ID   ELP3_DICDI              Reviewed;         559 AA.
AC   Q1ZXC6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Probable elongator complex protein 3;
DE            EC=2.3.1.48;
GN   Name=elp3; ORFNames=DDB_G0290103;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalytic histone acetyltransferase subunit of the RNA
CC       polymerase II elongator complex, which is a component of the RNA
CC       polymerase II (Pol II) holoenzyme and is involved in
CC       transcriptional elongation. Elongator may play a role in chromatin
CC       remodeling. May also have a methyltransferase activity (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
CC   -!- SUBUNIT: Component of the RNA polymerase II elongator complex
CC       (Elongator). Elongator associates with the C-terminal domain (CTD)
CC       of Pol II largest subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the ELP3 family.
CC   -!- SIMILARITY: Contains 1 N-acetyltransferase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AAFI02000153; EAS66831.1; -; Genomic_DNA.
DR   RefSeq; XP_001134514.1; -.
DR   GeneID; 4238187; -.
DR   KEGG; ddi:DDB_0231756; -.
DR   dictyBase; DDB_G0290103; elp3.
DR   BRENDA; 2.3.1.48; 424.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR000182; GCN5-rel_AcTrfase.
DR   InterPro; IPR005910; Hist_AcTrfase_ELP3.
DR   InterPro; IPR007197; Radical_SAM.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR01211; ELP3; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Nucleus; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    559       Probable elongator complex protein 3.
FT                                /FTId=PRO_0000327510.
FT   DOMAIN      408    559       N-acetyltransferase.
FT   METAL       111    111       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       121    121       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       124    124       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
SQ   SEQUENCE   559 AA;  63210 MW;  B69CD84788F24AE2 CRC64;
     MSLMNDPRPV SKKAGAKPVY GKNTPQFTKT VGEIVNALIN AYKEGKKVNL LKIKTELAAK
     NSLSDQPKSV DIISAIPESY KNTLLPLLKA KPVRTASGIA VVAVMCKPHR CPHLAMTGNI
     CVYCPGGPDS DFEYSTQSYT GYEPTSMRAI RARYNPFLQT RHRIDQLKRL GHNVEKVEFI
     IMGGTFMSLP SDYRDYFIRN LHDALSGHTS NNVAEAVKYS EQSNVKCVGI TIETRPDHCL
     KLHLSNMLTY GCTRLEIGVQ SVFEDIARDT NRGHTVRAVL ESFQLAKDSG FKVVAHMMPD
     LPNMGMERDI YGFMEFFENP AFRADGLKIY PTLVIRGTGL YELWKTGTYK NYSPDSLVDL
     IAKVLALVPP WTRIYRIQRD IPMPLVTSGV EYGNLRELCL ARMKDFGTKC RDVRTREVGI
     QEVHHKIKPD QVELIRRDYV ANGGWETFLS FEDPKQDILI GLLRLRKCSE TSFRPELKEN
     CSIVRELHVY GSVVGIHNRD PTKFQHQGYG TLLMEEAERI AREEHGSIKL AVIAGVGTRH
     YYRKLGYELD GVYVSKYLG
//