ID A0A0C4F1F4_PUCT1 Unreviewed; 656 AA.
AC A0A0C4F1F4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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};
OS Puccinia triticina (isolate 1-1 / race 1 (BBBD)) (Brown leaf rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=630390 {ECO:0000313|EnsemblFungi:PTTG_06924P0, ECO:0000313|Proteomes:UP000005240};
RN [1] {ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|Proteomes:UP000005240};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Fellers J., Bakkeren G., Szabo L., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblFungi:PTTG_06924P0}
RP IDENTIFICATION.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_06924P0};
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
RN [3] {ECO:0000313|Proteomes:UP000005240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|Proteomes:UP000005240};
RA Cuomo C.A., Bakkeren G., Szabo L., Khalil H., Joly D., Goldberg J.,
RA Young S., Zeng Q., Fellers J.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblFungi:PTTG_06924P0}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=isolate 1-1 / race 1 (BBBD)
RC {ECO:0000313|EnsemblFungi:PTTG_06924P0};
RX PubMed=27913634; DOI=10.1534/g3.116.032797;
RA Cuomo C.A., Bakkeren G., Khalil H.B., Panwar V., Joly D., Linning R.,
RA Sakthikumar S., Song X., Adiconis X., Fan L., Goldberg J.M., Levin J.Z.,
RA Young S., Zeng Q., Anikster Y., Bruce M., Wang M., Yin C., McCallum B.,
RA Szabo L.J., Hulbert S., Chen X., Fellers J.P.;
RT "Comparative analysis highlights variable genome content of wheat rusts and
RT divergence of the mating loci.";
RL G3 (Bethesda) 7:361-376(2017).
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}.
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DR EMBL; ADAS01007490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0C4F1F4; -.
DR EnsemblFungi; PTTG_06924T0; PTTG_06924P0; PTTG_06924.
DR OMA; MKCCHEM; -.
DR Proteomes; UP000005240; 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 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:UP000005240};
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 110..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 72020 MW; 8FCF714FA71FEFCC CRC64;
MELKVHHVAV LSCLGCGLLN FSRSMNHFRR ISIRLNHYHY NPRRLMASFP EPPPGYKAHQ
EASTQILIKL ENEQQPSEAF INPVQEYNRD LSIAAIKAWS SLRNQELEAK WTLSRTNHQR
KKNNKRPAGP PDPHPHNPKK LKQHEPDQQQ PDPTTVPEEP VANESAQQTA PPHEDIKSNK
QPPAFQPQKF TALEALSATG LRAIRYAKEI PTLRSIVAND LSPSAVALIK ANITHNGLDP
EDPSGQQEAK VRVTQGDACD LMYSHRQPDR QFDVVDLDPY GTAAPSSMRQ FNVSETAVSS
GSAYPEKCFS NYGGSSMRAE YSHEYALRQV IHTLASSAAR YGKQITPLLS LSIDFYVRIF
VRVSNSPAEV KKCITNTAVV YVCSGCAGFH FQAMGRTNTK PTKAGRGTNV SYQNACGPPM
PGATCEECGG KFHVAGPLWS GPLHDQGFCD RVLEVVEADE EPVKTAERIR GMVGLAKTEL
AEAPFFFTPA KLSGLFKCSS PSLLTVGSAI LNAGFALSRS HCQPGSIKTD APRAFIHDLM
KTWIDAQTAP TTSKPADPAP VFQPSSVGGA TAAGVADALT KDGEVKEAEA KDEEVKDCEV
KMEKARTMSK QKMVTYQVDL SYNKQVEKQL LTGLKIVRYQ ANPAPNWGPK ARALKK
//
