ID   A0A0J8QPX5_COCIT        Unreviewed;       250 AA.
AC   A0A0J8QPX5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=N-terminal acetyltransferase {ECO:0000313|EMBL:KMU73413.1};
GN   ORFNames=CISG_03548 {ECO:0000313|EMBL:KMU73413.1};
OS   Coccidioides immitis RMSCC 3703.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU73413.1, ECO:0000313|Proteomes:UP000054559};
RN   [1] {ECO:0000313|Proteomes:UP000054559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00025786}.
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DR   EMBL; DS268130; KMU73413.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8QPX5; -.
DR   STRING; 454286.A0A0J8QPX5; -.
DR   Proteomes; UP000054559; 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:UP000054559};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KMU73413.1}.
FT   DOMAIN          23..172
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          180..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   250 AA;  28167 MW;  16E63A52FCE2B00F CRC64;
     MVDIVPLCSY PSYLSLLPSI QTCNITNLPE NYFLKYYMYH ALSWPQLSFV AVVRSPPNGG
     KNKYSGDYPK VVGYVLAKME EEPLDGVAHG HITSLSVMRT HRRLGIAERL MRMSQRAMAE
     SHRAHYVSLH VRVSNTAALH LYRDTLGFEV EKVESKYYAD GEDAYAMRMD LRDLWVKEDK
     EPRTAASESK SAAKTKKQED DGDDDVQDEG DEVGSMGKKE DGKEGEKMVK VKIGRALGVG
     DLVERNEAVR
//