Q9VQZ6 (ELP3_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable elongator complex protein 3
EC=2.3.1.48

Gene names

Name:	Elp3
ORF Names:	CG15433

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	locomotory behavior Inferred from mutant phenotype. Source: FlyBase photoreceptor cell maintenance Inferred from mutant phenotype. Source: FlyBase regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB sleep Inferred from mutant phenotype. Source: FlyBase synaptic growth at neuromuscular junction Inferred from mutant phenotype. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB transcription elongation factor complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 552	552	Probable elongator complex protein 3		PRO_0000283992
Regions
	Domain	398 – 552	155	N-acetyltransferase
Sites
	Metal binding	101	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	111	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	114	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9VQZ6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 3CE7D4D46EEE0C1F	FASTA	552	62,821
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10731132] [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. , 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: 12537572] [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: 12537569] [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.
RefSeq	NP_608834.1. NM_134990.3.
UniGene	Dm.12505.
3D structure databases
ProteinModelPortal	Q9VQZ6.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9VQZ6.
Proteomic databases
PRIDE	Q9VQZ6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0077439; FBpp0077129; FBgn0031604.
GeneID	33649.
KEGG	dme:Dmel_CG15433.
NMPDR	fig|7227.3.peg.718.
UCSC	CG15433-RA. d. melanogaster.
Organism-specific databases
CTD	55140.
FlyBase	FBgn0031604. Elp3.
Phylogenomic databases
eggNOG	inNOG09044.
GeneTree	EMGT00050000002982.
InParanoid	Q9VQZ6.
OMA	GIQEVHH.
OrthoDB	EOG495X6W.
PhylomeDB	Q9VQZ6.
Gene expression databases
ArrayExpress	Q9VQZ6.
Bgee	Q9VQZ6.
Family and domain databases
InterPro	IPR000182. AcTrfase_GCN5-related_dom. IPR016181. Acyl_CoA_acyltransferase. IPR006638. Elp3/MiaB/NifB. IPR005910. Hist_AcTrfase_ELP3. IPR007197. rSAM. IPR023404. rSAM_horseshoe. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit. G3DSA:3.80.30.20. G3DSA:3.80.30.20. 1 hit.
KO	K07739.
Pfam	PF00583. Acetyltransf_1. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMs	TIGR01211. ELP3. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	784609.

Entry information

Entry name

ELP3_DROME

Accession

Primary (citable) accession number: Q9VQZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project