ID   A0A086JDF8_TOXGO        Unreviewed;       568 AA.
AC   A0A086JDF8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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}.
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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:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro.
DR   GO; GO:0160107; F:tRNA (adenine(58)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030488; P:tRNA methylation; IEA:InterPro.
DR   Gene3D; 3.10.330.20; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR049470; TRM61_C.
DR   InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR   PANTHER; PTHR12133; TRNA (ADENINE(58)-N(1))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR12133:SF2; TRNA (ADENINE(58)-N(1))-METHYLTRANSFERASE CATALYTIC SUBUNIT TRMT61A; 1.
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};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          133..238
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT                   subunit TRM61 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08704"
FT   DOMAIN          291..366
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT                   subunit TRM61 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08704"
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
//