ALA1/YOR335C Summary Help

Standard Name ALA1 1
Systematic Name YOR335C
Alias CDC64 2
Feature Type ORF, Verified
Description Cytoplasmic and mitochondrial alanyl-tRNA synthetase; required for protein synthesis; point mutation (cdc64-1 allele) causes cell cycle arrest at G1; lethality of null mutation is functionally complemented by human homolog (1, 3, 4 and see Summary Paragraph)
Name Description ALAnyl-tRNA synthetase 1
Chromosomal Location
ChrXV:949109 to 946233 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: 188 cM
Gene Ontology Annotations All ALA1 GO evidence and references
  View Computational GO annotations for ALA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 7 genes
Resources
Classical genetics
conditional
Large-scale survey
null
overexpression
reduction of function
repressible
Resources
82 total interaction(s) for 78 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 19
  • Affinity Capture-RNA: 3
  • Biochemical Activity: 7
  • Protein-peptide: 2
  • Reconstituted Complex: 6

Genetic Interactions
  • Dosage Lethality: 1
  • Negative Genetic: 39
  • Positive Genetic: 3
  • Synthetic Lethality: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 958
Molecular Weight (Da) 107,276
Isoelectric Point (pI) 5.27
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXV:949109 to 946233 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
This feature contains embedded feature(s): YOR335W-A
SGD ORF map
Genetic position: 188 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..2877 949109..946233 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005862
SUMMARY PARAGRAPH for ALA1

About aminoacyl-tRNA synthetases...

In a process critical for accurate translation of the genetic code, aminoacyl-tRNA synthetases (aka aminoacyl-tRNA ligases) attach amino acids specifically to cognate tRNAs, thereby "charging" the tRNAs. The catalysis is accomplished via a two-step mechanism. First, the synthetase activates the amino acid in an ATP-dependent reaction, producing aminoacyl-adenylate and releasing inorganic pyrophosphate (PPi). Second, the enzyme binds the correct tRNA and transfers the activated amino acid to either the 2' or 3' terminal hydroxyl group of the tRNA, forming the aminoacyl-tRNA and AMP (5, 6 and references therein).

Aminoacyl-tRNA synthetases possess precise substrate specificity and, despite their similarity in function, vary in size, primary sequence and subunit composition. Individual members of the aminoacyl-tRNA synthetase family can be categorized in one of two classes, depending on amino acid specificity. Class I enzymes (those specific for Glu, Gln, Arg, Cys, Met, Val, Ile, Leu, Tyr and Trp) typically contain two highly conserved sequence motifs, are monomeric or dimeric, and aminoacylate at the 2' terminal hydroxyl of the appropriate tRNA. Class II enzymes (those specific for Gly, Ala, Pro, Ser, Thr, His, Asp, Asn, Lys and Phe) typically contain three highly conserved sequence motifs, are dimeric or tetrameric, and aminoacylate at the 3' terminal hydroxyl of the appropriate tRNA (5, 6, 7 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for ALA1
1) Ripmaster TL, et al.  (1995) Wide cross-species aminoacyl-tRNA synthetase replacement in vivo: yeast cytoplasmic alanine enzyme replaced by human polymyositis serum antigen. Proc Natl Acad Sci U S A 92(11):4932-6
2) Bedard DP, et al.  (1981) New mutations in the yeast Saccharomyces cerevisiae affecting completion of "start". Curr Genet 4(3):205-14
3) Wrobel C, et al.  (1999) CDC64 encodes cytoplasmic alanyl-tRNA synthetase, Ala1p, of Saccharomyces cerevisiae. J Bacteriol 181(24):7618-20
4) Tang HL, et al.  (2004) Translation of a yeast mitochondrial tRNA synthetase initiated at redundant non-AUG codons. J Biol Chem 279(48):49656-63
5) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
6) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
7) Eriani G, et al.  (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347(6289):203-6