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Protein

Probable elongator complex protein 3

Gene

Elp3

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

Functioni

Catalytic histone acetyltransferase subunit of the RNA polymerase II elongator complex, which is a component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Elongator may play a role in chromatin remodeling. May also have a methyltransferase activity (By similarity).By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi111 – 1111Iron-sulfur (4Fe-4S-S-AdoMet)By similarity
Metal bindingi114 – 1141Iron-sulfur (4Fe-4S-S-AdoMet)By similarity

GO - Molecular functioni

  1. acetyltransferase activity Source: FlyBase
  2. histone acetyltransferase activity Source: UniProtKB-EC
  3. iron-sulfur cluster binding Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. phosphorylase kinase regulator activity Source: UniProtKB

GO - Biological processi

  1. cytoskeletal matrix organization at active zone Source: FlyBase
  2. hemopoiesis Source: FlyBase
  3. instar larval development Source: FlyBase
  4. locomotory behavior Source: FlyBase
  5. peptidyl-lysine acetylation Source: FlyBase
  6. regulation of photoreceptor cell axon guidance Source: FlyBase
  7. regulation of protein kinase activity Source: GOC
  8. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  9. sleep Source: FlyBase
  10. synapse organization Source: FlyBase
  11. synaptic growth at neuromuscular junction Source: FlyBase
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Probable elongator complex protein 3 (EC:2.3.1.48)
Gene namesi
Name:Elp3
ORF Names:CG15433
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0031604. Elp3.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. synapse Source: FlyBase
  3. transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 552552Probable elongator complex protein 3PRO_0000283992Add
BLAST

Proteomic databases

PaxDbiQ9VQZ6.
PRIDEiQ9VQZ6.

Expressioni

Gene expression databases

BgeeiQ9VQZ6.

Interactioni

Subunit structurei

Component of the RNA polymerase II elongator complex (Elongator). Elongator associates with the C-terminal domain (CTD) of Pol II largest subunit (By similarity).By similarity

Protein-protein interaction databases

BioGridi59843. 1 interaction.
IntActiQ9VQZ6. 1 interaction.
STRINGi7227.FBpp0077129.

Structurei

3D structure databases

ProteinModelPortaliQ9VQZ6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini398 – 552155N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ELP3 family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1243.
GeneTreeiENSGT00390000013141.
InParanoidiQ9VQZ6.
KOiK07739.
OMAiGYKVVSH.
OrthoDBiEOG7V765W.
PhylomeDBiQ9VQZ6.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01211. ELP3. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VQZ6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKAKKKLGVG LSRQERQVLV IGEIIQELLK AHEAKKDVNL NRMKSLVASK
60 70 80 90 100
YGLDSSPRLV DIIAAVPQDA KKILLPKLRA KPIRTASGIA VVAVMCKPHR
110 120 130 140 150
CPHINMTGNI CVYCPGGPDS DFEYSTQSYT GYEPTSMRAI RSRYDPFLQT
160 170 180 190 200
RHRVEQLKQL GHSVDKVEFI VMGGTFMCLP EEYRDYFIRN LHDALSGHSS
210 220 230 240 250
ANVAEAVRYS EKSRTKCIGI TIETRPDYCL KRHISDMLSY GCTRLEIGVQ
260 270 280 290 300
SVYEDVARDT NRGHTVRAVC ESFQLGKDAG YKIVTHMMPD LPNVDFERDI
310 320 330 340 350
EQFIEYFENP AFRSDGLKIY PTLVIRGTGL YELWKTGRYK SYPPSMLVDL
360 370 380 390 400
VAKILALVPP WTRVYRVQRD IPMPLVSSGV EHGNLRELAL ARMKDLGTTC
410 420 430 440 450
RDVRTREVGI QEIHNKVRPY EIELIRRDYV ANGGWETFLS YEDPEQDILV
460 470 480 490 500
GLLRLRKCSP DTFRPELKGE CSIVRELHVY GSVVPVNARD PTKFQHQGFG
510 520 530 540 550
MLLMEEAERI AREEHGSTKL AVISGVGTRN YYRKMGYQLD GPYMSKSIEE

NN
Length:552
Mass (Da):62,821
Last modified:May 1, 2000 - v1
Checksum:i3CE7D4D46EEE0C1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF51012.1.
AY089621 mRNA. Translation: AAL90359.1.
RefSeqiNP_608834.1. NM_134990.3.
UniGeneiDm.12505.

Genome annotation databases

EnsemblMetazoaiFBtr0077439; FBpp0077129; FBgn0031604.
GeneIDi33649.
KEGGidme:Dmel_CG15433.
UCSCiCG15433-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014134 Genomic DNA. Translation: AAF51012.1.
AY089621 mRNA. Translation: AAL90359.1.
RefSeqiNP_608834.1. NM_134990.3.
UniGeneiDm.12505.

3D structure databases

ProteinModelPortaliQ9VQZ6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59843. 1 interaction.
IntActiQ9VQZ6. 1 interaction.
STRINGi7227.FBpp0077129.

Proteomic databases

PaxDbiQ9VQZ6.
PRIDEiQ9VQZ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077439; FBpp0077129; FBgn0031604.
GeneIDi33649.
KEGGidme:Dmel_CG15433.
UCSCiCG15433-RA. d. melanogaster.

Organism-specific databases

CTDi55140.
FlyBaseiFBgn0031604. Elp3.

Phylogenomic databases

eggNOGiCOG1243.
GeneTreeiENSGT00390000013141.
InParanoidiQ9VQZ6.
KOiK07739.
OMAiGYKVVSH.
OrthoDBiEOG7V765W.
PhylomeDBiQ9VQZ6.

Miscellaneous databases

GenomeRNAii33649.
NextBioi784609.
PROiQ9VQZ6.

Gene expression databases

BgeeiQ9VQZ6.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01211. ELP3. 1 hit.
PROSITEiPS51186. GNAT. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiELP3_DROME
AccessioniPrimary (citable) accession number: Q9VQZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: May 1, 2000
Last modified: February 4, 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.