ID A0A2G7GBC9_9EURO Unreviewed; 398 AA.
AC A0A2G7GBC9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Sister chromatid cohesion acetyltransferase Eco1 {ECO:0000313|EMBL:PIG90152.1};
GN ORFNames=AARAC_007142 {ECO:0000313|EMBL:PIG90152.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG90152.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG90152.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG90152.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIG90152.1}.
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DR EMBL; NEXV01000019; PIG90152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G7GBC9; -.
DR STRING; 656916.A0A2G7GBC9; -.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000231358; 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 Reference proteome {ECO:0000313|Proteomes:UP000231358};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIG90152.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 154..191
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 327..395
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 44461 MW; 810442B6FA9E005A CRC64;
MPWTVTNSFK RGLMMKTYGR PVWRVYDDDQ SPAAKKRRVQ SGNESDEAEN SIQYAIRESS
AAVLSSPSRR NSILLSEGTQ DDDLSTPPSS PPPRLSSPPA NTRKPTFAFL KRKQSSNKET
GNSSPLTEVN SNSVRASVDP PKKKAASQQP VLKQMQLDLG HEVRRTCATC GMEYVPSNSE
DAALHKKFHD MNSTGVDLGK AFMRANASRW VYEATRFDEG YVVIVDRKAS PTAKNQAKKV
LEVINKELSS PEIQDDVLWS QIEPPTHLRK NGVSEKVDRY KVFLHMKDSR CVGACLTERI
WESRPVEKPS SQTNRADSAV TVRNETHPAI VGISRIWTSG SSRRKGIAMD LLDCVVSNFI
YGMEIPKEQM AFSQPTESGR ALAQSFFGGD EWHVYEES
//
