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Database: UniProt
Entry: A0A0L1J9A9_ASPNO
LinkDB: A0A0L1J9A9_ASPNO
Original site: A0A0L1J9A9_ASPNO 
ID   A0A0L1J9A9_ASPNO        Unreviewed;      2212 AA.
AC   A0A0L1J9A9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KNG88285.1};
GN   ORFNames=ANOM_002507 {ECO:0000313|EMBL:KNG88285.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG88285.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG88285.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG88285.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KNG88285.1}.
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DR   EMBL; JNOM01000056; KNG88285.1; -; Genomic_DNA.
DR   RefSeq; XP_015409208.1; XM_015547764.1.
DR   STRING; 1509407.A0A0L1J9A9; -.
DR   GeneID; 26804311; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000037505; 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   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; 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; 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; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF54; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR   Pfam; PF00698; Acyl_transf_1; 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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.
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:UP000037505};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          23..413
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2110..2185
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2212 AA;  243235 MW;  C5EDF7D63FA646CE CRC64;
     MQPKSLQHDE LAALIPDGRP GASPLVAIVG MAMRLPGGVR TTEDFWQFLI NKRDGHCEVP
     KMRYGIDGFY NAHDERYTHT RHGYFLPEDP AYFDAPFFSV TEQDASTMDP QQRLLLEVVW
     ECLENAGETN WEGKNIGCYV GVFGEDWLGL SHGDPLSIDR SHAISTGSYA LANTVSYKFD
     LRGPSMTIQT GCSSSMVGIH EACQSLATGA CSSAIVAGTN LILSPSMTTS MSGNMVLSTS
     GVCRTFDAEA DGYGRGEAIN ALYLKPLGDA IKANDAIRAI IRSTAANSDG GTSSIAVPSI
     IAQEHLILDA YRRGNINDLS ETAFVECHGT GTRAGDQVET TAVANVFEGQ EIVIGAVKPN
     FGHSEGASGI TSVIKAWLGG PSRAYELAGR RRRRVSVNAF GIGGTNAHVI LDSAHDVCAK
     DPAQGCIGPE NDVKLLVISA QDAKSLKARI DQVTDYANRH PERSQDLSFT LGVRRKHLAH
     RAFAVYDPTS PLSPSDFQSA HPHVSAQLTF VFTGQGAQWP GMGQGLIKAY QCFKMDILEL
     ENVLRSIEDP PQWSLMEELS CATASRINEA EFCQPLCTAV QIGVVNLLAA WGIRPASVVG
     HSSGEIAAAY AAGAISARSA IILAYYRGKL AQAQKGTGGM ASIGLGSDEV SPYLVDGVVI
     ACKNSPQSVT ISGEQGQIDQ MVRNIQNDLP DTFCRKLQLD MAYHSHYMAA VGPIYEKSIS
     NHLQLHQQML PMFSSVDVRM ITDPQTLNAA YWRRNLESTV LFSDAISSLF AERHKKHILV
     EIGPHCALSA PIQQIIRAYD LKICPAYIPT LFRNDANCQH QLLTSVGSIH RNGAFVDLLA
     VNGTGHVLTD ILPYPWQHGT RYWKESRMVR EWRLNEVPPH ELLGSRSTES TSLEPAWRQF
     ISLENIPWLS DHIIQGKVVF PAAAYIAMVG EAILQLSPGV VSYTVRNAIF KAPLVIEESE
     NVEVITTLRP ARLNDLADSE WFSFTIASYD GTNWIKNCSG QVRAGACGNI SPVSIKPYAR
     RVSSSKWYDT LASLGLSYGA QFRGLQDISV DPKGSRAVAK VNNKAGSPAC RYSLHPTMID
     QCLQVMSVAG AAGLPRRIAT GAIPASIDQI FIGEGENHME ATVDTVQESG SSLVGDATAI
     LGDKVVLKMK RGLCFALGNK NDSISPQTPL VARIQWKPDP DLCKPEDLLP RAATSLGRLD
     QMKKLGQVSL LYILETAERI KPLVPQSTHA SKWKSWILYE DAAVRNGEHT LLPESKAWAT
     QSSEERQALI KKLSTTQADQ PGEHNIIITC TEVIYENCLE IMANKISTLD LLMEENRLGR
     IYQFDQENSD WSIFITYLSH SNPWLRILEI GAGTGSATAE ALRSLCVSGM PMYSKYTFTD
     ISPGFMTAAQ GKFRENVNME YKVLDISSDP LKQSFVGQSF DLIIASNVLH ATPVLKQALK
     NVKRLLAPHG WLLLHELAPV MPYVDYIMGT LPGWWIGEDD GRINRPYISP EDWDKKLQYA
     GFTGTEAIRY DSDTYHLCVD IITRPAPVET ATQPIVLLTD GSPDLWAGKV FSELEKQNFI
     VEWGKLEEAP SGHACVVFLL EHRDPFLAKL SEKRYHCLQK YLMGVGQSKL LWVTKTTQFD
     CKDPDCGLVL GFARTLRQEM MLDFYTLEID VFDTESAKAV GPIVRKILKP TNRDNQDPNY
     EYAYHNNTVF TSQCYWGAAA NILRPSKPDT GKKLSMSIPG LLDTLEWLDS SYGSLGQDDV
     EVDIDLLFQF MLWHDEGKIK PIRPTTVFAA CEAIEAFRLM QQGTHIGKIL IRMPDDASQL
     SQRPSEVEVL FSSTASYLLV GGLGGLGRAV SRWMVEQGAR YLVYLSRTAG STEEHSEFIQ
     ELNAMGCHVE CIQGSVTRTE DVQAAISRCK SPLKGVFQMS MSLNDRPFPH MSYEEWSSSL
     SPKVQGTWNL HNSVLQEDLD FFVLFSSAVG ICGHGSQANY AAANTFLDGF TQYRRRLGLP
     SSAIALGAVG ETGLVAREAK VMQAMQSIGI WLLNEDEVLE GLKKCIGESN TVDCTESAAR
     LSAPLIIGLG NNKSLSNPDI QTMWRRDARF ASYTNLDSIS VKQESGSSVN KIRELIIKAE
     LDPLILLQKE TETTITQELN QLIAKSLPGA QDMDDEAKTS LAIDSLMAIE VRNWIRRNLQ
     VEISLPEISR ARTAGGLIDM TLTRLKMRYQ VSDTEGTQNA VAETSFDLDT SR
//
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