ID SUA5_YEAST Reviewed; 426 AA. AC P32579; D6VTY3; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 169. DE RecName: Full=Threonylcarbamoyl-AMP synthase; DE Short=TC-AMP synthase; DE EC=2.7.7.87; DE AltName: Full=L-threonylcarbamoyladenylate synthase; DE AltName: Full=Suppressor of upstream AUG protein 5; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein SUA5; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein SUA5; GN Name=SUA5; OrderedLocusNames=YGL169W; ORFNames=G1660; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF SER-107. RX PubMed=1325384; DOI=10.1093/genetics/131.4.791; RA Na J.G., Pinto I., Hampsey M.; RT "Isolation and characterization of SUA5, a novel gene required for normal RT growth in Saccharomyces cerevisiae."; RL Genetics 131:791-801(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8896267; RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1033::aid-yea983>3.0.co;2-v; RA Klima R., Coglievina M., Zaccaria P., Bertani I., Bruschi C.V.; RT "A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading RT frames have been detected in the DNA sequence of an 8.8 kb fragment of the RT left arm of chromosome VII of Saccharomyces cerevisiae."; RL Yeast 12:1033-1040(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [4] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [6] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] RP FUNCTION IN TELOMERE REPLICATION, AND DISRUPTION PHENOTYPE. RX PubMed=19369944; DOI=10.1038/emboj.2009.92; RA Meng F.-L., Hu Y., Shen N., Tong X.-J., Wang J., Ding J., Zhou J.-Q.; RT "Sua5p a single-stranded telomeric DNA-binding protein facilitates telomere RT replication."; RL EMBO J. 28:1466-1478(2009). RN [8] RP FUNCTION IN TRNA MODIFICATION. RX PubMed=19287007; DOI=10.1093/nar/gkp152; RA El Yacoubi B., Lyons B., Cruz Y., Reddy R., Nordin B., Agnelli F., RA Williamson J.R., Schimmel P., Swairjo M.A., de Crecy-Lagard V.; RT "The universal YrdC/Sua5 family is required for the formation of RT threonylcarbamoyladenosine in tRNA."; RL Nucleic Acids Res. 37:2894-2909(2009). RN [9] RP FUNCTION IN TRANSLATION, AND DISRUPTION PHENOTYPE. RX PubMed=19884342; DOI=10.1128/mcb.00754-09; RA Lin C.A., Ellis S.R., True H.L.; RT "The Sua5 protein is essential for normal translational regulation in RT yeast."; RL Mol. Cell. Biol. 30:354-363(2010). RN [10] RP FUNCTION. RX PubMed=21183954; DOI=10.1038/emboj.2010.343; RA Srinivasan M., Mehta P., Yu Y., Prugar E., Koonin E.V., Karzai A.W., RA Sternglanz R.; RT "The highly conserved KEOPS/EKC complex is essential for a universal tRNA RT modification, t6A."; RL EMBO J. 30:873-881(2011). RN [11] RP FUNCTION IN T(6)A TRNA MODIFICATION. RX PubMed=23258706; DOI=10.1093/nar/gks1287; RA Perrochia L., Crozat E., Hecker A., Zhang W., Bareille J., Collinet B., RA van Tilbeurgh H., Forterre P., Basta T.; RT "In vitro biosynthesis of a universal t6A tRNA modification in Archaea and RT Eukarya."; RL Nucleic Acids Res. 41:1953-1964(2013). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-70; LYS-93; ARG-95; RP ARG-174; SER-196; ASN-198 AND SER-234. RX PubMed=23620299; DOI=10.1093/nar/gkt322; RA Wan L.C., Mao D.Y., Neculai D., Strecker J., Chiovitti D., Kurinov I., RA Poda G., Thevakumaran N., Yuan F., Szilard R.K., Lissina E., Nislow C., RA Caudy A.A., Durocher D., Sicheri F.; RT "Reconstitution and characterization of eukaryotic N6- RT threonylcarbamoylation of tRNA using a minimal enzyme system."; RL Nucleic Acids Res. 41:6332-6346(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. Likely catalyzes the conversion of L-threonine, CC HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the CC acyladenylate intermediate, with the release of diphosphate. Required CC for normal translation, by ensuring translation fidelity at the level CC of codon recognition, appropriate translation initiation selection and CC maintenance of reading frame. Also involved in telomere replication. CC Binds to single-stranded telomeric (ssTG) DNA and positively regulates CC telomere length. {ECO:0000269|PubMed:19287007, CC ECO:0000269|PubMed:19369944, ECO:0000269|PubMed:19884342, CC ECO:0000269|PubMed:21183954, ECO:0000269|PubMed:23258706, CC ECO:0000269|PubMed:23620299}. 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:0000269|PubMed:23620299}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus CC {ECO:0000250}. Chromosome, telomere {ECO:0000269|PubMed:14562095}. CC -!- DISRUPTION PHENOTYPE: Causes increased leaky scanning through AUG CC codons, +1 frameshifting, and read-through of stop codons. Also causes CC progressive telomere shortening. {ECO:0000269|PubMed:19369944, CC ECO:0000269|PubMed:19884342}. CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}. 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; X64319; CAA45598.1; -; Genomic_DNA. DR EMBL; X85757; CAA59760.1; -; Genomic_DNA. DR EMBL; Z72691; CAA96881.1; -; Genomic_DNA. DR EMBL; BK006941; DAA07944.1; -; Genomic_DNA. DR PIR; S41991; S41991. DR RefSeq; NP_011346.1; NM_001181034.1. DR AlphaFoldDB; P32579; -. DR SMR; P32579; -. DR BioGRID; 33085; 79. DR DIP; DIP-2794N; -. DR IntAct; P32579; 2. DR MINT; P32579; -. DR STRING; 4932.YGL169W; -. DR MaxQB; P32579; -. DR PaxDb; 4932-YGL169W; -. DR PeptideAtlas; P32579; -. DR EnsemblFungi; YGL169W_mRNA; YGL169W; YGL169W. DR GeneID; 852707; -. DR KEGG; sce:YGL169W; -. DR AGR; SGD:S000003137; -. DR SGD; S000003137; SUA5. DR VEuPathDB; FungiDB:YGL169W; -. DR eggNOG; KOG3051; Eukaryota. DR GeneTree; ENSGT00390000015364; -. DR HOGENOM; CLU_031397_0_0_1; -. DR InParanoid; P32579; -. DR OMA; PLIERFW; -. DR OrthoDB; 5488554at2759; -. DR BioCyc; MetaCyc:G3O-30657-MONOMER; -. DR BioCyc; YEAST:G3O-30657-MONOMER; -. DR BRENDA; 2.7.7.87; 984. DR BioGRID-ORCS; 852707; 5 hits in 10 CRISPR screens. DR PRO; PR:P32579; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P32579; Protein. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005829; C:cytosol; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; IDA:SGD. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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; IDA:SGD. DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central. DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:SGD. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD. DR GO; GO:0000723; P:telomere maintenance; IMP:SGD. DR GO; GO:0070525; P:tRNA threonylcarbamoyladenosine metabolic process; IMP:SGD. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IDA:SGD. 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 1: Evidence at protein level; KW ATP-binding; Chromosome; Cytoplasm; DNA-binding; Nucleotide-binding; KW Nucleotidyltransferase; Nucleus; Reference proteome; Telomere; Transferase; KW Translation regulation; tRNA processing. FT CHAIN 1..426 FT /note="Threonylcarbamoyl-AMP synthase" FT /id="PRO_0000202013" FT DOMAIN 49..252 FT /note="YrdC-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00518" FT BINDING 72 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000250" FT BINDING 95 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 99 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000250" FT BINDING 170 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 174 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000250" FT BINDING 194 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000250" FT BINDING 196 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 234 FT /ligand="L-threonine" FT /ligand_id="ChEBI:CHEBI:57926" FT /evidence="ECO:0000250" FT BINDING 248 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT MUTAGEN 70 FT /note="T->A: Reduces t(6)A37 formation." FT /evidence="ECO:0000269|PubMed:23620299" FT MUTAGEN 93 FT /note="K->A: Severely impairs t(6)A37 formation." FT /evidence="ECO:0000269|PubMed:23620299" FT MUTAGEN 95 FT /note="R->A: Severely impairs t(6)A37 formation." FT /evidence="ECO:0000269|PubMed:23620299" FT MUTAGEN 107 FT /note="S->F: In SUA5-1; suppresses a translation initiation FT defect in a CYC1 allele at an aberrant ATG codon." FT /evidence="ECO:0000269|PubMed:1325384" FT MUTAGEN 174 FT /note="R->E: Severely impairs t(6)A37 formation." FT /evidence="ECO:0000269|PubMed:23620299" FT MUTAGEN 196 FT /note="S->A: Severely impairs t(6)A37 formation." FT /evidence="ECO:0000269|PubMed:23620299" FT MUTAGEN 198 FT /note="N->A: Severely impairs t(6)A37 formation." FT /evidence="ECO:0000269|PubMed:23620299" FT MUTAGEN 234 FT /note="S->V: Severely impairs t(6)A37 formation." FT /evidence="ECO:0000269|PubMed:23620299" FT MUTAGEN 423 FT /note="C->S: No phenotypes." SQ SEQUENCE 426 AA; 46538 MW; F7B54D4A07BCF8A0 CRC64; MYLGRHFLAM TSKALFDTKI LKVNPLSIIF SPDAHIDGSL PTITDPETEA ALVEAARIIR DTDETVAFPT ETVYGLGGSA LNDNSVLSIY RAKNRPSDNP LITHVSSIDQ LNRKVFNQPH LSGTSLFDNI PSIYRPLISS LWPGPLTILL PVPSSEHSAL SKLTTADQPT FAVRIPANPV ARALIALSDT PIAAPSANAS TRPSPTLASH VYHDLKDKIP IILDGGACKV GVESTVVDGL CNPPTLLRPG GFTYEEIVKL GGEAWSLCKV ENKKTVEKGE KVRTPGMKYR HYSPSAKVVL LVPHCEGDGI LKGVDRMERL KRLIETELKA NSNIKKIAIL TSLKLRDSDL QSKIFNEPDF SSKTFIIERL GQSGEEIQTN LFAALRKVDE NDKVDLIFVE GINEEGEGLA VMNRLRKAAA NNCIQF //