ID A0A1V6TWP8_9EURO Unreviewed; 2398 AA.
AC A0A1V6TWP8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQE30269.1};
GN ORFNames=PENFLA_c003G00473 {ECO:0000313|EMBL:OQE30269.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE30269.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
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:OQE30269.1}.
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DR EMBL; MLQL01000003; OQE30269.1; -; Genomic_DNA.
DR STRING; 254877.A0A1V6TWP8; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000191342; 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: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; 3.
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; 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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775:SF18; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 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; 3.
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; PS52004; KS3_2; 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:UP000191342};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 42..470
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2316..2396
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2398 AA; 260076 MW; 468F2369A4BE9649 CRC64;
MPGLSNGSMN GHAEVGGVGH ANHTLSEDAH GALPNGSSPY TQEPVAVVSM ACRLPDSCHT
PRAFWRFLEE GRIAINTPPG TRYSLNTHYD GSLKPQTMAS PGGMFLQDVD PRDIDAQFFR
LSGIEATSMD PQQRQLLEVV YEGLENAGVT LEQLDGASVG CFVSSFASDY GDMQARDPEN
RASATVVGVG RAMLSNRLSH FLNIKGPSMT IDTACSGALI GLDLAMRYLQ SNEISSAIVA
GANLYCSPEH VMDHYMGANG AASLSGRCHT FDSKADGYIK AEAVNMVYLK RLSDAIKDRD
PIRAVIRGTA TNSDGWTAGI ASPNPEAQSA AIRQAYNNAG IKDLSLTSYV EFHGTGTRAG
DSLEAEGVAT VFTPFQKPDR PLRIGSVKSN IGHSEPAAGL SGLLKTVLSL EHGVIPGNPT
FLSPSPKIDF EALRLYTSRT ATPWPKVDTR RASINSFGYG GSNAHVIIDE PKDLGHHHVS
SYINTETDDI FAEESATRPY LLVFSANDEK TLDAQAAALD RHLSDPAVKV SLRDLAYTLS
ERRSRHYHRA FAVTSTLTLD LPTLSRGHVS GQKPRVGFVF TGQGAQWPTM GRGLVETFPL
AARTIQHLDR VLQDAHDPPS WSLYAQLTAD DAQVQRPELS QPLVTALQLA ILAVFQLAGV
VPEAVVGHSS GEIAAAVAAG HLSPEQAILI AYYRGKATSE AVYEVPVGMM AVGLGPDQVL
PYVKGTTVEV ACVNSPQGVT LSGVKSELVA IEERVKDAGH FARLLRVDAA YHSHHMGSIA
GRYEELLRQH VEWPKHDGNK GSIMVSSTTG ETITNPLGPA YWVANMVSPV LFSQATQQLV
TGAEGVDYLL EIGPSDALLG PINQIKKAAS SSTGYGSAWK RGPVAVSTLL HAAGTLFTMG
YPISLQAFND DAANTPPMFV SDLPNYQWNH SVKYWHESES SHDWRYRKFP YHDLLGSKIL
GSPWTNPVWK NVLRLSDITW LRDHLLGDSV IFPAAGYIAM AIEAIYQKKY AMGEIPEGTL
ASELPFKLRN VTFPRMLTLD TNGGTKILLS LQPCSSSKES WHEFTVSTIT KDGSIEEHSR
GLVSVGDKSL PRPPTSAPDI APLQHPVPGA VWYKAMRHVG YHFGPAFQPC QQVEAKADSR
QCRALVRLQA PESRYPQSQY AMHPAAIDGC LQIATVALNR GHHSAINTLM PPALIDNLVI
FPHEVPSSGE AIVASEAVWS GVGRPDDNKR YVSDIRAISQ ESNELLFHLE GLRYHAINAS
ADRPHAFTQV VWNPDIDFIT SAQTAHILQA AVSSDKTNGD GNGDVAATLT QMAKLLALIA
HKRPSAKVIE VALRDGPTAG DSLYLDHVRA GAGPIARGCS YRLLAPSQHA GLVAHEKYAT
EPGVAVQVMD TEHGPFDDIE GKYDFIVLKV PEGEPELEQT IQRARDALAV NGYLVVVRVV
GLPFLNGGAS SPSGLDTVHD IHTPRGGILN LLYIGALREE TAKIGTPGPE RDNVHLLHFG
TPIPSSDVIR DELVQKGWDT LQHSLPFDEV PPTSTVLIID EMDRPVLSAL ADKQFVALRG
LLEQQCRVVW VTKGSQMRVT HPEQGLMFGV ARSLRAEYPS NLILCLDVES TTSIGSLEAI
DTSLRHITSV ADLQEADSEF VERDGMYHVS RVIADDVLNQ AQKESEEGEG GGAPVREDII
HDHMSHIRLV SERPGTLDKL VYREIPHLPK LADDEVEVEV HAAGMNFKDL ANAMGFVPAN
EHLFGLECTG IVTSIGDAVS TVKPGDRVLM VRRDGGCFAN RVRNRWHAVH PLPDWVSFEA
GTTLGIAVHT AVYGLVTLAN LQTGQSVLIH SASGGVGLAA IELCHYLGAE IYVTVGTDAK
RDFLAEQYGV SRDRMFSSRS TAFAKELMKA TNGRGVDVCL NSLTGDMLHE SWRCIAENGT
LVEIGKKDML DRNCLSMEPF DRNCSYRALD LSRKSISDET TYQTGVYIMD LVRQRHIKPL
HIGATFPFTK TVDAFRYMQR GKHIGKVVLS FEDSKTVPLP FRPAGPIFRL REDGSYLIAG
GLKGLCGSIA VYLARNGAKN IVVICRSGYD DARSQKIIYD CQCLGCHVDQ VTGDITSLDD
VRRAFTTASM PVIGVIQGAM VLRDRMFATM TPDEFRQPIA PKVAGTWNLH QASLEGSTSL
DFFTLLSSVS GLVGQLGQAN YAAGNTFLDS FAAYRLQQGL PACSINLGPI EEVGYLANDD
QGAMLNRVFE TRGWIPIHEA LLHQILRTSI LQQTHCLNPS HTGQLVTAIM PGNTPFEPVH
RFSALAGNNT TKIGGDVNAE SKSKLILLKK GSASDTDHAI LLAAAVELVN PVLMRSLGVA
EPLDPTRPLS NYGVDSLVAV ELRNWIRQQL EIEVSALEIV GARTLTALCE TLLDKLAR
//
