TRM14_ARCFU
ID TRM14_ARCFU Reviewed; 392 AA.
AC O28105;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=tRNA (guanine(6)-N2)-methyltransferase {ECO:0000250|UniProtKB:Q57880};
DE EC=2.1.1.256 {ECO:0000250|UniProtKB:Q57880};
DE AltName: Full=tRNA m2G6-methyltransferase {ECO:0000250|UniProtKB:Q57880};
GN Name=trm14 {ECO:0000250|UniProtKB:Q57880}; OrderedLocusNames=AF_2178;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC catalyzes the methylation of the guanosine nucleotide at position 6
CC (m2G6) in tRNA. {ECO:0000250|UniProtKB:Q57880}.
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:0000250|UniProtKB:Q57880};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; AE000782; AAB89073.1; -; Genomic_DNA.
DR PIR; B69522; B69522.
DR AlphaFoldDB; O28105; -.
DR SMR; O28105; -.
DR STRING; 224325.AF_2178; -.
DR DNASU; 1485406; -.
DR EnsemblBacteria; AAB89073; AAB89073; AF_2178.
DR KEGG; afu:AF_2178; -.
DR eggNOG; arCOG00048; Archaea.
DR HOGENOM; CLU_032119_0_0_2; -.
DR OMA; GFMYKAN; -.
DR PhylomeDB; O28105; -.
DR Proteomes; UP000002199; 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:0001510; P:RNA methylation; IEA:UniProt.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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; PS00092; N6_MTASE; 1.
DR PROSITE; PS51165; THUMP; 1.
DR PROSITE; PS01261; UPF0020; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..392
FT /note="tRNA (guanine(6)-N2)-methyltransferase"
FT /id="PRO_0000140479"
FT DOMAIN 73..183
FT /note="THUMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00529"
FT BINDING 199..203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 230..232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 275
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 303..304
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 317
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
SQ SEQUENCE 392 AA; 44374 MW; E960BF20A696AA6E CRC64;
MKRVQNLLVA VGLSPNYHRR TYPSGKKSLV VRFYATLTPG LEDVAAKEVE SFGCKVEEIR
ERRGRIFFSG EKSAIPLLNH FSRTLERLNV LLLRCEVEGL DDIYAAVKGL DFSFVKGKSF
AIRSLRVGEH DFTSMDIARV AGQAVIDSFM ESYGERLKVN LNQPDVIIRV ELVDSELFVG
VDTTGDDAMH KRWWRVYNHP AHLNAAIACG MLRIADWKVD ESLIDPMCGS GTIPIEAALM
VRNVPNLRDF AYKKLCEWEL AFEPNEVRLK LYGMEKFRKH LVGAIRNAVN AGVADTIEFR
QGDATEMTGE YDVIITNPPY GLRIHRKGAI ERLYHSFARA AKRCMNQNSR LVIITAEHRV
FANAAEEAGL QCTHERFVKY GGLLTKIMVF MI
