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Protein

Adenosine deaminase-like protein

Gene

Ada

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Putative nucleoside deaminase. May catalyze the hydrolytic deamination of adenosine or some similar substrate and play a role in purine metabolism (By similarity).By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141Zinc; catalyticBy similarity
Metal bindingi16 – 161Zinc; catalyticBy similarity
Binding sitei16 – 161SubstrateBy similarity
Binding sitei171 – 1711Substrate; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi198 – 1981Zinc; catalyticBy similarity
Active sitei201 – 2011Proton donorBy similarity
Sitei221 – 2211Important for catalytic activityBy similarity
Metal bindingi276 – 2761Zinc; catalyticBy similarity
Binding sitei277 – 2771SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-2161541. Abacavir metabolism.
R-DME-74217. Purine salvage.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine deaminase-like protein (EC:3.5.4.-)
Gene namesi
Name:Ada
ORF Names:CG11994
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0037661. Ada.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Adenosine deaminase-like proteinPRO_0000285094Add
BLAST

Proteomic databases

PaxDbiQ9VHH7.
PRIDEiQ9VHH7.

Expressioni

Gene expression databases

BgeeiQ9VHH7.
GenevisibleiQ9VHH7. DM.

Interactioni

Protein-protein interaction databases

STRINGi7227.FBpp0081451.

Structurei

3D structure databases

ProteinModelPortaliQ9VHH7.
SMRiQ9VHH7. Positions 3-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1097. Eukaryota.
COG1816. LUCA.
GeneTreeiENSGT00730000111081.
InParanoidiQ9VHH7.
KOiK01488.
OMAiCPTSNIA.
OrthoDBiEOG7H4DV1.
PhylomeDBiQ9VHH7.

Family and domain databases

InterProiIPR001365. A/AMP_deaminase_dom.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9VHH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQFLKGLPK VELHAHLNGS LGIKSLCDLG ERLYGTSCKD FLKLCAHFSR
60 70 80 90 100
FEKDMDACFE KFAFVHELTS TREGLRFATE LAIRDFAEDN VQYVEMRTTP
110 120 130 140 150
KANENYSRRD YLQIVIDAIK AASETYPEIT VKLLPSINRA EPVDVAEETV
160 170 180 190 200
SLAVELARAH PNLILGIDLS GNPGKGRFSD FAPILAQARD KGLKLAIHCA
210 220 230 240 250
EIENPSEVKE MLHFGMSRCG HGTFLTPEDI GQLKQRNIAI ECCLTSNVKS
260 270 280 290 300
GTVPSLEEHH LKRIMEADAP KVICTDDSGV FDTTLTKEFL IAAETFGLTR
310 320 330
EQCIDLTLEA VHHSFASEQE QIQMADRVGN YADILVK
Length:337
Mass (Da):37,576
Last modified:May 1, 2000 - v1
Checksum:i72FB9041DBE857C6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54337.1.
BT031009 mRNA. Translation: ABV82391.1.
RefSeqiNP_649866.1. NM_141609.3.
UniGeneiDm.18556.

Genome annotation databases

EnsemblMetazoaiFBtr0081971; FBpp0081451; FBgn0037661.
GeneIDi41092.
KEGGidme:Dmel_CG11994.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF54337.1.
BT031009 mRNA. Translation: ABV82391.1.
RefSeqiNP_649866.1. NM_141609.3.
UniGeneiDm.18556.

3D structure databases

ProteinModelPortaliQ9VHH7.
SMRiQ9VHH7. Positions 3-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0081451.

Proteomic databases

PaxDbiQ9VHH7.
PRIDEiQ9VHH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081971; FBpp0081451; FBgn0037661.
GeneIDi41092.
KEGGidme:Dmel_CG11994.

Organism-specific databases

CTDi100.
FlyBaseiFBgn0037661. Ada.

Phylogenomic databases

eggNOGiKOG1097. Eukaryota.
COG1816. LUCA.
GeneTreeiENSGT00730000111081.
InParanoidiQ9VHH7.
KOiK01488.
OMAiCPTSNIA.
OrthoDBiEOG7H4DV1.
PhylomeDBiQ9VHH7.

Enzyme and pathway databases

ReactomeiR-DME-2161541. Abacavir metabolism.
R-DME-74217. Purine salvage.

Miscellaneous databases

GenomeRNAii41092.
PROiQ9VHH7.

Gene expression databases

BgeeiQ9VHH7.
GenevisibleiQ9VHH7. DM.

Family and domain databases

InterProiIPR001365. A/AMP_deaminase_dom.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
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., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiADAL_DROME
AccessioniPrimary (citable) accession number: Q9VHH7
Secondary accession number(s): A8E767
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2000
Last modified: June 8, 2016
This is version 94 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

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 one 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.