ID A0A1C1CHV5_9EURO Unreviewed; 2150 AA.
AC A0A1C1CHV5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Conidial yellow pigment biosynthesis polyketide synthase {ECO:0000313|EMBL:OCT48088.1};
GN Name=wA {ECO:0000313|EMBL:OCT48088.1};
GN ORFNames=CLCR_03792 {ECO:0000313|EMBL:OCT48088.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT48088.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCT48088.1}.
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DR EMBL; LGRB01000012; OCT48088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CHV5; -.
DR STRING; 86049.A0A1C1CHV5; -.
DR VEuPathDB; FungiDB:CLCR_03792; -.
DR VEuPathDB; FungiDB:G647_08240; -.
DR eggNOG; KOG1202; Eukaryota.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
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; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
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; 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; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 375..807
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1634..1708
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1753..1830
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1599..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1711..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2150 AA; 233274 MW; 8E20153358FD843C CRC64;
MGRDIKVLVF GDQSEKRLDD LRQLVTVSDN PLLTTFFDKA YITLREEVNH LPFLTKGLPG
FTSIETLLWR YGEAGVRHPA IESALVCIHQ IATLLRHFGD GSEVYPKPAD TRLVASCTGL
LSAAAVSCAR TYRELVSIAV EALKLAFRVG AQVAQVCDEI EQTSLPLCWA AIFPGVGKED
AFLALEEYAE KTGIPPTSRP YVSATSLNSV TISAPPGDLE NLIEAKIFNT SRPIRLPIFG
PYHAPHFYND EIVASLAASI EDSITGEWEA RIPIINNGKH NAYESSNFRQ LVEEVLEDIL
LKPLHWERLC DNCVASVASA EPEQCRVVPI GAKNASASLV NALNQKASFK IMVDNRKTEA
TDEPKEPDPI GSRGKPKIAI VGMAGRFPDA MSPSLFWDLL KKGLDVHREV PPDRFDAQAH
YDPAGKRKNT SHTPYGCFIE HPGLFDSRFF NMSPKEAAQT DPMHRLALLT AYEALEMSGF
VPNRTPSTKV DRVGTFYGQT SDDWREIQDG QNIQTYFIPG GVRAFAPGRI NYHFGFSGPS
FSVDTACSSS LAAINIACNS LWLGDCDTAL AGGLNVLTNP DIFSGLSRGQ FLSKTGNCKT
FDDGADGYCR GDGAGTVILK RLEDAEADND PILAVILGTG TNHSADAVSI THPHAGAQEY
LFKKVLTESS LDPHDVSYVE MHGTGTQAGD AIEMESVLNA FAPASRQRSP DHPLYLGSVK
ANVGHGEAAS GITALVKILL MLENNLIPPH CGIKGEINHN FPDLGARNVH ISLGRETAWR
RPEGGKRRFF LNNFSAAGGN TSLLMEDGAQ HPLEGDDPRS TAVVAVAGKT KKSLVENTKN
LIGYISENKN VDLPSLSYTT TARREHYSYR TIVTGSDLAT IESALRKALD SEPAAVPSGI
QVVFAFTGQG SHYTGMGRQL YETNSQFRAD IRRFDLLARN QGLPAILPLV DGSTEIEKLG
PVVVQTGAVC VQIALVRLWQ SWGIKPAAVI GHSLGEYAAL QAAGVLSIND AIFLTGTRAK
SLEAHCTQNT HAMLSVVASV EEIEGFIDSK TLEIACINGP KATVISGESS NIDKLKEQVS
AKGMKSTKLA VPFAFHSAQV EPALDDFESA AAGVTYNAPK IPLIAPLLST VVTEKGTINA
EYLRRHCREP VNFLGALQAA KEKGIVKDKS QFVEIGGHSI CSGMVKSVLG STTVALPSLK
RDEDVYKTLT GTLCALHMAG LKINWNNYHE SFPRCHHCLK LPTYAWDASN YWIEYENNWT
LTKTNVAADD QDSQTKKLST STVQRIVTEK FQGQTGTLTT ETDISKPELE ETIKGHLVNG
SALTSSAVYA DMALTIGDYV HRKLQPEIEG FALNCANMVV EKPLIFKGGE QLLRVDCEAD
LTQAICYMTF YSVGPKGQKL LEHAHCEVRY GDSNSWSKEL ARQKYLVQSQ VDRLLQMGQN
GVLSRLQRKM AYKLFSALVD YQNAYKGMAE VILDSPLREG TARIELQTGR AGNFYMPPYH
IDSLCHLAGF IMNANDELDS AQTVYVNHGW DSLRFFEKPS PSKIYRSYVR MQPTGPDSKD
YSGDVFVFDA EGNIVGQIGG LTFQFLPKQV LDRVLPPAGG KATAAPAPAK KAASEPKKTA
PKATAKPKVA PAGPTIMNKA LNIMAEEIGV SVDELTDDTD LGALGVDSLM SLTISGKFRE
GLDIEIPSTL LADSETFKQV RDFLTQFESK DGGDATPSSP SAGSSDDSGS STPAAADTES
MTSASQPDEK PGGEAGGKLE AIRAAIAEET GMDPSEVTSD MDLEAMGIDS LMSLQILGIL
REDKDIDLPP SFFSDHATFG DIEKAMGGEG TQASKPKLPA KSEEMSTEQV VAEMQTNKGQ
QSAEPPKEQQ AAPAPSAQKK TYKASSVLLQ GNPKTATKTV FMFPDGSGCA ISYATIPPIS
PKDVALVALN CPYMKDPEAF EGGIPGVTAL YLEEIRRRQP QGPYILGGWS AGGICAYEAC
LQLSAMGESV EKLIYLDVPC PLPPQALPPR LHHFFDSIGL LGQEGEAPDW LIPHFTATIK
ALSSYRPRVM DPAKESIPTV YTVYAQDGVC KHDDDPRPEL TSEDPPHMKW LLFNREDFGP
LGWENLFSGS DHIVGLESIP NVNHFTMMRE PMVSEIPSRI RKALGVNGDE
//
