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Database: UniProt
Entry: A1CCB3_ASPCL
LinkDB: A1CCB3_ASPCL
Original site: A1CCB3_ASPCL 
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
//
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