ID   ELP3_BOVIN              Reviewed;         547 AA.
AC   Q2KJ61;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Elongator complex protein 3;
DE            EC=2.3.1.48;
GN   Name=ELP3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 and is involved in acetylation of histones H3 and
CC       probably H4. 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), which consists of IKBKAP/ELP1, STIP1/ELP2, ELP3,
CC       ELP4, and two yet unidentified proteins. IKBKAP/ELP1, STIP1/ELP2
CC       and ELP3 form the Elongator core complex. Elongator associates
CC       with the C-terminal domain (CTD) of Pol II largest subunit.
CC       Interacts with IKBKAP/ELP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       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; BC105500; AAI05501.2; -; mRNA.
DR   IPI; IPI00691160; -.
DR   RefSeq; NP_001124234.1; -.
DR   UniGene; Bt.40884; -.
DR   Ensembl; ENSBTAG00000002730; Bos taurus.
DR   GeneID; 784720; -.
DR   KEGG; bta:784720; -.
DR   HOVERGEN; Q2KJ61; -.
DR   OMA; Q2KJ61; GIQEVHH.
DR   BRENDA; 2.3.1.48; 251.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
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:0008607; F:phosphorylase kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription from RNA polyme...; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Nucleus;
KW   Phosphoprotein; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    547       Elongator complex protein 3.
FT                                /FTId=PRO_0000283985.
FT   DOMAIN      396    547       N-acetyltransferase.
FT   METAL        99     99       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       109    109       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       112    112       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   MOD_RES     202    202       Phosphotyrosine (By similarity).
SQ   SEQUENCE   547 AA;  62331 MW;  1B2F2B06FA019F81 CRC64;
     MRQKRKGDLS PAQLMMLTIG DVIKQLIEAH EQGKDIDLNK VKTRTAAKYG LSAQPRLVDI
     IAAVPPQYRK VLVPKLKAKP IRTASGIAVV AVMCKPHRCP HISFTGNICV YCPGGPDSDF
     EYSTQSYTGY EPTSMRAIRA RYDPYLQTRH RIEQLKQLGH SVDKVEFIVM GGTFMALPEE
     YRDYFIRNLH DALSGHTSNN IYEAVKYSER SLTKCIGITI ETRPDYCMKR HLSDMLTYGC
     TRLEIGVQSV YEDVARDTNR GHTVKAVCES FHLAKDSGFK VVAHMMPDLP NVGLERDIEQ
     FTEFFENPAF RPDGLKLYPT LVIRGTGLYE LWKSGRYKSY SPSDLIELVA RILALVPPWT
     RVYRVQRDIP MPLVSSGVEH GNLRELAFAR MKDLGIQCRD VRTREVGIQE IHHKVRPYQV
     ELVRRDYVAN GGWETFLSYE DPDQDILIGL LRLRKCSEET FRFELVGGVS IVRELHVYGS
     VVPVSSRDPT KFQHQGFGML LMEEAERIAR EEHGSGKIAV ISGVGTRNYY RKIGYRLQGP
     YMVKTLE
//