GenomeNet

Database: UniProt
Entry: A1CD09_ASPCL
LinkDB: A1CD09_ASPCL
Original site: A1CD09_ASPCL 
ID   A1CD09_ASPCL            Unreviewed;      2421 AA.
AC   A1CD09;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   SubName: Full=Polyketide synthase, putative {ECO:0000313|EMBL:EAW12416.1};
GN   ORFNames=ACLA_063870 {ECO:0000313|EMBL:EAW12416.1};
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:EAW12416.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW12416.1, 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).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS027050; EAW12416.1; -; Genomic_DNA.
DR   RefSeq; XP_001273842.1; XM_001273841.1.
DR   STRING; 344612.A1CD09; -.
DR   EnsemblFungi; EAW12416; EAW12416; ACLA_063870.
DR   GeneID; 4705895; -.
DR   KEGG; act:ACLA_063870; -.
DR   VEuPathDB; FungiDB:ACLA_063870; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   OMA; STIHCER; -.
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:0032259; P:methylation; IEA:UniProtKB-KW.
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; -; 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; 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; 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; 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; 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          5..429
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2339..2416
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2421 AA;  265871 MW;  4A0ADE9ACEDA9CD5 CRC64;
     MEQQTMPLAI IGMACQFAGD VSSPEKLWQL CADGNSAWKA IPESRFAQKE LYHPDNQKQG
     TTNVEGGHFL EEDVSLFDAA FFNFSSEVAN TMDPQFRLQL ETVYEALENA GIPLDQIAGY
     RTSVYAGAFF RDYHDSLMRD PATLTRFFMT GNGSAMASNR ISHFYDLRGP SMTVDTGCST
     TLTTLHLACQ SLRNGESDVS IVAGSNILLN PDMFESMSSL GFLSPSGKSY AFDHRASGYG
     RGEGVATLIV KPLTSALRDG DPIRAVIRET ALNQDGWTPT ITSPSQKAQE ELIRLFYQRA
     GLDPLETSYV EAHGTGTPAG DPVEAAALSA ALNTNRSSQE PLLIGSVKSN IGHTETASGL
     ASIIKVTMAL EKGYIPPSAN FEKPNKDIDM NGLNIEIPTL LRPWPQALRR ASVNNFGYGG
     ANSHVIIESP AVLTQPSPAI VSESGSLQSR VFVLSAKEGA AVSRMASRMA EHLRGLTLDD
     ESAYMRHLAF SLGQRRSNFP WKAAYLASTK KELIEKLEQG QVTPQQATEQ PRLGFVFTGQ
     GAQWYAMGRE LIEAYPVFKD ALLEADQCLK SFGAKFSIIE ELSRDEASSK VNTAMLSLPL
     CTAVQIALVK LLRSWNISPI GVTGHSSGEV AAAFTAGAID VRSAMAIVYM RGALTSSFQE
     KIGSGRGGMV AVGLGKEAAE AYVAKLTTGK VVVACINSPE SVTVSGDITA IEELESQLVG
     DGIFARKLKV EAAYHSHHMQ PFADEYSAAL QQILRDGKLD DDIIYSSPVS GTRTNGDEVS
     RAEHWVQNML QPVLFLDSLT NLCLSSDLNQ QVDTILEVGP HSALAGPVRQ TMGLPAFEGK
     RISYLSCLSR GENAVETMQS LAATLRSQGT RVDLSAVNFP INQEGLRVLH DLPSYPWNHA
     HGYWAEPRLN KEHRLRRQKH HDLLGSPLIG GNALSPTWRH IIRLSDTPWL RAHKVQSNII
     YPGTGYICMA IEAVHQLSQG QSHAMSSVSL KDVEILKILI VPETEAGVEV HLTLHESSDK
     VLTGQLWQEF HIYSCDNSGK WSEHCKGLIA RNQGNEAYQR NASSDDNVYL RQLKPQELYR
     TLQAKGIYHG KAFQNLVSIQ YNPGRSLCTL RVADTASSMP YGVEKPHVLH PTTLDSIFQA
     VYSSLPTSAL KANTAMVPRA FKRMDVRTSM SSTPGHVFQA QSMLHRANPQ GMESSVVVSD
     TTSKDPVLTV DGLYYQSLGI VPEADGEKND KQHHYTLQWA PDISFPTPRT LKAALQFAAD
     FDEIGIIRDI REACFYFIRR ALANLAEDRV MKLNWHQQRL WAWMKVQIKL AQLNELGPIS
     SEWAGMGGCT ELVLDALREQ DALGSRYRCA SYDFTDISSG FFEAASERFK EVGDVMEFKK
     LNIEEDPSEQ GFESNSYDLV IASQVLHATK NINRTLANVR KLLRPGGKLL LVEITRDEID
     LQLIFGTLPG WWLGEEAERQ SSPSLTIPEW QAAMKSTGFD GIDMELHDCE DEDFYAFSVL
     MASAAIPDPA IYPQFTIVYK EMPPPKWLHK LITSLEKLTT FKPDVQQLGA FDAEGKTCLF
     LGEMHEALLD EPGSAEFGFI QSLLIQAAGV LWVSRGSTIH CERPHNTLHT GLLRALRLEH
     SSKRLVSLDI DPTTARWPVS AIATILDIAR RRFLLAQNPS HLDNEYAERG GIMCVPRVFE
     TVDESSKTAR GIESPGTKTE LFHQSSQKLR LQVSTPGLLD TLGFVAEPMQ INPIPEESIE
     VEPKAFGLNF RDVMVAMGQL SMDIMGFECS GVVTQVGSLA SQHGFKIGDR VCALMRGHWE
     NRVCLHWTSV VAIPDGMTFE VAASIPMAFT TSYYALYETA RLQPGESVLI HAAAGGVGQA
     AIILAQRVGA EVFVTAGSPE KREYLSRQFG IPEDHIFSSR DAEFASQLME ITAGKGVDVV
     LNSLAGELLQ RTFNCVAPFG RFVEIGKRDL EQNKQLEMHA FTRHISFSSV DLIALGELKG
     AVVSRIMNDI MRLIKDEGLR LIQPITTYPI SRIHEAFRIL QAGRHIGKVI VIPGPDDRVN
     LLPSGWPLHL DSESTHLVIG GMGGVGRSIC EWLVQRGARN LIIMSRNAEQ QAQGSAYVNA
     LRASGCTVVV ASCDISDKFE LKQTLDGCLQ SMPPLRGVIH SGMVLQDTVY ENMSLEDYAR
     AVRPKVQGTW NLHQVLSDVD LVYFIMLSSL SGITGNVSQA NYSAGNTFQD AIARHRSARG
     LPAVAIDLGM VREVGYVAET DGVANRLERM GFRAVDEEEV LHLIQEAILR PLRHATDSQI
     LTGFNSHLST GDTNAFWAKD PILGGVLRAT GTKSTTRSNR VHDAMDLREQ LTNVPIPNDR
     LVVLETAIVR KLAAMFFVEE AAIQVGESLA RYGVDSLVAV ELRNWLVVQL GIEVSIFDIM
     QGASVKQLAS SLVAKWAAAA A
//
DBGET integrated database retrieval system