ID A0A317XE39_9EURO Unreviewed; 3711 AA.
AC A0A317XE39;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:PWY95188.1};
GN ORFNames=BO94DRAFT_620660 {ECO:0000313|EMBL:PWY95188.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY95188.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY95188.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY95188.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:PWY95188.1}.
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DR EMBL; MSFK01000003; PWY95188.1; -; Genomic_DNA.
DR STRING; 1450535.A0A317XE39; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000246702; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine 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; cd05930; A_NRPS; 1.
DR CDD; cd20483; C_PKS-NRPS; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013120; Far_NAD-bd.
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; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 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; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 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; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-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; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2094..2171
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3210..3286
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 3711 AA; 407199 MW; 7E2F201713B42E79 CRC64;
MIPVSSPDIA IIGMSCRVAG ANSPSELWNV LASSKDVRTE ISRFNSDGFY KPDGGPRKGL
TNVRHAYVMP DGVDKFDNTF FKISPLEAEA MDPQQRLLLE LTYEAIENAG VTLDEFEGSD
TAVYAGIFGN DYHTSLLRDV DATPKYMSTG TSNSIAANRI SYVFDLHGPS LVIDTACSST
MVALHQAVAG LKAGESSMAV VCGANLIISP DMFVHMSELG FLSPSGRCQS FDAAGDGYAR
GEGVMAILLK PLNEALQNGD PIRAVIRGTR INQDGRTQGI SLPSSEAQRQ NLFSLYKQLE
LDPGGVQYIE AHGTGTAVGD PLEMSAIDAV FGDSHSVDKL IVGSVKSSIG HLESCAALVG
IIKTVEALER ATIPPQMLFR TPNPKINFDR ISIPTNLTTW PTSTDGSRRA GVNSFGFGGT
NGHAVLEAFD STHAASRILD ENRPYLFKVS AANTSSLVGL SKSIADYVER ERPALCDLSH
TLLSRRSNLR KLAFIVASSH DELVSKLRVE PQELVRSNTA NKKVAFIFTG QGAQWQMGKQ
LLGTSPLFRS VITDCDNVLQ SLPDAPSWKI AEELVKSKEK SRLARASFSQ PMCTALQIGL
VEILRSWGIS PNGVVGHSSG EIGAAYAAGF LSLRDAITIA FYRGLYLGEN APVKRDGPAG
AMCAIGLGEA DCANMLERYQ GKVVLAAVNS PSSCTLSGDV DGIQKIVAEC TENGTFCRAL
RVDMAYHSHH MLPLAPAYEN AMNAAHVQPL SGNPTTCEMF SSVTRQKVTS GDCVPSYWRD
NMVSCVRFLD ALGQLATNVN PDVFFEIGPH PALKGPVGDV LSSMGKTEYQ YFHSCFRGQP
DHEAMLNTAG SMIAANLPVL ASRVNAAQTC HGLKSTYTTG RVLTDLPTYH WDHSTGFWAE
SRLSKNVRER RFPRHQLLGT RFHNDMPLAP RWRNVFCLQD LGDIAHTLTD RSFYGSVAIT
LSMILEAARQ IFIENQLDMP LVRLQDIAFQ HPIPFPEDPE APMEIHLVIH QDTATSGWRL
EIFSARSQSE MTWVKNCTSR LSFSRDETTL PESTECQHDE DKLEYALSFG TMQHPDLDDF
SFNKDSAYGR FSNPVLGYEN YKVDPAILST VLQLPELVLQ ASGLPAAYQL LEIGTLELDI
TMPAIEKGSF QVTFPTRGTT GGKAELAVYG ESGHGLVVRG MSLQRQKVIQ KDPILKSLFY
KSHLQPDIIR LSSTSALHIK RVTELVTGKW PMCDVGIINL DSTTTATLLS GLQGMESHQR
PKFRSLTIVG DHSVKQSDRV RTLDGLDGSL KLHCLIGKAC DVRSSTSNLL QNGVVCALLE
DHEDEAFFSE TFDSICDVTG LDEKTWRLGR LKPHANGTLV PDNVKVIAPF DIISAPSVAN
ASPKFEGILL ETQTLKQWTS ANASTDSFDA IIVDSADKSI LVDWKGAQIL PWLQFVVDHV
KVLLWVSIAD GLGNLSGSLL KTLQSEYPSV RFATLIFKGE KDMDFITRTT LALYDDIIHG
DREIQYVVQD RRFHILRYQP DDELSASVGI IPPVQEAAKR SPQLSIHQLT LSGPRSTLLL
SERAGIDVGR QQNTYRVVVD TSVVDLADTY RFNNRSLLDS PHLGRFFAGR AYSAFGSDSS
FIRVVGWHTN AHQSVLDLPA SQVFPIPEGT SVVDAVVQYA AFTTAATVLG DIARCRRGDR
LYIRVAGVLG EALTATAKLL GVTVVSEARS TDIVIEYASE RGLLLNGGPV CLQKLSATNA
FHNSVASRLG PRLALNSVVS TFNIKDHQVA FERAVEQPFA VVLSHSEHDD LGNAITWYPS
KKPLFRDDGA YIIIGGSGGL GQYLCSWMIQ NGAKNLYILS RRGILAPGAH ETVEAIERLH
GHLEVLSADA TDSSAVQEAL ESIRQVIPIR GCLNLAMILK NSPFSTMTDE QWDDVLRVKV
DTTWNLHQHT LQDDLDFFIM FSSISSICGN RAQANYATGN AFLNSMAEYR HGLGLPGTAV
ALGAMSGIGV LANNEELLRI LRQSGLDIVD AKGLEKVMEA AILSSQSRDH ATITVGLQMF
ETLDGKVQAE SDQTQIFWTE WPEFACLMDH KASGSGAAAE LSLLDQVLAL DSDAALGALL
KGFRVCLSNI TGQHESSFDP ASPLSMYGLD SLNAVGVRYW FFKEIGVDLP VFDVLGCTSI
NALLARAYQK LEGQKSATEA IKIPQPVAHT EVAVRPLSHS QQRLWFLYRF LSDKTVYNLL
LVCHIIGCVD ATKFATAWTV LMERHEVLRS KIVDTADGLQ QIPISERAFP LTVVETSDED
FQQREEALTQ IARVHNFDVE GGELIRGWLL RSPTKARFFL ASNHLAWDRS SVPTIFSETS
AIYKFLLAGE QPEEQLQPVP FQFIDYTLWQ NDWLNQEALT APMISYWEKK LAGVPQAVSL
LPFALKEQRP SMKVYEVGRV QHILDAELAT SIKNFCKRHA VTPFMFVTSA LGAVLSRLTG
DEDVVIGITD GDRGHSAFDQ LIGFTVNMLP LRSHITRHMP YMTFLEQFRT TCLEAYEHHA
VPFDYLLQKL NISRSTSHSP VFQITVNYQV QGGFPEVDFG EFKFAEYDHY NARSQSDIAL
EVEELGTGEL LCGWDFDSSL YDEAGVLELV EMYHLFIQDV IEKDGAGQIE DFQLVSSADK
ARIASALQPS YEDEPSLEQL NQSLFPVLFA AAVGENPNKT ALIDCHGSLS YSELKARTNA
VANTLLDNGA RMGDRIGICC EQSNSLVIAV YGILRAGCVY VPIDPDFPAE RISWMIEDVG
ISKILVDDLG DKKSQQILMC GFELEHLYEV EKVSQESSRM ETPVLPREIE PSDNFCCIFT
SGSTGRPKGV YIGHAQLRYQ MHGYNKYIGT SSDDLILLAS AMVFDMSLPA IFGTIQYGAT
MFVASREARY SAIEMISTLI TRQITNCIFT PTQVKVMLQA PNKKDLSLWT SLRRLVLGGE
SVSTHLVRDF FALELPQARF FNGYAPSETT VVNTLKELFP EDAGRSDIPL NVPFFPARLY
ILDEEMRPAP FGVPGELYIG GPNVNRGYVN RPEITAKAFL DDPFAPESEI QAGFGKLYRT
GDAFCLSRDG TVRALGRIGS DRQVKIRSMR VELQEIENAI WSAYEVLQEE GAPSLSLVAV
TYHRKGELDG LLAAYLAPSG SVEVSDDEQR HLTGYLRLAL KATLPVHMLP AAYVFVRDLP
RTITGKIDHL AISSWQAPTV NAANGVSSHE NLSETESIVA SVWKSVLHIG EALGPADDLF
ALGGHSLILL QIQSEIADKC GVTISLAEMF ANPSLREMGY LLAQYQRGDY DGHSKEAISD
EHEPSATIDW QKETLLPGPT WTVASSEAAN PAAIVVTGAT TMIGAHFVHL MLASSTVNVH
CIGVQATSEH EARASVLSTF SKWNLLDVSS AALDERLYVY RGSLSHPTLG LSDDIVRHLD
EQADQVYHFD SDVSLLKNYE ALRPTNIGSL HFLIDLARGS SGKVKPLHYL SSWGVPHLQS
WASSSLSNQG YIDGEKELTN LTPGSENTLG YLKCRWVCEA LLYEAAKRGL PVSIYRACMC
GSAPLSGRGL DRTDINRRIL EACLQTSLVP DFRSANGGGM SWISVDYLVQ SIKHLSSDST
PGTTGQTRIF NYQAEKHIPY TQLPAVLGGD PADGGVSLAV VPPAEWFKGL RESHNPEMIM
HAEVLEQWFD AGWTPFTLQG ETSGRLVEVG LVAPTVTREF LLKQVVGTVG F
//
