HAMAP rule MF_03180
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_03180 |
| Accession | MF_03180 |
| Dates | 17-OCT-2013 (Created)
03-SEP-2024 (Last updated, Version 19) |
| Name | GCP2_Kae1 |
| Scope(s) |
Eukaryota |
| Template(s) | Q9UXT7; P36132; [ Recover all ] |
| Triggered by |
case c? <OC:Eukaryota>
HAMAP; MF_01446 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| case <OC:Fungi> | |
| Identifier | KAE1 |
| 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 |
| 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:Viridiplantae> | |
| Protein name | + AltName: Full=Glycoprotease 2; |
| Gene name | Name=GCP2; |
| else case <OC:Dictyostelia> | |
| Gene name | Name=osgep; |
| else case <OC:Fungi> | |
| Gene name | Name=KAE1; |
| end case | |
Comments
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| 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 | Reaction=L-threonylcarbamoyladenylate + adenosine(37) in tRNA = N(6)-L- threonylcarbamoyladenosine(37) in tRNA + AMP + H(+); Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; |
| COFACTOR | Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Note=Binds 1 divalent metal cation per subunit.; |
| SUBCELLULAR LOCATION | Cytoplasm. Nucleus. |
| SIMILARITY | Belongs to the KAE1 / TsaD family. |
Keywords
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| Acyltransferase | |
| Cytoplasm | |
| Metal-binding | |
| Nucleus | |
| Transferase | |
| tRNA processing | |
| case <OC:Fungi> | |
| Activator | |
| Transcription | |
| Transcription regulation | |
| end case | |
Gene Ontology
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| 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 |
Cross-references
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| PROSITE | PS01016; GLYCOPROTEASE; 1; |
| Pfam | PF00814; Peptidase_M22; 1; |
| PRINTS | PR00789; OSIALOPTASE; 1; |
| NCBIfam | TIGR00329; Gcp_kae1; 1; |
Features
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| From: KAE1_PYRAB (Q9UXT7) | ||||||||||||
| Key | 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="ChEBI:CHEBI:60240" |
H | ||||||||
| BINDING | 111 | 111 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" |
H | ||||||||
| BINDING | 127 | 127 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" |
Y | ||||||||
| BINDING | 285 | 285 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" |
D | ||||||||
| BINDING | 159 | 159 | /ligand="substrate" | D | ||||||||
| BINDING | 172 | 172 | /ligand="substrate" | [GA] | ||||||||
| BINDING | 176 | 176 | /ligand="substrate" | [ED] | ||||||||
| BINDING | 257 | 257 | /ligand="substrate" | [NS] | ||||||||
Additional information
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| Size range | 325-407 amino acids |
| Related rules |
MF_01447 |
| Fusion | Nter: None Cter: 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). |