ID A0A2I2GMP1_9EURO Unreviewed; 2136 AA.
AC A0A2I2GMP1;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Ketoacyl-synt-domain-containing protein {ECO:0000313|EMBL:PLB54161.1};
GN ORFNames=P170DRAFT_504957 {ECO:0000313|EMBL:PLB54161.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB54161.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB54161.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB54161.1,
RC ECO:0000313|Proteomes:UP000234275};
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 -!- 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:PLB54161.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSFO01000001; PLB54161.1; -; Genomic_DNA.
DR STRING; 1392250.A0A2I2GMP1; -.
DR VEuPathDB; FungiDB:P170DRAFT_504957; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000234275; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; 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:0006508; P:proteolysis; IEA:InterPro.
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; 3.40.50.1820; alpha/beta hydrolase; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR049492; BD-FAE-like_dom.
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; IPR001375; Peptidase_S9.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF20434; BD-FAE; 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; PF00326; Peptidase_S9; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 890..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2136 AA; 235068 MW; 08D901BBF915C7CB CRC64;
MADTYSQSTE YPENAIAVVG MSCRLPGART PDEFWKLLLS GRSMGGDVPE TRFPLKNHWR
SQAMSRMQGN FMDDVDAFDH QFFGRSSREA AAMDPQQRLL LEETYHALET TNYFHPDSQF
DSNVGCYIGT FCNDYDDNLA GHPPNAFAAL GCLRAFLSGR VSNFFNWTGP SIIFDTACSS
SGVAIDAACK DLILGNCSAA VAGGVAVMSS PYVYQNLGGS SFLSPNGKSS PFDSNANGYS
RGEGVALVVL KRLDAAQAAG EHILGVICAS AVRQNSNNYP ITAPDPPSHE NLYRRILTTA
RMEPKEVNFV EAHSAGTRVG DVPEVAGVTN VFGRSSWDGP LHVTSVKANV GHTEGASGVV
SLIKILLMLR NGQIPPQANL KELHEKISNT QGNIIVPREA QPWNARPMVA CLNNFGAAGS
ISAMIVKEPP PHQPQTVMGI KEPLDIAFPI CICAHTSHAL KKNCTDIRDW IRDGIPNAEI
QDIAFNLSRR TNLSLSYRWA VTAKSIPALI DSLQAVEMAD AKTLTKLKTP KPIILLFSGQ
SAETSHISRH VYETCGSFRR HLDRCNRVLT GLGAKGLYPD IFEDRSCPDA ATLHARNFSI
QYSCARTWID SGLQVARALG HSIGQLIALC VSGTLSLHDG LKLVVGRAKL VDTKWSTEKG
AMFAVQTTLD QVQQVIEQHK DLDIACYNGP KSYVLAGSKM AVKSAMVTLR QRQIKHKRLH
VTHGYHSRLT EPILHYLREI ASDLAFLPPE FAVETCTPSR SWDIPTADLI SQQTREPVHF
HAAVQRISNE LGACTWLSAD LNPIVSQMAA AALPPETSKT STFLPALSIS SSSSASSLLQ
SLSDVVRILW QEGQIVGFWP FLNGGSQRYR YLTSPPYSFT QHRHWLEWKE SRASSQPQPS
GRQSSEPERS ETELVIFKGF ENVEGIGTAS FEVDTRAPSW PLLVDQHAVS GIGICPASLY
CEMVIQAAKL ARLSKREFDR SLVLVEDLRI FSPVGRDIGE KLKLTVRAAD PAPFYWDFAF
YLEHDTPRAT GRLRLADESM DSTSNIQHNS VLATLGVAGD TTPQQEQLGN GCSNMSGDVI
YRLLRSSVTY GKIYQLIRSF VLSHYVKAFI QLPGNAQISY SHDTIPPVVV EGVLQVAGAH
ANLFSTTSPC TGLRLCTQIK RIQFSHHRSW ESCHSGWEVV ARVNQQSPAF AEYDIVAFMP
QTGKLAMAIY GVRFQHASAQ SVNQILSTVS ADHGAVPLHP SDNALNDEKA EPNGGGNSLS
PITQETSVSE AQDDSFASTS PSMTPRNSFS ESVLDRSVES VDSKPCSKGS SCVAHRLRGL
LEAHLGPLEE TDPRVTLSSI GVDSLLSQEL IGDMEKEFSF PSSDIQLNSD TTFSELCANI
GAGDLDISIP EQTPKSAVED KTWQPQVVFD SIRERFPEFA ARTSWLSFWD KVHPLQFQLT
VSYVLDAFSN LGCDLRVMEA GHHVASILVA PQHGKIKDAL YEILQNAGII ASTGREYLRS
NQDVQGLSSG PIFDELFAKY PQHRQDHELL RVTGPELATF LSGQIDPLQR LFGIARHREL
LSQYYSDSPM FHTMTLMLCQ YLKQLTATWS SSRPIHILEL GAGTGGTTAA VLDTLHESGI
EFRYYFTDIA RSFVNAARRK FEAYQDSMEF IALDIEQPPP SELVGQFDIV VSTNCIHATR
DLNVSLHQAR QMLRSDGFIC LVETTIRMSF QDLIFGLLEG WWLFEDGRSH ALGSPTRWNN
ALLSAGFEQV MTSAGPSLES QTVQLICGFA SQNYAVEGHR PIREIGFETV VWKTSKPLLC
ADVYYLPDHP YKPKHKCPIA LLLHGGGHMM LSRKHVPREQ VSLLLEHGII PVSIDFRLCP
EVDIVNGPLS DARDAVRWAR GELPNLQFKP RGLSLDGEHL GAVGWSSGGT LALLLGHTLD
DPAYRPPDAI VSFYCPTDFE DESWTTFRNL PAPQERSSLD PDILKAIEPE PITGYEARHQ
DIGIPSRVDN NPRVRLFSHI LRYGQALQAY ASGLPSTRAA STTQKVESIP FSPPPPIEQI
RKSSPYASVV SGKYVSPTYL IHGQKDEQIP WQQAAKMHDA LRRCGVETEI ALPPDSSHLF
DTIGAEPSVS DEILATGYRW FAGHLDASPP SDEAQE
//
