ID A0A2I2GPA7_9EURO Unreviewed; 2570 AA.
AC A0A2I2GPA7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:PLB54712.1};
GN ORFNames=P170DRAFT_470157 {ECO:0000313|EMBL:PLB54712.1};
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:PLB54712.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB54712.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB54712.1,
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 -!- 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:PLB54712.1}.
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; PLB54712.1; -; Genomic_DNA.
DR STRING; 1392250.A0A2I2GPA7; -.
DR VEuPathDB; FungiDB:P170DRAFT_470157; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; cd05195; enoyl_red; 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; 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; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
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:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; SM00829; PKS_ER; 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; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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 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:UP000234275};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..442
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2488..2565
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2570 AA; 282350 MW; 26F2224E364D40A1 CRC64;
MPLIQDTNPN LPGDRDDAPA LAVVGLAFEF PQATSSDEFW EMISEGRSAS TDFPKERMNI
DAFYHPSQER PSSIPVRGGN FIQEDLGAFD APFFSITPGE AACMDPQHRR MLETTYHALE
DAGIPIEKCS GSDTAVYTGC FTNDYINLLQ QDFELEQKHA AMGVAPSMLA NRVSWFFNLK
GTSMNLDSAC SSSLIALHLA AQDLHAGNCS MALVGGANLV YHPHFMKIMS AFNFLSPDSR
SWSFDSRGNG YARGEGLVML VLKRVDDALR DGDCIRAVIR NTGSNQDGRT PGITQPSMQS
QLDLINRTYH QAGVSMTPTR YFEAHGPGTP VGDPIEANAI GQAFKDYRTK EDPLYVGSIK
ANIGHLEGAS GLAGLVKSIL ILEHGVIPPI AGFENLNPRI DATKLSLKFP KEALPWPSTG
LRRVCLNSFG FGGTNATVII DDAYHYLKHN NLNGFHRTRP LPPSYPALLT MGPNGDSQMT
TEASELQVPR LLVWSAADRS TAEKLGAAYH EYVRQYPQDI TDVTYTLAAR RSKLSWRAFT
VTGVDDQMPE LTRQNAPLKA RDGARLAFVF TGQGAQYLGM GRELLTHPVF LNTVNLMDDD
LKSLGCSWSL KWLLEASESE TPIDRPEYSQ PATTCLQIAL VDLLESLGVT AGVVLGHSSG
EIAAAYTTGA LSRSTAVKVA YYRGLLSSQL AEQRTDLSMM AVGISASDIQ LYLDRLQQLG
SSLEVEIGCV NSPKSITLTG SIDQLSTIQQ WLESDGVFAR RLRVPTAYHS TAMKAIAEDY
RLAMGDLARG PAAKTIPMIS SVTEDVVSSK GLASADYWVR NLTSPVKFEG ALSRLLLLAQ
NRIQPRKQLG RKLPVDFNIT HFLEIGPHKA LQGPISETIR ASPGSGKPTY MPLLERKQDA
HITLLKTAGQ LFCAGYPVDI LSVNGLEDIP RSMPSSLPSY PFNHERVYWK EGRISKNFRF
PQVARHDLLG TPNLDWNPQV AQWRNVVRLN ELPWLRDHTI DGQIIFPGTG MVIMAVEALR
QLPWAQSNLT SIEIKSAQFL HAIRFPDGLE ELETQLTLTT EKAKDSTEMP WSQFRLFTIE
DGSYIECCRG LIRGSVDREP RTPELPSSSG TSFEDWVAAL SAGCESPKNA YENTGSSVRY
GPCFQNLKDM RLGSGGKAFA HVDLSTWRSG ETDDWSPQYT VHPVTMDGLA QLVVPALAYE
CDNLPTMVPV RAETIWINLS GPSMSSDKEL LAAAQCSTRG NRGARADVVG TSSDGTQLVV
YIEALETTFI GEASTSTGQD IARSLCTNLV WKPDVDMLSD EQLLEEICRG RPSEPHGSLQ
RHESLQLALL SFLDEAVQYV DQHPDLSIPL YLRRYVDWMR YQQGRHHDSS LTKANDWVLR
DRSARDKLAL DIENTDNEGR FFIHVARNLI AILSGESDPL DVMFRNGLAD RYYEQMLASE
HHAYPISRYL DLQCFKNPSL KVLEIGAGTG GQTLGALKAL CSDGVPKCAQ YDYTDISPGF
FPQAKEKFKD FLDIMRFRTC DVTKDPVTQS FEPGSYDIIM ASHVLHATDR LDVSLQNIRK
LLKPDGKLVL METTDPDALP ISFAFGLLKG WWSPLDHEER TTYSPCITLS QWDERLKRNG
FSGIQIDVPG QELPVCRYSS IIVSSARAEN NVIDTTDDLI VIRDPTRAYQ CEVAASIALG
RRAVITTLGE AAQLNIRPST EIVVLLEMEA SVLSDLNNAS YTLLQRVMTA AKNVLWVTRP
LVKGERLPQH SLVEGFGRTL ASEDATRKFA TVALDGYEPA DQASATILRL MSQIARRPVE
NMETTFSTSE GVLKIPRVSQ NEEMNEVIHQ YTRPRREEQW YCDSETDSIQ GATLEVGAPG
GPHEVEYREN CESLSSTLAD DEVVIQVQAF GLTPRDYLIA SGQLKQGGLG TQCSGIVRQA
VAQSGFKEGD RVCAIGTAMA GTLIRAKSRA VIAIPSDLSF TQAAALPTPL WMAFYSLDHL
AKLEADETLL VHHACTSVGQ MVAQLAARQG ARVLATTTSK AQQTLLCATL CLPESDVFLS
SDPLLAQRLK QITEGQGVDV IVGSFDADAR SKMARCLAPG GRIVDISWGA SQRAQQMPLP
NTSHALIDMV ELFSCKPQRA HAFFQKAMKC YFEGQSKPPQ FIDVYKAGKE QDAFQRYLDM
DMIGELVIEF DRATAITVNC SSKPRYLFPE NSYVIAGGLG GLGRSFARWM ASRGARHLIL
LSRSGPSTST AQALVHELED MGVKVATPQV DISNLCHLEQ TLAKLSATMP PIRGCIQATV
ALRDNLYENM SYEDWTISTD SKVTGSWNLH RALPQDLDFF ILLSSLNGIF GSRAQANYAA
GNTFKDALAH HRLAQKQKAV SIDLGLMVAE GVVAESEFLL SAMRRIGHLM EIAQDELLAL
LDYYCNPGLP LLPATEAQII VGIELPDDIT AKGIDLHHSI RRPIFSHLFR IGSRNGTGAS
NGASGQAVDQ AGLIDRPAVL KALPSVGDAT DQIVEWVAAK VAHMLGLSAA DIDPGKPVHS
YGIDSLIAVD LKNWFDREIG ASITVFDLMG NAPLQRLGQV AAEKSRYRVQ
//
