AC MF_03146; DC Protein; auto c? TR HAMAP; MF_01116; -; 1; level=0 XX Names: TSR3_euk XX ID TSR3 DE RecName: Full=18S rRNA aminocarboxypropyltransferase; DE EC=2.5.1.-; case GN Name=TSR3; end case XX case CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the CC aminocarboxypropyl transfer on pseudouridine at position 1248 (Psi1248) CC in 18S rRNA. It constitutes the last step in biosynthesis of the CC hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine CC (m1acp3-Psi) conserved in eukaryotic 18S rRNA. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(1)-methylpseudouridine(1248) in human 18S rRNA + S-adenosyl- CC L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3- CC carboxypropyl]pseudouridine(1248) in human 18S rRNA + S-methyl-5'- CC thioadenosine; Xref=Rhea:RHEA:63292, Rhea:RHEA-COMP:11639, Rhea:RHEA- CC COMP:16308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63293; else case CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the CC aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) CC in 18S rRNA. It constitutes the last step in biosynthesis of the CC hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine CC (m1acp3-Psi) conserved in eukaryotic 18S rRNA. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(1)-methylpseudouridine(1191) in yeast 18S rRNA + S-adenosyl- CC L-methionine = H(+) + N(1)-methyl-N(3)-[(3S)-3-amino-3- CC carboxypropyl]pseudouridine(1191) in yeast 18S rRNA + S-methyl-5'- CC thioadenosine; Xref=Rhea:RHEA:63300, Rhea:RHEA-COMP:13852, Rhea:RHEA- CC COMP:16309, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63301; else CC -!- FUNCTION: Aminocarboxypropyltransferase that catalyzes the CC aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It CC constitutes the last step in biosynthesis of the hypermodified N1- CC methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi). CC -!- CATALYTIC ACTIVITY: CC Reaction=an N(1)-methylpseudouridine in 16S/18S rRNA + S-adenosyl-L- CC methionine = H(+) + N(1)-methyl-N(3)[(3S)-3-amino-3- CC carboxypropyl]pseudouridine in 16S/18S rRNA + S-methyl-5'- CC thioadenosine; Xref=Rhea:RHEA:63296, Rhea:RHEA-COMP:11634, Rhea:RHEA- CC COMP:16310, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74890, ChEBI:CHEBI:146234; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63297; end case case CC -!- SUBCELLULAR LOCATION: Cytoplasm. else case CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. end case CC -!- SIMILARITY: Belongs to the TDD superfamily. TSR3 family. XX DR Pfam; PF04034; Ribo_biogen_C; 1; trigger=no DR Pfam; PF04068; RLI; 1; trigger=no XX case or KW Cytoplasm end case case KW Nucleus end case KW Ribosome biogenesis KW S-adenosyl-L-methionine KW Transferase KW rRNA processing XX case or GO GO:0005737; C:cytoplasm end case case GO GO:0005634; C:nucleus end case GO GO:1904047; F:S-adenosyl-L-methionine binding GO GO:0006364; P:rRNA processing GO GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis XX FT From: TSR3_YEAST (Q12094) FT BINDING 62 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [ST] FT BINDING 110 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [VIL] FT BINDING 133 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [LI] FT BINDING 148 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [WY] XX Size: 247-421; Related: None; Template: Q12094; Q9UJK0; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.10 2022/11/19 //