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Database: UniProt
Entry: A0A319EQN8_ASPSB
LinkDB: A0A319EQN8_ASPSB
Original site: A0A319EQN8_ASPSB 
ID   A0A319EQN8_ASPSB        Unreviewed;       551 AA.
AC   A0A319EQN8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=CoA-dependent acyltransferase {ECO:0000313|EMBL:PYI12626.1};
GN   ORFNames=BO78DRAFT_7719 {ECO:0000313|EMBL:PYI12626.1};
OS   Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI12626.1, ECO:0000313|Proteomes:UP000248423};
RN   [1] {ECO:0000313|EMBL:PYI12626.1, ECO:0000313|Proteomes:UP000248423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI12626.1,
RC   ECO:0000313|Proteomes:UP000248423};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ826315; PYI12626.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319EQN8; -.
DR   STRING; 1448318.A0A319EQN8; -.
DR   Proteomes; UP000248423; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd19545; FUM14_C_NRPS-like; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:PYI12626.1};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW   Transferase {ECO:0000313|EMBL:PYI12626.1}.
FT   DOMAIN          1..71
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          78..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   551 AA;  62346 MW;  8A19123D796521CE CRC64;
     MDRLRHIWAD VLCLGADEFD DTDSFFELGG DSVKAIQLLG EAAAFAPDLD MDTFYRYPTL
     NAFYSYTKEC TEDRRLASRP RCNGNGVTDS QADVSYDGND VSSKSTVDAP GIEVRDIESP
     LRAVAIDKKA VVKAARITPI QEFFMHLAMA GNVGLLNYVY EIEGPLLLTG LQQLVQQLET
     KNPILRTTII QAEDEFIQIV LNQSMSEWVH SSDIHKYMQH TMTLKMTLGA RPVQYCLIMN
     DKTHGKNFFI ISIHHMFCDA FSRYLIEKEM LQILRSPSDY AQEPERPWFG DFVTHLRATR
     SDAEVAHYWD RYLQGADLAN IHSNSLSNDG PGELDGELIE IIPASIFGSH SHVSHTQVVL
     AAWSLALAKL SGLRDITFGL CRHGRSHPYQ DIRRMVGPLV SATPFRIKLL DDDQRVEDLV
     QGVQDEVTAT AHWEQGHIPG VYNLGDGRPF VQSLVNLKSE LYAMPDGYTD KEQNGDIWRL
     ATRRDLQNYD MKSDWPVLLL IHQQKGVFRL KMYYQSSLVD HEKAATLFHD LKHFVESLAS
     AECSTVGDLL R
//
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