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Protein

Probable deoxycytidylate deaminase

Gene

CG6951

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 2 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi102 – 1021Zinc; catalyticBy similarity
Active sitei104 – 1041Proton donorBy similarity
Metal bindingi128 – 1281Zinc; catalyticBy similarity
Metal bindingi131 – 1311Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_310550. Pyrimidine biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable deoxycytidylate deaminase (EC:3.5.4.12)
Alternative name(s):
dCMP deaminase
Gene namesi
ORF Names:CG6951
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036959. CG6951.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Probable deoxycytidylate deaminasePRO_0000171696Add
BLAST

Proteomic databases

PaxDbiQ9VWA2.
PRIDEiQ9VWA2.

Expressioni

Gene expression databases

BgeeiQ9VWA2.
ExpressionAtlasiQ9VWA2. differential.
GenevisibleiQ9VWA2. DM.

Interactioni

Protein-protein interaction databases

BioGridi65486. 3 interactions.
DIPiDIP-23043N.
IntActiQ9VWA2. 1 interaction.
MINTiMINT-939888.
STRINGi7227.FBpp0074597.

Structurei

3D structure databases

ProteinModelPortaliQ9VWA2.
SMRiQ9VWA2. Positions 25-186.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 163137CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2131.
GeneTreeiENSGT00390000000501.
InParanoidiQ9VWA2.
KOiK01493.
OMAiLMFEMAG.
OrthoDBiEOG7JDQZR.
PhylomeDBiQ9VWA2.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VWA2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVSAQDLI SQLSKSPESH KRKEYLHWDD YFMATSLLSA KRSKDPVTQV
60 70 80 90 100
GACIVDSQNR IVAIGYNGFP RNCSDDVFPW SKAKKGSQEF DPLEDKKMYV
110 120 130 140 150
VHAEANAILN SNGMSLSGTR LYTTLFPCNE CAKLIIQVGI SQVLYLSDKY
160 170 180 190 200
ADKPTYRASK RMLDAVGVEY KRHIPQKKTI TIDFDTFPEE DPNASLGLNE

LHL
Length:203
Mass (Da):22,857
Last modified:May 1, 2000 - v1
Checksum:i0E37ECB9F8A8CA5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49046.1.
AE014296 Genomic DNA. Translation: AAN11625.1.
BT011479 mRNA. Translation: AAR99137.1.
RefSeqiNP_649197.1. NM_140940.3.
NP_730502.1. NM_168838.3.
UniGeneiDm.2515.

Genome annotation databases

EnsemblMetazoaiFBtr0074828; FBpp0074597; FBgn0036959.
FBtr0074829; FBpp0074598; FBgn0036959.
GeneIDi40222.
KEGGidme:Dmel_CG6951.
UCSCiCG6951-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49046.1.
AE014296 Genomic DNA. Translation: AAN11625.1.
BT011479 mRNA. Translation: AAR99137.1.
RefSeqiNP_649197.1. NM_140940.3.
NP_730502.1. NM_168838.3.
UniGeneiDm.2515.

3D structure databases

ProteinModelPortaliQ9VWA2.
SMRiQ9VWA2. Positions 25-186.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65486. 3 interactions.
DIPiDIP-23043N.
IntActiQ9VWA2. 1 interaction.
MINTiMINT-939888.
STRINGi7227.FBpp0074597.

Proteomic databases

PaxDbiQ9VWA2.
PRIDEiQ9VWA2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074828; FBpp0074597; FBgn0036959.
FBtr0074829; FBpp0074598; FBgn0036959.
GeneIDi40222.
KEGGidme:Dmel_CG6951.
UCSCiCG6951-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0036959. CG6951.

Phylogenomic databases

eggNOGiCOG2131.
GeneTreeiENSGT00390000000501.
InParanoidiQ9VWA2.
KOiK01493.
OMAiLMFEMAG.
OrthoDBiEOG7JDQZR.
PhylomeDBiQ9VWA2.

Enzyme and pathway databases

ReactomeiREACT_310550. Pyrimidine biosynthesis.

Miscellaneous databases

GenomeRNAii40222.
NextBioi817648.
PROiQ9VWA2.

Gene expression databases

BgeeiQ9VWA2.
ExpressionAtlasiQ9VWA2. differential.
GenevisibleiQ9VWA2. DM.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiDCTD_DROME
AccessioniPrimary (citable) accession number: Q9VWA2
Secondary accession number(s): Q53XF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.