OSGP2_CAEEL
ID OSGP2_CAEEL Reviewed; 421 AA.
AC Q93170;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable 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=t(6)A37 threonylcarbamoyladenosine biosynthesis protein osgl-1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein osgl-1 {ECO:0000255|HAMAP-Rule:MF_03179};
DE Flags: Precursor;
GN Name=osgl-1 {ECO:0000255|HAMAP-Rule:MF_03179}; ORFNames=C01G10.10;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION IN MITOCHONDRIAL GENOME MAINTENANCE, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19578062; DOI=10.1093/nar/gkp557;
RA Oberto J., Breuil N., Hecker A., Farina F., Brochier-Armanet C.,
RA Culetto E., Forterre P.;
RT "Qri7/OSGEPL, the mitochondrial version of the universal Kae1/YgjD protein,
RT is essential for mitochondrial genome maintenance.";
RL Nucleic Acids Res. 37:5343-5352(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 (By similarity). Involved in mitochondrial genome
CC maintenance. {ECO:0000255|HAMAP-Rule:MF_03179,
CC ECO:0000269|PubMed:19578062}.
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: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03179}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03179,
CC ECO:0000269|PubMed:19578062}.
CC -!- DISRUPTION PHENOTYPE: Enhances longevity, resistance to oxidative
CC stress, and perturbs mitochondrial reticulum morphology.
CC {ECO:0000269|PubMed:19578062}.
CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000255|HAMAP-
CC Rule:MF_03179}.
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DR EMBL; Z81030; CAB02716.1; -; Genomic_DNA.
DR PIR; T18825; T18825.
DR RefSeq; NP_506713.1; NM_074312.4.
DR AlphaFoldDB; Q93170; -.
DR SMR; Q93170; -.
DR BioGRID; 45010; 6.
DR STRING; 6239.C01G10.10a; -.
DR EPD; Q93170; -.
DR PaxDb; Q93170; -.
DR PeptideAtlas; Q93170; -.
DR EnsemblMetazoa; C01G10.10a.1; C01G10.10a.1; WBGene00007237.
DR GeneID; 180015; -.
DR KEGG; cel:CELE_C01G10.10; -.
DR UCSC; C01G10.10; c. elegans.
DR CTD; 180015; -.
DR WormBase; C01G10.10a; CE20480; WBGene00007237; osgl-1.
DR eggNOG; KOG2707; Eukaryota.
DR GeneTree; ENSGT00940000153744; -.
DR HOGENOM; CLU_023208_1_2_1; -.
DR InParanoid; Q93170; -.
DR OMA; ANRMEHA; -.
DR OrthoDB; 656684at2759; -.
DR PhylomeDB; Q93170; -.
DR PRO; PR:Q93170; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007237; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW Acyltransferase; Metal-binding; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT CHAIN 23..421
FT /note="Probable tRNA N6-adenosine
FT threonylcarbamoyltransferase, mitochondrial"
FT /id="PRO_0000424535"
FT BINDING 133
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 156..160
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 308..309
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 336
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
FT BINDING 337
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03179"
SQ SEQUENCE 421 AA; 46276 MW; E084339219539C5E CRC64;
MNIPKILNNN LVLKRIFCRN YSVKVLGIET SCDDTAVAIV NEKREILSSE RYTERAIQRQ
QGGINPSVCA LQHRENLPRL IEKCLNDAGT SPKDLDAVAV TVTPGLVIAL KEGISAAIGF
AKKHRLPLIP VHHMRAHALS ILLVDDSVRF PFSAVLLSGG HALISVAEDV EKFKLYGQSV
SGSPGECIDK VARQLGDLGS EFDGIHVGAA VEILASRASA DGHLRYPIFL PNVPKANMNF
DQIKGSYLNL LERLRKNSET SIDIPDFCAS LQNTVARHIS SKLHIFFESL SEQEKLPKQL
VIGGGVAANQ YIFGAISKLS AAHNVTTIKV LLSLCTDNAE MIAYSGLLML VNRSEAIWWR
PNDIPDTIYA HARSDIGTDA SSEIIDTPRR KLVTSTIHGT ERIRFRNLDD FKKPKSPKTT
E
