ECO1_DEBHA
ID ECO1_DEBHA Reviewed; 288 AA.
AC Q6BJY5; B5RUP1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=N-acetyltransferase ECO1;
DE EC=2.3.1.-;
DE AltName: Full=Establishment of cohesion protein 1;
GN Name=ECO1; OrderedLocusNames=DEHA2F26356g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAR66419.1; -; Genomic_DNA.
DR RefSeq; XP_002770903.1; XM_002770857.1.
DR AlphaFoldDB; Q6BJY5; -.
DR SMR; Q6BJY5; -.
DR STRING; 4959.XP_002770903.1; -.
DR EnsemblFungi; CAR66419; CAR66419; DEHA2F26356g.
DR GeneID; 8999074; -.
DR KEGG; dha:DEHA2F26356g; -.
DR eggNOG; KOG3014; Eukaryota.
DR HOGENOM; CLU_039183_2_1_1; -.
DR InParanoid; Q6BJY5; -.
DR OMA; RIWVCRT; -.
DR OrthoDB; 1138803at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045132; P:meiotic chromosome segregation; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:InterPro.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
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 PANTHER; PTHR45884:SF2; PTHR45884:SF2; 1.
DR Pfam; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell cycle; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..288
FT /note="N-acetyltransferase ECO1"
FT /id="PRO_0000074547"
FT ZN_FING 50..74
FT /note="CCHH-type"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 288 AA; 32257 MW; D3DDE26F83035472 CRC64;
MKRDITQLLS PELSQSSSRN DKKRKPTNSN KKVQTVLNFP SSSPNASQST TCPTCGMTYY
SHVSKDNDVH NKYHFNFING IPWPTSFCNN VLERFIVVDH TTGKAKGTSK SKKSQAASKE
TLVMTIDRRA SKQVKRVEEI LKVVNGELNA ASDGKAWQKD HKGPIQGRAF IVVIDGRAIG
ICTTEPIQDV DQQCRWIIHR TQALVPNQVN RSIKLGISRI WIAPKWRRYG LARRLLDIVL
VHSVYGIVLD KKEIGFSQPS FSGGLLAKSF NGVTHKSGEI LIPVYLEE
