OSGEP_BOVIN
ID OSGEP_BOVIN Reviewed; 335 AA.
AC Q0VCI1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_03180};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase;
DE Short=t(6)A synthase;
DE AltName: Full=O-sialoglycoprotein endopeptidase {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP {ECO:0000255|HAMAP-Rule:MF_03180};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP {ECO:0000255|HAMAP-Rule:MF_03180};
GN Name=OSGEP {ECO:0000255|HAMAP-Rule:MF_03180};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal brain;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the EKC/KEOPS complex that is required for the
CC formation of a threonylcarbamoyl group on adenosine at position 37
CC (t(6)A37) in tRNAs that read codons beginning with adenine. The complex
CC is probably involved in the transfer of the threonylcarbamoyl moiety of
CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely
CC plays a direct catalytic role in this reaction, but requires other
CC protein(s) of the complex to fulfill this activity. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03180};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03180};
CC -!- SUBUNIT: Component of the EKC/KEOPS complex composed of at least GON7,
CC TP53RK, TPRKB, OSGEP and LAGE3; the whole complex dimerizes.
CC {ECO:0000250|UniProtKB:Q9NPF4, ECO:0000255|HAMAP-Rule:MF_03180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03180}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03180}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03180}.
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DR EMBL; BC120156; AAI20157.1; -; mRNA.
DR RefSeq; NP_001068787.1; NM_001075319.2.
DR AlphaFoldDB; Q0VCI1; -.
DR SMR; Q0VCI1; -.
DR STRING; 9913.ENSBTAP00000003557; -.
DR PaxDb; Q0VCI1; -.
DR PRIDE; Q0VCI1; -.
DR Ensembl; ENSBTAT00000003557; ENSBTAP00000003557; ENSBTAG00000002743.
DR GeneID; 507512; -.
DR KEGG; bta:507512; -.
DR CTD; 55644; -.
DR VEuPathDB; HostDB:ENSBTAG00000002743; -.
DR VGNC; VGNC:32470; OSGEP.
DR eggNOG; KOG2708; Eukaryota.
DR GeneTree; ENSGT00940000153744; -.
DR HOGENOM; CLU_023208_2_2_1; -.
DR InParanoid; Q0VCI1; -.
DR OMA; MRIMCEE; -.
DR OrthoDB; 829465at2759; -.
DR TreeFam; TF313621; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000002743; Expressed in caput epididymis and 104 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000408; C:EKC/KEOPS complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; ISS:UniProtKB.
DR HAMAP; MF_01446; Kae1; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR034680; Kae1_archaea_euk.
DR InterPro; IPR017860; Peptidase_M22_CS.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF14; PTHR11735:SF14; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
DR PROSITE; PS01016; GLYCOPROTEASE; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..335
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase"
FT /id="PRO_0000300637"
FT BINDING 109
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 113
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 130..134
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
FT BINDING 294
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03180"
SQ SEQUENCE 335 AA; 36502 MW; DA4A86337EF845C5 CRC64;
MPAVLGFEGS ANKIGVGVVR DGKVLANPRR TYVTPPGTGF LPGDTARHHR AVILDLLQEA
LTEAGLTSED IDCIAYTKGP GMGAPLVSVA VVARTVAQLW NKPLLGVNHC IGHIEMGRLI
TGATNPTVLY VSGGNTQVIA YSEHRYRIFG ETIDIAVGNC LDRFARVLKI SNDPSPGYNI
EQMAKRGKKL VELPYTVKGM DVSFSGILSF IEDVAQRMLA TGECTPEDLC FSLQETVFAM
LVEITERAMA HCGSQEALIV GGVGCNVRLQ EMMETMCQER GARLFATDER FCIDNGAMIA
QAGWEMFQAG HRTPLSESGI TQRYRTDEVE VTWRD
