ID A0A0P1BAR3_9BASI Unreviewed; 707 AA.
AC A0A0P1BAR3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|ARBA:ARBA00039099};
DE EC=2.1.1.216 {ECO:0000256|ARBA:ARBA00039099};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH12796.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH12796.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) 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; CCYA01000181; CEH12796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BAR3; -.
DR STRING; 401625.A0A0P1BAR3; -.
DR OrthoDB; 942596at2759; -.
DR Proteomes; UP000054845; 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 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; 2.
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:UP000054845};
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 66..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 75715 MW; 06CCB4498D352A5D CRC64;
MAPTPVALST SAAAALGISS DQSAFKEGSA VISIPKSDAA FLNPVQEFNR DLSVLAIRTW
AERRDREKRE KFEQAISKRK ERSANGRGKR RKLAHTATSN AGNAVSLDAA SSTSDIQADL
SASAPSAAAA AGDLSTASTS PHAHIDSSYR PFTFNIFEAL SATGLRSIRY AREIPNLKSV
HANDLSPTAV QAIWKNVALN FPANRDIKQW APELDQGEPE KDALEASSTA EAAAATARNT
LSSEAASAQF ANNGAANGAG HPAIHPNCKI HVTEQDAIEI LYTSRAKDKQ YSVIDLDPYG
SASMFIDGAV QAVADGGLLC VTCTDLVVLA GNAYPERAYS LYGGTTTRND FVHEVALRLV
LGLIATTAGR YGRAITPLLS LSIDFYLRVF VSVQTRPVDV KMLASTMGTV QTCPDCGNWD
ANAFGRNKAE GRADLIKYQA GTSHAAGTNC QECESRFHVA GPMWLGPLHM PSFAEEMLEV
LERAPVRFRT APRIRGMVGM ASKELSSPFF FIPPKISSYF HTTNIPLTTV VSCLLNAGYE
ASRSHAQPAS IKTNASPTVV RDLWRQWVKE KSPINEKNVH ENSPARRLLS KECATTFELD
KDHPQTRRVL GLDQDGKKDA GVKYQLNPLP NWGPGKAARP ESQKDRRRAA AAAAAAAAAS
NESNETGESR ANGSGLAASA EVDASAQGDA QANNQATSMD EDELRNS
//