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Annotation rule MF_03180
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General rule information [?]

Accession MF_03180
Dates 17-OCT-2013 (Created)
10-DEC-2019 (Last updated, Version 11)
Name GCP2_Kae1
Scope
Eukaryota
Templates Q9UXT7 (KAE1_PYRAB); P36132 (KAE1_YEAST): [Recover all]
case <OC:Eukaryota>
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

case <OC:Fungi>
Identifier
KAE1
Protein name
RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase;
EC 2.3.1.234;
AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein ;
AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein ;
else
Identifier
OSGEP
Protein name
RecName: Full=Probable tRNA N6-adenosine threonylcarbamoyltransferase;
EC 2.3.1.234;
AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein ;
AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein ;
end case
case <OC:Vertebrata>
Protein name
Full=O-sialoglycoprotein endopeptidase;
Gene name
OSGEP
else case <OC:Viridiplantae>
Protein name
Full=Glycoprotease 2;
Gene name
GCP2
else case <OC:Dictyostelia>
Gene name
osgep
else case <OC:Fungi>
Gene name
KAE1
end case

Comments [?]

case <OC:Fungi>
Function Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. @gn(KAE1) likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Subunit Component of the EKC/KEOPS complex composed of at least @gn(BUD32), @gn(CGI121), @gn(GON7), @gn(KAE1) and @gn(PCC1); the whole complex dimerizes.
else case <OC:Vertebrata>
Function Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. @gn(OSGEP) likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity.
Subunit Component of the EKC/KEOPS complex composed of at least @gn(TP53RK), @gn(TPRKB), @gn(OSGEP) and @gn(LAGE3); the whole complex dimerizes.
else
Function Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity.
Subunit Component of the EKC/KEOPS complex; the whole complex dimerizes.
end case
Catalytic activity RHEA:37059: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
EC 2.3.1.234
Cofactor a divalent metal cation
Note: Binds 1 divalent metal cation per subunit.
Subcellular location Cytoplasm. Nucleus.
Similarity Belongs to the KAE1 / TsaD family.

Keywords [?]

case <OC:Fungi>
end case

Gene Ontology [?]

GO:0005737; Cellular component: cytoplasm.
GO:0016747; Molecular function: transferase activity, transferring acyl groups other than amino-acyl groups.
GO:0002949; Biological process: tRNA threonylcarbamoyladenosine modification.

Cross-references [?]

PROSITE PS01016; GLYCOPROTEASE; 1;
Pfam PF00814; Peptidase_M22; 1;
PRINTS PR00789; OSIALOPTASE; 1;
TIGRFAMs TIGR00329; Gcp_kae1; 1;

Features [?]

From: KAE1_PYRAB (Q9UXT7)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     127     131       Substrate binding     x-x-[SA]-G-[GA]  
METAL     107     107       Divalent metal cation     H  
METAL     111     111       Divalent metal cation     H  
METAL (Optional)     127     127       Divalent metal cation     Y  
METAL     285     285       Divalent metal cation     D  
BINDING     159     159       Substrate     D  
BINDING (Optional)     172     172       Substrate; via amide nitrogen     [GA]  
BINDING     176     176       Substrate     [ED]  
BINDING     257     257       Substrate     [NS]  

Additional information [?]

Size range 325-407 amino acids
Related rules MF_01447 (KAE1B supersedes the current rule)
Fusion 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).