ID   YRDC_RAT                Reviewed;         280 AA.
AC   Q499R4; Q5I0E4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000305};
DE            EC=2.7.7.87 {ECO:0000250|UniProtKB:Q86U90};
DE   Flags: Precursor;
GN   Name=Yrdc {ECO:0000312|RGD:708492};
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=Lung, and Prostate;
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).
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; BC088428; AAH88428.1; -; mRNA.
DR   EMBL; BC099797; AAH99797.1; -; mRNA.
DR   RefSeq; NP_783194.2; NM_175604.2.
DR   AlphaFoldDB; Q499R4; -.
DR   SMR; Q499R4; -.
DR   STRING; 10116.ENSRNOP00000037600; -.
DR   iPTMnet; Q499R4; -.
DR   PhosphoSitePlus; Q499R4; -.
DR   jPOST; Q499R4; -.
DR   PaxDb; Q499R4; -.
DR   PRIDE; Q499R4; -.
DR   GeneID; 319113; -.
DR   KEGG; rno:319113; -.
DR   UCSC; RGD:708492; rat.
DR   CTD; 79693; -.
DR   RGD; 708492; Yrdc.
DR   VEuPathDB; HostDB:ENSRNOG00000025424; -.
DR   eggNOG; KOG3051; Eukaryota.
DR   HOGENOM; CLU_031397_5_1_1; -.
DR   InParanoid; Q499R4; -.
DR   OMA; LVDAFWP; -.
DR   OrthoDB; 1027994at2759; -.
DR   PhylomeDB; Q499R4; -.
DR   TreeFam; TF314358; -.
DR   ChiTaRS; Yrdc; rat.
DR   PRO; PR:Q499R4; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000025424; Expressed in pancreas and 20 other tissues.
DR   Genevisible; Q499R4; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
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:0051051; P:negative regulation of transport; ISO:RGD.
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; Phosphoprotein;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..56
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           57..280
FT                   /note="Threonylcarbamoyl-AMP synthase"
FT                   /id="PRO_0000341404"
FT   DOMAIN          68..258
FT                   /note="YrdC-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00518"
FT   MOD_RES         61
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U90"
SQ   SEQUENCE   280 AA;  29231 MW;  7F3CA66A913C47DE CRC64;
     MSTARPCAGL RAAVAAGMGL SDGPAGSSRG CRLLRPPAPA PALPGARLLR LPESEAVEAA
     SPERSGWTEA LRAAVAELRA GAVVAVPTDT LYGLACSASC SAALSCVYRL KGRSEAKPLA
     VCLGRVADVY RYCQVRVPRE LLEDLFPGPV TLVMERSEEL NKDLNPFTPL VGIRIPDHAF
     MLDLAQMFGG PLALTSANLS SQASSLSVEE FQDLWPHLSL VIDGGPIGDS ESPECRLGST
     VVDLSVPGKF GIIRSGCALE NTTAILQGKY GLLPSQGSCS