ID B2B664_PODAN Unreviewed; 2119 AA.
AC B2B664;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 2 {ECO:0000313|EMBL:CAP73289.1};
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:CDP25691.1};
GN ORFNames=PODANS_2_6850 {ECO:0000313|EMBL:CAP73289.1};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP73289.1};
RN [1] {ECO:0000313|EMBL:CAP73289.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC {ECO:0000313|EMBL:CAP73289.1};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|EMBL:CAP73289.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP73289.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
RN [4] {ECO:0000313|EMBL:CDP25691.1}
RP NUCLEOTIDE SEQUENCE.
RA Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CU640366; CAP73289.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP25691.1; -; Genomic_DNA.
DR RefSeq; XP_001911464.1; XM_001911429.1.
DR STRING; 515849.B2B664; -.
DR GeneID; 6195588; -.
DR KEGG; pan:PODANSg8506; -.
DR VEuPathDB; FungiDB:PODANS_2_6850; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_0_1; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000001197; Chromosome 2.
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; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; IPR049552; PKS_DH_N.
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; PF21089; PKS_DH_N; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 360..790
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1628..1702
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1744..1821
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1587..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2119 AA; 228860 MW; 207964934238C449 CRC64;
MTANTLLLFG DQTGEVLPSI QSLSRNASSN QTLATFLRKA TDRLRSAVLQ APAHYRRSFP
NFTSLSELAA AVSKQDHPSP ALYAALLCIA QIGDVIIYLE NNPGLLDASK DRLAIVGLCT
GLLPAAVVSC SRNLTEVIAL ADETVHLAFQ VGLAASKRSH EVDPSTGSWA TLVSQVDISA
AREAIGIFNR NSIPRHQVYI SAESPNSVTI SGPPSATEAF FSSTSIFGKC KRIPLPIAAA
FHADNLQPIQ PTVLLQNMNP SLHSKPVQHP FLLSPHSGLP YQESSFGNVL VEVVGDIFRH
PILFDACTEG LAKILSSQPN LLAFGPVSCE KAIQQALHGH GIKLETPSTA TTLNNTSSIP
NAIAIIGMSV RLPGSESLED FWQVLEDGRN LHEKIRPDRF DINTHVDPSG KAKNTSLTPY
GVFIDRPGYF DTRLFNMSPR EAAQTDPQQR LLLLTTYEAL EMAGYTPNAT PSTNTKRIGS
FMGQTGDDYR EVNASQNVDT YFITGNIRAF GPGRLNYHFG WEGPSYSVDT ACSSSAASIQ
LACSALLSSE VDMAVGGGAN LLTASDLFAG LSRGSFLSKT GGCKTFDHDA DGYVRADAVG
VIVLKRLDDA LADRDNILAV LRATATNHSA EASSITHPHA ETQERLFDSV LSKAGIDPIE
IDYAELHGTG TQAGDATESR SVTNVLSRNR PADKPLFIGT VKPNLGHGEA ASGVTSLIKA
ILMLSKNMIP PHIGIKGRIN EKLPPLADMN TRISFGKTPF RPRPGGDGKR KILINNFDAA
GGNTSMVIED PPMLPTEGVD PRNHHAITVS GKTPNSIMGN SKRLLEHLDQ NPDARLEDIA
YTTTARRMHH NLRKAHVASS IKTLRDSLQQ AITRETWTKV PAAPPQVVFL FTGQGSAYSG
MASNLFNTSA PFRELLQGND DICVSHGFRS FLPLVEDKNF DMTMASPVQV QLAIVSIELA
MAEYWKSLGV MPAAVVGHSL GEYPALCVAG VLSLSDCLYL VGKRAGLMVS NCSPGTHSML
AVQADQGDTE ALLKSVDDDS GIEIACRNGP TSIVVSGGSD QIRELQEKAL TRGLKTTVLE
VQYAFHSSQM DAILEDFSSV ANRVNFAAPA IPVASTVLGS IVEGAGIISA EYLLRGTRGP
VQFMDAVEAV KSLQNSPNQQ TVWIEIGPSP VCVGMVRSMA MEGAADQLLP SMKKGEDDWK
MLTTSVAKAF AAGLNIDWRE FHRPYELSLR LTALPHYAFD LKNYWIQYEG DWALRKGDAD
GLPRSPAAQD RLTKLPSTTL HRIESEVRDK AGISVIFASD ASEPKLNTAL CGHLVNGAGL
CPSSIYADMA FTAASYILGD AGLNMSLDVR DMQVDKPLVI QPGDTKQIIR VFATKKIGSD
QIEVTFASQD GSRNEHHATC SVVCGRGECW QHDWSKTAYL IKARIESLKE SSNKGQTHRI
LRSMVYKLFA ALVDYDTRYQ GLQEVFMDSN LFEAAANVKF NTSDSDGTFN HSPYWIDGFS
HLSGFVLNGG ERTPADAVYI SHGWDSMKIV GQLSAGKEYQ SYVRMQDTST RGVMEGDVYL
FEGDVVVAVC QGLRFQRIQR SIFDHLLPPP NKPSTPSQPM PSLGAKRQSL NSHIPTIKVE
LVDDDIVSSD FDQVLQLVAS EVGVDVEDLA DHTVFADLGV DSLLSITITA KLGQLWGKAI
PAGLFTEILT VAELRRYHLE NIDNSEDDDR ASSYGGSTCG NDIFSQPQSQ AYTPFTNTGL
SIGTPVEDRA GAIRKIIAAE LGMSIEEIDN DVPLADLGVD SLLSLSIMAA IKAQTGQIFP
SSFLMEYPSL AAIEAALGPR RTLPAQQLFK ALEKVQNNKS IPQSEAVLLQ GSSSSREPAL
FLLPDGSGSA SSYVGLPNLK LSGPVWGLDS PFLNNPEAFT IPLEELASSF AAEIRNKQAH
GPYRLAGWSI GGTYAYEVAL QLLSHGEVVE SLTLIDAPCP ASLPPLPIET ISLLDKVGAF
DGFKNKKKAG KTYMRETDHA HFAGSVKALE RYKPAAMQNI STPLIKSVTV VWARDGVWDT
VGPEVKARHI KALGQKNAAR DWMLDTKSDF GPNGWEMLLP GAEIQCKVVE GDHFTIMRDS
GVLKLGEVLQ GTIVGPARS
//
