ID   YRDC_BOVIN              Reviewed;         276 AA.
AC   Q0VC80;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000305};
DE            EC=2.7.7.87 {ECO:0000250|UniProtKB:Q86U90};
DE   Flags: Precursor;
GN   Name=YRDC;
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=Hippocampus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytoplasmic and mitochondrial threonylcarbamoyl-AMP synthase
CC       required for the formation of a threonylcarbamoyl group on adenosine at
CC       position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
CC       Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to
CC       give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate,
CC       with the release of diphosphate. Participates in t(6)A37 formation in
CC       cytoplasmic and mitochondrial tRNAs (By similarity). May regulate the
CC       activity of some transporters (By similarity).
CC       {ECO:0000250|UniProtKB:Q3U5F4, ECO:0000250|UniProtKB:Q86U90}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-
CC         threonylcarbamoyladenylate; Xref=Rhea:RHEA:36407, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:73682; EC=2.7.7.87;
CC         Evidence={ECO:0000250|UniProtKB:Q86U90};
CC   -!- SUBUNIT: Interacts with RSC1A1. {ECO:0000250|UniProtKB:Q3U5F4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86U90}.
CC       Mitochondrion {ECO:0000250|UniProtKB:Q86U90}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q3U5F4}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q3U5F4}. Note=A large fraction localizes in the
CC       cytoplasm, whereas a smaller fraction is imported to mitochondria.
CC       {ECO:0000250|UniProtKB:Q86U90}.
CC   -!- DOMAIN: The mitochondrial targeting sequence (MTS) is weak and only
CC       mediates import of a small fraction of YRDC in mitochondria.
CC       {ECO:0000250|UniProtKB:Q86U90}.
CC   -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}.
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DR   EMBL; BC120307; AAI20308.1; -; mRNA.
DR   RefSeq; NP_001069018.1; NM_001075550.1.
DR   AlphaFoldDB; Q0VC80; -.
DR   SMR; Q0VC80; -.
DR   STRING; 9913.ENSBTAP00000008530; -.
DR   PaxDb; Q0VC80; -.
DR   PRIDE; Q0VC80; -.
DR   Ensembl; ENSBTAT00000008529; ENSBTAP00000008530; ENSBTAG00000006510.
DR   GeneID; 512062; -.
DR   KEGG; bta:512062; -.
DR   CTD; 79693; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006510; -.
DR   VGNC; VGNC:37038; YRDC.
DR   eggNOG; KOG3051; Eukaryota.
DR   GeneTree; ENSGT00390000015364; -.
DR   HOGENOM; CLU_031397_5_1_1; -.
DR   InParanoid; Q0VC80; -.
DR   OMA; MLYPTDT; -.
DR   OrthoDB; 1027994at2759; -.
DR   TreeFam; TF314358; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000006510; Expressed in semen and 105 other tissues.
DR   ExpressionAtlas; Q0VC80; baseline.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR   GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR   GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; ISS:UniProtKB.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR006070; YrdC-like_dom.
DR   Pfam; PF01300; Sua5_yciO_yrdC; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00057; TIGR00057; 1.
DR   PROSITE; PS51163; YRDC; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Membrane; Mitochondrion; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..53
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           54..276
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000341401"
FT   DOMAIN          65..255
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT   REGION          22..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  28893 MW;  797E6BD82305CD10 CRC64;
     MSPARPCRGL RAVVAASMGL SEGPAGSARS GRLLRSPSPT PGARLLRLPG SGAGRAANPE
     RGGWTEALRA AVAELRAGAV VAVPTDTLYG LACSASCSEA LGAVYRVKGR SETKPLAVCL
     GRVADVYRYC HVRVPEGLLK DLLPGPVTLV MERSEELNKD LNPFTPLVGI RIPDHAFMQD
     LAQMFGGPLA LTSANLSSQS SSLNVEEFQD LWPHLSLIID GGPIGDGQSP ECRLGSTVVD
     LSVPGKFGII RPGCALESTS AILQEYGLLP SHGSCW