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   27-MAR-2024, entry version 154.
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; 108.
DR   DIP; DIP-6332N; -.
DR   IntAct; P53960; 2.
DR   MINT; P53960; -.
DR   STRING; 4932.YNL040W; -.
DR   MaxQB; P53960; -.
DR   PaxDb; 4932-YNL040W; -.
DR   PeptideAtlas; P53960; -.
DR   EnsemblFungi; YNL040W_mRNA; YNL040W; YNL040W.
DR   GeneID; 855688; -.
DR   KEGG; sce:YNL040W; -.
DR   AGR; SGD:S000004985; -.
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; KYDTTSW; -.
DR   OrthoDB; 5490212at2759; -.
DR   BioCyc; YEAST:G3O-33076-MONOMER; -.
DR   BioGRID-ORCS; 855688; 2 hits in 10 CRISPR screens.
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   Gene3D; 2.40.30.130; -; 1.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR43462; ALANYL-TRNA EDITING PROTEIN; 1.
DR   PANTHER; PTHR43462:SF1; ALANYL-TRNA EDITING PROTEIN AARSD1; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR   SUPFAM; SSF50447; Translation proteins; 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
//