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Database: UniProt
Entry: A0A2J6QI16_9HELO
LinkDB: A0A2J6QI16_9HELO
Original site: A0A2J6QI16_9HELO 
ID   A0A2J6QI16_9HELO        Unreviewed;       732 AA.
AC   A0A2J6QI16;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=NA56DRAFT_642159 {ECO:0000313|EMBL:PMD25906.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD25906.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD25906.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD25906.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) 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; KZ613469; PMD25906.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6QI16; -.
DR   STRING; 1745343.A0A2J6QI16; -.
DR   OrthoDB; 942596at2759; -.
DR   Proteomes; UP000235672; 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; 2.
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:UP000235672};
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          39..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  80096 MW;  AA82ACAEC572EA4B CRC64;
     MSSPQSITAP PAADQHIVHA EKEYTTVKEG LAYILIPASA SKTQQTTPKG DNQPQSVFYN
     PIQQFNRDLS VLAIKAYGEE VLEKRLKAYE NAKKRHGAKR DKKRKREDDG VGSEFRKAGK
     VGVGDRTEEQ PAATNCEDVN PASVNNKISG GQDSGVVDER KGNMTISVDE ESSSGAQLSP
     TQQDVPVAGL AEQGVEGRST ADGELRLGTQ PALSHQENTV EAGATSQSKK EIKPHFRILD
     ALSATGLRAL RYAQEIPFTT LVTANDLLET ATQAIKLNVQ HNKLEDKISV STGNALTHMY
     NFVGDDCKDM KGQPKASEKY DVIDLDPYGT AAMFLDAAVQ AVRDDGGLLC VTCTDAGVWA
     SNSYPEKSYS LYGGTPLKGV MSHEGGLRLI LHAIATSAAR YGLATEPLLS LSIDFYARVF
     VRITKSANDV KFLAGKTMII NNCDAGCGAW TTQTIGKNKL TKDKSGKSFF WKHVFGPASL
     GGDNCPHCGM KTHLAGPMYA GPIHSPEFIK RILDELPTLS KDTYHTTDRI EGMLNLALEE
     IFPLEENPDS PTATSKTRKY DHSIIDPAPF FFIPSALSKV IHCITPHENA IRGALRHLGY
     WCTRSHAKPG SIKTNAPWDV IWDIMREWTR QKEPIKKGAI RENTAGYNIM GMGDEKKPES
     NGANGTESKA DQSGEERPAD DNSPVDTPAE KKKLDIVFDE KLGKEKDTRK LVRYQLNPRE
     NWGPMNRAKG HA
//
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