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Database: UniProt
Entry: A0A5A8C1N6_CAFRO
LinkDB: A0A5A8C1N6_CAFRO
Original site: A0A5A8C1N6_CAFRO 
ID   A0A5A8C1N6_CAFRO        Unreviewed;       960 AA.
AC   A0A5A8C1N6;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=FNF29_07916 {ECO:0000313|EMBL:KAA0146674.1};
OS   Cafeteria roenbergensis (Marine flagellate).
OC   Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Bicosoecida;
OC   Cafeteriaceae; Cafeteria.
OX   NCBI_TaxID=33653 {ECO:0000313|EMBL:KAA0146674.1, ECO:0000313|Proteomes:UP000323011};
RN   [1] {ECO:0000313|EMBL:KAA0146674.1, ECO:0000313|Proteomes:UP000323011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BVI {ECO:0000313|EMBL:KAA0146674.1,
RC   ECO:0000313|Proteomes:UP000323011};
RA   Fischer M.G., Hackl T., Roman M.;
RT   "Genomes of Cafeteria roenbergensis.";
RL   Submitted (JUL-2019) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAA0146674.1}.
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DR   EMBL; VLTN01000081; KAA0146674.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5A8C1N6; -.
DR   Proteomes; UP000323011; 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; 2.
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:UP000323011};
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          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          918..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..706
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..960
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  98193 MW;  937166618C963600 CRC64;
     MSSSGPASSM SAAEGGHVPP GLTPPEGFKT IVEGSATALY PDGRAVFYNP AQVYNRDLST
     AALRVLAKER AIHWSSPDAA AHEVNRRSKR DSRDDGLGGW VPPAIKAILF APPAEELARL
     DEYHAKSAEE RSELASAAAA TASGPAPGAL GASLGVEVVE ALAATGLRSV RYASEVPGLG
     AVVVSDLDGA AVRACKHNVA FNGLDPAVVR PCQADAVSLM QAMRAPEWRV DWLDLDPYGT
     PSPFIESAVS AVHHGGILAM TATDMIVLAG SMRSAAHGKY GSMAVRSAAC HELALRALIF
     TVATAAARAK RTVEPLLSVN ANFYCRIFFR VRNNPAGAQN LSLMTGSLAQ CPQCGTRQWQ
     PVGRVSTQAA PGKYGSRKGK GGRPAFRGRR PRITRGGAAA ACRGTSSSSS SAASGSKPGA
     EAGNGADDAE TGDAAEATPS AGPDAEERAA QAERVRAAVL GLARGDDDAV RGAKAMPARV
     AVSPLCPSCG GNMHVAGPYW TGPIHSPPFV RAVREEVKAL ADSDSGKRGG GFPVAPGEGA
     VLPGRRLPME AVLSGQAGAG AHCAPAPSSS SSGGSTAAAG GAAAAAGSMV DGEPAVSPLG
     VSTGLGKKEA HDAGSNTDET VAASRRRLLS MLRLMSREVG GEELERMYAA LDGDGQGVAG
     SDAWNAALPR SGARPIGASG PAADGDQGEG SDGEGEGSDG EGEGSDGEGE GQSAQGAAPS
     ATSAAASATS GRGPSDAALA VSAEQRTLNG LLYWNANTLG MATKMPLPPR RGLAACIINE
     GFRVSDTHCD ETGFKTDAPI ALLWDALRTF GWSAEGMYPE QGLAKAREDL VTVRAKMAEA
     RAAQESGSGA GAEGGKRFPN KQRKRQAQLL GGQALASATL LASPITFTGL TFEPRTDAAR
     AALRKFLGYE ASADGETKVR KHFANPRGEW GPQQRAKGDK RPTDATDAES EPKRARPSEE
//
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