[1]	PROTEIN SEQUENCE. PubMed=6345541 [NCBI, ExPASy, EBI, Israel, Japan] Maley G.F., Guarino D.U., Maley F.; "Complete amino acid sequence of an allosteric enzyme, T2 bacteriophage deoxycytidylate deaminase."; J. Biol. Chem. 258:8290-8297(1983).

Comments

FUNCTION: Supplies the nucleotide substrate for thymidylate synthetase.
CATALYTIC ACTIVITY: dCMP + H₂O = dUMP + NH₃.
COFACTOR: Binds 2 zinc ions per subunit (By similarity).
ENZYME REGULATION: Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.
SUBUNIT: Homohexamer.
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

PIR

A01011; DUBPC2.

3D structure databases

SMR

P00814; 1-188.

ModBase

P00814.

Ontologies

GO:0004132;	Molecular function: dCMP deaminase activity (inferred from electronic annotation from EC).
GO:0009165;	Biological process: nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016192; APOBEC/CMP_deaminase_Zn-bd.
IPR002125; CMP_dCMP_Zn_bd.
IPR015517; Cyt_deaminase.
IPR016473; dCMP_deaminase.
Graphical view of domain structure.

PANTHER

PTHR11086; Cyt_deaminase; 1.

Pfam

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

PIRSF

PIRSF006019; dCMP_deaminase; 1.

PROSITE

PS00903; CYT_DCMP_DEAMINASES; 1.

Other

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

Keywords

Allosteric enzyme; Direct protein sequencing; Hydrolase; Metal-binding; Nucleotide biosynthesis; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 188`	`188`	`Deoxycytidylate deaminase.`	`PRO_0000171700`
`ACT_SITE`	`106 106`		`Proton donor (By similarity).`
`METAL`	`19 19`		`Zinc 1; structural (By similarity).`
`METAL`	`49 49`		`Zinc 1; structural (By similarity).`
`METAL`	`94 94`		`Zinc 1; structural (By similarity).`
`METAL`	`102 102`		`Zinc 2; catalytic (By similarity).`
`METAL`	`104 104`		`Zinc 2; catalytic (By similarity).`
`METAL`	`132 132`		`Zinc 2; catalytic (By similarity).`
`METAL`	`135 135`		`Zinc 2; catalytic (By similarity).`

Sequence information

Length: 188 AA [This is the length of the unprocessed precursor]

Molecular weight: 20599 Da [This is the MW of the unprocessed precursor]

CRC64: A13EAF89D5CEB14A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCD NYAAIEGWLL 

        70         80         90        100        110        120 
NKPKHTIIQG HKPECVSFGT SDRFVLAKEH RSAHSEWSSK NEIHAELNAI LFAARNGSSI 

       130        140        150        160        170        180 
EGATMYVTLS PCPDCAKAIA QSGIKKLVYC ETYDKNKPGW DDILRNAGIE VFNVPKLNWE 


NISEFCGE

P00814 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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