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Database: UniProt
Entry: A0A316VPB4_9BASI
LinkDB: A0A316VPB4_9BASI
Original site: A0A316VPB4_9BASI 
ID   A0A316VPB4_9BASI        Unreviewed;       733 AA.
AC   A0A316VPB4;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=IE81DRAFT_326820 {ECO:0000313|EMBL:PWN39154.1};
OS   Ceraceosorus guamensis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=1522189 {ECO:0000313|EMBL:PWN39154.1, ECO:0000313|Proteomes:UP000245783};
RN   [1] {ECO:0000313|EMBL:PWN39154.1, ECO:0000313|Proteomes:UP000245783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4658 {ECO:0000313|EMBL:PWN39154.1,
RC   ECO:0000313|Proteomes:UP000245783};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(2018).
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; KZ819490; PWN39154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316VPB4; -.
DR   STRING; 1522189.A0A316VPB4; -.
DR   InParanoid; A0A316VPB4; -.
DR   OrthoDB; 942596at2759; -.
DR   Proteomes; UP000245783; 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:UP000245783};
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          91..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   733 AA;  78241 MW;  FE848BF616F2E895 CRC64;
     MFPRRISTVC ASSFLSLQRP ALNLTMAPTP VALSTSAAAA LGISSDQSAF KEGSAVISIP
     KSDAAFLNPV QEFNRDLSVL AIRTWAERRD REKREKFEQA ISKRKERSAN GRGKRRKIAH
     TATSNASDAA SLDNASSTSA KRADLSASAS STAAATAAGD VSTASTSSHA HIDSSHRPFT
     FNIFEALSAT GLRSIRYARE IPNLKSVHAN DLSPTAVQAI WKNVALNFPA NRDIKQWAPE
     LDRGEPEKDD AEASSTAEAA AAAARSASSS EAASAQFASN GAANGAGHPA IHPKCKIHVT
     EQDAIEILYT SRAKDKQYSV IDLDPYGSAS MFIDGAVQAV ADGGLLCVTC TDLVVLAGNA
     YPERAYSLYG GTTTRNDFVH EVALRLVLGL IATTAGRYGR AITPLLSLSI DFYLRVFVSV
     HTRPVDVKML ASTMGTVQTC PDCGNWDANA FGRNKAEGRA DLIKYQAGTS HTVGTNCQEC
     DSRFHVAGPM WLGPLHTPSF AEEMLEVLER APVRFRTAPR IRGMVGMASK ELSSPFFFIP
     PKISSYFHTT NIPLTAVVSC LLNAGYEVSR SHAQPASIKT NASPTVVRDL WRQWVKEKSP
     INEKNVHENS PARRLLAKEC ATTFELDKDH PQTRQVLGLD QDGKKNAGVK YQLNPLPNWG
     PGKAARPESK KDRKRAAAAA AAAAASSESN GTGGGRANVS GLAASAGVDA SAQGDVQANN
     QAASMDEDEL RNS
//
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