(data stored in ACNUC8465 zone)

SWISSPROT: Q6FJH0_CANGA

ID   Q6FJH0_CANGA            Unreviewed;       557 AA.
AC   Q6FJH0;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 104.
DE   RecName: Full=Elongator complex protein 3 {ECO:0000256|PIRNR:PIRNR005669};
DE            EC=2.3.1.48 {ECO:0000256|PIRNR:PIRNR005669};
GN   OrderedLocusNames=CAGL0M06369g {ECO:0000313|CGD:CAL0136267,
GN   ECO:0000313|EMBL:CAG62600.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62600.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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. {ECO:0000256|PIRNR:PIRNR005669}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC         acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-
CC         COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005669};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR005669};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|PIRNR:PIRNR005669};
CC   -!- SIMILARITY: Belongs to the ELP3 family.
CC       {ECO:0000256|PIRNR:PIRNR005669}.
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DR   EMBL; CR380959; CAG62600.1; -; Genomic_DNA.
DR   RefSeq; XP_449624.1; XM_449624.1.
DR   STRING; 5478.XP_449624.1; -.
DR   EnsemblFungi; CAG62600; CAG62600; CAGL0M06369g.
DR   GeneID; 2891672; -.
DR   KEGG; cgr:CAGL0M06369g; -.
DR   CGD; CAL0136267; CAGL0M06369g.
DR   EuPathDB; FungiDB:CAGL0M06369g; -.
DR   eggNOG; KOG2535; Eukaryota.
DR   eggNOG; COG1243; LUCA.
DR   HOGENOM; HOG000227514; -.
DR   InParanoid; Q6FJH0; -.
DR   KO; K07739; -.
DR   OMA; TFETRPD; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0033588; C:Elongator holoenzyme complex; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0002098; P:tRNA wobble uridine modification; IEA:EnsemblFungi.
DR   Gene3D; 3.80.30.20; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR039661; ELP3.
DR   InterPro; IPR034687; ELP3-like.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR032432; Radical_SAM_C.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR023404; rSAM_horseshoe.
DR   PANTHER; PTHR11135; PTHR11135; 1.
DR   PANTHER; PTHR11135:SF0; PTHR11135:SF0; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   Pfam; PF16199; Radical_SAM_C; 1.
DR   PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1.
DR   SFLD; SFLDF00344; ELP3-like; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR01211; ELP3; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJH0.
DR   SWISS-2DPAGE; Q6FJH0.
KW   Acyltransferase {ECO:0000256|PIRNR:PIRNR005669};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Iron {ECO:0000256|PIRNR:PIRNR005669};
KW   Iron-sulfur {ECO:0000256|PIRNR:PIRNR005669};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR005669};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR005669};
KW   Transcription {ECO:0000256|PIRNR:PIRNR005669};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR005669};
KW   Transferase {ECO:0000256|PIRNR:PIRNR005669}.
FT   DOMAIN      405    557       N-acetyltransferase.
FT                                {ECO:0000259|PROSITE:PS51186}.
SQ   SEQUENCE   557 AA;  63572 MW;  5351E63970C01744 CRC64;
     MGRHGKGPKT NKQKLAPEKE RFLQCCTDIT LELTNSLTSG TTREINLNGL ITKYSKKYKL
     KQQPRLTDII NSIPDQYKKY LLPKLKAKPV RTASGIAVVA VMCKPHRCPH IAYTGNICVY
     CPGGPDSDFE YSTQSYTGYE PTSMRAIRAR YDPYEQARGR VEQLKQLGHS IDKVEYVVMG
     GTFMSLPKDY REDFIVKLHN ALSGYNGNDI DEAIRYSQQS LTKCVGITIE TRPDYCTETH
     LDDMLKYGCT RLEIGVQSLY EDVARDTNRG HTVKAVTETF AIAKDAGYKV VSHMMPDLPN
     VGMERDLQQF KEYFENPAFR TDGLKIYPTL VIRGTGLYEL WKTGRYKSYN ANALVDLVAR
     IMAMVPPWTR IYRVQRDIPM PLVTSGVDNG NLRELALARM KDLGVTSRDV RTREVGIQEV
     HHKVQPDQVE LIRRDYYANG GWETFLSYED PKQDILIGLL RLRKASKKYT YRKEFTSQRT
     SIVRELHVYG SVVPLHSRDP KKFQHQGFGT LLMEEAERIA KEEHGSSKIS VISGVGVRNY
     YAKLGYELDG PYMSKKI
//

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