ID   ECO1_CANGA              Reviewed;         261 AA.
AC   Q6FQ55;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=N-acetyltransferase ECO1;
DE            EC=2.3.1.-;
DE   AltName: Full=Establishment of cohesion protein 1;
GN   Name=ECO1; OrderedLocusNames=CAGL0I09042g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380955; CAG60576.1; -; Genomic_DNA.
DR   RefSeq; XP_447639.1; XM_447639.1.
DR   AlphaFoldDB; Q6FQ55; -.
DR   SMR; Q6FQ55; -.
DR   STRING; 5478.XP_447639.1; -.
DR   EnsemblFungi; CAG60576; CAG60576; CAGL0I09042g.
DR   GeneID; 2889020; -.
DR   KEGG; cgr:CAGL0I09042g; -.
DR   CGD; CAL0132682; CAGL0I09042g.
DR   VEuPathDB; FungiDB:CAGL0I09042g; -.
DR   eggNOG; KOG3014; Eukaryota.
DR   HOGENOM; CLU_039183_2_1_1; -.
DR   InParanoid; Q6FQ55; -.
DR   OMA; RIWVCRT; -.
DR   Proteomes; UP000002428; Chromosome I.
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..261
FT                   /note="N-acetyltransferase ECO1"
FT                   /id="PRO_0000074546"
FT   DOMAIN          102..261
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   ZN_FING         29..53
FT                   /note="CCHH-type"
SQ   SEQUENCE   261 AA;  29527 MW;  8193FEDEC8A00300 CRC64;
     MAVNHVRSKS SNGKRLVQSK LNINNETILK CPKCEMKYSP NSIDDVATHK KYHDLHINGR
     NWSQTWGIPI HDTTSSTIIA TPSSSPFKTG KSVNNKNNER IVMIQENKPA EVKAMLEIMD
     IVNQELNAPQ DENNFWRKPN AEHQGKAIVY IKDKKVVGAI TVEVLKQHKC RWMIYETRTL
     VEHVRPQFTL GISRIWVCRA QRGKGIAEKL LDAARISAIP GQNVDKMKLA WSQPSDSGGK
     LAKKYNGVKH KSGHILIPCY L