ID A0A091J3H9_EGRGA Unreviewed; 222 AA.
AC A0A091J3H9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=thiopurine S-methyltransferase {ECO:0000256|ARBA:ARBA00011905};
DE EC=2.1.1.67 {ECO:0000256|ARBA:ARBA00011905};
DE Flags: Fragment;
GN ORFNames=Z169_01958 {ECO:0000313|EMBL:KFP15182.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP15182.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP15182.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP15182.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK501480; KFP15182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091J3H9; -.
DR STRING; 188379.A0A091J3H9; -.
DR OrthoDB; 2902171at2759; -.
DR Proteomes; UP000053119; 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 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 ECO:0000313|EMBL:KFP15182.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFP15182.1}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP15182.1"
FT NON_TER 222
FT /evidence="ECO:0000313|EMBL:KFP15182.1"
SQ SEQUENCE 222 AA; 25294 MW; ECC4AC3962ADF8CC CRC64;
SEEEWLRKWE MGNIGFHKEQ GHPLLQKYLD VLLNGRSGLR IFFPLCGKAV EMKWLADMGH
SVVGVEVSEQ ALKEFFAEHS LPYCEEPVPE IPGAKKLQST SGNISLYCCS VYDLSSSIVG
KFDGFWDRGA LVAVNPCDRQ RYASLMITLM AKNSSYLLVT VSYDPNKHKG PPFYVPESEI
KGLFGNHCEI KCLQKVDDFS DRHRQWGLDY FLEVLYILKF VA
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