ID F2PXX3_TRIEC Unreviewed; 245 AA.
AC F2PXX3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=N-terminal acetyltransferase A complex catalytic subunit ard1 {ECO:0000313|EMBL:EGE06741.1};
GN ORFNames=TEQG_05736 {ECO:0000313|EMBL:EGE06741.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the acetyltransferase family. ARD1 subfamily.
CC {ECO:0000256|ARBA:ARBA00025786}.
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DR EMBL; DS995751; EGE06741.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PXX3; -.
DR VEuPathDB; FungiDB:TEQG_05736; -.
DR eggNOG; KOG3235; Eukaryota.
DR HOGENOM; CLU_013985_7_0_1; -.
DR Proteomes; UP000009169; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGE06741.1}.
FT DOMAIN 23..173
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 189..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 245 AA; 27549 MW; 00F5E0728BBCE97E CRC64;
MVDIVPLCSY PSYISLLPAV QTCNITNLPE NYFLKYYLYH ALSWPQLSFV AVVRDRSSKS
KDPFAPAANP KVVGYVLAKM EEEPSDGLPH GHITSLSVMR THRRLGIAER LMRMSQRAMA
ESHKAHYVSL HVRVSNNAAL RLYRDTLGFE VEKIEPKYYA DGENAYAMKM DLTNLWLKDD
DGYSVGLDGK SFKNTDEDAD EGDEVGDMGK AGDEARKEEK KIRVKVGRSL GVGDLVERNE
TRAQA
//
