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Q9VWA2

- DCTD_DROME

UniProt

Q9VWA2 - DCTD_DROME

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Protein

Probable deoxycytidylate deaminase

Gene

CG6951

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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

  1. dCMP deaminase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. nucleotide biosynthetic process Source: UniProtKB-KW
  2. pyrimidine nucleotide metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_204719. 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: 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.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2131.
GeneTreeiENSGT00390000000501.
InParanoidiQ9VWA2.
KOiK01493.
OMAiKCNKIII.
OrthoDBiEOG7JDQZR.
PhylomeDBiQ9VWA2.

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 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 .
RefSeqi NP_649197.1. NM_140940.3.
NP_730502.1. NM_168838.3.
UniGenei Dm.2515.

3D structure databases

ProteinModelPortali Q9VWA2.
SMRi Q9VWA2. Positions 25-186.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 65486. 3 interactions.
DIPi DIP-23043N.
IntActi Q9VWA2. 1 interaction.
MINTi MINT-939888.

Proteomic databases

PaxDbi Q9VWA2.
PRIDEi Q9VWA2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0074828 ; FBpp0074597 ; FBgn0036959 .
FBtr0074829 ; FBpp0074598 ; FBgn0036959 .
GeneIDi 40222.
KEGGi dme:Dmel_CG6951.
UCSCi CG6951-RA. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0036959. CG6951.

Phylogenomic databases

eggNOGi COG2131.
GeneTreei ENSGT00390000000501.
InParanoidi Q9VWA2.
KOi K01493.
OMAi KCNKIII.
OrthoDBi EOG7JDQZR.
PhylomeDBi Q9VWA2.

Enzyme and pathway databases

Reactomei REACT_204719. Pyrimidine biosynthesis.

Miscellaneous databases

GenomeRNAii 40222.
NextBioi 817648.
PROi Q9VWA2.

Gene expression databases

Bgeei Q9VWA2.
ExpressionAtlasi Q9VWA2. differential.

Family and domain databases

InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view ]
PANTHERi PTHR11086. PTHR11086. 1 hit.
Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMi SSF53927. SSF53927. 1 hit.
PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 104 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