ID A0A395HPG2_ASPHC Unreviewed; 2140 AA.
AC A0A395HPG2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:RAL09155.1};
GN ORFNames=BO97DRAFT_445644 {ECO:0000313|EMBL:RAL09155.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL09155.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL09155.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL09155.1,
RC ECO:0000313|Proteomes:UP000248961};
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 (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ824306; RAL09155.1; -; Genomic_DNA.
DR STRING; 1450537.A0A395HPG2; -.
DR VEuPathDB; FungiDB:BO97DRAFT_445644; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000248961; 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; 2.
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:UP000248961};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 373..804
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1643..1719
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1765..1839
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1719..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2140 AA; 233979 MW; B9A9BBF83F42E24A CRC64;
MEGPYHVYLF GDQTSDFEAG LRRLIQAKNN TIVQSFFQQA FHALRQEISK LPPAQRKIFP
RCTSLIDLLA RYCESGPSPV LESAFTCIYQ LGSFLNYYGD LGNAYPSDGC QLVGLCTGLL
SCAAISASRN VGELLPAAVE TVVVALRLGL CVLRVRELVD SEASSSSWSV LVSGLNEESA
SSLIEDYSTR LAIPPSSKPY ISAVSSNGVT ISAPPSVLDT FVETGLAGKY KPTRVPIHGP
YHAPHLYDSR DVERILESSP QDNIAHYTRH IQMLSSETGT PIEASKIKEV LKVAIEEILL
RRLCWDKVTE SCISIIESSQ SQSCRLMPIS TSATQSLHTA LKKAGVANLS LDTGIGEIPS
TADRPNSTGK TECSKIAIIG MSGRFPDSES PEKFWEILQK GLDVHRKVPA DRWDVDAHYD
ETGARRNTSK VQYGCWINEP GLFDPRFFNM SPREALQADP AQRLALLTAY EALEMAGFIP
DSSPSTQRDR VGIFYGMTSD DYREINSGQD IDTYFIPGGN RAFTPGRINY YFKFSGPSVS
VDTACSSSLA AIHMACNAIW RNDCDSAITG GVNILTNPDN HAGLDRGHFL STTGNCNTFD
DGADGYCRAD GVGSIVLKRL EDAQADNDPI IGVINGAYTN HSAEAVSITR PHVGAQSFIF
NKLLNEANVD PKDVSYIEMH GTGTQAGDAV EMQSVLDVFA PDYRRGPTQS LHLGSAKSNI
GHGESASGVT ALVKVLMMMR ENQIPPHCGI KNKINHNFPT DFAKRNVHIA FQPTPWNRPA
SGKRRAFVNN FSAAGGNTAL LIEDAPISET TGQDPRAFHV VAVSARSQSA LKNNIGSLLK
YLDSYGNSFG VKESSLVPNL AYTTTARRIH HPFRVTAVGS SLHSLRDSLH AAAQRDTFTA
VPAKTPGIGF VFTGQGAQYT GMGKELYNTC SPFRATIEHF DCIAQSQGLP AILPLIDGSI
AVEELSPVVI QVGTCCVQMA LISYWSSLGV KPSFVLGHSL GDYAALNAAG VLSTSDAIYL
CGRRAQLLTE QCQIGTHSML AIRASLAEIK HFLKDDVHTI ACVNAPAETV ISGLASDIDD
LAQKCLTENV KATKLRVPYA FHSPQVDPIL DTFEKISQGV TFHKPTTPFV SALLGEVITE
ANAQILGAKY LKDHCRGTVN FLGALEAIRH AKLADDKTIW VEIGSHTICS GMIKGTLGPQ
VTTVASLRRE EDTWKVLSNS MSALHLAGID LNWKQYHQDF SSCHQVLRLP AYSWDLKNYW
IPYTNNFCLS KGAPVAAIEA APTYEYLTTA AQKVIESRDD GATSTVVVEN DLDQPDLRRV
IQGHKVNGAN LCPSSLYADI AQTLAEYLIN KYKPEFKDMG LDVCDVSVPK TLIAKGGQQL
FRVSATATWA EQRVSLQIYS ITLEGKKTTE HATCTVKFFD CAATEREWKR MSYLIKRSID
RLHEIADNGE AHRLQRGMVY KLFATLVEYD DNFKSIREVV LDSDNHEATA RVKFQAGPGD
FHRNPFWIDS FGHLSGFIMN ASDGTDSKTQ VFVNHGWDSM RCLKKFSQDV TYRTYVRMQP
WKNSIWAGDV FVFEGDEIIA VYGSVQFQAL PRKILDTVLP PAGAAKAPAA VRPSASVIQK
AAPAAESKTR AKAPTPTKSL VKSGPSVIVR ALSILASEVG LSESEISDDL VFADYGVDSL
LSLNITGRYR EELNIDLDSS VFIDQPTVKD FKRLLAQISP SESSDGSTSD PESSFSFNDG
SDESGLSSPM VISPPNEKMM EVEQHATMKE IRAIIADEVG VTEDELKADE NLGEMGMDSL
LSLNVLGRIR ETLDMDLPGE FFIEHQTLEE VETALDLKPK AAPISEPIRL PEAVPAMKSI
VSVRAAQHPP ATSIVLQGNP KTATQSLFLF PDGSGSATSY ATIPRVGPDV CVYGLNCPYM
KTPEKLKFPL QELTFPYLAE VRRRQPKGPY NFGGWSAGGI CAYDAARYLI LEEGERVDRL
LLLDTPFPIG LEKLPRRLYR FFDSIGLFGE GKAAPPAWLL PHFLAFIDSL DAYRAVPLPF
NDPEWASKMP KVFLVWAKDG VCNKPDDPRP EPAADGSPDP REMVWLLNNR TDLGPNKWDT
LVGPNNVGGI TIMEEANHFT MTLGKKAKEL SNFIGHALAN
//
