P40825 (SYA_YEAST) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 116.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Alanine--tRNA ligase, mitochondrial EC=6.1.1.7 Alternative name(s): Alanyl-tRNA synthetase Short name=AlaRS | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome] | ||||||
| Taxonomic identifier | 559292 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › ![]() |
Protein attributes
| Sequence length | 983 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain By similarity. Ref.4 |
| Catalytic activity | ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_03133 |
| Cofactor | Binds 1 zinc ion per subunit Potential. |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Isoform Cytoplasmic: Cytoplasm Ref.5 Ref.7 Ref.9. Isoform Mitochondrial: Mitochondrion Ref.5 Ref.7 Ref.9. |
| Domain | Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP-Rule MF_03133 |
| Miscellaneous | Present with 33800 molecules/cell in log phase SD medium. HAMAP-Rule MF_03133 |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
| Sequence caution | The sequence AAC49007.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA89980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAA99658.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence DAA11096.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm Mitochondrion |
| Coding sequence diversity | Alternative initiation |
| Domain | Transit peptide |
| Ligand | ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | mitochondrial alanyl-tRNA aminoacylation Inferred by curator Ref.9. Source: SGD |
| Cellular_component | mitochondrion Inferred from direct assay Ref.7Ref.9PubMed 16823961. Source: SGD |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activityInferred from genetic interaction Ref.4. Source: SGD metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW tRNA bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform Mitochondrial (identifier: P40825-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Note: Produced by alternative initiation at 2 upstream redundant non-AUG codons in-frame of the first AUG used for isoform Cytoplasmic. | ||||||
| Isoform Cytoplasmic (identifier: P40825-2) The sequence of this isoform differs from the canonical sequence as follows: 1-25: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 24 | 24 | Mitochondrion HAMAP-Rule MF_03133 | ||||||
| Chain | 25 – 983 | 959 | Alanine--tRNA ligase, mitochondrial HAMAP-Rule MF_03133 | PRO_0000075287 | |||||
Sites | |||||||||
| Metal binding | 625 | 1 | Zinc Potential | ||||||
| Metal binding | 629 | 1 | Zinc Potential | ||||||
| Metal binding | 744 | 1 | Zinc Potential | ||||||
| Metal binding | 748 | 1 | Zinc Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 504 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 975 | 1 | Phosphoserine Ref.10 Ref.11 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 25 | 25 | Missing in isoform Cytoplasmic. | VSP_040236 | |||||
Experimental info | |||||||||
| Sequence conflict | 4 – 7 | 4 | TTGL → NYRI in AAC49007. Ref.4 | ||||||
| Sequence conflict | 16 | 1 | Missing in AAC49007. Ref.4 | ||||||
| Sequence conflict | 161 | 1 | R → S in AAC49007. Ref.4 | ||||||
| Sequence conflict | 490 – 492 | 3 | KDQ → RTK in AAC49007. Ref.4 | ||||||
| Sequence conflict | 865 – 866 | 2 | FE → LQ in AAC49007. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces cerevisiae chromosome XV: similarity to part of chromosome I." Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H. Yeast 12:999-1004(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. Kleine K.Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679. |
| [3] | Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c. |
| [4] | "Wide cross-species aminoacyl-tRNA synthetase replacement in vivo: yeast cytoplasmic alanine enzyme replaced by human polymyositis serum antigen." Ripmaster T.L., Shiba K., Schimmel P. Proc. Natl. Acad. Sci. U.S.A. 92:4932-4936(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-983, FUNCTION. |
| [5] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [6] | "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]. |
| [7] | "The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [8] | "Translation of a yeast mitochondrial tRNA synthetase initiated at redundant non-AUG codons." Tang H.L., Yeh L.S., Chen N.K., Ripmaster T., Schimmel P., Wang C.C. J. Biol. Chem. 279:49656-49663(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE INITIATION. |
| [9] | "An unusual pattern of protein expression and localization of yeast alanyl-tRNA synthetase isoforms." Huang H.Y., Tang H.L., Chao H.Y., Yeh L.S., Wang C.C. Mol. Microbiol. 60:189-198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [10] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-975, MASS SPECTROMETRY. |
| [11] | "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504 AND SER-975, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z49821 Genomic DNA. Translation: CAA89980.1. Different initiation. Z75243 Genomic DNA. Translation: CAA99658.1. Different initiation. U18672 Genomic DNA. Translation: AAC49007.1. Different initiation. BK006948 Genomic DNA. Translation: DAA11096.1. Different initiation. |
| PIR | S62065. |
| RefSeq | NP_014980.3. NM_001183755.3. |
3D structure databases | |
| ProteinModelPortal | P40825. |
| SMR | P40825. Positions 29-778. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-6286N. |
| IntAct | P40825. 10 interactions. |
| MINT | MINT-688621. |
| STRING | 4932.YOR335C. |
Proteomic databases | |
| PaxDb | P40825. |
| PeptideAtlas | P40825. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 854513. |
| KEGG | sce:YOR335C. sce:YOR337W. |
Organism-specific databases | |
| CYGD | YOR335c. |
| SGD | S000005862. ALA1. |
Phylogenomic databases | |
| eggNOG | COG0013. |
| KO | K01872. |
| OMA | EWFDFPK. |
| OrthoDB | EOG44BF9B. |
Gene expression databases | |
| Genevestigator | P40825. |
| GermOnline | YOR335C. Saccharomyces cerevisiae. |
Family and domain databases | |
| HAMAP | MF_00036_B. Ala_tRNA_synth_B. |
| InterPro | IPR002318. Ala-tRNA-lgiase_IIc. IPR018162. Ala-tRNA-ligase_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR023033. Ala_tRNA_ligase_euk/bac. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view] |
| PANTHER | PTHR11777:SF6. PTHR11777:SF6. 1 hit. |
| Pfam | PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view] |
| PRINTS | PR00980. TRNASYNTHALA. |
| SMART | SM00863. tRNA_SAD. 1 hit. [Graphical view] |
| SUPFAM | SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit. |
| TIGRFAMs | TIGR00344. alaS. 1 hit. |
| PROSITE | PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 976870. |
Entry information
| Entry name | SYA_YEAST | ||||||||
| Accession | Primary (citable) accession number: P40825 Secondary accession number(s): D6W330 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |
| Yeast chromosome XV Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names |
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with
