AC   MF_03179;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_01445; -; 1; level=0
XX
Names: GCP1_TsaD
XX
case <OC:Fungi>
ID   QRI7
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial;
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>
ID   OSGL1
DE   RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial;
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
ID   OSGP2
DE   RecName: Full=Probable tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial;
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>;
end case
case <OC:Vertebrata>
DE   + AltName: Full=O-sialoglycoprotein endopeptidase-like protein 1;
GN   Name=OSGEPL1;
else case <OC:Viridiplantae>
DE   + AltName: Full=Glycoprotease 1;
GN   Name=GCP1;
else case <OC:Caenorhabditis>
GN   Name=osgl-1;
else case <OC:Saccharomycotina>
GN   Name=QRI7;
end case
XX
CC   -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on
CC       adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read
CC       codons beginning with adenine. Probably involved in the transfer of the
CC       threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6
CC       group of A37. Involved in mitochondrial genome maintenance.
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.;
case <OC:Vertebrata>
CC   -!- SUBUNIT: Monomer.
else
CC   -!- SUBUNIT: Homodimer.
end case
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the KAE1 / TsaD family.
case not <AnyFeature:TransitM>
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted.
end case
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
DR   NCBIfam; TIGR03723; T6A_YgjD; 1; trigger=no
DR   General; TransitM; -; 0-1; trigger=yes
XX
KW   Acyltransferase
KW   Mitochondrion
KW   Metal-binding
KW   Transferase
KW   tRNA processing
XX
GO   GO:0005739; C:mitochondrion
GO   GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups
GO   GO:0002949; P:tRNA threonylcarbamoyladenosine modification
XX
FT   From: QRI7_YEAST (P43122)
FT   BINDING         170..174
FT                   /ligand="substrate"
FT   Condition: x-x-S-G-x
FT   BINDING         328..329
FT                   /ligand="substrate"
FT   Condition: x-N
FT   BINDING         145
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         149
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         361
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: D
FT   BINDING         203
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         217
FT                   /ligand="substrate"
FT   Condition: [GA]
FT   BINDING         221
FT                   /ligand="substrate"
FT   Optional; Condition: [DE]
FT   BINDING         360
FT                   /ligand="substrate"
FT   Condition: [ST]
FT   From: OSGL1_HUMAN (Q9H4B0)
case <OC:Mammalia>
FT   MOD_RES          74
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         140
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         203
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         230
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         240
FT                   /note="N6-acetyllysine"
FT   Condition: K
FT   MOD_RES         299
FT                   /note="N6-acetyllysine"
FT   Condition: K
end case
XX
Size: 376-560;
Related: None;
Template: P43122; O22145; O05518; P05852; P36175; Q2FWL2;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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).
XX
# Revision 1.16 2023/06/01
//