ID A0A1V6QQX6_9EURO Unreviewed; 389 AA.
AC A0A1V6QQX6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Sister chromatid cohesion acetyltransferase Eco1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSOL_c051G00893 {ECO:0000313|EMBL:OQD91623.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD91623.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD91623.1}.
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DR EMBL; MDYO01000051; OQD91623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QQX6; -.
DR STRING; 60172.A0A1V6QQX6; -.
DR OrthoDB; 22809at2759; -.
DR Proteomes; UP000191612; 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:UP000191612};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 145..181
FT /note="N-acetyltransferase ESCO zinc-finger"
FT /evidence="ECO:0000259|Pfam:PF13878"
FT DOMAIN 318..386
FT /note="N-acetyltransferase ESCO acetyl-transferase"
FT /evidence="ECO:0000259|Pfam:PF13880"
FT REGION 57..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 43854 MW; 93FD011F15DEFD04 CRC64;
MPWTVTNSFK RGLMKTYGRP TWRVYDDERA AKKRRVDESD EAEANLQYAI RESSAAVLSS
PSRRNSLLSE GTLDDIDDLT TPPSSPPPRL TPPPANTRKP TFAFLKRKHK EITAGSPLTE
VNSNSVRASV DPPKQKGQKQ PVMRQMQIDL GNDTRKTCAT CGMEYIPSNT EDAALHKKFH
EMNATGIDLG KAFMRANASR WVYEATRFDE GYVVIVDRKA SPSAKSQAKK VLEVVNKELS
SPEIDDETLW SQTEPPKHLQ DGPTEKVDRY RVFLHMKDSR CVGLCLTERI WESRPVVKEP
NGDAHNGSSV STRDEIRPAI VGVSRIWTSG SSRRKGIALD LLDCVVINFI YGMEITKGQI
AFSQPTESGN RLAHKFFEDE ETWHVYNER
//
