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Database: UniProt
Entry: A0A0K6FR21_9AGAM
LinkDB: A0A0K6FR21_9AGAM
Original site: A0A0K6FR21_9AGAM 
ID   A0A0K6FR21_9AGAM        Unreviewed;       378 AA.
AC   A0A0K6FR21;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   SubName: Full=N-acetyltransferase {ECO:0000313|EMBL:CUA68542.1};
GN   ORFNames=RSOLAG22IIIB_03580 {ECO:0000313|EMBL:CUA68542.1};
OS   Rhizoctonia solani.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA68542.1, ECO:0000313|Proteomes:UP000044841};
RN   [1] {ECO:0000313|EMBL:CUA68542.1, ECO:0000313|Proteomes:UP000044841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA68542.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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; CYGV01000446; CUA68542.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K6FR21; -.
DR   Proteomes; UP000044841; 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   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:UP000044841};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUA68542.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          105..140
FT                   /note="N-acetyltransferase ESCO zinc-finger"
FT                   /evidence="ECO:0000259|Pfam:PF13878"
FT   DOMAIN          308..372
FT                   /note="N-acetyltransferase ESCO acetyl-transferase"
FT                   /evidence="ECO:0000259|Pfam:PF13880"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  40844 MW;  2C0C3CE91EE441CC CRC64;
     MESRQTSTLK VYGSRAGVRS IHNSSSQGLD GDATTSVASD SGLFPEHKAS ISGLKRKSTS
     ANNLHSFFGA SQPTKKLRLA GKSQKSSSSK QASSNEEAKA PALTQLHFLP SKPILVTCKA
     CDLSYTRGAK EDEELHRTHC LRIARGLEWS REERSLEQPL GTGTSEVELI EECCKLSNGV
     VGRILRIRCD ATRGKLGPKV TTLLSTINKV LSAPPLPSSS LKVSKAYVMV IPTKSSKSHD
     PRLKKDTPTT RFSTERIVGC VVTTHIAEAM RIVDIKKLEA SNSPRSELVC VDFSSSEGGV
     YCDPNPIPAT LGIPRLFVVP SHRRQGIARA LLDAAAKTAI WGCPLDPTSG QIAFSQPTAS
     GHAVMTDWGK HNIRIYQE
//
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