TRM14_PYRFU
ID TRM14_PYRFU Reviewed; 365 AA.
AC Q8U248;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=trm14 {ECO:0000303|PubMed:22337946};
GN OrderedLocusNames=PF1002 {ECO:0000312|EMBL:AAL81126.1};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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, AND CATALYTIC ACTIVITY.
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:3TLJ, ECO:0007744|PDB:3TM4, ECO:0007744|PDB:3TM5}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH
RP S-ADENOSYL-L-METHIONINE; S-ADENOSYL-HOMOCYSTEINE AND INHIBITOR SINEFUNGIN,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DOMAIN.
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: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 -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE009950; AAL81126.1; -; Genomic_DNA.
DR RefSeq; WP_011012139.1; NZ_CP023154.1.
DR PDB; 3TLJ; X-ray; 2.20 A; A/B=1-365.
DR PDB; 3TM4; X-ray; 1.95 A; A/B=1-365.
DR PDB; 3TM5; X-ray; 2.27 A; A/B=1-365.
DR PDBsum; 3TLJ; -.
DR PDBsum; 3TM4; -.
DR PDBsum; 3TM5; -.
DR AlphaFoldDB; Q8U248; -.
DR SMR; Q8U248; -.
DR STRING; 186497.PF1002; -.
DR EnsemblBacteria; AAL81126; AAL81126; PF1002.
DR GeneID; 41712814; -.
DR KEGG; pfu:PF1002; -.
DR PATRIC; fig|186497.12.peg.1061; -.
DR eggNOG; arCOG00048; Archaea.
DR HOGENOM; CLU_032119_0_0_2; -.
DR OMA; GFMYKAN; -.
DR OrthoDB; 47556at2157; -.
DR PhylomeDB; Q8U248; -.
DR BRENDA; 2.1.1.256; 5243.
DR Proteomes; UP000001013; 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:0006400; P:tRNA modification; IEA:UniProt.
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.
DR PROSITE; PS01261; UPF0020; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..365
FT /note="tRNA (guanine(6)-N2)-methyltransferase"
FT /id="PRO_0000441405"
FT DOMAIN 69..182
FT /note="THUMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00529"
FT BINDING 198..202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22362751,
FT ECO:0007744|PDB:3TM4"
FT BINDING 228..230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22362751,
FT ECO:0007744|PDB:3TM4"
FT BINDING 248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22362751,
FT ECO:0007744|PDB:3TM4"
FT BINDING 276..277
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22362751,
FT ECO:0007744|PDB:3TM4"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:22362751,
FT ECO:0007744|PDB:3TM4"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:3TM4"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:3TM4"
FT TURN 88..92
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 119..130
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 306..320
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 321..330
FT /evidence="ECO:0007829|PDB:3TM4"
FT HELIX 332..341
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 344..354
FT /evidence="ECO:0007829|PDB:3TM4"
FT STRAND 357..365
FT /evidence="ECO:0007829|PDB:3TM4"
SQ SEQUENCE 365 AA; 41000 MW; A35C4FAC96E0F975 CRC64;
MKFLLTTAQG IEDIAKREVS LLLKKLGISF QIEEKPLGIE GRLLLEAEKA YYVDEKGRKR
ELSISTYLNE NSRLLHRVII EIASEKFNGI EKDESEEALK RIKDFVSSLP VEQFVKVSET
FAVRSFRKGD HNITSIDIAR TVGEAIFERL SRFGTPLVNL DHPAVIFRAE LIKDVFFLGI
DTTGDSSLHK RPWRVYDHPA HLKASIANAM IELAELDGGS VLDPMCGSGT ILIELALRRY
SGEIIGIEKY RKHLIGAEMN ALAAGVLDKI KFIQGDATQL SQYVDSVDFA ISNLPYGLKI
GKKSMIPDLY MKFFNELAKV LEKRGVFITT EKKAIEEAIA ENGFEIIHHR VIGHGGLMVH
LYVVK
