P53960 (YNE0_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative alanyl-tRNA editing protein alaX
Short name=AlaX
Short name=AlaXp
Short name=AlaXp-II

Alternative name(s):
Alanyl-tRNA deacylase alaX

Gene names

Ordered Locus Names:	YNL040W
ORF Names:	N2679

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala) Potential. Ref.5
Cofactor	Binds 1 zinc ion per subunit Potential.
Miscellaneous	Present with 1470 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.
Caution	Conflicting data shows that it is not able to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala) in trans (Ref.4). Another paper shows that this protein can edit mischarged Ser-tRNA(Ala) but not Gly-tRNA(Ala) in trans (Ref.5). Experiments are not well detailed in either paper.

Ontologies

Keywords
Biological process	Protein biosynthesis
Ligand	Metal-binding Zinc
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from direct assay PubMed 11914276PubMed 14562095. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro Ser-tRNA(Ala) hydrolase activity Inferred from direct assay Ref.5. Source: UniProtKB alanine-tRNA ligase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 456	456	Putative alanyl-tRNA editing protein alaX		PRO_0000203457
Sites
	Metal binding	125	1	Zinc Potential
	Metal binding	129	1	Zinc Potential
	Metal binding	240	1	Zinc Potential
	Metal binding	244	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	P53960 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 5F636037485D1707	FASTA	456	50,964
	10 20 30 40 50 60 MPTPMTPVKV GALACQRNSF LFDGFKTLVV SCEPTKNKKG EIEGYEIELQ DTILFPEGGG 70 80 90 100 110 120 QPSDSGFLKI VEGNRNSSKI EKILVSHVSR FGLHAKHHVN DYIEPGTTVE VAVDEQKRMD 130 140 150 160 170 180 YMQQHTGQHL LSAILERNYK VDTVSWSMGG IITKKKPVLE PSDYFNYIEL NRKLTLDEIT 190 200 210 220 230 240 NVSDEINQLI INFPQEIIVE ERIGEETVDE VSTSKIPDDY DLSKGVLRTI HIGDIDSNPC 250 260 270 280 290 300 CGTHLKCTSQ IGSILILSNQ SAVRGSNSRL YFMCGKRVSL YAKSVNKILL DSKNLLSCSE 310 320 330 340 350 360 TQISEKITRQ TKQIQQLNKR EQYWIKRLAR TASEELMNTL KASGKKRAYF MEEEYGTLEL 370 380 390 400 410 420 LLQIHKEVSN FLKDDTEGYE IILCGYERQT NTGSLLILSE SGEKIANLAA NLGSILQNLK 430 440 450 GGGGKKGGKW QGKITSISNA EFAALSDYLS HDFASC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"Trans-editing of mischarged tRNAs." Ahel I., Korencic D., Ibba M., Soll D. Proc. Natl. Acad. Sci. U.S.A. 100:15422-15427(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LACK OF EDITING ACTIVITY ON MISCHARGED TRNA(ALA).
[5]	"Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma." Guo M., Chong Y.E., Shapiro R., Beebe K., Yang X.L., Schimmel P. Nature 462:808-812(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS TRNA(ALA) EDITING PROTEIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z71316 Genomic DNA. Translation: CAA95907.1. BK006947 Genomic DNA. Translation: DAA10505.1.
PIR	S62962.
RefSeq	NP_014358.3. NM_001182879.3.
3D structure databases
ProteinModelPortal	P53960.
SMR	P53960. Positions 49-276.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6332N.
IntAct	P53960. 1 interaction.
STRING	4932.YNL040W.
Proteomic databases
PaxDb	P53960.
PeptideAtlas	P53960.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL040W; YNL040W; YNL040W.
GeneID	855688.
KEGG	sce:YNL033W. sce:YNL040W.
Organism-specific databases
CYGD	YNL040w.
SGD	S000004985. YNL040W.
Phylogenomic databases
eggNOG	COG2872.
GeneTree	ENSGT00510000046493.
HOGENOM	HOG000230967.
KO	K07050.
OMA	TLSWSMG.
OrthoDB	EOG4VT961.
Gene expression databases
Genevestigator	P53960.
GermOnline	YNL040W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR018164. Ala-tRNA-synth_IIc_N. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
Pfam	PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	979998.

Entry information

Entry name

YNE0_YEAST

Accession

Primary (citable) accession number: P53960
Secondary accession number(s): D6W1D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program