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Database: UniProt
Entry: A1CCS9_ASPCL
LinkDB: A1CCS9_ASPCL
Original site: A1CCS9_ASPCL 
ID   A1CCS9_ASPCL            Unreviewed;      2556 AA.
AC   A1CCS9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   SubName: Full=Polyketide synthase, putative {ECO:0000313|EMBL:EAW12336.1};
GN   ORFNames=ACLA_063030 {ECO:0000313|EMBL:EAW12336.1};
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:EAW12336.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW12336.1, 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; EAW12336.1; -; Genomic_DNA.
DR   RefSeq; XP_001273762.1; XM_001273761.1.
DR   STRING; 344612.A1CCS9; -.
DR   EnsemblFungi; EAW12336; EAW12336; ACLA_063030.
DR   GeneID; 4706058; -.
DR   KEGG; act:ACLA_063030; -.
DR   VEuPathDB; FungiDB:ACLA_063030; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   OMA; EYGIDSH; -.
DR   OrthoDB; 5396558at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; 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; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; 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; 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; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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          36..463
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2475..2549
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2556 AA;  280401 MW;  76BAD2AD53D16DC2 CRC64;
     MTANSFEGPT NPVPLPPSTP NTDMEDDIPN VVGDVSMPIA IIGMGFRGPA DATDVERLWR
     MIVEGREAWS PIPESRWNSG AFYHPDHARH GTVNVQGGHF LAEDVSLFDA PFFNMTSDEA
     AAMDPQQRLL LEVTYEGLEN AGLPLSKIMG SQTSCFVGSF NADYTDLLLR DPDAIPMYQC
     TNAGQSRAMM SNRVSYFFDL KGPSVTVDTA CSGSLVALHL ACQTLRTGDA QMAIAAGVNV
     ILSHEFMSTM TMMKFLSPDG RCHTFDEKAN GYARGEGIGC LILKPLKDAI RDKDTIRAVI
     RGSGSNQDGR TPGITLPNGA SQEALIRHVY AMAGLEPHET DFVETHGTGT QAGDPIETGA
     LTKVFCPKRS PEQPLRVGSI KTNVGHLEGT SGVAGVIKAV LMLENRTFLH NRNFSSLNPR
     ILLDEWKLKI QLHPEAWEST RPRRVSVNSF GYGGSNAHVI VEDAEGYLLL HGLQALVGKQ
     PTLYVEKPAE SKSNGTCAHP TQPIRTRLFI LSAFDEYSLT KQLENLESYL LARCKIADDR
     YLNNLAYTLN RRRTTLMCRA AIIGDDAMSI SEALKANLKI RKATKKPVVG FVFTGQGAQW
     CGMGRELLRA YPVFRQSMER IDAHITQIGS SFSVIDEILE NQDASRLNQP LHSQTICTAL
     QIALVDLLGS WDIHPESVTG HSSGEIAAAY AIGALGLEDA MSAAYYRGIA ASRLSQNEEV
     RGAMLAVGMP SDSIQPFLDS LKTGKAVVAC INSPTSVTVS GDVTAIGELE GVLREREIFH
     RRLMVNVAYH SHHMELVGGE YLGLISNITP QAGDQVQQSR NRVVSFFSSV TGGEVQASDL
     GSQYWTRNLL GQVKFVESVR ALCYGTNNTT RRTKRVGGMR KVGVDVLLEV GPHAALSGPI
     RQILKEDSKL DAAGVQCISI LTRKSNSVTT ALEAAGTLAC LGYQVNFEAI NDPLQNIGDP
     QVLIDLPCYV WNHNRSYWAE ARMSKAYRQR KNPRTDLLGV IDRMSCPFEP RWRNHLRVSE
     LPWLRDHKIQ SNIVYPAAGY ISMAIEAVNQ HISDPEPHLN ISGFVLQDVS IQAALVIHEG
     SSIEVMISLK ACQSAMSSAD QLFGFRVYSV SGENRWTEHC HGLIGAHTTS VYPDFEVPPP
     QPSKTTDFSI IDMPDFYERL ATIGLEYGPC FTNLTHAHCV DNICLAEVII PDTAAVMPMS
     FQYPFVVHPC VLDSIFHSIF VHMKNDDDPA IPIHIDELFV SRGVEREPGA KMHVNTEIER
     RTRDGILASI TVSGRDDSLA IRVKGLQCKS LANGSLKNTG KSMDRIGYMV TWKPDPDLLS
     NNELFSFLKE INARPENNCS DRSLLESCAS YFVHKAVEYL DKSGELQAHR RRQLDFMLSR
     AEKNQLDMQF DTINPNLDYV SASGAEGRLL CALGEILPAT MRDQDPAPSP IDPSIWSAYW
     DAVRSDPVYD KVARYLELIS HKNPMISILE VEGTIGEASL SFIERMMGIA GQAPGCSEYT
     LTHPNLSIPE THSQRLSDMS QWLSLKRLDV EQTLETQGFD KYQYDVVLVP YGLYMARSKR
     QALRNLRDLL KPQGQLIIVD PVSQSDGLVN SLIFAGFSAC WSGDQFGTSQ DDWKKAILEA
     GFSDLKDFSN SSEGPLLMVT HPLQVHPRSK PDILIISEED ENGVDVLALQ KHLSSISSTI
     EITNFAHAEP EERLCVLLSG LTSPLMTNLD KRGLEILQQI LLRATGVLWV TRGSTMNAMD
     PNGAITTGFA RTARSESGIE RIVTLDLDGQ NPLSSDRAAD IIYTIVHECI IGGNDRVDME
     YAERDGVLLI PRVVENKTFN ESFASSRESK TISYENFHQT SKPIKAMIPE TADADSFCFE
     EDSSIAHLPT DYVRIQVHAT CVDKQNAQAL KGLGISSTEA SGCGISGVVE KVGQSVHGFL
     PGDRVACFGF ETVASYHQDA ASAFQKLPSN MSVESAAALP VSYCTALYAT QYLARAGSAA
     RILIYGAARA NRQAFAELCQ HIGANAFFLV RSEAEKNFII SEDIIDCDQI VDIRDLTYVP
     SCGRAAKGKD FDVIISCVSP DNGTLRLLWK SIATSGTFIQ LCNHGDSEKR TWTIPRVSSD
     VTFATFDIHQ LWRDKPVLLH KIWSEAMRLF NEGRIPVPKA SAVHRVSDMM EALTKLESDE
     DMDLITLTAQ PGDVVKVVTP KLQGKLFQPD VSYMLVGGLG GIGRATALWM SDNGARTLIF
     VNRSGLTTVA SQGTAKELEE NGTRVIVHAC DISDSTQVEN MLNELAHNAP PIRGVIQAAM
     VLRDIHIEKM TIEDYHAALQ PKHAGTWNLH RYLPSELDWF IMLSSISGII GNATQAAYAA
     GSTFLDAFAA YRNALGQPAV SLDLGAITDA GYLADNRELA SKMAQQGFHG TDTATLMSII
     ETAIRTPFAA GASPQVITGL GHWKAGQSLS NFDAPLFAHF RRQFQERGGG EHAEELSGKL
     RESLREIKSL EEASGIIYTA LSERIASHLS MLVESISPSN AITEYGIDSH MAVELRNWVA
     KNMESTVPIL DILASSTLLD LAGKIASKSN LVNLEE
//
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