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Database: UniProt
Entry: A0A0P1BLY2_9BASI
LinkDB: A0A0P1BLY2_9BASI
Original site: A0A0P1BLY2_9BASI 
ID   A0A0P1BLY2_9BASI        Unreviewed;       143 AA.
AC   A0A0P1BLY2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Ribosomal-protein-alanine acetyltransferase {ECO:0000313|EMBL:CEH17717.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH17717.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH17717.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CCYA01000265; CEH17717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BLY2; -.
DR   STRING; 401625.A0A0P1BLY2; -.
DR   OrthoDB; 2781792at2759; -.
DR   UniPathway; UPA00113; UER00529.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR43233; FAMILY N-ACETYLTRANSFERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G03350)-RELATED; 1.
DR   PANTHER; PTHR43233:SF1; FAMILY N-ACETYLTRANSFERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G03350)-RELATED; 1.
DR   Pfam; PF13508; Acetyltransf_7; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW   Transferase {ECO:0000313|EMBL:CEH17717.1}.
FT   DOMAIN          1..124
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          119..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   143 AA;  15705 MW;  73D15AB61102AC01 CRC64;
     MRFEAGLTPP PTAEIAEIGL KSSVYCVVAR DTSTASKEAI GMARVVGDIT MSLLIVDVCV
     LPTHQHKGIG HRIFQHLLAW VDANSPSAFL SLSADPPGMK LYERNGFKVT PNETGMQRLG
     QDIENRRRFA REQRAKGREG EGE
//
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