ID W7HXR9_9PEZI Unreviewed; 245 AA.
AC W7HXR9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|ARBA:ARBA00039099};
DE EC=2.1.1.216 {ECO:0000256|ARBA:ARBA00039099};
GN ORFNames=DRE_06496 {ECO:0000313|EMBL:EWC44718.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC44718.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC44718.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC44718.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}.
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DR EMBL; KI966435; EWC44718.1; -; Genomic_DNA.
DR AlphaFoldDB; W7HXR9; -.
DR HOGENOM; CLU_1133573_0_0_1; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
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 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:UP000024837};
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 128..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 245 AA; 27454 MW; CA1AC100BDD26F31 CRC64;
MPTQLSRVLH CDAPPLAAIR GALLGLGYRV SKSHCRPGSL KTDASWRVLW RVMRAWVRTH
PIKPGSLTES MPGYRILYPR TQHPDDEHEN LDEIVFDEAL GREKEKGKGE VNYQLNPNAY
WGPMARAGRR GMTAQELSKE GNAEKDKRRR EERERRKLEG LTRVADNGEE AEGKRRRRQD
RRHGIEAAAA ASSSVDVSDR RDCGNGVEET PVRTNTTDGA QYGLAGISAS DLDRLEEEAV
GKLKS
//
