ID U4UMV3_DENPD Unreviewed; 857 AA.
AC U4UMV3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
GN ORFNames=D910_08821 {ECO:0000313|EMBL:ERL91491.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL91491.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL91491.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03055};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03055}.
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DR EMBL; KB632288; ERL91491.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UMV3; -.
DR STRING; 77166.U4UMV3; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000030742; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025763; Trm8_euk.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF235; CHITINASE-LIKE PROTEIN IDGF1-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03055};
KW Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03055}; S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03055};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03055};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03055};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03055}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..857
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004656264"
FT TRANSMEM 647..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 30..447
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT ACT_SITE 571
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 492
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 515..516
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 548..549
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 568
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ SEQUENCE 857 AA; 96487 MW; 206A70ED4EC7FE4A CRC64;
MIPVRILTVF ATLIVGSWGA VTTPSTPGGK VVVCNYETKS HLREGQGKFD LTFLEPALQY
CTHLLYGYAA INEESLKLVP LNEQFDVLKD NYRHVTDLKI RHPNLKVLLS VGGNEDVSGE
GSEKNLKYRQ VLETSAHRLA FINSAHTLVK GFGFDGIDLA WEFPETKPKK IKSGFGKFWS
SVKKTFAGET VVDENAQEHR DQFVALIREL KATFRPDNFL VSLTVLPNVN STVYYDPRGL
APSVDFVTLH AFDFYTAQRN PKLADFPAPL YDLIDRRQDE NIDAWVKYWL GQGFPAKKLI
VGIPTYGRTW KLDEDAKVDN VPIEGLDGAG EPGPQTKDAG ILSYPEICVR VQGGTGNVSP
SGYRKVPDST NKRGPYAYKP HDEEKGEDGV WIAYEDPQSA ASKATYVRNK GLGGIAVDDL
TLDDFRGVCN NNKYSILKAA VAALQRAHSN PMADHCFDYP TSPERMDWSK YYPEKFKPNE
EHNAKVEFVD IGCGYGGLLI TLSPMYPESL ILGMEIRVKV SDYVMDRIAA LRSQSPSQFQ
NIACLRSNAM KYLPNFFKKG QLKKMFFLYP DPHFKKAKHK WRIINKSLLA EYAYVLMEGG
IVYTVTDVKD LNEWMVQHFT EHPLFEPIQG DELQYSTSKM PSEYAEMIAA IAFGVLSAIF
VSAFVILIVI CRRQRLFFKS TYLDGAYETR PEKHLIEPER PELELGEVNF NFDNILSDGQ
WIDDATGLIP HCLAILKTCG YLTEQLTTLA TNSTPMSGNF SQIVDSAKRI SCRVDDMVKS
MYPPLDPKLL EARATALTLS VTLLALITKY ECGQKGKHNL HFIDKLLQKL DGHVSFLRDA
SLYQEHINKF PMHTNSV
//
