UniProt: A0A2G7EN52

Database: UniProt
Entry: A0A2G7EN52_9EURO

LinkDB:  A0A2G7EN52_9EURO 
Original site:  A0A2G7EN52_9EURO

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Ontology (8)   
   GO (8)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (46)   
   InterPro (25)   
   Pfam (10)   
   PROSITE (5)   
   SMART (6)   
All databases (55)   

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ID   A0A2G7EN52_9EURO        Unreviewed;      2570 AA.
AC   A0A2G7EN52;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:PIG69495.1};
GN   ORFNames=AARAC_007811 {ECO:0000313|EMBL:PIG69495.1};
OS   Aspergillus arachidicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG69495.1, ECO:0000313|Proteomes:UP000231358};
RN   [1] {ECO:0000313|EMBL:PIG69495.1, ECO:0000313|Proteomes:UP000231358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG69495.1,
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.
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:PIG69495.1}.
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DR   EMBL; NEXV01000729; PIG69495.1; -; Genomic_DNA.
DR   STRING; 656916.A0A2G7EN52; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000231358; 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:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR   GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd02440; AdoMet_MTases; 1.
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; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; 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; IPR013217; Methyltransf_12.
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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 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; PF08242; Methyltransf_12; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
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          9..434
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2485..2562
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2570 AA;  283087 MW;  2554B569161BCB96 CRC64;
     MSTCSEQGLP PLAIVGISLK FPGDAVTPDD FWKMLLEGRA AASEFPPDRV NIDALYHPDR
     ERLDQLSTRG ANFMKGDLGA FDAGFFTINT TEAEAMDPQQ RLILEASYRA LENAGITMAE
     ASGSKTCVFT GSFSHDYNIL QVKDPMTLPK WHATGTSMNM LSNRVSWFFN LQGPSATVDT
     ACSSSLMAID LACQSIWTGN SSMGLAIGSN TILALEMSLC LDNLGLLSKD GRSFSFDQRG
     NGYARGEGVG VLVIRPLEEA IRHGDTIRAV IRSTSSNQDG RTPGIMQPSG TMQEKLIRDT
     YVRGGLDLAT TRYFEAHGTG TAVGDPIEAR AIGSIFRDYR SADDPLYIGS VKSSIGHLEG
     ASGVAGVIKV VLALEKGIIP PSAGLEKLNH RIDDEFLHIK VPQTPVAWPV DGLRRASVSS
     FGFGGSNIHI VIDDALNYLQ INGLQGNHNT TARLSTMCVE SHHTNGTLDT TAEEAKLLVW
     SAADENGISR IQDKWRSFFS SLHSTDKEKK EYLSNLAYTL ANRRSHHLWR TFATVKCSDD
     WSVIVDKFAR PCRSISSPNL AFVFTGQGAQ WYAMGRELIS GYSVFRDSVK AANRYLQTLG
     CQWDLLEELQ KPEESSNVNK TEYSQPLCTA LQVGLVDLLS HFKISPKVVV GHSAGEIAAA
     YCASAIDRHS AWKIAFYRGK WSSQLEKSSY VKGSMIAVAL SPKDVEPYLE KIAGECEILR
     LTVACINSPK SVTISGEEMQ IDMLKSALSA ENVFCRKLKV KVAYHSFQMH EIAAQYQSAM
     GELEKGTEHK TSIEMVSSVT GTWIKPEDLR APEYWVQNMV SPVKFSDALF NLCSNTETPR
     RKIDRSHRRA YPIHHLVELG PHSALQAPIK ENLSSLNRQS VTYHSLLVRG VPATDTVMTA
     AGYLHAAGYS IDLGAVNNLE SLEEEGLLKS IPDLPEYPFN HSKSYWHESQ ISRNHRLPKI
     GRNDLLGTPD PNWNPLEPRW RNIIKLSEMP WVRDHQINGT ILYPAAGMVV MAVEAAKQLA
     IAGRQISSFN IKDVTLHAAI PIQEQNETVE TAFHMRPVKA LTSAASHWYE FALYMNTDSS
     WVSNCTGTIQ VAYHPEKPDP VDCRHIERDL VNQQIDAYLQ ASKECTSPTE VEALYSHLKA
     CGYEYGDAFQ GITALSVNPS DYTCVTGEVS NRPSISYETI HPTALDALIQ TALWPTTRCG
     AEVIPTAVPT HIESIALSVD GLSTTKDLFK VHTRVEPSGN SDICANITAF DDKLGKAIVT
     VDGLRCTAVN ELAIAETHNS TDDKLCHRVE WKPDIRLLKN DDINEICRPP GVDTSALEEF
     FIEVDFLLLA RLLEALDVLA ERSLCPSNLQ VKKYLEWAAT QKRLLCDGQL VFSSEPWKSR
     FHDIEYIQTL DTQLYESNPQ GKFLVSFSRN LTKFLCEELD PLEFIFTCGL IDDFYYDTLD
     RSSSSRRITA YLELLVHANP QMRILEIGAG TGSATRIFLR TLGRGQDDSQ TSRYAHWEYT
     DISRSFFGEA ASQFAAEGDR MRFNTLDIEH DPQQQGFECG TYDIVVASLV IHATSDLTKT
     LTHVRKLLKP GGKLIMNEMT NPARSAYVFG LLEGWWLGCE SYRSLGPCVG ERQWHELLSQ
     TGFSGCDLVF PDVENATCQE NAFIIATASE DTPEAARGHH IQIVHDPTDC LQTELARRLE
     EGCRELTGST VECVSLEETG SSDDLLRVFL LEYSKPVLCD MQEEVYTRLQ ALLLSTKNTL
     WVTEGGGKDF GRPHLHLIEG LFRVLSEEDG GRDRYIISLE RQQTERHPHH RLVLDLISHI
     LSPVSSVIDS DYKEHQGVLQ VGRMVNHHPL NNAISVQTNP QQAITRPFGC GTQLRLDASS
     SSMTNGFRFI EAEWGDQPLA ANEVELEVSY VGVNFRDVLI ALGQLNVGGI GLECSGTITR
     VGTACRKFRT GDKVVGFLPN CYSTHLRFRE TDPVVHIPQG VSLPAAAAVP ANFITAYMGL
     KELARIQPGE SVLVHSGAGG TGQAAIQIAK HFGAQVYTTV GSESKKKFLM QTYGIPESHI
     YSSRSTFFSQ AILQQTAGKG VDIVFNSLSG ESLIKSWECI APYGRFIEIG KKDILSNSKL
     PMIQFAKNTT FISLDLGSWA RDRPAACVSA LAEILALLVE GKFQPPSPIA TYGVCELEKA
     FRLMQGGKHH GKLVIEMRRD DPVMTVLKPK PISFFDPNAT YVISGGLGGL GQNAVNWLVS
     RGARNLLLLS RSGGDSPEGR KLLDQLHSQG VEAMAPACNV SDAQSLRKVL DACQSHLPPI
     KGCIQGAMVL HDVSYEDMSY TAWQTAVNPK VQGSWNLHEL LPKGMDFFIL LSSINGLIGS
     RGQANYAAGN TFQDALAHYR VSIGERATSF DLGLFTFAGA VAKDPRLREM MRNNSVLEPV
     TEAQFHALLD TYCNPDVARD LGLSCQTAIG VHPVAMERGA GRAYWLEKPL FGLLQLDQAS
     EGDQQGQVRG VNIAAALQSA TSLAEATTLT AEALTLKLCR VLSLSESDID ENKALHEYGV
     DSLVAVELRS WFSKEMQADV AVFDIMGRAT VTSLAQLAVG RSKLEKGWSV
//

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