ID E9DK00_COCPS Unreviewed; 2070 AA.
AC E9DK00;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Non-reducing polyketide synthase nscA {ECO:0000256|ARBA:ARBA00018393};
DE AltName: Full=Conidial yellow pigment biosynthesis polyketide synthase nscA {ECO:0000256|ARBA:ARBA00031359};
DE AltName: Full=Neosartoricin B biosynthesis protein A {ECO:0000256|ARBA:ARBA00033379};
GN ORFNames=CPSG_10149 {ECO:0000313|EMBL:EFW13280.1};
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN [1] {ECO:0000313|Proteomes:UP000002497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
RN [2] {ECO:0000313|Proteomes:UP000002497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005179}.
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DR EMBL; GL636526; EFW13280.1; -; Genomic_DNA.
DR STRING; 443226.E9DK00; -.
DR VEuPathDB; FungiDB:CPSG_10149; -.
DR VEuPathDB; FungiDB:D8B26_004007; -.
DR VEuPathDB; FungiDB:D8B26_004008; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_3_1; -.
DR OMA; CASDYND; -.
DR Proteomes; UP000002497; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 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; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
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; 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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
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; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
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:UP000002497};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..421
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1289..1363
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1398..1474
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1476..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2070 AA; 228344 MW; 71D5DDB246CB405C CRC64;
MDEDYPENAI AVIGMACKFP GAESLEEFWD LLLAGKSMCQ GAPSERFATK NNRRHQDKSI
YNGNFISSIE SFDHKFFRKS GREASSMDPQ QRLLLEVAYQ ALESAGYFGE TDPNTDVGCY
VGVCASDYND NVANHPPNAF STLGTLRAFL TGKISHFFGW SGPSVTFDTA CSSSAVAIDA
ACKAILQGGC HMALAGGVSI FTSPYFFQNL SAASFLSPTG ATKSFDADAD GYCRGEGVGL
VMLKKLSHAV ANNDNILGVI MSSAVKQSSN LVPITVPYSP SQTALYRKVL ALANVSPEQV
TYLEAHGTGT RIGDPQEFQG IKEVFGGPKR QENLYFASVK GNIGHTEGAS GVAGLIKTVL
MIQKRKIVRQ ASFQQLNPKI ILEGEKLAVP TDTLTWKAET LIGCVNNYGA AGSIAAMVIK
EPPAPSTELG HAKPLSRYPI FLSANSPKAL SEYAAKLRAF MTRLPPSSSN TLADLACNLS
DKQNRSLPYS LEVTVPSMTE LDDQLRVVAS GSSTPSSSEA PSKPKHVILV FGGQTNRLIG
LNKMVLESSP ILRSYLDQCD EKLQAFGMQS IYPGIFETEP RDDIVMLQTM QFALQYAVAK
TWIDSGLHID CVLGHSFGQL VALTISGVLS LEDGLKLVHG RALLMAQKWG PERGSMIALD
ADIETTARLI AAAHTLDQNY RLEIACYNGP RSHVVVGSEA AVQGLVGLLN QSAAVKYKQL
NVTHGFHSEF TEPILKDLDQ LAKTLTFNQP KIPIETCSEG QSWGFVTPAL VTEHTRIPVY
FEEAVDRLIR RYGPCTWVEA GSNSSIVSMA RRAIRGTASK HSFFPINLSR EDAMGSLADT
TVNLWKNGHH VQFWPFNRLK RRHYTQINLP PYQFEKVKHW LDWVEVEPAS TSGAGKNIQE
QSEKEEPGPA KLLSFSGFGD RERRQAVFCI DPRCEEWQRL VQGHAVLQNP LCPAPLYVEL
VSRAIMLHLH DPSAITLSSA GLCLRSLDVV APLGIGHDIY VKLLLTQLGA NNDRWSFAFY
TMPRPFRSEE ADLPLHATGE VTISSKAEVR SEFERTARLL PYQHLESLIA QTDGEGMTGS
LIYRVFDRVV QYDTYYKGVS RIASKAGEVV AQVILQNPEL PWGKEQVSNP LALDNFLQVA
GLHVNSLNVC GESNVFVCTK VDRIQFSPEM QLSNGNGSWS VYSNMHMLND KEVENDIYVF
DAIRRHLVMV ILGARFNRVL ITSLGKVLAR ANATGAGVDL IAKGFPAASH IPATDPRISK
ESDFGMPVPP IQLDQSSTIP RPIEERVKPD LEKELRQLLN KITDVPESEF KDEATLEDLG
IDSLMATEIV TEVGAVFKVD IPQSDVQDLI TFRALRDYVL QRVAPGHKVL TQTMTATLTE
AVLPREKKDN APKASFAGPN EQVSRRIAQL VASHLECSAD FLRSTNLADQ GLDSLLCMEL
ATDIERLYGI KIDVTQLTTE STFGDLCDMI IGSGSSSGSS TADDFAASTP AAELTTDTED
ENVPVPGPQA AAKLLEVQHA FENIRYDFEM YAKETGFLGF WKNVFPAQSR LVLAYVVEAF
RDLGCPLDVL QPGQIVPDLL VLPRHQRLRC VFYEVLRDGQ LVDFTGTDYI RSEKPIDHTP
SHEIYSQIVR DHPQHAKEHE LLNICGSIMA SLVNGQKDPL QLLFGTKRNK DLLEDVYRNG
PMYLAVTRLL GSFLEKSLRN RGEGKIHVLE VGAGTGATTR WVVDVLSRAG VDFTYTFSDI
SPSLVAAAKR KFSTYGNMNF MVLDIEKAPP EELTGRFHII LSTNCIHATS SLPRSLTRIC
EMLRPGGFVS LVEFTKNMFW FDMVFGLLEG WWLFEDGREH VLADEAFWER SMKHAGFKHV
AMTDGSSLEA NTVRIITGFT EHAVSSNTQS WVEKKNEATD SETLVFGVTD DKTLLRADIH
YPVSESKCSH PWPVALLIHG GGHTMLSRKD VHPKQVQYLL KHRILPVSVD YRLCPETTLV
DGPMRDVQDA FIWVKTKLPS LKLRSSSYLS IDSDRVAVVG WSTGGTLALS LSWTIESSQQ
IRPPDAILSF YCPTDYEDPC KFPGLPRLIC
//
