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Database: UniProt
Entry: A0A150UUF1_9PEZI
LinkDB: A0A150UUF1_9PEZI
Original site: A0A150UUF1_9PEZI 
ID   A0A150UUF1_9PEZI        Unreviewed;       226 AA.
AC   A0A150UUF1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
DE   Flags: Fragment;
GN   ORFNames=M433DRAFT_546626 {ECO:0000313|EMBL:KYG41964.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG41964.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG41964.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG41964.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA   Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA   Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00025786}.
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:KYG41964.1}.
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DR   EMBL; JPDO01000547; KYG41964.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150UUF1; -.
DR   STRING; 766039.A0A150UUF1; -.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
DR   GO; GO:0031415; C:NatA complex; IEA:InterPro.
DR   GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR045047; Ard1-like.
DR   InterPro; IPR000182; GNAT_dom.
DR   PANTHER; PTHR23091; N-TERMINAL ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR23091:SF4; N-TERMINAL AMINO-ACID N(ALPHA)-ACETYLTRANSFERASE NATA; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..151
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          158..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KYG41964.1"
SQ   SEQUENCE   226 AA;  25048 MW;  891FA0C0BE4E0B76 CRC64;
     PHVQQTNITN LPENYFCKYY LYHALSWPQL SYVAVDVSRP KKTPYDPPKI VGYVLAKMEE
     DPQDGIPHGH ITSLSVMRTH RRLGLAEKLM RQSQRAMYES YNAVYVSLHV RVSNVAALSL
     YKSTLGFKVV GTEAKYYADG EDAHSMRKDL EYLRHEALDA KSDEEDEVES SVGNDEGDAV
     GSAGKADAGE GAEGKKKEKK LKVKVGRGLG VGELVERNEA TQTNGA
//
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