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Database: UniProt
Entry: A0A1V6Q235_9EURO
LinkDB: A0A1V6Q235_9EURO
Original site: A0A1V6Q235_9EURO 
ID   A0A1V6Q235_9EURO        Unreviewed;      1034 AA.
AC   A0A1V6Q235;
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=PENANT_c017G00205 {ECO:0000313|EMBL:OQD83289.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD83289.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
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:OQD83289.1}.
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DR   EMBL; MDYN01000017; OQD83289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6Q235; -.
DR   STRING; 416450.A0A1V6Q235; -.
DR   OrthoDB; 20296at2759; -.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1901336; P:lactone biosynthetic process; IEA:UniProt.
DR   GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR   CDD; cd05274; KR_FAS_SDR_x; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF46; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          952..1029
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1034 AA;  113254 MW;  FF9E4F1BE826DFF6 CRC64;
     MIADMYEEEG VKTFRVQTDV GFHSPMMIPL GKPLIGALQD VLHPTKPSVK LYSTALADPQ
     SQDLRDTEYW MRNMINPVRL TDAVESAVED GHRVFLKVAS HPLVSHSVTE TLLDGEIEDF
     LVASTLRRDQ PAEKSLVNCL GQLHCSGVEI NWKAQMPGPW AQGLPTGPWL HQPTLPKVSS
     NLTSMGSHET NQHSLVGHRI AVAGTATVVY TSILDKDSKP FPGDHPVSGT EIVPAACLLN
     TFLKSTRGRQ LQNIYLKVPL AIDVQRTIQV VVQGNKVRIM SQLSHTEHAD DCSWLTHTTA
     SWNVTSALDE EKIDLSESGC RSRKRQPDSF TIDYLASVGV SAMGFPWKVL EHYGDSSEMI
     ARVDVAPGVD VFDWDQSSWA PFLDAATSIG SCIFFEKARL RMPSQVQQVD IFTNHSPPKL
     GWVHVRRNPS SESCSDVRIL DDQGDLLVKF TCMQFSEIEG TTGTNKTVRG LVHRVAWPPA
     RPAEEPLRIE QLILVSGDPS LMQKYASSLP GHVKLLQVSG PDELQSFLDS TFAESTAIAY
     IPAEVASFAE VFEATKNHTC QLLQIMKCAV HASSPVKVFT STTNVMQGQS AAALANAPLV
     GLSRVIASEH PDDFGGLIDS ENYAVPLTTI KYIQDADVIR VLDGVPRTAR LRALPTDLRT
     QPICRSLPRP QGTYLVTGGM DALGLATAEF LAENGAQRLV FLSRRSLPPR STWNNVQVDL
     QPIIAKIQDL EQRGVSVHAL ALDISAPTAT RELLNGLQRL DLPPVVGVVH AAGVLENELI
     LESIQTAFHR VFAPKVNGAL VLHEAFPPGT LDFFLLFSSC GQLLGFPGQG SYGSANTFLD
     TLATHRRHLG ENSVSFQWTS WKEMGMGSDS EFVAAELEGK GITDITRNEA FQAWNHLAQY
     DLDHGVVLRT RALGSNSPVL QDIVTRSLDV NAQGDGSLNS ETSNTIPSSG PELRTYLDEH
     IRSCVASVLQ LSPSDADSRA AMSDLGLDSV MSVAFRRQLQ QTLKIPVPPT LAWNHPTVKH
     LVEWFVKKLD TQNV
//
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