ID   A0A1V6S713_9EURO        Unreviewed;       736 AA.
AC   A0A1V6S713;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=PENVUL_c005G09092 {ECO:0000313|EMBL:OQE09842.1};
OS   Penicillium vulpinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE09842.1, ECO:0000313|Proteomes:UP000191518};
RN   [1] {ECO:0000313|Proteomes:UP000191518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE09842.1}.
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DR   EMBL; MDYP01000005; OQE09842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6S713; -.
DR   STRING; 29845.A0A1V6S713; -.
DR   OrthoDB; 2479255at2759; -.
DR   Proteomes; UP000191518; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05195; enoyl_red; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191518};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          653..730
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   736 AA;  78686 MW;  9385D61FAD702772 CRC64;
     MAIDSGPNAA RRDAYTNGRP QPQPETSTMP IAIIGMACRL GGDASSPSKL WEMCTSARDA
     WSPIPQERFN AKALYHPNRE RVGRNHAVGG YFLNEDVALF DAGFFNFSGD VASTGIYYTS
     VAKIPESVGW VEAAALPSPF IAAYYALITL AALQSGESVL IHDAASDVGQ AAIVLSQKLG
     ATIFTLSKSS AEAELLTKTH NLAAGYNFSN DETGLSSIIG AQTDGLGVHV VFNTRSSPLV
     DSTWDCLRRF GRYVDLNGAS PPCSKAAQRG ATYSAFDVLQ VLEYRGSAAQ AALVEGIRIS
     HERTEVPILP LVTWPISELD RALTRIESQD NLGKIVVVPG ENDHVKILPQ PKIFSLDDPD
     TTYLIVGGLG GIAYTVASWM LEKGAKNLVI LSRHAAQHPK AAELQAVAQS QGSALQIRSC
     DASNEGDLLA HLAEVSHSFP PIKGVINGAM VLEDSVWERM THTQWQRAVA AKVAVTTNLD
     RYLSDLSFFI LLSSLTGVVG SASQANYAAG GAFQDALARH RTANGLPAVA LGLSAVESVG
     FVAETGDDAR RHIERLGSDS VSIETVLQLI QAAIRDPLRR SPAESQVIIG LTSWDRLAEN
     AATRRDRRFS TLRVGSKKTI ADAGISSGDE AGRSNSSAAL LRKLAEGHLE ATEAQGLFLD
     VIASKLASIF NIDAAGLDRE APLAQFGVDS LVAVDLRNWL GTSVKAKMSI FEILQSPSLQ
     EFASFVAQRS EWMSRG
//