ID   ELP3_CAEEL              Reviewed;         547 AA.
AC   Q23651;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   16-JUN-2009, entry version 70.
DE   RecName: Full=Probable elongator complex protein 3;
DE            EC=2.3.1.48;
GN   Name=elpc-3; ORFNames=ZK863.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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.
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DR   EMBL; Z78019; CAB01454.2; -; Genomic_DNA.
DR   PIR; T28062; T28062.
DR   RefSeq; NP_506055.2; -.
DR   UniGene; Cel.23487; -.
DR   Ensembl; ZK863.3; Caenorhabditis elegans.
DR   GeneID; 179669; -.
DR   KEGG; cel:ZK863.3; -.
DR   NMPDR; fig|6239.3.peg.19930; -.
DR   WormBase; WBGene00014123; elpc-3.
DR   WormPep; ZK863.3; CE40344.
DR   OMA; Q23651; GIQEVHH.
DR   BRENDA; 2.3.1.48; 672.
DR   NextBio; 906382; -.
DR   ArrayExpress; Q23651; -.
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; Complete proteome; Iron; Iron-sulfur; Metal-binding;
KW   Nucleus; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    547       Probable elongator complex protein 3.
FT                                /FTId=PRO_0000283994.
FT   DOMAIN      392    547       N-acetyltransferase.
FT   METAL        95     95       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       105    105       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL       108    108       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
SQ   SEQUENCE   547 AA;  61910 MW;  6C7FAAEC59D8C6A6 CRC64;
     MDQKGSQRAL LAQTINEIVK LLIEAHNQKK DVNLNRLKCI VAQKNGLSFQ PKLVDIIAGV
     PSDYKDSLLP KLKAKPVRTA SGIAVVAVMS KPHRCPHINF TGNICVYCPG GPDSDFEYST
     QSYTGYEPTS MRAIRARYNP YLQTRGRLNQ LMQLGHSVDK VEFIVMGGTF MSLPEDYRDF
     FIRNLHDALS GHTSASVEEA VAYSERSKMK CIGITIETRP DYCLPRHLND MLLYGCTRLE
     IGVQSTYEDV ARDTNRGHTV KSVCETFHMA KDTGYKVVIH MMPDLPNVGL ERDKEQFLEL
     FESPAFRPDG LKLYPTLVIR GTGLYELWKT GRYQSYPPSV LVDLIATILS LVPPWTRVYR
     VQRDIPMPLV SSGVEHGNLR EHAMAKMKEL GLKCRDVRTR EVGIQEIHNK VRPEDVELIR
     RDYTANGGWE TFISYEDPKQ DILIGLLRLR KISDKAHRPE LKGNVSVVRE LHVYGSVVSV
     ADRDPKKFQH QGYGSLLMEE AERIAREEHG SDKIAVISGV GTREYYRKLG YELDGPYMSK
     MLDSAAA
//