ID Q758Q3_ASHGO Unreviewed; 418 AA. AC Q758Q3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 13-SEP-2023, entry version 102. DE RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000256|ARBA:ARBA00015492, ECO:0000256|PIRNR:PIRNR004930}; DE Short=TC-AMP synthase {ECO:0000256|PIRNR:PIRNR004930}; DE EC=2.7.7.87 {ECO:0000256|ARBA:ARBA00012584, ECO:0000256|PIRNR:PIRNR004930}; DE AltName: Full=L-threonylcarbamoyladenylate synthase {ECO:0000256|ARBA:ARBA00029774, ECO:0000256|PIRNR:PIRNR004930}; GN ORFNames=AGOS_AEL300C {ECO:0000313|EMBL:AAS52384.1}; OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OS (Yeast) (Eremothecium gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52384.1, ECO:0000313|Proteomes:UP000000591}; RN [1] {ECO:0000313|EMBL:AAS52384.1, ECO:0000313|Proteomes:UP000000591} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces RT cerevisiae genome."; RL Science 304:304-307(2004). RN [2] {ECO:0000313|Proteomes:UP000000591} RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056 RC {ECO:0000313|Proteomes:UP000000591}; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning CC with adenine. {ECO:0000256|PIRNR:PIRNR004930}. 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:0000256|ARBA:ARBA00001803, CC ECO:0000256|PIRNR:PIRNR004930}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|PIRNR:PIRNR004930}. CC -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000256|ARBA:ARBA00007663, CC ECO:0000256|PIRNR:PIRNR004930}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016818; AAS52384.1; -; Genomic_DNA. DR RefSeq; NP_984560.1; NM_209913.1. DR AlphaFoldDB; Q758Q3; -. DR STRING; 33169.AAS52384; -. DR EnsemblFungi; AAS52384; AAS52384; AGOS_AEL300C. DR GeneID; 4620735; -. DR KEGG; ago:AGOS_AEL300C; -. DR eggNOG; KOG3051; Eukaryota. DR HOGENOM; CLU_031397_0_0_1; -. DR InParanoid; Q758Q3; -. DR OMA; PLIERFW; -. DR OrthoDB; 5488554at2759; -. DR Proteomes; UP000000591; Chromosome V. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC. DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central. DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IEA:EnsemblFungi. 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:0000723; P:telomere maintenance; IEA:EnsemblFungi. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:EnsemblFungi. DR Gene3D; 3.90.870.10; DHBP synthase; 1. DR Gene3D; 3.40.50.11030; Threonylcarbamoyl-AMP synthase, C-terminal domain; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR006070; Sua5-like_dom. DR InterPro; IPR038385; Sua5/YwlC_C. DR InterPro; IPR005145; Sua5_C. DR InterPro; IPR010923; T(6)A37_SUA5. DR NCBIfam; TIGR00057; L-threonylcarbamoyladenylate synthase; 1. DR PANTHER; PTHR17490; SUA5; 1. DR PANTHER; PTHR17490:SF16; THREONYLCARBAMOYL-AMP SYNTHASE; 1. DR Pfam; PF03481; Sua5_C; 1. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR PIRSF; PIRSF004930; Tln_factor_SUA5; 1. DR SUPFAM; SSF55821; YrdC/RibB; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR004930, ECO:0000256|PIRSR:PIRSR004930- KW 1}; Cytoplasm {ECO:0000256|PIRNR:PIRNR004930}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004930, KW ECO:0000256|PIRSR:PIRSR004930-1}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004930}; KW Reference proteome {ECO:0000313|Proteomes:UP000000591}; KW Transferase {ECO:0000256|PIRNR:PIRNR004930}; KW tRNA processing {ECO:0000256|PIRNR:PIRNR004930}. FT DOMAIN 52..251 FT /note="YrdC-like" FT /evidence="ECO:0000259|PROSITE:PS51163" FT BINDING 75 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 98 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 102 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 107 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 169 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 173 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 193 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 195 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 203 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 233 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 247 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" FT BINDING 291 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR004930-1" SQ SEQUENCE 418 AA; 45932 MW; F38E88F5B47D3F62 CRC64; MQRSFSFLRR SGFHSAMSYN TKVLRVDPSA IHFSATAHID GSLPRISDPE TEKHLLEAAR LIRDDGETVA FPTETVYGLG GSSLNDASVR NIYKAKNRPS DNPLISHVSS IAQLNRRIYQ QDREGDVLRN IPVVYHELVR QLWPGPLTIL LPINEETALS VLTTAGQPTF AVRIPADPVA RALIALSDTP IAAPSANVST RPSPTAAEHV YHDLKGKIPL ILDGGSCRVG VESTVIDGLV NPPMLLRPGG FTYEEIIELG GEQWSHCKVE NRMTVGSGEK VRTPGMKYKH YSPRASTVAF APINDDLPTS ERMKIVTSEI MKYMTSHGTD KRQKVGLLTS IMFPNNLLES ITDEVDVVVY SLGSSGKEVQ SNLFAMLRRL DEEDEVDLIF VEGISDRNEG LAVMNRLRKA AGGNVVSF //