 |
|
Annotation rule MF_03180 |
General rule information
[?]
Accession |
MF_03180 |
Dates |
17-OCT-2013 (Created) 14-MAY-2022 (Last updated, Version 15) |
case <OC:Eukaryota>
end case
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Fungi>
Protein name |
RecName:
|
Full=tRNA N6-adenosine threonylcarbamoyltransferase;
|
|
EC 2.3.1.234;
|
AltName:
|
Full=N6-L-threonylcarbamoyladenine synthase;
|
|
Short=t(6)A synthase;
|
AltName:
|
Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein ;
|
AltName:
|
Full=tRNA threonylcarbamoyladenosine biosynthesis protein ;
|
|
else case <OC:Vertebrata>
Protein name |
RecName:
|
Full=tRNA N6-adenosine threonylcarbamoyltransferase;
|
|
EC 2.3.1.234;
|
AltName:
|
Full=N6-L-threonylcarbamoyladenine synthase;
|
|
Short=t(6)A synthase;
|
AltName:
|
Full=O-sialoglycoprotein endopeptidase;
|
AltName:
|
Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein ;
|
AltName:
|
Full=tRNA threonylcarbamoyladenosine biosynthesis protein ;
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|
else
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:Viridiplantae>
else case <OC:Dictyostelia>
else case <OC:Fungi>
end case
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. |
case <OC:Fungi>
end case
GO:0005737; Cellular component: cytoplasm.
GO:0016747; Molecular function: acyltransferase activity, transferring groups other than amino-acyl groups.
GO:0002949; Biological process: tRNA threonylcarbamoyladenosine modification.
From: KAE1_PYRAB (Q9UXT7) |
Key
|
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From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
BINDING
|
|
127
|
|
131
|
|
/ligand="substrate
|
|
|
|
x-x-[SA]-G-[GA]
|
|
|
BINDING
|
|
107
|
|
107
|
|
/ligand="a divalent metal cation" /ligand_id="60240
|
|
|
|
H
|
|
|
BINDING
|
|
111
|
|
111
|
|
/ligand="a divalent metal cation" /ligand_id="60240
|
|
|
|
H
|
|
|
BINDING (Optional)
|
|
127
|
|
127
|
|
/ligand="a divalent metal cation" /ligand_id="60240
|
|
|
|
Y
|
|
|
BINDING
|
|
285
|
|
285
|
|
/ligand="a divalent metal cation" /ligand_id="60240
|
|
|
|
D
|
|
|
BINDING
|
|
159
|
|
159
|
|
/ligand="substrate
|
|
|
|
D
|
|
|
BINDING (Optional)
|
|
172
|
|
172
|
|
/ligand="substrate
|
|
|
|
[GA]
|
|
|
BINDING
|
|
176
|
|
176
|
|
/ligand="substrate
|
|
|
|
[ED]
|
|
|
BINDING
|
|
257
|
|
257
|
|
/ligand="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). |