Reviewed,
UniProtKB/Swiss-Prot P36428 (SYA_ARATH)
Last modified
November 3, 2009.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alanyl-tRNA synthetase, mitochondrial EC=6.1.1.7 Alternative name(s): Alanine--tRNA ligase Short name=AlaRS | ||||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 1003 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)
| Catalytic activity | ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). |
| Subunit structure | Monomer By similarity. |
| Subcellular location | |
| Domain | The C-terminal 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 Potential. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm Mitochondrion |
| Coding sequence diversity | Alternative initiation |
| Domain | Transit peptide |
| Ligand | ATP-binding Nucleotide-binding RNA-binding tRNA-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro response to cadmium ionInferred from expression pattern. Source: TAIR |
| Cellular component | chloroplast Inferred from direct assay. Source: TAIR mitochondrionInferred from direct assay. Source: TAIR |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activityInferred from electronic annotation. Source: EC nucleic acid bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform Mitochondrial (identifier: P36428-1) 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. | ||||||
| Isoform Cytoplasmic (identifier: P36428-2) The sequence of this isoform differs from the canonical sequence as follows: 1-48: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 49 | 49 | Mitochondrion | ||||||
| Chain | 50 – 1003 | 954 | Alanyl-tRNA synthetase, mitochondrial | PRO_0000035793 | |||||
Amino acid modifications | |||||||||
| Modified residue | 52 | 1 | Phosphoserine Ref.5 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 48 | 48 | Missing in isoform Cytoplasmic. | VSP_018903 | |||||
Experimental info | |||||||||
| Sequence conflict | 194 | 1 | G → R in CAA80380. Ref.1 | ||||||
| Sequence conflict | 194 | 1 | G → R in CAA80381. Ref.1 | ||||||
| Sequence conflict | 731 | 1 | V → A in CAA80380. Ref.1 | ||||||
| Sequence conflict | 731 | 1 | V → A in CAA80381. Ref.1 | ||||||
| Sequence conflict | 910 | 1 | R → Q in CAA80380. Ref.1 | ||||||
| Sequence conflict | 910 | 1 | R → Q in CAA80381. Ref.1 | ||||||
| Sequence conflict | 985 | 1 | S → F in CAA73145. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The same Arabidopsis gene encodes both cytosolic and mitochondrial alanyl-tRNA synthetases." Mireau H., Lancelin D., Small I. Plant Cell 8:1027-1039(1996) [PubMed: 8672889] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CYTOPLASMIC AND MITOCHONDRIAL). Strain: cv. Columbia. |
| [2] | "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. Davis R.W.Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC). Strain: cv. Columbia. |
| [4] | "An Arabidopsis embryonic lethal mutant with reduced expression of alanyl-tRNA synthetase gene." Ge S.J., Yao X.L., Yang Z.X., Zhu Z.P. Cell Res. 8:119-134(1998) [PubMed: 9669027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 753-1003. Strain: cv. Columbia. |
| [5] | "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, MASS SPECTROMETRY. Tissue: Seedling. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| Z22673 mRNA. Translation: CAA80380.1. Z22673 mRNA. Translation: CAA80381.1. AC007980 Genomic DNA. Translation: AAD50044.1. Different initiation. BT002526 mRNA. Translation: AAO00886.1. BT008807 mRNA. Translation: AAP68246.1. Y12555 mRNA. Translation: CAA73145.1. | |
| IPI | IPI00537243. IPI00760312. |
| PIR | D96538. |
| RefSeq | NP_175439.2. |
| UniGene | At.1836 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P36428. |
Proteomic databases | |
| PRIDE | P36428. |
| ProMEX | P36428. |
Genome annotation databases | |
| GeneID | 841442. |
| GenomeReviews | Gene locus AT1G50200 in contig CT485782_GR. |
| KEGG | ath:AT1G50200. |
Organism-specific databases | |
| GeneFarm | 2386. |
| TAIR | At1g50200. |
Phylogenomic databases | |
| OMA | PTDRIYA. |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.7. 302. |
Gene expression databases | |
| ArrayExpress | P36428. |
| Genevestigator | P36428. |
| GermOnline | AT1G50200. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR002318. Ala-tRNA-synth_IIc. IPR018165. Ala-tRNA-synth_IIc_cons-reg. IPR018164. Ala-tRNA-synth_IIc_N. IPR003156. Pesterase_DHHA1. IPR012947. tRNA_SAD. [Graphical view] |
| Pfam | PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view] |
| PRINTS | PR00980. TRNASYNTHALA. |
| TIGRFAMs | TIGR00344. alaS. 1 hit. |
| PROSITE | PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYA_ARATH | ||||||||
| Accession | Primary (citable) accession number: P36428 Secondary accession number(s): O04159, Q8GUG2, Q9SX40 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


