SUA5_YEAST
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 03-AUG-2022, entry version 162.
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}.
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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; 76.
DR DIP; DIP-2794N; -.
DR IntAct; P32579; 2.
DR MINT; P32579; -.
DR STRING; 4932.YGL169W; -.
DR MaxQB; P32579; -.
DR PaxDb; P32579; -.
DR PRIDE; P32579; -.
DR EnsemblFungi; YGL169W_mRNA; YGL169W; YGL169W.
DR GeneID; 852707; -.
DR KEGG; sce:YGL169W; -.
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 BioCyc; YEAST:G3O-30657-MON; -.
DR BRENDA; 2.7.7.87; 984.
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; 3.40.50.11030; -; 1.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR038385; Sua5/YwlC_C.
DR InterPro; IPR005145; Sua5_C.
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 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
