ID E9DHA4_COCPS Unreviewed; 2679 AA.
AC E9DHA4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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_09203 {ECO:0000313|EMBL:EFW14129.1};
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.
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DR EMBL; GL636508; EFW14129.1; -; Genomic_DNA.
DR STRING; 443226.E9DHA4; -.
DR VEuPathDB; FungiDB:CPSG_09203; -.
DR VEuPathDB; FungiDB:D8B26_002495; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; KMRGGEF; -.
DR Proteomes; UP000002497; 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: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: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; cd02440; AdoMet_MTases; 1.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 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; IPR013154; ADH-like_N.
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; 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; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
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 10..434
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2586..2664
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 475..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2679 AA; 294292 MW; 4C2481C8C73F1535 CRC64;
MDTSNFNHDT TPLAVIGFAT RFAQEATSAD RFWELLLRRR QAATPFPKER FNSSAFYHPD
PEHGGTFYVK GAHFLSEDPL GFDAPFFNVN KTEILSLDPQ QRVAMENVYH ALENAGIPME
KAVGSKTSVY ASGFNRDHMI LMDADFEIAM KHKPTGGQQS IISNRVSWFY DFSGPSITID
TACSSGIVAV HLAAQSLKSG DAEMAVVTGG SIISHVPDII AMSHSGFLGP EGKCFSFDHR
AEGYGRGEGV GTVVMKTLAN ALRDGDTIRA VIRATGVNQD GRTPGITLPS STAQTNLIKE
VYRKASLDRN TTMFVEAHGT GTAAGDPIEA RGIADGFTSM ERESPLYIGA LKSNIGHLEG
GAGIAGIIKS VMVLESGIIP PNANFEKANP QIPTKEWQID FPTECIPWPK SGLRRVSVNS
FGFGGTNAHC VLDDAYHFLE ENGLSGNHNT RQSAPTKQEI SELLARLQRL YLDGDVNHSN
GTAELTNGEA AKESHEPVES TAPNETNGAS EQANGETAKE SREAECSTSN GVDLTTDKDV
NEPQEVIESA PIQETNGPIE QGHEEITNGS SEAAELSPNN NGTNGIAEHP NGETGVASPT
PSGINGATTQ SEVPRLLILS TADKEGMSRV ATSLREYLAS KPDLPMYAAE SLLDDLAYTL
SEKRSRLRWK SYLLANSISA LEENLADEKA LSKCFNARSS PRLGFVFTGQ GAQYHRMGQQ
LLVYPVFRKS LEEATEYMKA LGSSWSLMDE ILKDKGDSRI STPSFSHPAC ASIQVALVEL
LASWNIIPSR VVGHSSGEIA AAYCAGKLSR EAAWKTAYYR GFVSAKQNDP KGAMLAVGLD
QEALRPYLEK IHADYDGELI IACYNSPKNN TVAGDETMVD VLKTLLDADG IFARKLNVQN
AYHSAHMKAV ADEYFELMGT LEPGRSSDLD IQMHSTVTGK VIMDSVLDAS YWVDNMVSPV
KFTTGLRSML FQSNDDNSEN KAVVDEIIEI GPHGAMQSAV KEIIAASSSD IPVSYSSVLN
RNEPTVSTLL NTIGTLACKT FPVNLQEVNQ SVHRGEKRPQ FLVNLPPYAF NHEEKGYYES
RLAKNVRQRE FPRHQLLGAP VQDWTRFNRK WRQFFRLSEN PWLRDHVVTD NCIFPGAGYL
VMALEAVKQT AGEAVEVTGI RFKDVSIKAA LLIPDTNTGV EVSLSVLPVN ESNQWTSTVW
KYFQVSSYIP SYNDWVEHCS GYVALEYEAS APDVVGNGRE GKAAKQAWDD ALDQAAEVCQ
TPLDAGKVYE NLETIGMKYG PLFRNLSNLS VSGKRKGTIF GEMKVPNLGS VMPKGYIHPH
VIHPTTLDNT LVAGLVAICD DIGQTVLKHP MVPTFIKEAW ISTGISSQEG TKFRCYGEVS
TAAYESYDYS SKCWDLEANE PRIMLSGVRM TPLASDNTSE SNIQIGYGID WKPAINILET
KEFLDLDPVM AKTPYEKQLS AAVNLQLGTA LMIADGLADL KENPPAKPLE GHMKIYFDWM
ERVIAELESG TLQHVPLELF KKYSEDKGLK EQLYESLKRD YATDGEILIR SGVQIAPVVR
EEVDPLYLLF GQDDLLARHY EEVIVLNDGL RTVQNYLSMV SDNFNGLEIL EVGSGTGSFT
KLMLKSLCPR SEDGQNGHGA GKIANYTFTD ISPSFFSKAK ERLEPWKDLL IFHKLDIGTD
PLAQGFSAAK YDIIVANNVL HATPDLQKTL EHCRLMLKPG GKFLIQEGVR PDIHWVSLVF
GQLPGWWLSK EPVRKWCPYI TVPEWNSFLQ DAGFSGLDID IPSSHFPELA HVSTMVATAV
EDTSKSGVKD KEVVILCHVS ENETDLIAEL KAEIANDLGA TNCLVLQPCD LVEKGMSDAI
CISLLELQTP VIFDLSEEEF KRVQCFLSSC RKLLWITGDS RVEPAFNMIN GMLRTIRWER
DAESLDFTTL AIADFGSTPN KQLVHAISKV FRFHFVSGQT DHANSEYLMR NKLVYTNRIV
DYPTATNFLA SQSSTPAPEM TAWKDVRRPV KLQNPAPGLL NKLQWVTDTS LSQSLEENEV
EIEIRAVGLN FVDLLTVMGE LPWDVVGREA AGVVTKVGSA VHWLQPGDRV VYLVDTPKKG
TFQTYSRVDQ GVVARIPNDM SFEVAAGLPV IYATVIYGLE NVGRLAEGEK VLIHSAAGGV
GQAAIQYAQA VGAEIFATVS TVEKKELIMK EYGIAEDHIF SSRDFSFVKG VKRLTGNTGV
DVVLNSLSRE ALRRSWECVA PFGRFIEIGK KDLVAGGKLD MSPFVHNIMF AGVDLLALAE
HRPKVVQQVL KRTMQLWTER KITGARPNTA LSYAQLEEGL RMLQSGKHTV FLSRSGNITR
PVEEMVSALE GKGCQVKIFK CDVSNVERMR SVVEECQQTL PPIKGCIQGS MILRDGAFEN
LSYLDWNTVT KPKVQGSLNL YEALPKDLDF FLMLSSVGGI MGGRSQANYA AGNTYQDALA
RSLVSKGVRA ASLDLGSVLS VGFVAENKDY TRHVSRTIGS MREDEVHSMV EYLIDPRHSL
TESTCQVIFG LGTVKSFQDR GVPPPECFNY PAYTILRNTT TSGDQAGGDT QMYHVQALLA
TAKSRDEAAE VVSNGINRKL SVLLNVAGDQ IDSSRSIRDN GVDSLIAMEF RTWLAKELGA
ELPLIEIMAE GSITDLSKKV AALSKYVQDN FREASKQSS
//
