OSGL1_RAT
ID OSGL1_RAT Reviewed; 414 AA.
AC Q4V7F3;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03179};
DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE Short=t(6)A synthase {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=O-sialoglycoprotein endopeptidase-like protein 1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE Flags: Precursor;
GN Name=Osgepl1 {ECO:0000255|HAMAP-Rule:MF_03179};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=19694617; DOI=10.1042/bj20091023;
RA Haussuehl K., Huesgen P.F., Meier M., Dessi P., Glaser E., Adamski J.,
RA Adamska I.;
RT "Eukaryotic GCP1 is a conserved mitochondrial protein required for
RT progression of embryo development beyond the globular stage in Arabidopsis
RT thaliana.";
RL Biochem. J. 423:333-341(2009).
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 {ECO:0000255|HAMAP-Rule:MF_03179}.
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_03179};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03179};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03179};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179,
CC ECO:0000269|PubMed:19694617}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03179}.
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DR EMBL; BC097950; AAH97950.1; -; mRNA.
DR RefSeq; NP_001019958.1; NM_001024787.1.
DR RefSeq; XP_017451887.1; XM_017596398.1.
DR AlphaFoldDB; Q4V7F3; -.
DR SMR; Q4V7F3; -.
DR STRING; 10116.ENSRNOP00000005408; -.
DR PaxDb; Q4V7F3; -.
DR PRIDE; Q4V7F3; -.
DR Ensembl; ENSRNOT00000005408; ENSRNOP00000005408; ENSRNOG00000004001.
DR GeneID; 314548; -.
DR KEGG; rno:314548; -.
DR UCSC; RGD:1305575; rat.
DR CTD; 64172; -.
DR RGD; 1305575; Osgepl1.
DR eggNOG; KOG2707; Eukaryota.
DR GeneTree; ENSGT00940000153744; -.
DR HOGENOM; CLU_023208_1_2_1; -.
DR InParanoid; Q4V7F3; -.
DR OMA; HLEGHIY; -.
DR OrthoDB; 656684at2759; -.
DR PhylomeDB; Q4V7F3; -.
DR PRO; PR:Q4V7F3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000004001; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; Q4V7F3; RN.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; ISS:UniProtKB.
DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; ISS:UniProtKB.
DR HAMAP; MF_01445; TsaD; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000905; Gcp-like_dom.
DR InterPro; IPR017861; KAE1/TsaD.
DR InterPro; IPR022450; TsaD.
DR PANTHER; PTHR11735; PTHR11735; 1.
DR PANTHER; PTHR11735:SF6; PTHR11735:SF6; 1.
DR Pfam; PF00814; TsaD; 1.
DR PRINTS; PR00789; OSIALOPTASE.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00329; gcp_kae1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Metal-binding; Mitochondrion;
KW Reference proteome; Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT CHAIN 30..414
FT /note="tRNA N6-adenosine threonylcarbamoyltransferase,
FT mitochondrial"
FT /id="PRO_0000307780"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 151
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 169..173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 329..330
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 358
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4B0"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4B0"
FT MOD_RES 203
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4B0"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4B0"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6PEB4"
SQ SEQUENCE 414 AA; 44851 MW; DE3B69028E0AAF9F CRC64;
MLMLSKTAGA IPRPPRSNVR GFIRRFNVQP RALFHHKLVL GIETSCDDTA AAVVDETGNV
LGEALHSQTE VHLKTGGIVP PVAQQLHREN IQRIVEEALS ASGVSPSDLS AIATTIKPGL
ALSLGVGLSF SVQLVNQFKK PFIPIHHMEA HALTIRLTHK VGFPFLVLLI SGGHCLLALV
QSVSDFLLLG KSLDIAPGDM LDKVARRLSL IKHPECSTMS GGKAIEHLAK EGNRFHFTIN
PPMQNAKNCD FSFTGLQHVT DKLITHKEKE EGIEKGQILS SAADIAAAVQ HATACHLAKR
THRAILFCQQ KNLLSPANAV LVVSGGVASN LYIRRALEIV ANATQCTLLC PPPRLCTDNG
IMIAWNGIER LRAGLGILHD VEDIRYEPKC PLGIDISREV AEAAIKVPRL KMTL
