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
//