ID A0A1Y2VB41_9PEZI Unreviewed; 685 AA.
AC A0A1Y2VB41;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=M434DRAFT_29596 {ECO:0000313|EMBL:OTA94759.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA94759.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA94759.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA94759.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112451; OTA94759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2VB41; -.
DR STRING; 1001938.A0A1Y2VB41; -.
DR Proteomes; UP000194361; 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 CDD; cd02440; AdoMet_MTases; 1.
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 NCBIfam; TIGR00308; TRM1; 1.
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:UP000194361};
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 80..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 75209 MW; 140044890AA4AE8F CRC64;
MAKESNNGTP AATTEIETIT RDGQEFTEVK EGLARILVPF SAKDAANKKP NDVEEQQKVF
YNPIQQFNRD LTVLAIKAYG EEVLAKRRPA NADKVAKRKR EKSDTGGERP KKQEKLESAN
GATSTAEEPK DNGTQASEPD MSLPDTQDGQ EQGSQADSLN KAEGSTEDIS NIDQSAGGAQ
PTKEGQKSTD SKGDGLAHGP RFTILDALSA TGLRALRYAQ ELPFVTSVTA NDLSPSAVEA
IKRNAEHNGV ESRVNATSGD ARAHMYSLLT QEVADDGAKK KHHKKGPPKP TKYDVIDLDP
YGTAATFFDA ALNAIRDDGG LLCVTCTDSG VWASHGYPEK TFALYGGIPV KGFHSHEAGL
RLIIHGLAST AARYGLAIEP LLSLSIDYYT RIFVKVRKSP AQAKFLAGKT MVVYNCDQGC
GAWETQFLVR NKKAPNKSGK GVFYKHGLAM APTTDRFCKE CGTKMHLAGP MYGGPLHSND
FIKKILDDLP NAPDDVYGTK QRIEGMLQTA LEEFIPPPED GLQSSKEDEF AVVEPYPFFF
HPTGLARVVH CICPDEDSFR GALRHLGYQV TRSHCKPGSL KTNAPWSVIW HIMREWVRQK
APVNVENIKE NTPAYTLLRL NKNDKATKDE SAKDETTKDA ECDSVDKLEV VFDKKLGRDT
SKKGLIRYQT NPRENWGPLS RARAH
//
