ID   ELP3_XENLA              Reviewed;         549 AA.
AC   Q5HZM6;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   06-MAR-2013, entry version 55.
DE   RecName: Full=Elongator complex protein 3;
DE            EC=2.3.1.48;
GN   Name=elp3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-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. May also have a methyltransferase activity (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
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.
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DR   EMBL; BC088956; AAH88956.1; -; mRNA.
DR   RefSeq; NP_001088974.1; NM_001095505.1.
DR   UniGene; Xl.16750; -.
DR   ProteinModelPortal; Q5HZM6; -.
DR   GeneID; 496354; -.
DR   KEGG; xla:496354; -.
DR   CTD; 55140; -.
DR   Xenbase; XB-GENE-957353; elp3.
DR   HOVERGEN; HBG107845; -.
DR   KO; K07739; -.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008607; F:phosphorylase kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0016573; P:histone acetylation; IEA:GOC.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.80.30.20; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR005910; Hist_AcTrfase_ELP3.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
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   SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 1.
DR   TIGRFAMs; TIGR01211; ELP3; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Iron; Iron-sulfur; Metal-binding; Nucleus;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    549       Elongator complex protein 3.
FT                                /FTId=PRO_0000283990.
FT   DOMAIN      398    549       N-acetyltransferase.
FT   METAL       101    101       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       111    111       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       114    114       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
SQ   SEQUENCE   549 AA;  62577 MW;  3DBC66E707E42063 CRC64;
     MKPDRGMRGN MSQAELMMMT VADVIKQLVE AHEQGKDVNL NKLKTKTSAK YGLSAQPRLV
     DIIAAVPPQY RKILVPKLKA KPIRTASGIA VVAVMCKPHR CPHINFTGNI CVYCPGGPDS
     DFEYSTQSYT GYEPTSMRAI RARYDPYLQT RHRVEQLKQL GHNVDKVEFI VMGGTFMALP
     EDYRDFFIRN LHDALSGHTS NSVSEAVRYS ERSNTKCVGI TIETRPDYCL KRHLSDMLCY
     GCTRLEIGVQ SVYEDVARDT NRGHTVKAVC ESFHLSKDAG FKVVSHMMPD LPNMGLERDI
     EQFIEFFENP AFRPDGMKLY PTLVIRGTGL YELWKTGRYR SYSPSTLVDL VARILALVPP
     WTRVYRVQRD IPMPLVSSGV EHGNLRELAL ARMKDLGTEC RDVRTREVGI QEIHHKVRPY
     QVELIRRDYV ANGGWETFLS YEDPEQDILI GLLRLRKCSE ESFRPELKGG VSIVRELHVY
     GSVVPISSRD PSKFQHQGFG MLLMEEAERI ARDEHGSWKI AVISGVGTRN YYRKIGYELE
     GPYMVKRLD
//