Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q23651 (ELP3_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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:elpc-3
ORF Names:ZK863.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length547 AA.
Sequence statusComplete.
Protein existenceInferred 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 + 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_processembryonic morphogenesis

Inferred from genetic interaction PubMed 19593383. Source: WormBase

olfactory learning

Inferred from mutant phenotype PubMed 19593383. Source: WormBase

oocyte development

Inferred from genetic interaction PubMed 19593383. Source: WormBase

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

spermatogenesis

Inferred from genetic interaction PubMed 19593383. Source: WormBase

tRNA wobble uridine modification

Inferred from mutant phenotype PubMed 19593383. Source: WormBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

translation

Inferred from mutant phenotype PubMed 19593383. Source: WormBase

vulval development

Inferred from genetic interaction PubMed 19593383. Source: WormBase

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

transcription elongation factor complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionhistone 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 – 547547Probable elongator complex protein 3
PRO_0000283994

Regions

Domain392 – 547156N-acetyltransferase

Sites

Metal binding951Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1051Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1081Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q23651 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 6C7FAAEC59D8C6A6

FASTA54761,910
        10         20         30         40         50         60 
MDQKGSQRAL LAQTINEIVK LLIEAHNQKK DVNLNRLKCI VAQKNGLSFQ PKLVDIIAGV 

        70         80         90        100        110        120 
PSDYKDSLLP 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 KISDKAHRPE LKGNVSVVRE LHVYGSVVSV 

       490        500        510        520        530        540 
ADRDPKKFQH QGYGSLLMEE AERIAREEHG SDKIAVISGV GTREYYRKLG YELDGPYMSK 


MLDSAAA 

« Hide

References

[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z78019 Genomic DNA. Translation: CAB01454.2.
PIRT28062.
RefSeqNP_506055.2. NM_073654.4.
UniGeneCel.23487.

3D structure databases

ProteinModelPortalQ23651.
SMRQ23651. Positions 440-542.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.ZK863.3.

Proteomic databases

PaxDbQ23651.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaZK863.3.1; ZK863.3.1; ZK863.3.
ZK863.3.2; ZK863.3.2; ZK863.3.
GeneID179669.
KEGGcel:CELE_ZK863.3.
UCSCZK863.3. c. elegans.

Organism-specific databases

CTD179669.
WormBaseZK863.3; CE40344; WBGene00014123; elpc-3.

Phylogenomic databases

eggNOGCOG1243.
HOGENOMHOG000227514.
InParanoidQ23651.
KOK07739.
OMAGYKVVSH.
PhylomeDBQ23651.

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

NextBio906382.
PROQ23651.

Entry information

Entry nameELP3_CAEEL
AccessionPrimary (citable) accession number: Q23651
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: September 5, 2006
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase