ID A0A319ACH4_ASPLB Unreviewed; 1728 AA.
AC A0A319ACH4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Ketoacyl-synt-domain-containing protein {ECO:0000313|EMBL:PYH57756.1};
GN ORFNames=BO96DRAFT_494027 {ECO:0000313|EMBL:PYH57756.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH57756.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH57756.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH57756.1,
RC ECO:0000313|Proteomes:UP000247441};
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.
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DR EMBL; KZ821346; PYH57756.1; -; Genomic_DNA.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; 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; 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; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; 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; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775:SF53; ATROCHRYSONE CARBOXYLIC ACID SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43775; 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; 1.
DR Pfam; PF16073; SAT; 2.
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; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 366..796
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1651..1728
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1609..1645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1728 AA; 190743 MW; 51BBC911146AB0B7 CRC64;
MRLFFFSNKF PIDDLPDLFR RLRLCSQSPR HVVLRRFLEE ATRVVREEIY RLPPELRSLI
PPFQSILDLA QNYHWHKGPL CGIFECIFLC LVQLGLFVGN YEIRPHEFSF NTQESLFTGL
GLGFLAATAV VASPSLLDLP ITAAEVVRIA MRAGILLYQK SQDLEQLSLD SSLESWTTVE
TPPSSRIYIS VVEPDGSVFI SGPPSGLREF FNKSGKVQSA PRAPLPVYGG PCHAAHLYDR
THTEWVVSKV NPEIASRRLS GHPLVLSMGD GQPLAGENAR DLFESATYVL LTSIIRWDSV
LAAVKKLPHW KQDTKLQLET FRPSSPAVHG LISAVQSEYP DCTVSVDDLG DWIIDNSLEP
PTIPIDSRIA VVGMSCRLPG GSDDLQRFWE LLEDGRDVHQ KVPGNRYDVE SHTDMTGRRL
NTSHTPFGCF IDSPGLFDAS FFDMSPREAG QTDPTHRLAL LTAYEALEYS GYVPNRTRST
TRDRVGTVYG QCSDDYREAN AGQNIDMYFI PGNYRAFAPG RISYFFKFSG PSFNCDTACS
ASLAAVQIAC SALIRGEADM VVAGGLNILT GSDSFAGLSR GFFLSKTGNC KVFDDGADGY
CRADGIGSIV LKRLSDAQQD NDNILGVILG TATNHSSHAI SITHPHAPTQ EHLYRSVLSQ
AGIGPHDVDL VEMHGTGTQA GDAAEIESVT RVFSPPVPRR SHPLYISSVK ANLGHGEAAA
GITALMKALL IFQHNAIPRH VGIKTALNSK FPDLERLNVH IPKETIPWPY RSNRKRYVMI
NNFSAAGGNT SLLLEEPPVR PDPQGPPQTR FVVALSAKST TSLRRNLESL ITWLEGNRSA
RLASLAYTTT ARRMHHKHRI AVHGASVAEI IQALHQRGSR AELGLLVSKP PSVAFIFSGQ
GSFYAGVGSQ LFKEYPPYRE QLQRLDEICQ QNGFGSILPA ITDTDADVSQ LSALVTQLTT
VCVQIALCRL WRTLGVKPAV VIGASLGEYA ALYAAGALSA SDAIFLVGQR ALLMQKLCTA
NSYGMLAVQG SVDDIRRCVQ DRTYEVACIN APRSITICAS IKDIVDIQQS LVSQGYRSVK
LNVPFAFHSS QMDPILDRYE EIAKAVSFRS LQIPLISSTL ADAAVQSRSL VASLFLRENT
RAPARFAEAV AKAQDMGLVN SHTVWVEIGV HSTYSGAVRA TVADLQAIVP SLRSDETNWH
TLAVSMCTLQ ETGVPLDWNE WYRPFEPEVR LLDLPSYRWD LKNHWIQYNG DWLLVKDKRP
RTDQISAATP SLRTALVHQI MEESFRPDGG EIVVQSDVMD KEFFAVASGH KMSGRPLVSV
FSYPDIAFTL ARYMYSRLKP ESPLPAMDFG QVRVLQGLLP RKDRSKPQWV RMRMRADPQC
AALQLSISGL SDESSRHVEE KLASGVVRCG DRQSWQDEWA DYAHLLTTRI VTLQQMAENG
QASRVSRDLV YTLFKNIVDY ADHYRGIQSA VLHGLEAVAD VILAPSNDSR WTAPPHHIDP
ITHVGGLVLN AGHATDHHNT IYVMEGWKSM RFAEELVAGE LYRSYVKMNP ARDGSGFFVG
DVYVMREDHI VGKVRGMTLR PLPRILMNRF FDPPDDGDGL ATQHIQPHDL PQVQHQPSPT
TDSGPDDDPK DPNTGPLTPE VDLPVAPSVE KANTKLVRGA LALLAAETGV EPDGLTDETE
VSALGIDSLL SLVLVEKFAT ELQVNIQSSF FLESPTIREL KEYLTASW
//
