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Database: UniProt
Entry: A0A1Y2M9A5_EPING
LinkDB: A0A1Y2M9A5_EPING
Original site: A0A1Y2M9A5_EPING 
ID   A0A1Y2M9A5_EPING        Unreviewed;       432 AA.
AC   A0A1Y2M9A5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=N-acetyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B5807_03040 {ECO:0000313|EMBL:OSS52694.1};
OS   Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX   NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS52694.1, ECO:0000313|Proteomes:UP000193240};
RN   [1] {ECO:0000313|EMBL:OSS52694.1, ECO:0000313|Proteomes:UP000193240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS52694.1,
RC   ECO:0000313|Proteomes:UP000193240};
RA   Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT   "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT   strain isolated from New Zealand.";
RL   Genome Announc. 0:0-0(2017).
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; KZ107839; OSS52694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2M9A5; -.
DR   STRING; 105696.A0A1Y2M9A5; -.
DR   InParanoid; A0A1Y2M9A5; -.
DR   OMA; WHVYEES; -.
DR   OrthoDB; 22809at2759; -.
DR   Proteomes; UP000193240; 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:UP000193240};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          162..197
FT                   /note="N-acetyltransferase ESCO zinc-finger"
FT                   /evidence="ECO:0000259|Pfam:PF13878"
FT   DOMAIN          363..430
FT                   /note="N-acetyltransferase ESCO acetyl-transferase"
FT                   /evidence="ECO:0000259|Pfam:PF13880"
FT   REGION          1..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..94
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  46704 MW;  2DEBD150363393F9 CRC64;
     MFPCSTKKAP RTYSRAKRPV YDEEPPTKRR RVEQRQAVKD GDGETAGASS PTRAVSAPEP
     SSSPQRTCSS DADAPARSTP PSSPPRPPTA ERSSPAPPAL DATLKATRRP VFALFKRQAK
     LQHSASAPAV LSSPPGPKQN ARTAAKPPSP PQQQPRKPRL VQMQLDLASQ QRKTCTCGME
     YVPSNAQDAA LHSKFHAANA GGVDCTRAMV ERLRGKQVWG GGEDGGFVAC VGRRDAAGLR
     KKASEVLHVV NTELAAVPIE DEELWSQMTL GPEGDSKAEK CDRFKVFLYI RGYKCVGACL
     AERVSGAYAV LGQGGRAADE LHEQEQEQQQ QQQQQQQQQQ IPAASSSSHS SSISVSTTAD
     PAVLLGISRI WVSSASRRRG LARTLLDCAR ANFSYGLVVD KRRTAFSQPT ESGGRLARRY
     FGCEAGWHVY MG
//
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