[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3023902 [NCBI, ExPASy, EBI, Israel, Japan] McIntosh E.M., Haynes R.H.; "Sequence and expression of the dCMP deaminase gene (DCD1) of Saccharomyces cerevisiae."; Mol. Cell. Biol. 6:1711-1721(1986).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=8091229 [NCBI, ExPASy, EBI, Israel, Japan] Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.; "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."; Science 265:2077-2082(1994).
[3]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).

Comments

FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.
CATALYTIC ACTIVITY: dCMP + H₂O = dUMP + NH₃.
COFACTOR: Zinc (By similarity).
ENZYME REGULATION: Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.
MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M13010; AAA34561.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U10397; AAB68985.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S46762; S46762.

RefSeq

NP_012014.1; -.

3D structure databases

ModBase

P06773.

Protein-protein interaction databases

DIP

DIP:4028N; -.

IntAct

P06773; -.

Organism-specific databases

YHR144c; -.

S000001187; DCD1.

Gene expression databases

GermOnline

YHR144C; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0004132;	Molecular function: dCMP deaminase activity (inferred from genetic interaction from SGD).
GO:0006221;	Biological process: pyrimidine nucleotide biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR016192; APOBEC/CMP_deaminase_Zn-bd.
IPR002125; CMP_dCMP_Zn_bd.
IPR015517; Cyt_deaminase.
Graphical view of domain structure.

PANTHER

PTHR11086; Cyt_deaminase; 1.

Pfam

PF00383; dCMP_cyt_deam_1; 1.
Pfam graphical view of domain structure.

PROSITE

PS00903; CYT_DCMP_DEAMINASES; 1.

Genome annotation databases

Ensembl

YHR144C; Saccharomyces cerevisiae. [Contig view]

856548; -.

U00093_GR; YHR144C.

sce:YHR144C; -.

fig|4932.3.peg.3178; -.

Phylogenomic databases

HOGENOM

P06773; -.

Other

LinkHub

P06773; -.

NextBio

982352; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Allosteric enzyme; Complete proteome; Hydrolase; Metal-binding; Nucleotide biosynthesis; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 312`	`312`	`Deoxycytidylate deaminase.`	`PRO_0000171697`
`ACT_SITE`	`235 235`		`Proton donor (By similarity).`
`METAL`	`233 233`		`Zinc; catalytic (By similarity).`
`METAL`	`260 260`		`Zinc; catalytic (By similarity).`
`METAL`	`263 263`		`Zinc; catalytic (By similarity).`
`CONFLICT`	`78 78`		`V -> A (in Ref. 1; AAA34561).`

Sequence information

Length: 312 AA [This is the length of the unprocessed precursor]

Molecular weight: 35646 Da [This is the MW of the unprocessed precursor]

CRC64: 780B47CDA561D24B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLIGVSGTKF CGCEDVINML VDHFHFELLN HLDNPEEILD YATKNYTKNS VIFLEKLSLL 

        70         80         90        100        110        120 
EKLEKRPFFV HLSIDAPVTT RVALYRKTTQ AESLSLEQII QAIDQHDFQP EGIKLREKSH 

       130        140        150        160        170        180 
LRFKIVNEDR RGRRQSLINN ITTQLKILDD KEKQMAPLMR PSWDSYFMKL ATLAASRSNC 

       190        200        210        220        230        240 
MKRRVGCVIV RECRVIATGY NGTPRHLTNC FNGGCPRCND GDSRNLHTCL CLHAEENALL 

       250        260        270        280        290        300 
EAGRDRVGQN ATLYCDTCPC LTCSVKIVQT GISEVVYSQS YRMDEESFKV LKNAGITVRQ 

       310 
FSFTEEPRIV MI

P06773 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools