ID A0A086JDF8_TOXGO Unreviewed; 568 AA. AC A0A086JDF8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 14-DEC-2022, entry version 23. DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase {ECO:0000256|ARBA:ARBA00012796}; DE EC=2.1.1.220 {ECO:0000256|ARBA:ARBA00012796}; GN ORFNames=TGP89_306630 {ECO:0000313|EMBL:KFG30176.1}; OS Toxoplasma gondii p89. OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma. OX NCBI_TaxID=943119 {ECO:0000313|EMBL:KFG30176.1, ECO:0000313|Proteomes:UP000028828}; RN [1] {ECO:0000313|EMBL:KFG30176.1, ECO:0000313|Proteomes:UP000028828} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=p89 {ECO:0000313|Proteomes:UP000028828}; RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B., RA Roos D., Caler E., Lorenzi H.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. 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:KFG30176.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AEYI02002091; KFG30176.1; -; Genomic_DNA. DR AlphaFoldDB; A0A086JDF8; -. DR EnsemblProtists; KFG30176; KFG30176; TGP89_306630. DR VEuPathDB; ToxoDB:TGP89_306630; -. DR Proteomes; UP000028828; Unassembled WGS sequence. DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro. DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14. DR PANTHER; PTHR12133; TRNA (ADENINE(58)-N(1))-METHYLTRANSFERASE; 2. DR Pfam; PF08704; GCD14; 2. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51620; SAM_TRM61; 1. PE 4: Predicted; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, KW ECO:0000313|EMBL:KFG30176.1}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFG30176.1}. FT REGION 1..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 242..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 381..430 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 497..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 242..258 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 381..395 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 397..414 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 415..429 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..511 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 568 AA; 61789 MW; 3D3E830DA53FC462 CRC64; MGMISGQRSS SAPSFAESHP PSDFVSPSGV DTLQNTEMKE DSTSRDRGAA AVDTDAGLRK TESPLSTVSE QVDHREYPRY GDFVILYGSH QLVIPVLLER GRVSNSRLGN YRHDDIVTTA YGSKVQDRKS KRWLVVLRPS PDLFSLALTH RTQILYHSDI SLVLMLLDAC PGRRICEAGT GSGSLSCHLA RAVAPTGHIF TFEFHQQRKM EAEADFKRLG LSSYLSCYHR DVCTDGFVSV STASGEDVSS NSSETSRVLP LEEKGKTAGA LADSETPDDG GAAEKVDLPA AGSIDSLFLD VPSPWLALDH VDAALREGGR FVNFSPCVEQ VQRVCECLHE RGYHGIRTFE VIRKPWGVWT TKPTARSSAV GDLGRIPEEP ILARDSKRLK KTGAETTAAS EDPTQASTTR SRKGNGNTRR SEVDGCQGDG NDKEISLATF PLLISQLLGQ SVPEEFWTPA MKLECASDSV EAGCEQGAAE NKGTCKKVCH SKSTLRVPPC SSGTETGTNE RTEGVSVDRN KEKTRLRTFP IDFEATHYPL PLRGHTGYLT VAVKHRVRAL SGKMSAPC //