ID A0A1V6Q769_9EURO Unreviewed; 2214 AA.
AC A0A1V6Q769;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQD85073.1};
GN ORFNames=PENANT_c011G04625 {ECO:0000313|EMBL:OQD85073.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD85073.1, 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:OQD85073.1}.
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DR EMBL; MDYN01000011; OQD85073.1; -; Genomic_DNA.
DR STRING; 416450.A0A1V6Q769; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000191672; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase 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:1901336; P:lactone biosynthetic process; IEA:UniProt.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 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; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
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; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
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:UP000191672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..443
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2131..2208
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1275..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2214 AA; 241385 MW; BDD68A87E8B1E617 CRC64;
MGGDTGFEST PDSEKSVPRP IAIIGYACRL PGQATSPSEL WELCTRARSG WSPIPKDRFS
LDAFHHPNPS KIGAFNPVGG YFLDEDIARF DAPFFNVTVQ EATSMDPQQR LLLECSYEAL
ESAGIPKENL ARRNVGVFAG GNFADYELNN MRDIETIPMH QATGCAPSLQ SNRISYFFDL
QGPSITVDTA CSSSLVALHY AVQSLRSGES KEALVAGCRL NVVPDLFVSM SMSQLFNDEG
KTYSFDERAT SGFARGEGAG VVILKPLDAA MRDRDPIRAV IANSGVNQDG RTKGITLPNG
EAQEDLIRRV YQDANLNPEE CGFAEMHGTG TKAGDPIEAA AIYAALGKGR TPRNPLYIGS
VKSNIGHLEG ASGIAAIIKG AMMLDRDLML PNAEFRKPNP NIPMDEWNMK VLTTTRPWPS
RKKYLSVSNY GFGGTNAHVV LEKAPLESKA PTEAVEDFEV DPKRKLFLVS ANDKESLRHR
IKDFGIYFEQ HPEVFEKALF GNFAYTLGNK MSQLSYRVGV SATSLDELGM RLAQLKINPF
LVLGTPILSF VFTGQGAQWA QMGIPLMHEY PVFASAIIRA DECLRDLGAE FSLLGELEKD
NATSQINSPH LSQPACTVLQ IALVDLLRSW DIRPSSVVGH SSGEISAAYA AGIYDLEAAV
ALAYRRGQMT SLLKDRFPTL KGTMIAIGAS RDDVQPVLKT LSGYATVACV NSPSSVTVSG
DVQAIDDLEQ ILQDKQIFNR RLKIDVAYHS DHMKNVADSY FTAIQNIQPS ASSTSAFYSS
VFGRLAEPSE LGPAYWVANL TSPVLFPDAL AKIVSIDETR PNLLVEIGPH SALKGPIMDT
LKSLGPIASK IGYTPTILRN ADAAESILDT AGAAYMRGVN LNMTELNFPK TGAVNRWFLT
NLPRYPWQHG TRYWHDARIS QKHITRDRAR NDILGLLANY SNDLEPTWRN ILRLDDIPWL
RDHRMQGIPV FPLAGYLVMA IEAARRGAEQ HDILFTHFEL REVIVGSALC LGDDTDAELT
ITLRPYTEGT RGASDTWSEF RVCSWNSKRA WTEHCTGLIR TCTAQKPQAA AIGNCSHAQT
RFVENQIVKV KESAVNHTDM PHMYQALSDL GAGYGPTFQD LENCYASACS SLADLVVPDT
RSVMPKNYES PLTVHPSFLD ALLHLVWPIL GQGQGRMELD TLYMPTMIKQ LSVSRNLPTT
AGEYVKAYCN GSPSLPKPEP TRFDLFATHE GSTEPLITME GLVMTPLRDT NTHREVVRKV
CYKIDWHSLA EIKNAKDETE ESDSEVVPNG NGHVNGANIT NGQTKLTEPV HSNGDIAKRR
EVFVSHFGKS DDTADKLSNM LSKTAGWEVS VKVLGETDFA EKHLVLLQTG TSSLRHLTED
VFENLKNALL NARSVLWVYQ TGSPDAQMTV GLTRTLRSET LSKVATLGIE PEDLKPPEGP
ILAAIDSLWP TDGIEPVADF EFKAKGSELF VQRIVEDDAA NAFVHNETHD MTISAQPFIQ
PGRRFKIQVG SLGALDSLYW VDDSPPPLGE NQIELEVKAT GLNFKDIVVT MGQLSQPYIG
IECSGVISSV GSNVKNVKVG QRVMALPEGA FSTYARCPAT SVAEIPDTMS FEVAATIPVV
FCTAYYSLFD LGQLQSSECI LIHAGAGGVG QAAIMIAQMI GADIFVTVGS LDKKQFLMTQ
YGIPENRIFY SRDTSFARGI QRATGGTGVD VVINSLAGDL LRETWECLAP FGRFIEIGKA
DITKNTRLDM LPFENNVTFA SVDLTKVAKF RPQLMKRLMG DICRLVREKS VHPILPLSTY
PISDIEKAFR ALQTGKSMGK IVVVPRDVDL VKAVTPKTSS NLLCSNASYI LIGGTGGLGR
SMAKWMATKG AKSIVLVSRR AAINEKVQSL IDSLAPLGVR IIVKACDVSN PESVEALVKE
EMKDLPPVRG VIQGAMVLRD MLFENMSLDD FTAVVSSKVE GTWNLHNTLI DSPLDFFIAL
SSVAGIVGNR GQAAYSAANV FLDGFMEYRQ SLGLPGTSID LAAVSDVGYL ADSNSQRRQE
VLKNIGSQTI DESEVLALIA AALTGDLNQS CVGQCITGLA LDSLDNNFWI QDAKFSVLYE
AAKGQSGSSS QRDGPSVPLQ VTLQAASSHE EALLMCYEAL AAKLAQVLVI SSEDMDPSIT
VASLGLDSLV AIEIRNWIAR EANANVQVLE LLSSGTLMAL AEIILNKSQA YTSS
//
