ID C5DN17_LACTC Unreviewed; 542 AA.
AC C5DN17;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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};
GN OrderedLocusNames=KLTH0G13420g {ECO:0000313|EMBL:CAR25178.1};
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR25178.1, ECO:0000313|Proteomes:UP000002036};
RN [1] {ECO:0000313|EMBL:CAR25178.1, ECO:0000313|Proteomes:UP000002036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC {ECO:0000313|Proteomes:UP000002036};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928171; CAR25178.1; -; Genomic_DNA.
DR RefSeq; XP_002555615.1; XM_002555569.1.
DR AlphaFoldDB; C5DN17; -.
DR STRING; 559295.C5DN17; -.
DR GeneID; 8293898; -.
DR KEGG; lth:KLTH0G13420g; -.
DR eggNOG; KOG1253; Eukaryota.
DR HOGENOM; CLU_010862_4_1_1; -.
DR InParanoid; C5DN17; -.
DR OMA; MKCCHEM; -.
DR OrthoDB; 942596at2759; -.
DR Proteomes; UP000002036; Chromosome G.
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:UP000002036};
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 71..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60748 MW; A5B0F79915DC1BD5 CRC64;
MIRAALAKVR SRFVKPAPKP DASKFTVVTE GKAHILFPEK ETVFYNPIQQ FNRDLSVSCI
KAWDNLYGQA KQEKSRGKGK KRGLEHGEEA SKKRKLEDGS SAEVKASSSR PYIKILEALS
ATGLRAIRYA HEIPNVKEVV ANDLLPEAVD AIQRNVDYNK VGHIVKPNID DANVLMYRNK
AAHKRYHVID LDPYGTATPF IDAALQNIED DGLMLVTCTD LSVLAGNGYP EKCFALYGGV
NMAGHDATHE SALRLVLNLL GQSAAKYKKS IEPLLSLSID FYVRVFVKVK TNPTKVKDLQ
HNTMITYVCS GCRSYHSQRL GKQTERESKK GKPYLKYSLA QGPPVDKKCH YCGGAHHLTG
PMYAGPLHNR EFIDEVLRIN RDVHGDDVYK TRKRIEGMLT LAKNEVDAPF YFTPNRVSSI
LKFQVPSLKT VVAGLGSLGY ECSLTHAQPS SLKTDAPWGA IWYVMKRYCL DNGLCNVEKM
NQNSWGYKIL SNDLVAEAAQ YGDQLSFEPN DQSGRVEKLR KLKIVRYQEN PTKNWGPKAR
PQ
//
