YNE0_YEAST
ID YNE0_YEAST Reviewed; 456 AA.
AC P53960; D6W1D9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative alanyl-tRNA editing protein alaX;
DE Short=AlaX;
DE Short=AlaXp;
DE Short=AlaXp-II;
DE AltName: Full=Alanyl-tRNA deacylase alaX;
GN OrderedLocusNames=YNL040W; ORFNames=N2679;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
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 [3]
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 [4]
RP LACK OF EDITING ACTIVITY ON MISCHARGED TRNA(ALA).
RX PubMed=14663147; DOI=10.1073/pnas.2136934100;
RA Ahel I., Korencic D., Ibba M., Soll D.;
RT "Trans-editing of mischarged tRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15422-15427(2003).
RN [5]
RP FUNCTION AS TRNA(ALA) EDITING PROTEIN.
RX PubMed=20010690; DOI=10.1038/nature08612;
RA Guo M., Chong Y.E., Shapiro R., Beebe K., Yang X.L., Schimmel P.;
RT "Paradox of mistranslation of serine for alanine caused by AlaRS
RT recognition dilemma.";
RL Nature 462:808-812(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: May function in trans to edit the amino acid moiety from
CC incorrectly charged tRNA(Ala). {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Alax-L subfamily. {ECO:0000305}.
CC -!- CAUTION: Conflicting data shows that it is not able to edit the amino
CC acid moiety from incorrectly charged Ser-tRNA(Ala) in trans
CC (PubMed:14663147). Another paper shows that this protein can edit
CC mischarged Ser-tRNA(Ala) but not Gly-tRNA(Ala) in trans
CC (PubMed:20010690). Experiments are not well detailed in either paper.
CC {ECO:0000305|PubMed:14663147, ECO:0000305|PubMed:20010690}.
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DR EMBL; Z71316; CAA95907.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10505.1; -; Genomic_DNA.
DR PIR; S62962; S62962.
DR RefSeq; NP_014358.3; NM_001182879.3.
DR AlphaFoldDB; P53960; -.
DR SMR; P53960; -.
DR BioGRID; 35784; 107.
DR DIP; DIP-6332N; -.
DR IntAct; P53960; 2.
DR MINT; P53960; -.
DR STRING; 4932.YNL040W; -.
DR MaxQB; P53960; -.
DR PaxDb; P53960; -.
DR PRIDE; P53960; -.
DR EnsemblFungi; YNL040W_mRNA; YNL040W; YNL040W.
DR GeneID; 855688; -.
DR KEGG; sce:YNL040W; -.
DR SGD; S000004985; YNL040W.
DR VEuPathDB; FungiDB:YNL040W; -.
DR eggNOG; KOG2105; Eukaryota.
DR GeneTree; ENSGT00940000156241; -.
DR HOGENOM; CLU_004485_7_1_1; -.
DR InParanoid; P53960; -.
DR OMA; DREFKYD; -.
DR BioCyc; YEAST:G3O-33076-MON; -.
DR PRO; PR:P53960; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53960; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:InterPro.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..456
FT /note="Putative alanyl-tRNA editing protein alaX"
FT /id="PRO_0000203457"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
SQ SEQUENCE 456 AA; 50964 MW; 5F636037485D1707 CRC64;
MPTPMTPVKV GALACQRNSF LFDGFKTLVV SCEPTKNKKG EIEGYEIELQ DTILFPEGGG
QPSDSGFLKI VEGNRNSSKI EKILVSHVSR FGLHAKHHVN DYIEPGTTVE VAVDEQKRMD
YMQQHTGQHL LSAILERNYK VDTVSWSMGG IITKKKPVLE PSDYFNYIEL NRKLTLDEIT
NVSDEINQLI INFPQEIIVE ERIGEETVDE VSTSKIPDDY DLSKGVLRTI HIGDIDSNPC
CGTHLKCTSQ IGSILILSNQ SAVRGSNSRL YFMCGKRVSL YAKSVNKILL DSKNLLSCSE
TQISEKITRQ TKQIQQLNKR EQYWIKRLAR TASEELMNTL KASGKKRAYF MEEEYGTLEL
LLQIHKEVSN FLKDDTEGYE IILCGYERQT NTGSLLILSE SGEKIANLAA NLGSILQNLK
GGGGKKGGKW QGKITSISNA EFAALSDYLS HDFASC
