TRM10_THEKO
ID TRM10_THEKO Reviewed; 370 AA.
AC Q5JD38;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=tRNA (guanine(9)-/adenine(9)-N1)-methyltransferase;
DE EC=2.1.1.218;
DE EC=2.1.1.221;
DE AltName: Full=tRNA(m1G9/m1A9)-methyltransferase;
DE Short=tRNA(m1G9/m1A9)MTase;
GN OrderedLocusNames=TK0422;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20525789; DOI=10.1093/nar/gkq451;
RA Kempenaers M., Roovers M., Oudjama Y., Tkaczuk K.L., Bujnicki J.M.,
RA Droogmans L.;
RT "New archaeal methyltransferases forming 1-methyladenosine or 1-
RT methyladenosine and 1-methylguanosine at position 9 of tRNA.";
RL Nucleic Acids Res. 38:6533-6543(2010).
CC -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of
CC either N(1)-methyladenine or N(1)-methylguanine at position 9 (m1A9 or
CC m1G9) in tRNA. {ECO:0000269|PubMed:20525789}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218;
CC Evidence={ECO:0000269|PubMed:20525789};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000269|PubMed:20525789};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
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DR EMBL; AP006878; BAD84611.1; -; Genomic_DNA.
DR RefSeq; WP_011249377.1; NC_006624.1.
DR PDB; 6EMS; X-ray; 2.00 A; A=1-344.
DR PDB; 6EMT; X-ray; 1.79 A; A=97-272.
DR PDB; 6EMU; X-ray; 2.30 A; A/B/C=97-272.
DR PDB; 6EMV; X-ray; 2.90 A; A/B/C=97-272.
DR PDBsum; 6EMS; -.
DR PDBsum; 6EMT; -.
DR PDBsum; 6EMU; -.
DR PDBsum; 6EMV; -.
DR AlphaFoldDB; Q5JD38; -.
DR SMR; Q5JD38; -.
DR STRING; 69014.TK0422; -.
DR EnsemblBacteria; BAD84611; BAD84611; TK0422.
DR GeneID; 3234336; -.
DR KEGG; tko:TK0422; -.
DR PATRIC; fig|69014.16.peg.414; -.
DR eggNOG; arCOG00967; Archaea.
DR HOGENOM; CLU_061952_0_0_2; -.
DR InParanoid; Q5JD38; -.
DR OMA; LNIRWED; -.
DR OrthoDB; 79589at2157; -.
DR PhylomeDB; Q5JD38; -.
DR BioCyc; MetaCyc:MON-16682; -.
DR BRENDA; 2.1.1.218; 5246.
DR BRENDA; 2.1.1.221; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR007364; RNA_MeTrfase_TK0422/Sfm1.
DR InterPro; IPR016742; tRNA_m1G_mtfrase_arc.
DR Pfam; PF04252; RNA_Me_trans; 1.
DR PIRSF; PIRSF018978; tRNA_m1G_mtfrase_arc_prd; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..370
FT /note="tRNA (guanine(9)-/adenine(9)-N1)-methyltransferase"
FT /id="PRO_0000407926"
FT DOMAIN 87..292
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:6EMS"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6EMS"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:6EMS"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6EMS"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6EMS"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:6EMS"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:6EMS"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6EMS"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:6EMS"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:6EMS"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:6EMS"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6EMT"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:6EMT"
FT HELIX 113..133
FT /evidence="ECO:0007829|PDB:6EMT"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:6EMT"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6EMT"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6EMT"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6EMS"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6EMT"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:6EMT"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:6EMT"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6EMT"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:6EMT"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:6EMT"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:6EMT"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:6EMT"
FT HELIX 247..258
FT /evidence="ECO:0007829|PDB:6EMT"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:6EMT"
SQ SEQUENCE 370 AA; 42996 MW; DC931EAC78571464 CRC64;
MKTLADVFRE ALKEKGISSI GTLSKRFRKS KNKLQDIAIE IVHGKGAVFR VPEKTAVAWD
LNGNRVDGSY YAYAPLCMRE KFEPVLTPEE LREKLPDWPY FIIDLYHWDK HTQKEKGKIC
LQVNQSYGLL RDYFTGSELA VTWANEEFRE MFHGPLDRIT TYGGPTSEFL KENGINEVVL
LDPWAEEVLS EKDFDVKAFI IGGIVDTGGN KKKTTPKIGE ELESAGIKVR RRKIVLRGDV
VGVPDRINRI LGIILKMMVE GKSMDEAVYE MQEPLHARWR LRKELPKRAT RYMVEGKVYR
VVEKELFDEY SKWLKIRWED FVKVLRELDL VALERKRIHH LNKISNARII NGKLHRVILL
KRAAMLCYNC
