ID   ECO1_KLULA              Reviewed;         271 AA.
AC   Q6CW60;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=N-acetyltransferase ECO1;
DE            EC=2.3.1.-;
DE   AltName: Full=Establishment of cohesion protein 1;
GN   Name=ECO1; OrderedLocusNames=KLLA0B06644g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382122; CAH02222.1; -; Genomic_DNA.
DR   RefSeq; XP_451829.1; XM_451829.1.
DR   AlphaFoldDB; Q6CW60; -.
DR   SMR; Q6CW60; -.
DR   STRING; 28985.XP_451829.1; -.
DR   EnsemblFungi; CAH02222; CAH02222; KLLA0_B06644g.
DR   GeneID; 2896862; -.
DR   KEGG; kla:KLLA0_B06644g; -.
DR   eggNOG; KOG3014; Eukaryota.
DR   HOGENOM; CLU_039183_2_1_1; -.
DR   InParanoid; Q6CW60; -.
DR   OMA; HISASRK; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0043596; C:nuclear replication fork; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0140588; P:chromatin looping; IEA:EnsemblFungi.
DR   GO; GO:0006260; P:DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0006302; P:double-strand break repair; IEA:EnsemblFungi.
DR   GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IEA:EnsemblFungi.
DR   GO; GO:0018393; P:internal peptidyl-lysine acetylation; IEA:EnsemblFungi.
DR   GO; GO:0045132; P:meiotic chromosome segregation; IEA:InterPro.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IEA:EnsemblFungi.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:EnsemblFungi.
DR   GO; GO:0032200; P:telomere organization; IEA:EnsemblFungi.
DR   GO; GO:0070058; P:tRNA gene clustering; IEA:EnsemblFungi.
DR   InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR033257; Eco1/CTF7.
DR   InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR45884:SF2; PTHR45884:SF2; 1.
DR   Pfam; PF13880; Acetyltransf_13; 1.
DR   Pfam; PF13878; zf-C2H2_3; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 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_0000074548"
FT   DOMAIN          109..271
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   ZN_FING         26..50
FT                   /note="CCHH-type"
SQ   SEQUENCE   271 AA;  30936 MW;  3D0275DB1472EF24 CRC64;
     MSKYRSPKTK KSIQATLQFK STPTLVKCPK CSITYSTNSP SDLVQHKRYH DLHLNGKRWS
     QSWGDIINRV EALKTEKQLK YSMVSEKDKK VMSFQLPSQT LYEEDEYIVM ISPKKANEVK
     AALDLMSIVN EELNAPHDEN AFWSEVDKSG KSQGKAFIYV KKNRAVGVIT IEYIENTNRG
     KWMVLDTKAI VPNVVPDVKL GISRIWVCRN QRQHGIATRL LEVARKKSIY GCIVNKWELA
     WSQPSQSGSI LAKSYNAAKH RSGKLLIPCY I