ID V4CEX6_LOTGI Unreviewed; 224 AA.
AC V4CEX6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=thiopurine S-methyltransferase {ECO:0000256|ARBA:ARBA00011905};
DE EC=2.1.1.67 {ECO:0000256|ARBA:ARBA00011905};
GN ORFNames=LOTGIDRAFT_112328 {ECO:0000313|EMBL:ESP00540.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP00540.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP00540.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-
CC homocysteine + a thiopurine S-methylether.; EC=2.1.1.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000903};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TPMT family. {ECO:0000256|ARBA:ARBA00008145}.
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DR EMBL; KB200701; ESP00540.1; -; Genomic_DNA.
DR RefSeq; XP_009048659.1; XM_009050411.1.
DR AlphaFoldDB; V4CEX6; -.
DR STRING; 225164.V4CEX6; -.
DR EnsemblMetazoa; LotgiT112328; LotgiP112328; LotgiG112328.
DR GeneID; 20230837; -.
DR KEGG; lgi:LOTGIDRAFT_112328; -.
DR CTD; 20230837; -.
DR HOGENOM; CLU_085515_2_0_1; -.
DR OMA; LWCGDFF; -.
DR OrthoDB; 2902171at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008119; F:thiopurine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00812; Thiopur_methtran; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025835; Thiopurine_S-MeTrfase.
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 PIRSF; PIRSF023956; Thiopurine_S-methyltransferase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51585; SAM_MT_TPMT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 224 AA; 26218 MW; D5B3577823DD5FD0 CRC64;
MTVEDWEKRW KLEQTGFHMD QVHPMLVKYY SKLTRDKPKL RFYLPLCGKS VDLKWLSDNG
HDVVGCDGSD IGCQDFFKEN SLPYTSEALP ESTGGGVLYQ NKEKNIKLYR CDFFKLSPEI
IGQFDCIWDR GSFVAIPVTE RGRYAELILQ SLKPTGRYLL DTFQLPHQNY QGPPFNTEED
EVNKYFGQKC TIEKLAVNNV FNQKHLEQWK VEYFNEIVYL LTSK
//
