L., Versees W.;
RT "Crystallization and preliminary X-ray crystallographic analysis of
RT putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus
RT thermophilus.";
RL Acta Crystallogr. F 67:1432-1435(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=22337946; DOI=10.1261/rna.030411.111;
RA Roovers M., Oudjama Y., Fislage M., Bujnicki J.M., Versees W.,
RA Droogmans L.;
RT "The open reading frame TTC1157 of Thermus thermophilus HB27 encodes the
RT methyltransferase forming N2-methylguanosine at position 6 in tRNA.";
RL RNA 18:815-824(2012).
RN [4] {ECO:0007744|PDB:3TMA}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF HIS-263.
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=22362751; DOI=10.1093/nar/gks163;
RA Fislage M., Roovers M., Tuszynska I., Bujnicki J.M., Droogmans L.,
RA Versees W.;
RT "Crystal structures of the tRNA:m2G6 methyltransferase Trm14/TrmN from two
RT domains of life.";
RL Nucleic Acids Res. 40:5149-5161(2012).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC catalyzes the methylation of the guanosine nucleotide at position 6
CC (m2G6) in tRNA(Phe). {ECO:0000269|PubMed:22337946,
CC ECO:0000269|PubMed:22362751}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(6) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-
CC methylguanosine(6) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51116, Rhea:RHEA-COMP:12888, Rhea:RHEA-COMP:12889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.256;
CC Evidence={ECO:0000269|PubMed:22337946, ECO:0000269|PubMed:22362751};
CC -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:22102250,
CC ECO:0000269|PubMed:22337946, ECO:0000269|PubMed:22362751}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22102250}.
CC -!- DOMAIN: Consists of an N-terminal THUMP domain fused to a catalytic
CC Rossmann-fold MTase (RFM) domain. {ECO:0000269|PubMed:22362751}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the gene leads to a total absence
CC of m(2)G in tRNA but does not affect cell growth or the formation of
CC other modified nucleosides in tRNA(Phe). {ECO:0000269|PubMed:22337946}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE017221; AAS81499.1; -; Genomic_DNA.
DR RefSeq; WP_011173568.1; NC_005835.1.
DR PDB; 3TMA; X-ray; 2.05 A; A=1-335.
DR PDBsum; 3TMA; -.
DR AlphaFoldDB; Q72IH5; -.
DR SMR; Q72IH5; -.
DR STRING; 262724.TT_C1157; -.
DR EnsemblBacteria; AAS81499; AAS81499; TT_C1157.
DR KEGG; tth:TT_C1157; -.
DR eggNOG; COG0116; Bacteria.
DR HOGENOM; CLU_032119_0_0_0; -.
DR OMA; WFDSTKL; -.
DR BRENDA; 2.1.1.256; 2305.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR000241; RNA_methylase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004114; THUMP_dom.
DR Pfam; PF02926; THUMP; 1.
DR Pfam; PF01170; UPF0020; 1.
DR SMART; SM00981; THUMP; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..335
FT /note="tRNA (guanine(6)-N2)-methyltransferase"
FT /id="PRO_0000441406"
FT DOMAIN 47..150
FT /note="THUMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00529"
FT BINDING 195..197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 243..244
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT MUTAGEN 263
FT /note="H->A: 75% decrease in activity."
FT /evidence="ECO:0000269|PubMed:22362751"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3TMA"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 107..122
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 271..286
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:3TMA"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:3TMA"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:3TMA"
SQ SEQUENCE 335 AA; 36980 MW; 07967F4407A685C2 CRC64;
MWLEATTHPG LEDLLLEELS ALYPGEGAEV DARKGRVRIP RAWVGEEALG LRLAHHLVLF
RARLLLSRED PLGALERAAL ALPWPELEGA GSFRVEARRE GEHPFTSPEV ERRVGEALHR
AYGVPVDLKR PAVRVRVDVR GEEAFLGVQL TERPLSRRFP KAALRGSLTP VLAQALLRLA
DARPGMRVLD PFTGSGTIAL EAASTLGPTS PVYAGDLDEK RLGLAREAAL ASGLSWIRFL
RADARHLPRF FPEVDRILAN PPHGLRLGRK EGLFHLYWDF LRGALALLPP GGRVALLTLR
PALLKRALPP GFALRHARVV EQGGVYPRVF VLEKL
