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Database: UniProt
Entry: W6KLF5_9TRYP
LinkDB: W6KLF5_9TRYP
Original site: W6KLF5_9TRYP 
ID   W6KLF5_9TRYP            Unreviewed;       762 AA.
AC   W6KLF5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=GSEM1_T00007133001 {ECO:0000313|EMBL:CCW61853.1};
OS   Phytomonas sp. EM1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW61853.1, ECO:0000313|Proteomes:UP000027080};
RN   [1] {ECO:0000313|EMBL:CCW61853.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW61853.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW61853.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW61853.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
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; HF955066; CCW61853.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6KLF5; -.
DR   EnsemblProtists; CCW61853; CCW61853; GSEM1_T00007133001.
DR   OrthoDB; 942596at2759; -.
DR   Proteomes; UP000027080; 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; 3.
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:UP000027080};
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          40..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..697
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   762 AA;  82417 MW;  87F6A6E42548CF43 CRC64;
     MKSGLFNRDA ITKECPEGYI KICEGTTAVL LAPTMPADAS KTSVDATHQG NERHFSKTTS
     AQLRSDNHNA EHGNEDQSVF YNPAQVVNRD LSVCAIETFS QIRLREPRRR GGVSAGLTIL
     EALSATGLRA IRYYKEISNI RYIIANDLDA GAVECIARNC AYNNVPLAQP TLDENFPSSL
     VTVSLPSNAE NEGMGRIPGE ITSGGGIVPN LDDAVDLMHR LALNPGVHSG KRFCLLEKKP
     AVVDGGGMPS EEWGAPRPVL QQELMDVVDL DPYGTASPFL DAAFGCIKEG GLMLVTSTDS
     AILCGNYPGT CHAKYDSIPY KSAHCHEMAV RILLACMERA ANKHKKYIAP LLSLHIDFYV
     RCFVRVFTQP AEVKLSASKL GYQLQCTNCP AFWVRPIAVA RGPRPPRRGK KRPREPNQPQ
     PPFSDASNEE RMKPNSPDAS LEETKAGVPS IEDSDMVRWE PEIFPPAPSR TNDPKLTALT
     LQMLPQLVCQ DSKRGSAEQG SPADPGSKAA GGLRVKPTDA VGNPPLPPRV SDDLHGSGCG
     VSKGDFCPVC GSSIALSGPI YAAPTQNGDF LTDLMQTVQS RAEEGKITAA ARITGLVQVA
     LEELPQCPLF YRLPDLASYV KTRCPPTPLF VAALARLGYS CSQVHCEPSG IKTDCPPPIL
     FAVMLRWKQL SEGNPAESEE ESKASDAMEE SASAPRKPRG DDLGGGVPKI LVSPLKSADF
     SYDRQHDFRR QVTGLAKFIP NAPGWGPKRR HQGTAPIASE EF
//
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