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Protein

Deoxycytidylate deaminase

Gene

Dctd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Supplies the nucleotide substrate for thymidylate synthetase.By similarity

Catalytic activityi

dCMP + H2O = dUMP + NH3.

Cofactori

Zn2+By similarity

Enzyme regulationi

Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi84Zinc; catalyticBy similarity1
Active sitei86Proton donorBy similarity1
Metal bindingi110Zinc; catalyticBy similarity1
Metal bindingi113Zinc; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processNucleotide biosynthesis
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxycytidylate deaminase (EC:3.5.4.12)
Alternative name(s):
dCMP deaminase
Gene namesi
Name:Dctd
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1359671. Dctd.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001716941 – 178Deoxycytidylate deaminaseAdd BLAST178

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei174PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5M9G0.

Interactioni

Subunit structurei

Homohexamer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017670.

Structurei

3D structure databases

ProteinModelPortaliQ5M9G0.
SMRiQ5M9G0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 145CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST132

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3127. Eukaryota.
COG2131. LUCA.
HOGENOMiHOG000015715.
HOVERGENiHBG025823.
InParanoidiQ5M9G0.
KOiK01493.
PhylomeDBiQ5M9G0.
TreeFamiTF105971.

Family and domain databases

CDDicd01286. deoxycytidylate_deaminase. 1 hit.
InterProiView protein in InterPro
IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_dom.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
IPR035105. Deoxycytidylate_deaminase_dom.
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiView protein in Pfam
PF00383. dCMP_cyt_deam_1. 1 hit.
PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiView protein in PROSITE
PS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5M9G0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDISCKKRD DYLEWPEYFM AVAFLSAQRS KDPSSQVGAC IVNTENKIVG
60 70 80 90 100
IGYNGMPNGC SDDLLPWRRT AENKLDTKYP YVCHAELNAI MNKNSADVKG
110 120 130 140 150
CSMYVALFPC NECAKLIIQA GIKEVIFMSD KYHDSEETTA ARLLFKLAGV
160 170
TFRKFTPKYS KIVIDFDSIN SRPSQKPQ
Length:178
Mass (Da):20,059
Last modified:February 1, 2005 - v1
Checksum:iA53ED5C676965029
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087138 mRNA. Translation: AAH87138.1.
RefSeqiNP_001013904.2. NM_001013882.2.
NP_001154984.1. NM_001161512.1.
UniGeneiRn.105816.

Genome annotation databases

GeneIDi290741.
KEGGirno:290741.

Similar proteinsi

Entry informationi

Entry nameiDCTD_RAT
AccessioniPrimary (citable) accession number: Q5M9G0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: February 1, 2005
Last modified: November 22, 2017
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families