DIA4/YHR011W Summary Help

Standard Name DIA4 1
Systematic Name YHR011W
Feature Type ORF, Verified
Description Probable mitochondrial seryl-tRNA synthetase; mutant displays increased invasive and pseudohyphal growth (1, 2, 3 and see Summary Paragraph)
Name Description Digs Into Agar 1
Chromosomal Location
ChrVIII:127780 to 129120 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All DIA4 GO evidence and references
  View Computational GO annotations for DIA4
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 2 genes
Resources
Classical genetics
null
Large-scale survey
null
Resources
92 total interaction(s) for 86 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 5
  • Affinity Capture-RNA: 1
  • Two-hybrid: 37

Genetic Interactions
  • Negative Genetic: 18
  • Phenotypic Suppression: 1
  • Positive Genetic: 25
  • Synthetic Growth Defect: 3
  • Synthetic Lethality: 2

Resources
Expression Summary
histogram
Resources
Length (a.a.) 446
Molecular Weight (Da) 50,390
Isoelectric Point (pI) 9.15
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrVIII:127780 to 129120 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1341 127780..129120 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 | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001053
SUMMARY PARAGRAPH for DIA4

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 (4, 5 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 (4, 5, 6 and references therein).

Last updated: 2008-07-14 Contact SGD

References cited on this page View Complete Literature Guide for DIA4
1) Palecek SP, et al.  (2000) Genetic analysis reveals that FLO11 upregulation and cell polarization independently regulate invasive growth in Saccharomyces cerevisiae. Genetics 156(3):1005-23
2) Rokov-Plavec J, et al.  (2002) Maize seryl-tRNA synthetase: specificity of substrate recognition by the organellar enzyme. Arch Biochem Biophys 397(1):40-50
3) Yokogawa T, et al.  (2000) Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase. J Biol Chem 275(26):19913-20
4) Delarue M  (1995) Aminoacyl-tRNA synthetases. Curr Opin Struct Biol 5(1):48-55
5) Arnez JG and Moras D  (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem Sci 22(6):211-6
6) 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