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Database: UniProt
Entry: A0A1X7S6B6_ZYMTR
LinkDB: A0A1X7S6B6_ZYMTR
Original site: A0A1X7S6B6_ZYMTR 
ID   A0A1X7S6B6_ZYMTR        Unreviewed;       401 AA.
AC   A0A1X7S6B6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=N-acetyltransferase ECO1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ZT3D7_G10334 {ECO:0000313|EMBL:SMQ55179.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ55179.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ55179.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT853702; SMQ55179.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7S6B6; -.
DR   STRING; 1276538.A0A1X7S6B6; -.
DR   Proteomes; UP000215127; Chromosome 11.
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   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR028005; AcTrfase_ESCO_Znf_dom.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
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.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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:UP000215127};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          104..141
FT                   /note="N-acetyltransferase ESCO zinc-finger"
FT                   /evidence="ECO:0000259|Pfam:PF13878"
FT   DOMAIN          312..399
FT                   /note="N-acetyltransferase ESCO acetyl-transferase"
FT                   /evidence="ECO:0000259|Pfam:PF13880"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  43679 MW;  C67B2C9ACE9A2470 CRC64;
     MAANASSDGG APPSTPVPEV FSDEATRPGT PPSSPPAFPW ESKEGHEAKH DAKENTPPIR
     PAVMNVFSIL GKRKALDETT ANARATKKHV AHRKSSAKDA GMIQTQMNLG QSIQTTCKQC
     GMEYVLSSAE DRNLHAKFHK QNSEGVEVGA SFVDGTEAHK QFVGVAKRPA DAVIVVDSSD
     KKTRQKKSQA VLEVVQRELG AVSIPEADVW EKPKDAASDS EPQYHSYLYV REGKCIGYLL
     TQSIAEAYTV VIPSGCKAEP PDKDTHIQGE ESMSALARLK ARKLAKEQAE ETKRKRLEHA
     ARQPICLSKT RVPVVLGISR IWTSPMHRGQ GIAMALLDTA VEGYNAHFGA SRVGTADWTQ
     RPTLSKIKSK TQVAFSQPTE SGAKLARKWT GRLFGWSVYV D
//
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