TMG10_ARCFU
ID TMG10_ARCFU Reviewed; 320 AA.
AC O29011;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=tRNA (guanine(10)-N2)-dimethyltransferase;
DE EC=2.1.1.213;
DE AltName: Full=tRNA:G10 dimethyltransferase;
GN Name=trmG10; OrderedLocusNames=AF_1257;
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: Catalyzes the adenosylmethionine-dependent methylation of the
CC exocyclic amino group (N(2)) of guanosine at position 10 of various
CC tRNAs. Acts via a two-step process that leads to the formation of
CC either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G) (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(10) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(2)-dimethylguanosine(10) in tRNA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43124, Rhea:RHEA-COMP:10355, Rhea:RHEA-COMP:10358,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.213;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Trm-G10
CC family. {ECO:0000305}.
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DR EMBL; AE000782; AAB89985.1; -; Genomic_DNA.
DR PIR; H69406; H69406.
DR RefSeq; WP_010878752.1; NC_000917.1.
DR PDB; 6ZXV; X-ray; 1.88 A; A/B=1-320.
DR PDB; 6ZXW; X-ray; 2.19 A; G=1-320.
DR PDB; 6ZXY; X-ray; 2.75 A; B=1-320.
DR PDBsum; 6ZXV; -.
DR PDBsum; 6ZXW; -.
DR PDBsum; 6ZXY; -.
DR AlphaFoldDB; O29011; -.
DR SMR; O29011; -.
DR STRING; 224325.AF_1257; -.
DR PRIDE; O29011; -.
DR DNASU; 1484481; -.
DR EnsemblBacteria; AAB89985; AAB89985; AF_1257.
DR GeneID; 24794860; -.
DR KEGG; afu:AF_1257; -.
DR eggNOG; arCOG00047; Archaea.
DR HOGENOM; CLU_057819_1_0_2; -.
DR OMA; FFHPGVM; -.
DR OrthoDB; 47556at2157; -.
DR PhylomeDB; O29011; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; 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 InterPro; IPR005885; TrmG10.
DR Pfam; PF02926; THUMP; 1.
DR Pfam; PF01170; UPF0020; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01177; TIGR01177; 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;
KW tRNA-binding.
FT CHAIN 1..320
FT /note="tRNA (guanine(10)-N2)-dimethyltransferase"
FT /id="PRO_0000140478"
FT DOMAIN 46..136
FT /note="THUMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00529"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 53..65
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:6ZXW"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:6ZXV"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 276..288
FT /evidence="ECO:0007829|PDB:6ZXV"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 297..308
FT /evidence="ECO:0007829|PDB:6ZXV"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:6ZXV"
SQ SEQUENCE 320 AA; 36673 MW; A879F320AA8CD637 CRC64;
MKFLFYLSAD NLEIARKEVL VLAERYGWVE DYQFEERLLL LDYAGEKFFE RLAYTNEVTK
IYDICSVSEL EQVFSEIPVY DRLCCVRVKG GKGKTALERK LGALLWKRGA KVSVSNPEIV
YKVYIQDDKC YVGLLEFERD TRQFFLRRPD RRPFLMPSAI KPKLARALVN LTGVLEGETL
LDPMCGTGSF LIEAGLMGIN PIGIDFIEKI VRGCRVNLEY YGIEGSVLLG DAKNLPLRDE
SVRGIATDYP YLRSTKAAGT LDELYSKTSE EFERVLKKGG RAAIVTNIDV ESFFSNFEIE
MKTEERVHGS LTRRIYLLRR
