CDD1/YLR245C Summary Help

Standard Name CDD1 1
Systematic Name YLR245C
Feature Type ORF, Verified
Description Cytidine deaminase; catalyzes the modification of cytidine to uridine in vitro but native RNA substrates have not been identified, localizes to both the nucleus and cytoplasm (2, 3, 4 and see Summary Paragraph)
Name Description CytiDine Deaminase 1
Chromosomal Location
ChrXII:626930 to 626502 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All CDD1 GO evidence and references
  View Computational GO annotations for CDD1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Classical genetics
Large-scale survey
23 total interaction(s) for 17 unique genes/features.
Physical Interactions
  • PCA: 1
  • Two-hybrid: 15

Genetic Interactions
  • Negative Genetic: 6
  • Positive Genetic: 1

Expression Summary
Length (a.a.) 142
Molecular Weight (Da) 15,536
Isoelectric Point (pI) 7.12
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXII:626930 to 626502 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..429 626930..626502 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004235

Cdd1p is a cytidine deaminase (EC capable of deaminating cytidine into cytosine, which is important for the pyrimidine salvage pathway (1). Null mutants are viable and display weak 5-fluorocytidine resistance, which indicates a partial impairment in cytidine metabolism (1). The active enzyme is a homotetramer. Thus the enzyme complex contains four active sites, each of which is complexed with Zn2+ (4). It is found in both the cytoplasm and the nucleus (2).

Cdd1p has been shown to deaminate cytidine to uridine in an ectopically expressed fragment of human apolipoprotein B (apoB) mRNA, which suggests that mRNA C>U editing may exist in Saccharomyces cerevisiae (2). However, native substrates for Cdd1p-dependent RNA editing have not been identified, thus it is not clear if this activity is biologically relevant (2). Cdd1p has also been shown to deaminate deoxycytidine in vitro (1), but the biological significance of this has also not been established (5).

The Cdd1 protein has similarity to a number of proteins from other species, from bacteria to mammals. Cdd1p is similar to mouse activation-induced cytidine deaminase, human activation-induced deaminase protein (AICDA) and to human RNA-editing enzyme apolipoprotein B editing catalytic subunit 1 protein (APOBEC-1) (4, 1). Mutations in the AICDA protein have been detected in humans with hyper-IgM type 2 syndrome (4). Cdd1p contains a tertiary fold with high structural homology to the catalytic domains of Escherichia coli cytidine deaminase and Bacillus subtilis cytidine deaminase (4, 1). Cdd1p also contains putative ZDD motifs that align with regions in various proteins including S. cerevisiae Dcd1p, Erv1p, Fcy1p, Rib2p, Tad1p, Tad2p, and Tad3p, Trypanosoma cruzi ADAT1h, Caenorhabditis elegans ADAR, rat APOBEC-1, mouse APOBEC-2, and human AICDA, APOBEC1, APOBEC2, APOBEC3B, ADAR; ADARB1, and GFER proteins (2).

Last updated: 2005-12-19 Contact SGD

References cited on this page View Complete Literature Guide for CDD1
1) Kurtz JE, et al.  (1999) New insights into the pyrimidine salvage pathway of Saccharomyces cerevisiae: requirement of six genes for cytidine metabolism. Curr Genet 36(3):130-6
2) Dance GS, et al.  (2001) Identification of the yeast cytidine deaminase CDD1 as an orphan C-->U RNA editase. Nucleic Acids Res 29(8):1772-80
3) Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
4) Xie K, et al.  (2004) The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1. Proc Natl Acad Sci U S A 101(21):8114-9
5) Kurtz JE, et al.  (2002) The URH1 uridine ribohydrolase of Saccharomyces cerevisiae. Curr Genet 41(3):132-41