ID A0A317VRJ3_9EURO Unreviewed; 2484 AA.
AC A0A317VRJ3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:PWY77014.1};
GN ORFNames=BO70DRAFT_409460 {ECO:0000313|EMBL:PWY77014.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY77014.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY77014.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY77014.1,
RC ECO:0000313|Proteomes:UP000247233};
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:PWY77014.1}.
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DR EMBL; MSFL01000019; PWY77014.1; -; Genomic_DNA.
DR STRING; 1448321.A0A317VRJ3; -.
DR VEuPathDB; FungiDB:BO70DRAFT_409460; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000247233; 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; 3.40.47.10; -; 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 SMART; SM01294; PKS_PP_betabranch; 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:UP000247233};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 372..788
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1569..1643
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1543..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2484 AA; 274751 MW; CB92D32812D375EA CRC64;
MAPFHPTLPH GPNSKSILLF GCQSLNFDAH AFLLLRQTIL SDPNNHWVLD ILAELPVYWR
TAVRYVPQFD AVPGAQLLHD LNRWFRTGEV SDDHFPLPYI QHAPLFVIHH LTQYERYLGL
TQPEYVADGV LADESPVVDI VGFCIGFLSA AVAASVRSRE QLRTYGAVGI RLAILLGAMG
DAQEREQKYT SLSTVWKNSE LEHELPRAYI TVRYDSNRVT IMTPRNTLGP LQQSLQSAGF
SAYHVDFNGR YHWAGHQKTV DALVEMCEAD PALQLPDASQ LVRRTWTNIS GEAVSSGPLH
HLVLQSVLSH QCMWYQTFQA VQEENPSAVV FEFGRERCVP PSFLRNQRTR VIHYADLELD
AFPRTLSTQV YDDDIAVVGM ACRVAGADDL EEFWRILCSG ESQQREIPPE RYKDYETPWR
PDAARPWLGN FIRDIDAFDH KFFKKLPREI MSQDPQQRLL LQVAYQALEQ SGYFHKKNIT
RDIGCYVACC TVDYEHNVNC HPATAYSATG LLRSFMAGKL SHYFGWHGPA LCIDTACSGS
AVALHHACRS ILNGDCKAAL VGGANAITSP LGFDNLNGAS FLSPTGPCKP FDAKADGYCR
GEGFAAIFIK KMSDALADGD HILGTIAGTA VEQNDNCTPV VVPHAPSLAA LFEKVTRRAR
IHPHDISVVE AHGTGTQAGD PAEYSSVRQV MGGPQRKAPL SLGSVKGLVG HTEGVSGMIA
LVKVLLMIHE GQIPPQPNFQ TLNPYIKSSA DDQIEIPTQL KPWSAHYRAA LINNYGACGS
NASIVITQAP VESPPSAIHA SGLALPFRIC GLDDARLREY AQRLRLFLRR EDLSSHHLSL
ANISFSASRQ SNPTLDRQLV FSCASTADLD AKLSVVAEGD TSKFIRLKKP ASTVVLCFGG
QVSTFLGLDR VVYDSMRVLR HHLDQCNRLL ESLGYCSLYP GIFEHTPITD QVKLQTQLFS
LQYACARSFG ELTAMCVSGI LSLEDTLILI TRRATLIRDG WGADPGAMIA VDGDRMNVES
LLDEHAKAIP AGTSPATIAC FNGPRSFTLA GATTAIDAVQ QALARPAMSH LRYKRLEVTN
AFHSTLVGRL MAELKRITHD MTFHEPAIHL ERATEQPAGV SPNIVADHLR NPVYFSHAIQ
RLSEQHGPHH FQSINITGNN GVQSLTDATM ALWKQGLPVK YWAHHHSQTS DYGVVLLPPY
QFEKSRHWMD NKLLPAAQIQ QTATADCQEF TFLGYDQDRV ATFRINTTHP KYIEALSGHI
GVQTAPLAPA SFMLDSVVEA LRSLPEGKDR VPHVRNVTSD APLGLDGSRD VYMSLHPHDK
EKTVWEVKYT SQDREKGARS QTVHCSARIE MLSPEHPTLQ AEFSRYSRLI SHQHCHDLLH
DPDVDDVLQG RNIYRYFAEV VDYAEQYRGV RKLVGKGNES AGLVVKRYSG ETWADTFLSD
SFSQVAGFWV NCMTDRSSSD IYIASGMEQW MRAPTYADPS TPRPETWDVL AKHERSDGLY
TSDIFVFDPS SGQLVEIFIG MQYSRVPKAV FSKILSKLNP GAQKVAPTEV NSRPEQSPKP
VVKKQKSASD LPARIKAVVA DFCAVDPSEI QDDNNIADAG VDSLMAMEMA RELEEAFNCS
LPATDLMEAE TFRELVRAVQ RAMGVDEADG SDSTASESES DRDSVVNDTP TTESITSVST
DTPDLQLPHD LVLEAFGETK ALTDQFLSDN HCSGRVHSFN PLQMQLCVTM TLEAFEKMGS
PIRTATRGQR LERISHDPQH KELVDYLYRR LEEARLVDMD GTAAVRTGIS WTSRSSAAIL
EDIGRAYPEF AGASKLAFFT GSKLAAVLRG EQDGLQLIFG TKEGQELVSW MYGDESHNVT
GYKQMLDFIQ RLARKLGSES GSLKILEMGA GTGGGTKWLL PGLVKLGIAV EYTFTDISPA
FLAQARRRWK EYPLLQYRVH DIEKPPADDL VGNQHIIIAS NAVHATSNLQ VSTGHMRKAL
RRDGVLLMLE MTRPQFAIDI VFGLFRGWWV FNDGRTHAIT GEQRWESDMH AVGYGHVDWT
DGYSPEVSVQ RVIFATSTGE QKARLPLGPK PPSVDLLAGV DNVARGRATD EYIRRAADGF
TAPSLGTDTV AGPIGVLITG ATGSLGSHLV AHLARLPTVH SVVCINRHGT EDPLVRQKRS
LTERGISLST DELKKLAVFE TDGSEPLLGL SNEQYESLKK SVTHIIHNAW PMNGARGLSG
FEPQFCMIRN LIGLARDIAS IRSGRIAFQL ISSISTVGHR PLVTDEAVVP EVRSTIDWVL
ANGYSEAKFV CEQVLAQTLG QHPDRFNAMV VRPGQIAGSS TSGYWNAAEH FPALVKSSQT
LKLLPDLGGV LSWTPVGDVA ATLSDLVLTE DPHPVYHIDN VARQPWPEMV RFLAQELSIP
PDNIIPFPEW IHRVKAFPGS REDNPASVMA DWLADNFERM SCGGLLLDTS RACEHSAALR
SVRPVEGAVI RRFFRHWRQT EFLH
//
