ID A0A0F0IK88_ASPPU Unreviewed; 2571 AA.
AC A0A0F0IK88;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Beta-ketoacyl synthase N-terminal domain protein {ECO:0000313|EMBL:KJK67566.1};
GN ORFNames=P875_00117035 {ECO:0000313|EMBL:KJK67566.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK67566.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK67566.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-2015) 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:KJK67566.1}.
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DR EMBL; JZEE01000188; KJK67566.1; -; Genomic_DNA.
DR STRING; 1403190.A0A0F0IK88; -.
DR Proteomes; UP000033540; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 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; 2.
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; IPR013120; Far_NAD-bd.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 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; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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:UP000033540};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 385..801
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1643..1717
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1720..1758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1741..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2571 AA; 284662 MW; B1FF71A0CBF4B2C8 CRC64;
MVSQLEPPPG GKTVLIFGCQ CLSFNIEDFH RLRATVLETP EHHWVQDVLS ELPVYYRTAS
TTYVQKLKNI PGIQQLRNLA EWFRTGQVPT DSFPLPYIQL APLLVITHFT EYWKYLRIRH
PKGPTCVNES SAESPVVEIV GFCIGFLSAA VVSAARNQDQ LSKYAAVALR LATLMGALGD
AQEREEEYTS LATVWKAADL EKRLPLVLEA FPESYVTVRF DTNRVTIMTP RRTIKQLENE
LQSAGFNTTQ VEFNGRYHWA GHEDTLRALS LMCDSDPALQ LPDASQSAVP TRPNIPMDTP
PKGPLHELVL WSILAKQCQW FDTFSKVYQA HLEDTPSLII EFGPERCIPP MYMRKLQGRT
VHFADLDLNT LSRTSPLYQT PRSYDSDIAV VGMACRVAGA DDLEEFWKLL CSGASQHQEM
PLERYENFET PWRPSAIRPW YGNFVRDIDA FDHKFFKKVP REAMSQDPQQ RLLLQVAYQA
VQQSGYFHRS NINRNIGCYI ASCTVDYEHN VNCHPASAYS ATGLLRSFMA GKLSHYFGWR
GPAFCIDSAC SGSAVALHQA CQSIIRGECT AALVGGANAI MSPLAYDNLA GASFLSPTGP
CKPFDASADG YCRGEGFAAI FIKKMSDALA DGDIVLGTIA STAVEQNNNC TPIVVPDASS
LAGLFTQVTG KAHLHPRDIS VVEAHGTGTQ AGDPAEYVSI RKTLAGPHRT SPLSLGSVKG
LIGHTEGVSG LIALVKILLM INEGIIPPQP NFQTLNPYFK ASPDDQIHIT VTLEEWRANF
RAALINNYGA SGSNASMVIT EAPYASEHRI SSSFHTFAVA LPIRICASDE GRLIDCARRL
RQFLHHQAIS AAPATDLGNL SFNICRQSNP TLDSQVAFSC CSKSELASKM SSIIDGDTNH
IFRFIKSPRP IVLCFGGQVS TFVGLDRTVY DSISLLRHWL DQCDSLAQSS GYGSLFPGIF
EHNPIFDQVQ LHIQLFSLQY SCARCWIDSG LAVAALVGHS FGELTALCIS GALSLGDTIT
LIARRAAIIR DGWGHDHGAM LAVEGNKEGI MSLIDEAYRD APTDMAPATI ACFNGPRSFT
LAGTTAAIDA IQATLKSPSY ISLKAKRLLV TNAFHSDLVD PLLPALEDVM CGIHPQEPII
PCEKATENGS TGTVTSDMVA KHLRQPVYFH HAVQRLAEKH GPCVWLEAGS NSTITSMVNR
ALALSSGHHF QAVNITTERG MQSLSDATVG LWKASVSVAF WAHHSQQAQE YVPIFLPPYQ
FEKSRHWLSN KKLLGPAHEA GATPAVSASA LRFVGYQDTQ QLVARFSIDT AHPQYQESIA
GHVVSHTSPV APASFMLDYV VEALRSLPEC KGKIPQVQNV TSDAPLCLDM SRDLWIELYA
QDTHKHIWDL RYLSEQLQIG PRSQVLHCSA RFTMFDPDDA QIQSEFTRYG RLVSHRYCKE
LLNDPNVSDM IQGRNVYRTF AEIVDYSEPY RGVQKLVGKD NESAGRVLKR YAGQTWVDTY
LCDSFSQVGG FWVNCMTDRA PSDMYLASGM ERWMRSPIYA DPATPRPDTW DVLAKHERGD
DCYTSDIFVF NPTTGQLVEV FLGLQYTRVK KATFSKIIGK FMPQCAAHSS DANKLETAVS
HAAVPVPQVA KAKSDSSGPK SRINLTARIK AVVAEFCAMD PSEITEDGNM VDAGVDSLMA
MELAREMEEA FHCTLPAADL MEADTFRDLV NCVKVAVGES DSDEHESSSR SSEEISFKDR
SPNGDYNTPN TEAPTSVASD TLDLELPFES VLEAFGETKA LTDRFLDDNR CSGRIHIFAP
LQTELCVTLT LEAFEQLGSH IRTASRGQRL NRIPFDPQHQ ELINYLYKRL EEARLVDLDS
NTVIRTAISA PNKSSLSILE EIKCSYPEYA GASKLAYFTG SKLASVLCGK QDGLQLIFGT
KEGQELVSWM YGDEPHNVVG YMQMLDFIKR LIQKVLLTGA EVGALKILEM GAGTGGGTKW
FLPVLSKLDI PVEYTFTDIS PAFLAQARRH FKEYSFVRYR LHDIEKPPPG DLVGTQHIII
ASNAVHATSS LQESTRNMRK ALRSDGVVLM LEMTRPAFAI DIVFGLFRGW WVFNDGRNHA
ITNEHRWETD MHTVGYGHVD WTDGYSPEVS VQRVIFATAT GTQSERLPLG NPLEKVHPVQ
RVDNASRRKV IDKYIRRSIE NFTLPVTSQN GFGSDGQVVL LTGATGSLGS HIVAQLAQRQ
SVKTIFCLNR GNPNEESIQK QTSALQKRGI SLAAHEMSKV KALTATISHH KLGLSSELYD
TLKTTVTHII HNAWPMNGRL ELSGFEKQFQ AMRHLVDLAS DIACYRPTDS KVRFQFVSSI
ATVGNYPIIT CQNNVPEQST DIEFVLSNGY SGAKFVCERI LQETLQRYPS RFQAMVVRPG
QIAGSSSSGC WNIAEHFPAM VKSAQTLRAL PDLQGDLSWT PVNDIAASIV ELLVTDNTPY
PVYHLDNPIR QPWHDMIRIL ASELSIPTGN IVPFSEWIQR VRSFPGSRED NPAGMMADWL
EENFERMSCS GVLLETTRAR EHSSTLAGVG PVSEEVTRRY LHSWKQCGFL H
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