ID W7TXC6_9STRA Unreviewed; 292 AA.
AC W7TXC6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=Naga_100004g165 {ECO:0000313|EMBL:EWM28158.1};
OS Nannochloropsis gaditana.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM28158.1, ECO:0000313|Proteomes:UP000019335};
RN [1] {ECO:0000313|EMBL:EWM28158.1, ECO:0000313|Proteomes:UP000019335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-31 {ECO:0000313|EMBL:EWM28158.1,
RC ECO:0000313|Proteomes:UP000019335};
RX PubMed=23966634; DOI=10.1093/mp/sst120;
RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT Nannochloropsis gaditana in Nitrogen Depletion.";
RL Mol. Plant 7:323-335(2014).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EWM28158.1}.
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DR EMBL; AZIL01000352; EWM28158.1; -; Genomic_DNA.
DR AlphaFoldDB; W7TXC6; -.
DR EnsemblProtists; EWM28158; EWM28158; Naga_100004g165.
DR OrthoDB; 116813at2759; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000019335; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
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; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23417:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03055};
KW Reference proteome {ECO:0000313|Proteomes:UP000019335};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03055}.
FT ACT_SITE 170
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 114..115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 147..148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 167
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 245..247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ SEQUENCE 292 AA; 33798 MW; E9669F309E1522FB CRC64;
MADILETHES RSGGSMKRPW VPPKFVQEAL GHLPLVEDGQ HPQKRFYRSR AHCNPLSHND
ACEYPPHPGK MNWSVLYPGL TDPVVRFLDV GCGFGGLTVA LSALFPDKII LALEIRAKVC
EFVRLRIEEM RKEASPRARN AAVLKTNAMK YLPHFFRKGQ LQKIFFCFPD PHFKTKNHRR
RIVSERLLTE YAYLLQEGGI LYAITDVEEL HQWHVAKLSE HLSFERVPEE TLAGDVTVTA
ITRETEESKK VERAGGRKYW CVFRRRPDAV VINASRRRWP VWSSDEEKHE EE
//
