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O14023 (ELP3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable elongator complex protein 3

EC=2.3.1.48
Gene names
Name:elp3
ORF Names:SPAC29A4.20
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Acts as catalytic subunit of the RNA polymerase II elongator complex, which is a major histone acetyltransferase component of the RNA polymerase II (Pol II) holoenzyme and is involved in transcriptional elongation. Association with elongating RNAPII requires a hyperphosphorylated state of the RNAPII C-terminal domain (CTD). Elongator binds to both naked and nucleosomal DNA, can acetylate both core and nucleosomal histones, and is involved in chromatin remodeling 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.

Subcellular location

Cytoplasm Ref.2.

Sequence similarities

Belongs to the ELP3 family.

Contains 1 N-acetyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 544544Probable elongator complex protein 3
PRO_0000310360

Regions

Domain393 – 544152N-acetyltransferase

Sequences

Sequence LengthMass (Da)Tools
O14023 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: ACF2CF7C49C6AB5B

FASTA54461,850
        10         20         30         40         50         60 
MSTSSLAFLK AKACAEIVAE LIASENQNKV INLNALKMRI SKKHQLSESP RLTDIIAAIP 

        70         80         90        100        110        120 
PDAYLKESLM RKLRAKPVRT ASGIAVVAVM CKPHRCPHIA MTGNVCVYCP GGPDSDFEYS 

       130        140        150        160        170        180 
TQSYTGYEPT SMRAIRARYD PYEQARGRVE QLRSLGHTVD KVEYIIMGGT FMSLPESYRH 

       190        200        210        220        230        240 
TFIANLHNAL SGATTEDLDE AVKFSEQSET KCVGITIETR PDYCLDQHLD EMLRYGCTRL 

       250        260        270        280        290        300 
EIGVQSVYED VARDTNRGHT VKAVCETFQL AKDTGYKVVT HMMPDLPNVG MERDIFQFQE 

       310        320        330        340        350        360 
YFENPAFRTD GLKLYPTLVI RGTGLYELWK TGRYKNYTPN ALVDLIARIL ALVPPWTRIY 

       370        380        390        400        410        420 
RIQRDIPMPL VSSGVETGNL RELALNRMRD LGTKCRDIRA REVGMQEVHH KIHPEQVELL 

       430        440        450        460        470        480 
RRDYTANGGW ETFLSYEDPK QDILIGLLRL RQCSDKTYRP EFTSQPTSLV RELHVYGSAV 

       490        500        510        520        530        540 
PVHSRDPKKF QHQGFGTLLL EEAERIAKYE HGSKKISVIS GVGVRKYYQK LGYTLDGPYM 


SKWL 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB10146.1.
PIRT38469.
RefSeqNP_594862.1. NM_001020291.2.

3D structure databases

ProteinModelPortalO14023.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278111. 333 interactions.
MINTMINT-4669868.
STRING4896.SPAC29A4.20-1.

Proteomic databases

MaxQBO14023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC29A4.20.1; SPAC29A4.20.1:pep; SPAC29A4.20.
GeneID2541614.
KEGGspo:SPAC29A4.20.

Organism-specific databases

PomBaseSPAC29A4.20.

Phylogenomic databases

eggNOGCOG1243.
HOGENOMHOG000227514.
KOK07739.
OMAGYKVVSH.
OrthoDBEOG7Z95VX.
PhylomeDBO14023.

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

NextBio20802708.
PROO14023.

Entry information

Entry nameELP3_SCHPO
AccessionPrimary (citable) accession number: O14023
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names