ID A0A3D8RS11_9EURO Unreviewed; 2434 AA.
AC A0A3D8RS11;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Polyketide synthase, putative (JCVI) {ECO:0000313|EMBL:RDW76877.1};
GN ORFNames=DSM5745_06869 {ECO:0000313|EMBL:RDW76877.1};
OS Aspergillus mulundensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1810919 {ECO:0000313|EMBL:RDW76877.1, ECO:0000313|Proteomes:UP000256690};
RN [1] {ECO:0000313|EMBL:RDW76877.1, ECO:0000313|Proteomes:UP000256690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5745 {ECO:0000313|EMBL:RDW76877.1,
RC ECO:0000313|Proteomes:UP000256690};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW76877.1}.
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DR EMBL; PVWQ01000007; RDW76877.1; -; Genomic_DNA.
DR STRING; 1810919.A0A3D8RS11; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000256690; 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: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; -; 2.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF49; SYNTHASE, PUTATIVE (JCVI)-RELATED; 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; 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 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; 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:UP000256690};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 8..420
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 2434 AA; 266812 MW; 18512E5D0AF47B7E CRC64;
MRTHHESPPP IAIIGMAARL PGGVNSIPSM YQFLRGKKDG LREVPESRFN IDGFHNDGDV
AYSMRQQKAY FLDDDISMMD ASFFGSSDME AAGSDPRARL LLEVVYECLE NAGKTTYRGE
RMGCYIGAWG VDWSELTLKD GQQRNPMIGA AAGSFFLSSY IAWNLDLHGP TMSIETACSA
SMVALHEACQ ALYSGECSSA IVGGANLILT PTLHMSLSSS GVLSPDGICK TFDASADGFG
RAEAVNAVLV KPLDAAIRDG DAVRAVIRAT TVNNDGHTLI LTTPSAEAQE ELIRQAYKKA
GIEDTDQTAY FECHGTGTMA GDTAEMSAVS KVFPKGIHVG SVSIENRGRD ETDEVRRNQT
LAIPKGHPGS PVLSKQSFPF ESANLTVPKE ELPWPADRKE RISVNNFGVG GTNVHVILDS
ASSLGLNNAR NGLATSLSHP RLLVVSANSE KSLARRIADI EIYVKENPNN LADLAFTLGE
RREHLAQRAF LLETEARESG SFHVGTADCK ATPEVTFVFT GQGAQWPAMG KALIETFEGF
RRSIEQLDRA LEHLDRPPAW RLKDLLSKNS APDEFNRAEL AQPLCCAVQI GLVNLLARWG
IAPASVIGHS SGEIAAAYAA GAITAEDSII IAYHRGKILN KVTRKGGMAA VSLGREQVTP
YLVDGVVIAC ENSQHSVTLS GDFDELNCIV DNIKSDDPDA LCRILRVDKA YHSAHMQDAG
EDYEVSLHGL SANDELSMLP FFSSVTGKKI TDPTELGAGY WRQNLESPVL FLTATRAILE
SEEEDTRRVF LEIGPHSALS GPLRQILSEH QRGESCFYVA SLVRGEDPTT SVLYTAGNLY
NLGVPVNLSA VNGKGSLLVD LPPYPWQHDT RHWDQTPAVE AWRLRKYPHH ELLGSRVLGA
TDIEPSWRNN LVLDDAPWLY GHRIMGKTLF PGAGYIAMAG EAIQQLTSKP NVSYQISHLL
LKYALFLDTN ECVELITNLR PVRISDIQDS DWHEFSITAV QAGEAIRLCV GQVRIAPPSA
SSSMPLEEKT KLKRRVASTA WYKALREVGM DYNREFRGLD DVYGDPIRHE ATATVKTTKV
SPSRYVMHPT TIDRCLQVIS VAMFHGLARN INIRSLPVLF EDIFIGPEAE ELCVQAQADL
GNGNFVLGDL GASADEETVL SIKGMRLHVL GDDGSLQQDS ELATRPAWMP HIDFLSPKAL
AKPPPPMTQD SELRNRVVDL YILESARRAK DVEPTEEHLL KYKRWLMMSE SRIAKQSTWR
LSDYGYAPDC PFDSSNSLEL TNWLRDQADQ FPVIAPLLAC IQRLLDNIVG VLDGTSNALH
LLMEDDGLKQ VYDFVLSFDS CQQFFAILGH SNPELNILEV GAGTGGATAR FLEYLHAPDG
SRMYARYTFT DVSAGFLAAA KERFSKFDAM EYAVLNINED PAQQGYKLGT YDLIIASNVV
HATPSLKRSL ANLKSLLAPG GRLFLQEIGE EFAIAEYIFG LLPGWWVGEN DQRVDKPYVP
VDRWRQELTA VGFDGIDFAI HEESQMVNLV STCPLPPSED QTVNLLVQEP HCPWVVDVER
YFSDKGYQVN MCSLGRPPQA EGIVISLLDA TEPFLFNVTE DTFQQLKDFL LSPLVKHVLW
VTRMSQITSG DPRYGLIHGF LRALHAESHS EGKFLSMFDI DDIDGNSVSH LLKVHDHWRR
NCSTEEDSRR DEYALVDGVV HVSRYEATDT ETELQRPAKD IVPRRLGIES TGLIDSMFWR
EDNPAAPGKD EDIITALGLI ASPEQLGLEG SGVIDSVGPG VSKLRKGDRV IFLGPGCFAT
HVTVPAAKVI PLPAEWSLEE GATSPIVSLT AAVCLLRLGN LRRGQSVLIH AAAGGVGIAA
IRICKGVGAK IYATVGNDEK AQYLVDTFGI RRSHIFHSRD SSFYADLMRE TDGRGADIVL
SSLSGELLRT SWKCVAPGGT MFDISRRDVL ADAMLPMKHF VGRRSFVTVD LGEYMDEATL
DSSAEFSDSV KKGLVGAVSP VSCFAAADVA DAFRYMQIGQ HMGKILVRMP DDLSELPTKD
TRAQVSFSPD NAYLLCGGLG GLGRALSNWM VERGARCLLY LSPSAGEGED HQAFAEELKC
QGCRVVYVKG TASETHDVQR TISQSPKPVK GVVQLALALR DTSLERMTFE DWTVPLAAKA
HGTWNLHQAF QDTPLDFFLM FGSIAGVTGM AGQCNYSAAN SFIHALARHR HSLGQPASVL
DLGPVADIGY VSRSPEIVKN FSGRFEWRFT KEQEVLDAVE ALIYHSSKSK AKSKSTEDNG
SRYDLHHIVF GLVSVAPWAH RTGDTRMSIL SNRAQRMQDS SGEADDIVDF VAQVEADPEM
LNRPSTEEFL IRKAGYMIKS PAKAKGGKSD VAGKQDLKAM GNIPIDSLIA IEARAWARKR
LGVQIPLSEI TAAGNVKGLV GLAIQEMKKR HSVT
//
