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P53960 (YNE0_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Putative alanyl-tRNA editing protein alaX
PRO_0000203457

Sites

Metal binding1251Zinc Potential
Metal binding1291Zinc Potential
Metal binding2401Zinc Potential
Metal binding2441Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
P53960 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5F636037485D1707

FASTA45650,964
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
[6]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z71316 Genomic DNA. Translation: CAA95907.1.
BK006947 Genomic DNA. Translation: DAA10505.1.
PIRS62962.
RefSeqNP_014358.3. NM_001182879.3.

3D structure databases

ProteinModelPortalP53960.
SMRP53960. Positions 13-276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35784. 26 interactions.
DIPDIP-6332N.
IntActP53960. 1 interaction.
MINTMINT-4499377.
STRING4932.YNL040W.

Proteomic databases

PaxDbP53960.
PeptideAtlasP53960.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL040W; YNL040W; YNL040W.
GeneID855688.
KEGGsce:YNL040W.

Organism-specific databases

CYGDYNL040w.
SGDS000004985. YNL040W.

Phylogenomic databases

eggNOGCOG2872.
GeneTreeENSGT00510000046493.
HOGENOMHOG000230967.
KOK07050.
OMAYIELPEK.
OrthoDBEOG73FQWN.

Enzyme and pathway databases

BioCycYEAST:G3O-33076-MONOMER.

Gene expression databases

GenevestigatorP53960.

Family and domain databases

InterProIPR018164. Ala-tRNA-synth_IIc_N.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
ProtoNetSearch...

Other

NextBio979998.
PROP53960.

Entry information

Entry nameYNE0_YEAST
AccessionPrimary (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: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families