ID A0A1F5LLG7_9EURO Unreviewed; 1663 AA.
AC A0A1F5LLG7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGE53946.1};
GN ORFNames=PENARI_c007G07676 {ECO:0000313|EMBL:OGE53946.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE53946.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE53946.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE53946.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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:OGE53946.1}.
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DR EMBL; LXJU01000007; OGE53946.1; -; Genomic_DNA.
DR STRING; 1835702.A0A1F5LLG7; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000177622; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF24; NON-REDUCING POLYKETIDE SYNTHASE APTA-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000177622};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 316..747
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1586..1663
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1663 AA; 181631 MW; 0C9ECA31E408665C CRC64;
MDWVENLEDL QKSPAGGALE GALLCVLELG MLIGHYESQG ILYDLPVSDG MVLAGMSIGL
FSAAAVATSS SLFELAHTGS TSVRVAFRFG LHVGRVSHML EPLGEVRKSW AYVVAGLDVA
EVQDALDAYN TDTKNSDICR VCISHADSIS VGITGPPSRL ESLFRHSPVL RNAKRSPLPI
YGGLCHVSHI YSHEDVHEIL RGFGTAKENR RPVYIPLLSP NSGKPFIADD AAQLYEAICT
EALTMPLFPD KLSSGITLNL SSVESKECEV YQFHRSVASD QILASIGASL PSIQLKTQNL
MDWIHKETKL PSPNPSQKLA IVGMSCRLPG GANDPELFWK LLMEGRNTCT TVPQDRFDLE
THFDPTGKTI NATESPFGNF IDHPGLFDSG FFNMSPREAD QTDPMQRLAL VTAYEALEMS
GYAPDRTAST CRKRVGTFYG QASDDYRETN AGQQIGTYGI PGGERAFGNG RINYFFNFGG
PSFNIDTACS SGLAAVNAAC SSLWAGETDM VIAGGLNVIT NSDIYCMLSK GHFLSKTGQC
KVWDKSADGY CRSDGVGSVV IKKLEDALAD NDPIIATIVS GATNHSCEAV SITHPHAGAQ
KDNYRQVMHT AGVSPLDVSY VELHGTGTQA GDGVESESVA SVFAPLTQAR QQRLHLGAVK
ANIGHGEAAA GVTSLIKVLL AFENEEIPRH IGITTEINPI VMQNTKNRNT GLVMEHTKWP
RPEKRGRYAI VNSFGAHGGN TTLLLEDAPR KPKVTPESRA AYPITLSAKS KASLKENTKA
LIHFIDANPD VTLGDLSYTT CARRMHHHTR IATSATNKAQ LRSFLESSIE KVGSLRPVPA
TAPGVAFVFT GQGAFYRGAA AQLLRSFPFF RDQVAQLDKV SLNLGFPSVF ATLERTEEAN
NVSPILSQLA ILILEIALLK LWELLGIRPS FVMGHSLGEY AALVAAKVLA PADAIYLVGR
RAELVMASCT AGSHVMLSVR ASVEEIRNIS ESHVYEISCM NDLKSTVISG VREEIEVVRS
TLEARGIKCM ELDLPFAFHT AQLDPILDEF EQTARHITFH PPQIPIISTL LGKCIFDGNT
VDAKYLRRAS REPVNFLGAM NTARGLGITE EAVWLEVGHH ALCSSFVKSH VSDAPIVQSL
RKGEDNHVTL TKAMAAMHCE GLPVCWNEYF KPEEHSYNVL RLGAYRWNNK NHWIQYEGTW
TLDKGNAQRG GKQAIPSGQS IDSTSVQQIV SQKITDSTVE VTAVTDVKRS DFMNAVLGHT
INGIGVVSAS IWTDMALTLG SYLYKLIAPS DEQPSMNLTN MLVQSPQKLD QSSSGSQLLQ
IDATLNQATS TANITWYTQS VSGQRSKDSF ATATITYENP TAWTKEWGRQ SHLLKSRIDT
LMAMASTGEA SRLSRSMVYE LFRNIVDYSP IYQGMQSVVL NQFEACAEIC LPVDRHGKWH
TPPHWTDSLF QLAGFVMNGS DATNTKQFAY ITPGWKDLRC IESFEPGVKY TSYVHMIPEK
GDPNTFLGDL YVLRENEIVG LLGDIKFRRI PRALLGAMFA TPAAAVEKTS ATQPTRALLP
KPLVPAETTL PSRPPVVESS SPTVVANEPA VITDCLRLIG QETGYPPSDL ADEATFPELG
VDSLMSLVLA EKFRNELRLE VRSSLFLECP TVKEFKDWIK QYC
//