AC   MF_03180;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01446; -; 1; level=0
XX
Names: GCP2_Kae1
XX
case <OC:Fungi>
ID   KAE1
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase;
DE            EC=2.3.1.234;
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase;
DE            Short=t(6)A synthase;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein <gene_name>;
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein <gene_name>;
else case <OC:Vertebrata>
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase;
DE            EC=2.3.1.234;
DE   AltName: Full=N6-L-threonylcarbamoyladenine synthase;
DE            Short=t(6)A synthase;
DE   AltName: Full=O-sialoglycoprotein endopeptidase;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein <gene_name>;
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein <gene_name>;
else
ID   OSGEP
DE   RecName: Full=Probable tRNA N6-adenosine threonylcarbamoyltransferase;
DE            EC=2.3.1.234;
DE   AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein <gene_name>;
DE   AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein <gene_name>;
end case
case <OC:Viridiplantae>
DE   + AltName: Full=Glycoprotease 2;
GN   Name=GCP2;
else case <OC:Dictyostelia>
GN   Name=osgep;
else case <OC:Fungi>
GN   Name=KAE1;
end case
XX
case <OC:Fungi>
CC   -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC       formation of a threonylcarbamoyl group on adenosine at position 37
CC       (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC       is probably involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. @gn(KAE1) likely
CC       plays a direct catalytic role in this reaction, but requires other
CC       protein(s) of the complex to fulfill this activity. The EKC/KEOPS
CC       complex also promotes both telomere uncapping and telomere elongation.
CC       The complex is required for efficient recruitment of transcriptional
CC       coactivators.
CC   -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least
CC       @gn(BUD32), @gn(CGI121), @gn(GON7), @gn(KAE1) and @gn(PCC1); the whole
CC       complex dimerizes.
else case <OC:Vertebrata>
CC   -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC       formation of a threonylcarbamoyl group on adenosine at position 37
CC       (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC       is probably involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. @gn(OSGEP)
CC       likely plays a direct catalytic role in this reaction, but requires
CC       other protein(s) of the complex to fulfill this activity.
CC   -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least
CC       @gn(TP53RK), @gn(TPRKB), @gn(OSGEP) and @gn(LAGE3); the whole complex
CC       dimerizes.
else
CC   -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC       formation of a threonylcarbamoyl group on adenosine at position 37
CC       (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC       is probably involved in the transfer of the threonylcarbamoyl moiety of
CC       threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Likely plays a
CC       direct catalytic role in this reaction, but requires other protein(s)
CC       of the complex to fulfill this activity.
CC   -!- SUBUNIT: Component of the EKC/KEOPS complex; the whole complex
CC       dimerizes.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP +
CC         H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC       Note=Binds 1 divalent metal cation per subunit.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family.
XX
DR   PROSITE; PS01016; GLYCOPROTEASE; 1; trigger=no
DR   Pfam; PF00814; Peptidase_M22; 1; trigger=no
DR   PRINTS; PR00789; OSIALOPTASE; 1; trigger=no
DR   NCBIfam; TIGR00329; Gcp_kae1; 1; trigger=no
XX
KW   Acyltransferase
KW   Cytoplasm
KW   Metal-binding
KW   Nucleus
KW   Transferase
KW   tRNA processing
case <OC:Fungi>
KW   Activator
KW   Transcription
KW   Transcription regulation
end case
XX
GO   GO:0005737; C:cytoplasm
GO   GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups
GO   GO:0002949; P:tRNA threonylcarbamoyladenosine modification
XX
FT   From: KAE1_PYRAB (Q9UXT7)
FT   BINDING         127..131
FT                   /ligand="substrate"
FT   Condition: x-x-[SA]-G-[GA]
FT   BINDING         107
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         111
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         127
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Optional; Condition: Y
FT   BINDING         285
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: D
FT   BINDING         159
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         172
FT                   /ligand="substrate"
FT   Optional; Condition: [GA]
FT   BINDING         176
FT                   /ligand="substrate"
FT   Condition: [ED]
FT   BINDING         257
FT                   /ligand="substrate"
FT   Condition: [NS]
XX
Size: 325-407;
Related: MF_01447!;
Template: Q9UXT7; P36132;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: Was originally (PubMed:17766251) thought to have endonuclease activity, but it
 could not be confirmed with orthologs purified from M. jannaschii (PubMed:18951093) and
 S. cerevisiae (PubMed:21183954).
XX
# Revision 1.17 2023/06/01
//