Reviewed, UniProtKB/Swiss-Prot Q60LW7 (ELP3_CAEBR)

Names and origin

Protein names

Recommended name:
    Probable elongator complex protein 3
    EC=2.3.1.48

Gene names

Name:	elpc-3
ORF Names:	CBG23399

Organism

Caenorhabditis briggsae [Complete proteome]

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	548 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 + acetylhistone.
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
Gene Ontology (GO)
Biological process	regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB transcription 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 ion binding Inferred from electronic annotation. Source: UniProtKB-KW iron-sulfur cluster 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 – 548	548	Probable elongator complex protein 3		PRO_0000283993
Regions
	Domain	392 – 548	157	N-acetyltransferase
Sites
	Metal binding	95	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	105	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	108	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q60LW7-1 [UniParc]. Last modified November 23, 2004. Version 1. Checksum: D4E1EAD89305B037	FASTA	548	61,970
	10 20 30 40 50 60 MDDKGSQRAL LAQTVNEIVK LLIEAHNQKK DVNLNRLKCI VAQKNGLSFQ PKLVDIIAGV 70 80 90 100 110 120 PADYKDTLLP KLKAKPVRTA SGIAVVAVMS KPHRCPHINF TGNICVYCPG GPDSDFEYST 130 140 150 160 170 180 QSYTGYEPTS MRAIRARYNP YLQTRGRLNQ LMQLGHSVDK VEFIVMGGTF MSLPEDYRDF 190 200 210 220 230 240 FIRNLHDALS GHTSASVEEA VAYSERSKMK CIGITIETRP DYCLPRHLND MLLYGCTRLE 250 260 270 280 290 300 IGVQSTYEDV ARDTNRGHTV KSVCETFHMA KDTGYKVVIH MMPDLPNVGL ERDKEQFLEL 310 320 330 340 350 360 FESPAFRPDG LKLYPTLVIR GTGLYELWKT GRYQSYPPSV LVDLIATILS LVPPWTRVYR 370 380 390 400 410 420 VQRDIPMPLV SSGVEHGNLR EHAMAKMKEL GLKCRDVRTR EVGIQEIHNK VRPEDVELIR 430 440 450 460 470 480 RDYTANGGWE TFISYEDPKQ DILIGLLRLR KISDKAHRAE LKGNVSVVRE LHVYGSVVSV 490 500 510 520 530 540 ADRDPKKFQH QGYGSLLMEE AERIAREEHE SDKIAVISGV GTRDYYRKLG YELDGPYMSK TLDASSAA

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed: 14624247] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CAAC02000606 Genomic DNA. Translation: CAP39624.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GenomeReviews	Gene locus elpc-3 in contig CU538968_GR.
UCSC	ZK863.3. c. elegans.
Organism-specific databases
WormBase	WBGene00041763. Cbr-elpc-3.
Phylogenomic databases
OMA	WQHRGYG.
Enzyme and pathway databases
BRENDA	2.3.1.48. 261794.
Family and domain databases
InterPro	IPR006638. Elp3/MiaB/NifB. IPR000182. GCN5-rel_AcTrfase. IPR005910. Hist_AcTrfase_ELP3. IPR007197. Radical_SAM. [Graphical view]
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]
TIGRFAMs	TIGR01211. ELP3. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ELP3_CAEBR

Accession

Primary (citable) accession number: Q60LW7
Secondary accession number(s): A8Y404

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	November 23, 2004
Last modified:	November 3, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project