ID   A0A0J9XAD4_GEOCN        Unreviewed;       331 AA.
AC   A0A0J9XAD4;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=N-acetyltransferase ECO1 {ECO:0000256|ARBA:ARBA00022043};
DE   AltName: Full=Establishment of cohesion protein 1 {ECO:0000256|ARBA:ARBA00032212};
GN   ORFNames=BN980_GECA05s07138g {ECO:0000313|EMBL:CDO53784.1};
OS   Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Geotrichum.
OX   NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO53784.1, ECO:0000313|Proteomes:UP000242525};
RN   [1] {ECO:0000313|EMBL:CDO53784.1, ECO:0000313|Proteomes:UP000242525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO53784.1,
RC   ECO:0000313|Proteomes:UP000242525};
RA   Casaregola S.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily.
CC       {ECO:0000256|ARBA:ARBA00005816}.
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DR   EMBL; CCBN010000005; CDO53784.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J9XAD4; -.
DR   STRING; 1173061.A0A0J9XAD4; -.
DR   OrthoDB; 22809at2759; -.
DR   Proteomes; UP000242525; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR   InterPro; IPR028009; ESCO_Acetyltransf_dom.
DR   PANTHER; PTHR45884; N-ACETYLTRANSFERASE ECO; 1.
DR   PANTHER; PTHR45884:SF2; N-ACETYLTRANSFERASE ECO; 1.
DR   Pfam; PF13880; Acetyltransf_13; 1.
DR   Pfam; PF13878; zf-C2H2_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDO53784.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          56..92
FT                   /note="N-acetyltransferase ESCO zinc-finger"
FT                   /evidence="ECO:0000259|Pfam:PF13878"
FT   DOMAIN          214..273
FT                   /note="N-acetyltransferase ESCO acetyl-transferase"
FT                   /evidence="ECO:0000259|Pfam:PF13880"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   331 AA;  36426 MW;  2266D08E6408E426 CRC64;
     MISDNSDEEE ETIMKSHRQK EKANTCARGT SVISDIKRKR RKTDPGPQTA GSKMVQTRLA
     LGDEFQTTCK ECGMSFMPTY SLDVKLHAKF HSKSVDGRDW SLDWGSPVKF PTHVAKVMEG
     YTVVKVTPSS RVAAKKAAQD MIQLVNTELS APPENPTWNN GPAGAGAAYL YVCKKNKKAV
     GILVVERVSR GRPMVVSTSE ILPSDTMAIH ARFPVVMGVS RIFTVRNYRR MGISTALLDI
     ARYDFIFGLR SQKLQVAWSQ PSASGAKLAL KWAPITLKPA EKEDSFKSLL SPPPSSPAID
     GNKQDGNKQD GDLASPRLAI LTYLERDAIV R
//