ID Q758Q3_ASHGO Unreviewed; 418 AA. AC Q758Q3; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 07-SEP-2016, entry version 77. DE RecName: Full=Threonylcarbamoyl-AMP synthase {ECO:0000256|PIRNR:PIRNR004930}; DE Short=TC-AMP synthase {ECO:0000256|PIRNR:PIRNR004930}; DE EC=2.7.7.87 {ECO:0000256|PIRNR:PIRNR004930}; DE AltName: Full=L-threonylcarbamoyladenylate synthase {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 OS Y-1056) (Yeast) (Eremothecium gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; 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 RT Saccharomyces 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 CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. {ECO:0000256|PIRNR:PIRNR004930}. CC -!- CATALYTIC ACTIVITY: L-threonine + ATP + HCO(3)(-) = L- CC threonylcarbamoyladenylate + diphosphate + H(2)O. CC {ECO:0000256|PIRNR:PIRNR004930}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR004930}. CC -!- SIMILARITY: Belongs to the SUA5 family. 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 ProteinModelPortal; Q758Q3; -. DR EnsemblFungi; AAS52384; AAS52384; AGOS_AEL300C. DR GeneID; 4620735; -. DR KEGG; ago:AGOS_AEL300C; -. DR HOGENOM; HOG000076160; -. DR InParanoid; Q758Q3; -. DR KO; K07566; -. DR OMA; HYSPAVP; -. DR OrthoDB; EOG092C2HER; -. DR Proteomes; UP000000591; Chromosome V. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. 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; IBA:GO_Central. DR Gene3D; 3.90.870.10; -; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR005145; SUA5. DR InterPro; IPR010923; t(6)A37_SUA5. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF03481; SUA5; 1. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR PIRSF; PIRSF004930; Tln_factor_SUA5; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00057; TIGR00057; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PIRNR:PIRNR004930, KW ECO:0000256|PIRSR:PIRSR004930-1}; KW Complete proteome {ECO:0000313|Proteomes:UP000000591}; KW 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 YrdC-like. {ECO:0000259|PROSITE:PS51163}. FT BINDING 75 75 L-threonine. {ECO:0000256|PIRSR: FT PIRSR004930-1}. FT BINDING 98 98 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 102 102 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 107 107 L-threonine. {ECO:0000256|PIRSR: FT PIRSR004930-1}. FT BINDING 169 169 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 173 173 L-threonine. {ECO:0000256|PIRSR: FT PIRSR004930-1}. FT BINDING 193 193 L-threonine; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 195 195 ATP; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 203 203 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 233 233 L-threonine. {ECO:0000256|PIRSR: FT PIRSR004930-1}. FT BINDING 247 247 ATP. {ECO:0000256|PIRSR:PIRSR004930-1}. FT BINDING 291 291 ATP. {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 //