ID   ECO1_YARLI              Reviewed;         271 AA.
AC   Q6C668;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=N-acetyltransferase ECO1;
DE            EC=2.3.1.-;
DE   AltName: Full=Establishment of cohesion protein 1;
GN   Name=ECO1; OrderedLocusNames=YALI0E12023g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Probable acetyltransferase required for the establishment of
CC       sister chromatid cohesion and couple the processes of cohesion and DNA
CC       replication to ensure that only sister chromatids become paired
CC       together. In contrast to the structural cohesins, the deposition and
CC       establishment factors are required only during S phase. Acts by
CC       acetylating the cohesin complex component SMC3 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR382131; CAG79437.1; -; Genomic_DNA.
DR   RefSeq; XP_503844.1; XM_503844.1.
DR   AlphaFoldDB; Q6C668; -.
DR   SMR; Q6C668; -.
DR   STRING; 4952.CAG79437; -.
DR   EnsemblFungi; CAG79437; CAG79437; YALI0_E12023g.
DR   GeneID; 2912808; -.
DR   KEGG; yli:YALI0E12023g; -.
DR   VEuPathDB; FungiDB:YALI0_E12023g; -.
DR   HOGENOM; CLU_1027468_0_0_1; -.
DR   InParanoid; Q6C668; -.
DR   OMA; RIWVCRT; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IEA:InterPro.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR   InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR   InterPro; IPR033257; Eco1/CTF7.
DR   InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR   PANTHER; PTHR45884:SF2; PTHR45884:SF2; 1.
DR   Pfam; PF13880; Acetyltransf_13; 1.
DR   Pfam; PF13878; zf-C2H2_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell cycle; Metal-binding; Nucleus; Reference proteome;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..271
FT                   /note="N-acetyltransferase ECO1"
FT                   /id="PRO_0000074549"
FT   ZN_FING         80..104
FT                   /note="CCHH-type"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   271 AA;  29891 MW;  3E8A22B09F703CC3 CRC64;
     MKTYRAKRKY LSESEDDVFS SSPTQSPETS PLQPPNESRL NIKAAQAVSP CQKRAKVVKK
     PAKTKAPVQM TLSLGQTTST TCKTCGMTYQ VAYGPDISAH KSFHSTALNG PKWKPSVSAV
     VVDKSKTYTV YKSRLLSHPC VSQFLKLVNS ELNAPEPILS SQAAVYVYVV DQRAVGCVLV
     DRITKCRHVD IQTGTLGLKE YPAVMGVSRM YVSQLFRRTG IVTKLLDLAK SDFIYGMELE
     KNQVAFTQPS EGGLKVAENW AGTVRVYREG E