ID A1CCB3_ASPCL Unreviewed; 2561 AA.
AC A1CCB3;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 116.
DE SubName: Full=Polyketide synthase, putative {ECO:0000313|EMBL:EAW12170.1};
GN ORFNames=ACLA_061310 {ECO:0000313|EMBL:EAW12170.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW12170.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW12170.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027050; EAW12170.1; -; Genomic_DNA.
DR RefSeq; XP_001273596.1; XM_001273595.1.
DR STRING; 344612.A1CCB3; -.
DR EnsemblFungi; EAW12170; EAW12170; ACLA_061310.
DR GeneID; 4705752; -.
DR KEGG; act:ACLA_061310; -.
DR VEuPathDB; FungiDB:ACLA_061310; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; HWVRNLT; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000006701; 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:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase 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; 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; 2.
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; 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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
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; 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; PF13602; ADH_zinc_N_2; 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.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..460
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2474..2551
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2561 AA; 279249 MW; E7C10DAB0EFEBA1B CRC64;
MAPISNPNPT QPGDSPRTNG VTMNGSELPR QHAPSVPIAI VGMACRFSGN VRNPTQLWEL
CANGKDGWSP IPDSRFDVKS LYHPDNSKAG RSHVIGGYFL DDDIACFDAA FFNLASDVAS
GLDPQARLLL ETVYEATEDA GIPLNKLAGT NTSVYTGTFN KDYHEIQTKD AEVLTRSFLA
GTGTAMLSNR VSHFFDLQGP SLSIDTGCSS GLVAVHQACQ SIRTGESNIS IVGASSTLLS
QDAFISASTI GAIGSEGKCF AWDSRAAGYG RGEGVAALIL KPLDAALLAG DQIHAVIKDS
GVNQDGKTTT ITSPSADAQV NLIEQCYRRA GLDIAQTGYV EAHMTGTAAG DPVEAEAIAR
TFGKARQADD KVLVGSVKTN VGHTEPVSGL AAVIKTTFAL KTASIPPNLN YETPNPSIDL
DKGHLEVPTR LTPWPEDKIL RASINNFGYG GTNAHVILEP APAPTAIYHL NGQSTSEGSR
SGDNSRVFVV SARDSAACRT VMDRLASHII KTSPSPESLA YTLNERRSLH PWVAAVRATS
IEDLAERLRE SERKPSFAYK KPRLGFVFNG QGAQWHAMAR ELLTVYPVFG HAISNAGKIL
KEYGASWSLI DELNRDETST RVSEIHLSQP ISVAIQLGLV DLLKSWGITP SAITSHSSGE
IAAAYAAGAL PFEQALGVAY YRGELARKQL KVCSLTGGML AVGIDQQSAE RHIAEITPSG
GVVVACVNSP SSVTLSGDLD TLGEIAARFE KEGVFTRKLK VPMAYHSHHM MPMVAEYTER
LEELLDLPVT PEWNGPLFVS PVTGEAVTAV KTFGAEHWVQ NLTKPVQFSR AFENMCFSSS
DSSAPSANVD LILEIGPHST LAGPIRQILK GKDVKMPYAS CLRRPINAVE TMQDLACELL
SQGYPVDLKS VNSPIGDAHH TFVANLPSYP WNHSTRFWVE PRIAKEQRFK KFPPHELLGT
PLNGSNALTP TWRNFLRLSE IEWLKDHQID DTVVFPGAGY IAMAIEAIRL ITDPSESTIR
KYRLRDIDIM NALVLPDSEM GVEVQLQLRR CSDRELDHEG WYQFELFSLA SADAPWIEHC
KGYVTVETES ETRIIALNDG REISREDAFF ADGVDPCPID IDSLFAGLRK RGIYHGPLFQ
NIIDSHAARN RAITNFAISD IACQEHEYVL HPTTLDSILQ SSFSSLPDDI GQDSMVLPRS
IRTIDVPWNF KRQGGERLRA LSEMVTGDTR GYSSDITVVS DNSDATRSFL EIKDFFGSAI
PRRVQDSGEE AGICSINCWE LDILHNPPAS FRESMVIPVK DHEIEQERKL SRMSYIFIHD
AAAELESQES ESWQWHHKRL YAWMREVVTL GEAGKLGPNS QLWSKLSPGA KRILADELSA
GNAAGRLTVR IGEKLASIIR GDIMPLELMM EGDLLNQFYM QHEALKTRSY SHLARVAELY
AVKNPGANIL EIGGGTGGAT STILEAFGKR GSDNGTILGH YTFTDISPGF FEAAREKFAP
WARMMDFKKL DIEIDPLAQS FTSGSFDLIV AASVLHATKN LHTTMKHVRK MLKPGGTLLL
IEATADRLEG QLIFGTLPGW WLGEEPERQK SPNAPFEMWD RVLRDTGFTG VDFEISDYEE
PEFQSARVML SRTSATVQAP ISIVVEDKTA EDPQEWLAEL SDAIREKTGV LPKLVDLSDV
DSFKDTVCIV ALEMGNPFVH SMDADAFQKL KSLLLLSSGV LWLSCGGLVH SQNPAFSASE
GLLRTMRQED SHTRWIRLGF ENDENPWTSG KIGHVIHVLE RSFDKDAETS NIEWEYSVAD
SQLHVPRIFP EKTLDAIARD LKLPLEPALE AFHQPDKPLV WETSPSTGLD PYFVENPVIL
STDVPSGMVE VEARAFGLNF REVMVALGQL EEPLTGYECS GIITRLGPNT EQSGLKVGDR
VAALCKGRIA SKGRTYWTSV VKVPDEMPSK MAASFPAAYT TAYGSLIQVA GLQKGESVLI
HAASGATGQA AIVIAQHVGA EVFATCSTEG KRDLLVEHYG IKPDHIFASR SGSFAAGIMT
KTNGKGVDVI LNSLSGPLLK ASWDCMARFG RFVDITKVDM EANRWLQTAP FSRCSMFSSF
DLLQLTECRG RLTHAALSES LNIIRERGIS PVHPITPYPI SEMATAMRQM QGGMHMGKLV
LVPHDEDRIK LIRRPSPVSL DSPGETYLVV GGLGGIGRAI ATWMIENGAK NLVLVSRHAT
SHPEAPALAK MAETAGCRLQ IHDCDVSNEM SLLQLIRDCS ETLPPFRGVI NGAMVLDDTV
LERMTFEQWS NAVRPKIHSS WNLHTHLPNL AFFVMLSSVA GVAGHMSQAN YSAGNSFEDA
LARYRTARGL PAVTIDLGAV KSVGYVADRE ASGDDRLRAR VENVGFGSVD LDHVLRMVGH
GISESLRQSP SQSQVIVGPN FHTLASESVM SHDRRFGTLR IASQRGIETA ATSTSKTSTA
ALAQALSKAS TLTEAVALLV QAIVAKIAEI FNIPLSDIDA ELPMSRYGVD SLVAVELRNW
LSSGAKAKVT VFDILQSASL NEFGALVASR SEDLTSRELP A
//