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Q9VQZ6 (ELP3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable elongator complex protein 3

EC=2.3.1.48
Gene names
Name:Elp3
ORF Names:CG15433
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

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

Subunit structure

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

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the ELP3 family.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandIron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytoskeletal matrix organization at active zone

Inferred from mutant phenotype PubMed 22153374. Source: FlyBase

locomotory behavior

Inferred from mutant phenotype PubMed 20626565. Source: FlyBase

peptidyl-lysine acetylation

Inferred from direct assay PubMed 22153374. Source: FlyBase

regulation of photoreceptor cell axon guidance

Inferred from mutant phenotype PubMed 18996918. Source: FlyBase

regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: GOC

regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

sleep

Inferred from mutant phenotype PubMed 20626565. Source: FlyBase

synapse organization

Inferred from mutant phenotype PubMed 18996918. Source: FlyBase

synaptic growth at neuromuscular junction

Inferred from mutant phenotype PubMed 20626565. Source: FlyBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

synapse

Inferred from direct assay PubMed 22153374. Source: FlyBase

transcription elongation factor complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionacetyltransferase activity

Inferred from direct assay PubMed 22153374. Source: FlyBase

histone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

iron-sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphorylase kinase regulator activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Probable elongator complex protein 3
PRO_0000283992

Regions

Domain398 – 552155N-acetyltransferase

Sites

Metal binding1011Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1111Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1141Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9VQZ6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3CE7D4D46EEE0C1F

FASTA55262,821
        10         20         30         40         50         60 
MKAKKKLGVG LSRQERQVLV IGEIIQELLK AHEAKKDVNL NRMKSLVASK YGLDSSPRLV 

        70         80         90        100        110        120 
DIIAAVPQDA KKILLPKLRA KPIRTASGIA VVAVMCKPHR CPHINMTGNI CVYCPGGPDS 

       130        140        150        160        170        180 
DFEYSTQSYT GYEPTSMRAI RSRYDPFLQT RHRVEQLKQL GHSVDKVEFI VMGGTFMCLP 

       190        200        210        220        230        240 
EEYRDYFIRN LHDALSGHSS ANVAEAVRYS EKSRTKCIGI TIETRPDYCL KRHISDMLSY 

       250        260        270        280        290        300 
GCTRLEIGVQ SVYEDVARDT NRGHTVRAVC ESFQLGKDAG YKIVTHMMPD LPNVDFERDI 

       310        320        330        340        350        360 
EQFIEYFENP AFRSDGLKIY PTLVIRGTGL YELWKTGRYK SYPPSMLVDL VAKILALVPP 

       370        380        390        400        410        420 
WTRVYRVQRD IPMPLVSSGV EHGNLRELAL ARMKDLGTTC RDVRTREVGI QEIHNKVRPY 

       430        440        450        460        470        480 
EIELIRRDYV ANGGWETFLS YEDPEQDILV GLLRLRKCSP DTFRPELKGE CSIVRELHVY 

       490        500        510        520        530        540 
GSVVPVNARD PTKFQHQGFG MLLMEEAERI AREEHGSTKL AVISGVGTRN YYRKMGYQLD 

       550 
GPYMSKSIEE NN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014134 Genomic DNA. Translation: AAF51012.1.
AY089621 mRNA. Translation: AAL90359.1.
RefSeqNP_608834.1. NM_134990.3.
UniGeneDm.12505.

3D structure databases

ProteinModelPortalQ9VQZ6.
SMRQ9VQZ6. Positions 492-541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid59843. 1 interaction.
STRING7227.FBpp0077129.

Proteomic databases

PaxDbQ9VQZ6.
PRIDEQ9VQZ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0077439; FBpp0077129; FBgn0031604.
GeneID33649.
KEGGdme:Dmel_CG15433.
UCSCCG15433-RA. d. melanogaster.

Organism-specific databases

CTD55140.
FlyBaseFBgn0031604. Elp3.

Phylogenomic databases

eggNOGCOG1243.
GeneTreeENSGT00390000013141.
InParanoidQ9VQZ6.
KOK07739.
OMAGYKVVSH.
OrthoDBEOG7V765W.
PhylomeDBQ9VQZ6.

Gene expression databases

BgeeQ9VQZ6.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR01211. ELP3. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi33649.
NextBio784609.
PROQ9VQZ6.

Entry information

Entry nameELP3_DROME
AccessionPrimary (citable) accession number: Q9VQZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase