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Database: UniProt
Entry: A0A2G7G1W1_9EURO
LinkDB: A0A2G7G1W1_9EURO
Original site: A0A2G7G1W1_9EURO 
ID   A0A2G7G1W1_9EURO        Unreviewed;      2141 AA.
AC   A0A2G7G1W1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Polyketide synthetase PksP {ECO:0000313|EMBL:PIG86829.1};
GN   ORFNames=AARAC_002933 {ECO:0000313|EMBL:PIG86829.1}, BDV24DRAFT_176958
GN   {ECO:0000313|EMBL:KAE8346018.1};
OS   Aspergillus arachidicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG86829.1, ECO:0000313|Proteomes:UP000231358};
RN   [1] {ECO:0000313|EMBL:PIG86829.1, ECO:0000313|Proteomes:UP000231358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG86829.1,
RC   ECO:0000313|Proteomes:UP000231358};
RA   Moore G., Beltz S.B., Mack B.M.;
RT   "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT   Aspergillus arachidicola.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAE8346018.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 117612 {ECO:0000313|EMBL:KAE8346018.1};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics study of 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; ML737117; KAE8346018.1; -; Genomic_DNA.
DR   EMBL; NEXV01000221; PIG86829.1; -; Genomic_DNA.
DR   STRING; 656916.A0A2G7G1W1; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000231358; Unassembled WGS sequence.
DR   Proteomes; UP000325558; 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   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; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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; 2.
DR   Pfam; PF16073; SAT; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231358};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          376..807
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1646..1722
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1764..1841
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1609..1646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1721..1764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2141 AA;  233944 MW;  E20C41E6F56704CF CRC64;
     MEGPRGVYLF GDQTSDFDAG LRRLLQVKNN TIVASFFQRC FHALRQEIAR LPPSERKIFP
     RFTSIVDLLA RHRESDPNPA LESALTCIYQ LGCFINYYGD LGNVYPSASD CHIVGLCAGL
     LSSAAVSCST NVGELLPAAV EAVVVALRLG LCVLRVRELV SSDQASSTSW SVLISGISEK
     DASQLIGEFT AERAIPPSSK PYISAVGYNS ITISAPPKVL DDLIDSRLSK SHKPVRAQIH
     GPYHAAHLYD GRDVDRIIES CHNEVVSNYT PRIPVLSSTT GQPIEAKQMK DLLKAALEEI
     LLHQLCWEKV TDACSSILQT ARHQPCKLFP ISSTATQSLF TALTKAGITD IEVENGLGDV
     PTNPKDNLNI SGRADCSKIA IIGMSGRFPE ADGTESFWDL LYDGLDVHRK VPAERWDVDA
     HVDPTGTKRN TSKVPYGCWI NEPGLFDPRF FNMSPREALQ ADPAQRLALL TAYEALEMAG
     FIPDSTPSTQ RDRVGLFYGM TSDDYREINS GQDIDTYFIP GGNRAFTPGR INYYFKFSGP
     SVSVDTACSS SLAAIHMACN SIWRNDCDAA IAGGVNILTN PDNHAGLDRG HFLSRTGNCN
     TFDDGADGYC RADGVGTIIL KRLEDAQVDN DPILGVINGA YTNHSAEAVS ITRPHVGAQA
     FIFNKLLNDA NIDPKDVSYV EMHGTGTQAG DAVEMQSVLD TFAPDYRRGP GQSLHLGSAK
     ANVGHGESAS GVTALVKVLL MMKKNTIPPH CGIKTKINHN FPTDLAQRNV HIAFQPTPWN
     RPASGKRQCF INNFSAAGGN TALLVEDAPI AEVKGQDTRP VHVVSVSARS QSALKSNINS
     LVKYIDEQGR SFNVNEADFI PSLAYTTTAR RIHHPFRVTA IGSSLQELRD SLNNSSRLES
     FTPVPATAPG VGFVFTGQGA QHTGMGRHLY EKCSQFRTTM QHFDCISQSQ GFPSILPLVD
     GSVPVEELGP VVTQLGTTCL QMALVNYWGS LGIKPAFVLG HSLGEFAALN TAGVLSTSDT
     IYLCGRRATL LTEHCQVGTH AMLAVKASYP QVKQLLKEGV DEVACVNSPS ETVVSGLTAD
     IDDLAQRCST EGWKSTKLRV PFAFHSAQVT PILERFQEEA QGVTFRKPSL PFVSSLLGEV
     ITESNYDVLG AQYMVKQCRR SVNFLGALEA TRYAKLMTDK TVWLEVGAHT ICSGMIKATF
     GPQVTTVASL RREENAWKVL SNSLSALHLA GIDINWKEYH QDFSSSHQVL PLPSYKWDLK
     NYWIPYTNNF CLTKGAPQTA IQAAPQTTFL TTAAQKVVES RDDGTTATVV VQNDIADPEL
     NRVIQGHKVN GAALCPSSLY ADIAQTLGEY LVEKYKPEFK DLGLDVCDMV VPKPLIAKGG
     EQLFRVSATA NWAEKKASVQ VYAVNADGKK TVDHAYCTVK FFDTNASELE WKRISYLVKR
     SIDSLHQNAE TGEAHRIQRG MVYKLFSALV DYDENFKSIR EVILDSDNNE ATARVKFQAP
     PGNFHRNPFW IDSFGHLSGF IMNASDATDS KNQVFVNHGW DSMRCLKKFS PDVTYRTYVR
     MQPWQNNIWA GDVYIFEGDD IIAVFGGVKF QALARKILDT VLPPVGGSKA PITAKPTPPA
     RAQKANTGAK ARPKAPVPSK SFTKSSGPSV VVRALSILAS EVGLAESEIS DDMVFADYGV
     DSLLSLTVTG RYREELNLDL DSSVFTDHPT VNDFKRLIAQ VSPSESHDGS SSEQESNFSF
     NGGESSSAST PDITSPPNEK VAQVEQNDTM KEIRNIMAEE IGVPAEEIDP AENLGEMGMD
     SLLSLTVLGR IRETLDMDLP GEFFIENQTL NDIEVALDLK PKTTAAPIPM PEPVKFPEAI
     HDLQPKLAQH PKATSILLQG NPRTATKTLF LFPDGSGSAT SYATIPGISP DVCVYGLNCP
     YMKTPEKLKC SLDELTAPYV AEIRRRQSKG PYSFGGWSAG GICAYDAARH LMFEEGEQVD
     RLLLLDTPFP IGLEKLPQRL YGFFNSIGLF GEGKTAPPSW LLPHFLAFID SLDAYKAAPL
     PFTDKKWAKK LPKTYIIWAK DGVCGKPGDP RPDPPTDGSK DPKEMVWLLN DRTDLGPNKW
     DTLVGPENIG GITVMEDANH FTMTKGEKAK ELSTFMANAM A
//
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