ID A0A024G6G1_9STRA Unreviewed; 500 AA.
AC A0A024G6G1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN ORFNames=BN9_032150 {ECO:0000313|EMBL:CCI42431.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI42431.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI42431.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI42431.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:CCI42431.1}.
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DR EMBL; CAIX01000034; CCI42431.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024G6G1; -.
DR STRING; 65357.A0A024G6G1; -.
DR InParanoid; A0A024G6G1; -.
DR OrthoDB; 275667at2759; -.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR43618; 7-ALPHA-HYDROXYSTEROID DEHYDROGENASE; 1.
DR PANTHER; PTHR43618:SF8; 7ALPHA-HYDROXYSTEROID DEHYDROGENASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053237}.
FT DOMAIN 321..471
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 500 AA; 54875 MW; 96963E4047CEF6C2 CRC64;
MEVSNLFSVS DKIVLVTGGG RGIGKMIADG FVRNGAKVYI ASRNYASCKK AAAELKHQGP
GTCIALQGDI SSEKGCAHLA QQFASYESKL DVLVNNSGIA IPTAFDKHEE KVWQETFSVN
VAAAYFLARD LLPQLDRAAD LNGSARIINI GSVAGFSPSK MDVMAYDASK AALHHLTRVL
AAKLARRPNG GHINVNAIAP GVIPTDMTEI IRSAAASSFN NMGRTLPLGR CGDSKDIAGV
ALFLASRASE WITGIVVVVD GGHIRASFRL PLAKFNIKSN NVRKQESVDE LDIAIFNTES
DLDPTDRLIN VITIAQINPM VCIRNATVND LIQMQHTNLW CLPENYQMKY YLYHIMSWPQ
LLYVAESSNG KIVGYVLAKM EEEASVPHGH ITSLAVLRTH RKCGIATNLM KAAQRAMVEN
FAAEYVSLHV RESNEAAIHL YRHTLQYQVY DIESGYYADG EDAYDMRKSF SEKCSQAFAS
RTNKFQKIME EKDAAKVESS
//