ID A0A4Y9YQI0_9APHY Unreviewed; 591 AA.
AC A0A4Y9YQI0;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|ARBA:ARBA00039099, ECO:0000256|PROSITE-ProRule:PRU00958};
DE EC=2.1.1.216 {ECO:0000256|ARBA:ARBA00039099, ECO:0000256|PROSITE-ProRule:PRU00958};
GN ORFNames=EVJ58_g2891 {ECO:0000313|EMBL:TFY64033.1};
OS Rhodofomes roseus.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Rhodofomes.
OX NCBI_TaxID=34475 {ECO:0000313|EMBL:TFY64033.1, ECO:0000313|Proteomes:UP000298390};
RN [1] {ECO:0000313|EMBL:TFY64033.1, ECO:0000313|Proteomes:UP000298390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105464 {ECO:0000313|EMBL:TFY64033.1,
RC ECO:0000313|Proteomes:UP000298390};
RA Buettner E., Kellner H.;
RT "Genome sequencing of the rare red list fungi Fomitopsis rosea.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00958};
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}.
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:TFY64033.1}.
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DR EMBL; SEKV01000112; TFY64033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9YQI0; -.
DR STRING; 34475.A0A4Y9YQI0; -.
DR Proteomes; UP000298390; Unassembled WGS sequence.
DR GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0160104; F:tRNA (guanine(26)-N2)-dimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR Gene3D; 3.30.56.70; N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10631:SF3; TRNA (GUANINE(26)-N(2))-DIMETHYLTRANSFERASE; 1.
DR Pfam; PF02005; TRM; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; Reference proteome {ECO:0000313|Proteomes:UP000298390};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00958};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU00958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00958}; tRNA processing {ECO:0000256|PROSITE-ProRule:PRU00958};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW ProRule:PRU00958}.
FT REGION 63..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 64671 MW; 35083816DE7EC2D2 CRC64;
MATASEPEQI TIPEGYTLHT ENTTRILLPP GNQAFLNPVQ EFNRDLSVAC IRTWSELLNE
EKEAKWRQTQ ERRAKKAERG PKAKRVKTEE GAAAVAPAAG SAQEAAGEGS VKLEDTAPAT
AEPVAGPSTK KQPEYQPYRS VILEALSATG LRSIRYAKEI PLVKYAANDL SPSAVEAMKR
NVELNGLAAP EPTKSETPGK RENGPAKPQL GRVRVNQSDA CALMYNYRTE RNRVDVLDLD
PYGTAAPFID AGIQCVQDGG YPFTDLSVLA TVNYPEKCFS NYGGLPVKAQ YCHEAALRLV
LHSLSTSASR YGRYIQPVLS LSIDFYVRIF VRIFSAPIEV KKAFSKTATY YICSGCQHWY
EQPLGRIVEN VHQPSGNVNL QFKAHTGPPV ANNCPECNSK LHIAGPMWSG PIHDPSFIGR
VLDHVDASSD SYGTSTRMKG MLTVAKEELT QPFYFTPSVI AGHFHCVCPP LDGMSSALLH
AGHKVSRSHA CPGSLKTSAT LADVHDIFRS WIKKNPVRMD KIPPNSPAIH LLSKEPKAEA
NFKHHPQSVT SSSKVKIVRY QNNPTAHWGP GKKAGTGPAP TGKRKREGDD E
//
