HAMAP logo

HAMAP rule MF_03179

Send feedback

General rule information [?]

Accession MF_03179
Dates 17-OCT-2013 (Created)
1-JUN-2023 (Last updated, Version 16)
Name GCP1_TsaD
Scope(s) Eukaryota
Template(s) P43122 (QRI7_YEAST); O22145 (OSGP2_ARATH); O05518 (TSAD_BACSU); P05852 (TSAD_ECOLI); P36175 (TSAD_MANHA); Q2FWL2 (TSAD_STAA8); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_01445 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Fungi>
Identifier QRI7
Protein name RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial;
                 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>
Identifier OSGL1
Protein name RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial;
                 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
Identifier OSGP2
Protein name RecName: Full=Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial;
                 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 ;
end case
case <OC:Vertebrata>
Protein name + AltName: Full=O-sialoglycoprotein endopeptidase-like protein 1;
Gene name Name=OSGEPL1;
else case <OC:Viridiplantae>
Protein name + AltName: Full=Glycoprotease 1;
Gene name Name=GCP1;
else case <OC:Caenorhabditis>
Gene name Name=osgl-1;
else case <OC:Saccharomycotina>
Gene name Name=QRI7;
end case

Comments [?]

FUNCTIONRequired for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
CATALYTIC ACTIVITY Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; 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.;
case <OC:Vertebrata>
SUBUNITMonomer.
else
SUBUNITHomodimer.
end case
SUBCELLULAR LOCATIONMitochondrion.
SIMILARITYBelongs to the KAE1 / TsaD family.
case not <AnyFeature:TransitM>
MISCELLANEOUSThis protein may be expected to contain an N-terminal transit peptide but none has been predicted.
end case

Keywords [?]

Acyltransferase
Mitochondrion
Metal-binding
Transferase
tRNA processing

Gene Ontology [?]

GO:0005739; Cellular component:mitochondrion
GO:0016747; Molecular function:acyltransferase activity, transferring 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;
NCBIfam TIGR00329; Gcp_kae1; 1;
NCBIfam TIGR03723; T6A_YgjD; 1;
General TransitM; -; 0-1;

Features [?]

From: QRI7_YEAST (P43122)
Key From To Description Tag Condition FTGroup
BINDING 170 174 /ligand="substrate" x-x-S-G-x
BINDING 328 329 /ligand="substrate" x-N
BINDING 145 145 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"		 H
BINDING 149 149 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"		 H
BINDING 361 361 /ligand="a divalent metal cation"
/ligand_id="ChEBI:CHEBI:60240"		 D
BINDING 203 203 /ligand="substrate" D
BINDING 217 217 /ligand="substrate" [GA]
BINDING 221 221 /ligand="substrate" [DE]
BINDING 360 360 /ligand="substrate" [ST]
From: OSGL1_HUMAN (Q9H4B0)
Key From To Description Tag Condition FTGroup
case <OC:Mammalia>
MOD_RES 74 74 /note="N6-acetyllysine" K
MOD_RES 140 140 /note="N6-acetyllysine" K
MOD_RES 203 203 /note="N6-acetyllysine" K
MOD_RES 230 230 /note="N6-acetyllysine" K
MOD_RES 240 240 /note="N6-acetyllysine" K
MOD_RES 299 299 /note="N6-acetyllysine" K
end case

Additional information [?]

Size range 376-560 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments The well-known t(6)A modification appears to be a hydrolyzed artifact of natural cyclic t(6)A (ct(6)A) that occurs during the preparation and handling of tRNA in E.coli, B.subtilis and many other species including fungi and plants (PubMed:23242255). In these species, the t(6)A modification is processed further by dehydration into ct(6)A, a reaction catalyzed by tRNA threonylcarbamoyladenosine dehydratase (TcdA).



View rule in raw text format (no links)