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Database: UniProt
Entry: A0A0S4INW4_BODSA
LinkDB: A0A0S4INW4_BODSA
Original site: A0A0S4INW4_BODSA 
ID   A0A0S4INW4_BODSA        Unreviewed;       387 AA.
AC   A0A0S4INW4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Thiopurine S-methyltransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BSAL_57775 {ECO:0000313|EMBL:CUE96581.1};
OS   Bodo saltans (Flagellated protozoan).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Eubodonida; Bodonidae; Bodo.
OX   NCBI_TaxID=75058 {ECO:0000313|EMBL:CUE96581.1, ECO:0000313|Proteomes:UP000051952};
RN   [1] {ECO:0000313|Proteomes:UP000051952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; CYKH01000219; CUE96581.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S4INW4; -.
DR   VEuPathDB; TriTrypDB:BSAL_57775; -.
DR   OMA; FRQIHLH; -.
DR   OrthoDB; 122133at2759; -.
DR   Proteomes; UP000051952; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR008854; TPMT.
DR   PANTHER; PTHR10259; THIOPURINE S-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10259:SF11; THIOPURINE S-METHYLTRANSFERASE; 1.
DR   Pfam; PF05724; TPMT; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51585; SAM_MT_TPMT; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        48..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   387 AA;  43701 MW;  A44F691187E7971D CRC64;
     MALRRSLIRR LSVNIPGAEE VGSQIAYKRY LERRIRAPGF SGWGASQYLT WLVAGGIIVG
     GGVVLGPWIV DETRSAYGYN VRIVDASTVL PEFTPDWWEN EWRKMLTTWR RGEYVEDFHV
     PQYKYIESIV GRDMAEEPLQ RFTQRVGPSS SSSSPWWRKL LGQQSDSSRS KSVADALANK
     PRALVPMCGD SPILRVLIEQ GYQVDGVDCS ETAIRTAVEK LEARLPASAF SNIQLHYKDI
     FAPSLWTTDL AGRRYDFIYD RQALSALNPE RREDYAYLLK QALKEDGILY VEGVFRTGRV
     KGNKVRGPPF GLSRAQLRDL FSEKDGFFVQ CKDTEDNAIA LLDAQSKVLR RVPKELHITT
     FPCVVFREAS IGLPPLTSNS SSEPLKL
//
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