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Protein

NAD-dependent protein deacetylase Sirt7

Gene

Sirt7

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

NAD-dependent protein deacetylase.By similarity

Catalytic activityi

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.PROSITE-ProRule annotation

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei211 – 2111Proton acceptorPROSITE-ProRule annotation
Metal bindingi219 – 2191ZincPROSITE-ProRule annotation
Metal bindingi222 – 2221ZincPROSITE-ProRule annotation
Metal bindingi249 – 2491ZincPROSITE-ProRule annotation
Metal bindingi252 – 2521ZincPROSITE-ProRule annotation
Binding sitei339 – 3391NAD; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 15020NADBy similarityAdd
BLAST
Nucleotide bindingi191 – 1944NADBy similarity
Nucleotide bindingi292 – 2943NADBy similarity
Nucleotide bindingi321 – 3233NADBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
NAD-dependent protein deacetylase Sirt7 (EC:3.5.1.-)
Alternative name(s):
Regulatory protein SIR2 homolog 7
SIR2-like protein 7
Gene namesi
Name:Sirt7
ORF Names:CG11305
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039631. Sirt7.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 771771NAD-dependent protein deacetylase Sirt7PRO_0000417363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei716 – 7161Phosphothreonine1 Publication
Modified residuei717 – 7171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9VAQ1.

PTM databases

iPTMnetiQ9VAQ1.

Expressioni

Gene expression databases

BgeeiQ9VAQ1.
ExpressionAtlasiQ9VAQ1. differential.
GenevisibleiQ9VAQ1. DM.

Interactioni

Protein-protein interaction databases

BioGridi68304. 7 interactions.
IntActiQ9VAQ1. 5 interactions.
MINTiMINT-829015.
STRINGi7227.FBpp0084733.

Structurei

3D structure databases

ProteinModelPortaliQ9VAQ1.
SMRiQ9VAQ1. Positions 104-357.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini114 – 355242Deacetylase sirtuin-typePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi605 – 6117Poly-Glu
Compositional biasi718 – 7247Poly-Asp

Sequence similaritiesi

Belongs to the sirtuin family. Class IV subfamily.Curated
Contains 1 deacetylase sirtuin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1905. Eukaryota.
COG0846. LUCA.
GeneTreeiENSGT00530000063706.
InParanoidiQ9VAQ1.
KOiK11417.
OMAiTHRLCHR.
OrthoDBiEOG7M98GV.
PhylomeDBiQ9VAQ1.

Family and domain databases

Gene3Di3.40.50.1220. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 2 hits.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VAQ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKDLGEEKD QDQEQNTEME PKQEMDVAQS YITRAKMNPA KKDNEKRRRK
60 70 80 90 100
DAMRRVSMIL RKCDSMRTTE DRQFLEKHPD MVKTTKKRKE RVEIYKERVV
110 120 130 140 150
EREDAPHVIE AKVEQLANII SQAKHLVCYT GAGISTAALI PDYRGSQGIW
160 170 180 190 200
TLLQKGQDIG EHDLSSANPT YTHMALYELH RRRLLHHVVS QNCDGLHLRS
210 220 230 240 250
GLPRNSLSEI HGNMYVEVCK NCRPNSVYWR QFDTTEMTAR YCHKTHRLCH
260 270 280 290 300
RCSEPLYDTI VHFGERGNVK WPLNWAGATA NAQRADVILC LGSSLKVLKK
310 320 330 340 350
YTWLWQMDRP ARQRAKICVV NLQWTPKDAI ASIKINGKCD QVMAQLMHLL
360 370 380 390 400
HIPVPVYTKE KDPIFAHASL LMPEELHTLT QPLLKNADEE EAFTTTTEET
410 420 430 440 450
QDSTISSESC SFNYSDLPIG KGPRIRTPIK NGRRVKTNLE LRQKFKTLNG
460 470 480 490 500
QDEEIKVEHV KTNGEVKTEK DLITLESSIK IETEVKLEKL ECSDTNFQQE
510 520 530 540 550
LKLLELLPKL EPLSLKEETE ETPSNGFPEL PKLVAIQKTH AECLSAVPTE
560 570 580 590 600
SRLKPLQLPP LVPIGAPLST PFVEPKLVLP PASQSSSIQI KSEGDGDSST
610 620 630 640 650
ENDNEEEEES ELAQMDLLRQ NNDEELLRQL PTWYDAKYAY SGLHSILIPP
660 670 680 690 700
PADLNIWNSQ VVPNFAMNRS AASCFFCFDR YAELECQFYR RWNLSQRKHK
710 720 730 740 750
KRARSGRFVV CECCPTSDDD DDYDENISLA HIAAAETAKR RQQLSTSFPR
760 770
KLARTQAGWY GKGYKKGRKR R
Length:771
Mass (Da):88,469
Last modified:March 1, 2001 - v2
Checksum:i1AEC2B558B02CA63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF56851.2.
BT044225 mRNA. Translation: ACH92290.1.
RefSeqiNP_651664.2. NM_143407.3.
UniGeneiDm.1364.

Genome annotation databases

EnsemblMetazoaiFBtr0085364; FBpp0084733; FBgn0039631.
GeneIDi43433.
KEGGidme:Dmel_CG11305.
UCSCiCG11305-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF56851.2.
BT044225 mRNA. Translation: ACH92290.1.
RefSeqiNP_651664.2. NM_143407.3.
UniGeneiDm.1364.

3D structure databases

ProteinModelPortaliQ9VAQ1.
SMRiQ9VAQ1. Positions 104-357.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68304. 7 interactions.
IntActiQ9VAQ1. 5 interactions.
MINTiMINT-829015.
STRINGi7227.FBpp0084733.

PTM databases

iPTMnetiQ9VAQ1.

Proteomic databases

PaxDbiQ9VAQ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085364; FBpp0084733; FBgn0039631.
GeneIDi43433.
KEGGidme:Dmel_CG11305.
UCSCiCG11305-RA. d. melanogaster.

Organism-specific databases

CTDi51547.
FlyBaseiFBgn0039631. Sirt7.

Phylogenomic databases

eggNOGiKOG1905. Eukaryota.
COG0846. LUCA.
GeneTreeiENSGT00530000063706.
InParanoidiQ9VAQ1.
KOiK11417.
OMAiTHRLCHR.
OrthoDBiEOG7M98GV.
PhylomeDBiQ9VAQ1.

Miscellaneous databases

GenomeRNAii43433.
NextBioi833897.
PROiQ9VAQ1.

Gene expression databases

BgeeiQ9VAQ1.
ExpressionAtlasiQ9VAQ1. differential.
GenevisibleiQ9VAQ1. DM.

Family and domain databases

Gene3Di3.40.50.1220. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR003000. Sirtuin.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERiPTHR11085. PTHR11085. 2 hits.
PfamiPF02146. SIR2. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
PROSITEiPS50305. SIRTUIN. 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. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.E.
    Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-716 AND SER-717, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiSIR7_DROME
AccessioniPrimary (citable) accession number: Q9VAQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 115 of the entry and version 2 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.