ID Q5JID5_THEKO Unreviewed; 331 AA.
AC Q5JID5;
DT 15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=N2, N2-dimethylguanosine tRNA methyltransferase {ECO:0000313|EMBL:BAD85170.1};
GN OrderedLocusNames=TK0981 {ECO:0000313|EMBL:BAD85170.1};
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 {ECO:0000313|EMBL:BAD85170.1, ECO:0000313|Proteomes:UP000000536};
RN [1] {ECO:0000313|EMBL:BAD85170.1, ECO:0000313|Proteomes:UP000000536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1
RC {ECO:0000313|Proteomes:UP000000536};
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] {ECO:0007829|PDB:5E71, ECO:0007829|PDB:5E72}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=27325738; DOI=10.1093/nar/gkw561;
RA Hirata A., Nishiyama S., Tamura T., Yamauchi A., Hori H.;
RT "Structural and functional analyses of the archaeal tRNA m2G/m22G10
RT methyltransferase aTrm11 provide mechanistic insights into site specificity
RT of a tRNA methyltransferase that contains common RNA-binding modules.";
RL Nucleic Acids Res. 44:6377-6390(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AP006878; BAD85170.1; -; Genomic_DNA.
DR RefSeq; WP_011249932.1; NC_006624.1.
DR PDB; 5E71; X-ray; 1.70 A; A=1-331.
DR PDB; 5E72; X-ray; 1.74 A; A=1-331.
DR PDBsum; 5E71; -.
DR PDBsum; 5E72; -.
DR AlphaFoldDB; Q5JID5; -.
DR SMR; Q5JID5; -.
DR IntAct; Q5JID5; 1.
DR MINT; Q5JID5; -.
DR STRING; 69014.TK0981; -.
DR EnsemblBacteria; BAD85170; BAD85170; TK0981.
DR GeneID; 78447494; -.
DR KEGG; tko:TK0981; -.
DR PATRIC; fig|69014.16.peg.959; -.
DR eggNOG; arCOG00047; Archaea.
DR HOGENOM; CLU_057819_1_0_2; -.
DR InParanoid; Q5JID5; -.
DR OrthoDB; 7080at2157; -.
DR PhylomeDB; Q5JID5; -.
DR BRENDA; 2.1.1.214; 5246.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0016423; F:tRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd11715; THUMP_AdoMetMT; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR000241; RlmKL-like_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004114; THUMP_dom.
DR InterPro; IPR005885; TrmG10.
DR NCBIfam; TIGR01177; TIGR01177 family methyltransferase; 1.
DR PANTHER; PTHR14911; THUMP DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14911:SF13; TRNA (GUANINE(6)-N2)-METHYLTRANSFERASE THUMP3; 1.
DR Pfam; PF02926; THUMP; 1.
DR Pfam; PF01170; UPF0020; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SMART; SM00981; THUMP; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF143437; THUMP domain-like; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5E71, ECO:0007829|PDB:5E72};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:BAD85170.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000536};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00529};
KW S-adenosyl-L-methionine {ECO:0007829|PDB:5E72};
KW Transferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000313|EMBL:BAD85170.1}.
FT DOMAIN 42..143
FT /note="THUMP"
FT /evidence="ECO:0000259|PROSITE:PS51165"
FT BINDING 193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007829|PDB:5E72"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007829|PDB:5E72"
FT BINDING 235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007829|PDB:5E72"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007829|PDB:5E72"
FT DISULFID 96..131
FT /evidence="ECO:0007829|PDB:5E71, ECO:0007829|PDB:5E72"
SQ SEQUENCE 331 AA; 37443 MW; 5DB6BEFFE57CC9C0 CRC64;
MLYVEILGNL PEMARDEVKA MLELGGGEII GQDYLFLKVD AGEKAFPFLD RLGLAHEYGL
LLVEADSVEE LLQKAGEVEW PIKGAFKVDT ETMANCRHDV LDLPRKLGAV IHAQGFRVNL
SKPDTVVRVY CGERLYAGIR LRYFDPKDFE KRKAHHRPFF RPISLHPRVS RALVNLTKAT
REILDPFMGA GGILIEAGLL GLRVYGVDIR PEMVEGAETN LKHYGVRDYT LKLGDATRLE
DLFPDKKFEA VATDPPYGTA ATLAGRKRDE LYRKALRSIY NVLEDGGRLA IAFPTDFNGK
AEAEAVGFRT LGRYYQRVHK SLERYFYVFE K
//
