ID B2VXS7_PYRTR Unreviewed; 2106 AA.
AC B2VXS7;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Conidial yellow pigment biosynthesis polyketide synthase {ECO:0000313|EMBL:EDU45846.1};
GN ORFNames=PTRG_03323 {ECO:0000313|EMBL:EDU45846.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU45846.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231616; EDU45846.1; -; Genomic_DNA.
DR RefSeq; XP_001933656.1; XM_001933621.1.
DR STRING; 426418.B2VXS7; -.
DR EnsemblFungi; EDU45846; EDU45846; PTRG_03323.
DR GeneID; 6341553; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR InParanoid; B2VXS7; -.
DR OMA; YCRGDGC; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000001471; 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; -; 2.
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; 3.
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; 2.
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; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 370..802
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1609..1683
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1732..1806
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1684..1732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2106 AA; 227064 MW; 866AFF10CE0E77AD CRC64;
MNVLIFGDQT ADQYALLRKA CTWKNNSTLT TFLDRISVVV REEVQKLPKT QRDQIPNFLT
TWDLIEAYYA KGTKVPQLES CMVTIAQLAH YIGYYAENPS EMPNASNTRI VGLCTGLLAG
SVVASARSLS ELLPLATEAV RIAFRTGTCV GAAKEALEQA SSTKETWSTI VTNISESSAK
DAIDEFHQEQ RTPTLAHAYI SAVSTMALTI SGPPATMKLL LQRAAFAESA RVPIPVYAPY
HAAHLYSQAD IDRILDKDAI RHLQQFRPLS LVHSASSGKC QTATNTLDLI RTALSEILIE
PVRWDSLLSE IVSQVTSASS AESSVSAIGV TSITNSLASA LKNGGQSSVT VRDHTAWVAA
EHNSRGHTQN DKIAIVGMSG RFPGAASPEA LWDLLEKGLD VHREVPADRF DAQAHCDPSG
KGKNKSHTPF GCFIDEPGLF DPRFFNMSPR EAAQTDPMGR LALTTAYEAL EMSGYVPNRT
PSTKLERIGT FYGQTSDDWR EINAAENIDT YFITGGVRAF APGRINYYFK FSGPSYSVDT
ACSSSLAAIQ LACTSLWAGD CDTACAGGLN VLTNPDIFSG LSKGQFLSKT GSCKTYDNDA
DGYCRGDGCG SVVLKRYEDA IADKDNILGC ILGAATNHSA EAVSITHPHA GAQEYLYNKV
LSNAGVDAHD ISYVEMHGTG TQAGDGIEMT SVTNAFAPRH RQRRPEQTLH LGAIKANIGH
GEAASGINSL VKVLMMMKNN AIPANVGIKG VMNKSFPKDL LQRNVHISTT QVPWPRNGAE
KRKIFLNNFS AAGGNTAVIL EDGPLPEAPK GIDPRTMHTI TVSARSIASL KKNINNLMQF
LDENPKTTLP SFAYTTTARR IQHNYRVAFA VSDMSKVKDG LQAQLKDTYS PLPMVPTKTA
FTFTGQGSQY TGLGQKLYED LETFKNDIDQ LDNLARLHSL PSILPLLTGT DVATLSPVVV
QLGMACIQVA LARMWASWGI RPVAVIGHSL GEAALGDKMT EIACMNGPEE TVLCGTVEVV
ESTNSALTAQ GFKATKLNVP FAFHSAQVEP ILEKFKTAAS SVVFNKPTVP VMSPLTGEII
REAGIINAEY LARHARETVN FHAALTTGQD EKAFDAKTAW LEVGAHPVCS GMVKSSLGGS
PVAAGSLRRN EDPWKTLSNT LVTMYLAGVY IDFNEYHKLF NDAHEMYTLP TYAFDSKKYW
LDYHNNWTLT KGEVLEAPTA KAIEAAPAQE APSKLSTTSC HKIVREELQA NSGTVVVQSD
LSDPQLKATI TGHQVNGTPL TPSSLYADQA MTIANYLYEQ LRPGMTTPGL NVCSMEVTKT
LIPQYPPPAS GQHLQIEGNA DLETDQVKIT FRTVTADGSK VLAEHAVGIV KYEDVNAWKE
EWGRIQYMVQ SQIDMLQMKL QTGAAHKVLR GMAYKLFKAL VTYADNYRGM EEVILDGKTT
EATASVQFQT TAADGNFLCS PYWIDSLAHL SGFIVNASDH LDSENSVYIS HGWGSIKIAG
KLSPEKKYRS YVRMQPAPGN ISVGDVYIMD GAEIIGMVMG LKFQNIPRRA LNIMMPPAGK
AAAAPASKAV AAKPAPKAIA AAPLKAAPAK AATKPVAKAA KAVKIAAPAG VTAKVMKIVA
EEIDVDMSEL VDEAAFENLG VDSLLSLTIS ARFREDLDMD IPSTLFTDCP TVGELKKHFA
QYDGAAPVED DSSDVSEEPT PFETPVESDS TPASSTGSDA DEEEVKPSAP VAGGASLARK
LVAEEMGVDV SEITDDLDLT DIGMDSLMSL TILGSMREAT GIDLPADFLT VNVTIKDIET
ALDMRPKPPQ QKKASKPASK VSAQSPQLAE VSRKLASLPD VSSLPPATSV LLQGNPKVAS
KKFFLVPDGS GSATSYISIP NISPDMAVYG LNCPFMKCPD KWTCGVEGVS RLYLQEIKRR
QPQGPYIVGG WSAGGVMAYE VAQQLVNAGD KVENLVLIDA PCPVALDPLP ARLHIFFDQI
GLLGTGKPGG TPSWLLPHFA SAIQNLKDYD PTPMDPKIAP PVLAIWCTDG VCPNEDDPRP
PPGEGEDPAP MKWLLNNRTD FSDNGWAQLL PKEKFQYAVM GGNHFTMMKG DHGVTLGKLI
QQGLKL
//
