ID S3BWR2_OPHP1 Unreviewed; 2270 AA.
AC S3BWR2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:EPE03871.1};
GN ORFNames=F503_01761 {ECO:0000313|EMBL:EPE03871.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE03871.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE03871.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE03871.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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DR EMBL; KE148164; EPE03871.1; -; Genomic_DNA.
DR STRING; 1262450.S3BWR2; -.
DR VEuPathDB; FungiDB:F503_01761; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR OMA; CRMPGNV; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 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 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF13; POLYKETIDE SYNTHASE 1; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 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; 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; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 60..484
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2186..2263
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2270 AA; 244544 MW; 680813AD22DEFD57 CRC64;
MAPIAMTPDT SASPSGESDN GYFDSDNGRY VNERASTNPS RKSSVDSDAQ DDASNAPKKP
MPIAIVGIAC RMPGDVSSPA EFWELLSRSR TGFSEVPAKR FNADTFYHPN AGKGGSFHAK
GGNFLSCDLE SFDAPFFGLT EKEAISMDPQ QRLLLECSFE ALENAGIPKQ NIVGKDVGVF
VGGSFPEYES HLFRDSDTIP MHQATGCAYA MQSNRLSHFF DLRGPSFTSD TACSSSMVAV
HQACQSIRLG ESSMALVGSC HLNMLPEFWV SFSSCRLLSD SGRSIAFDER GTGFGRGEGC
GMVVLKPLDQ ALRDNDPVRA VIVGTGLNQD GKTPGITMPN GDAQEALMRQ VYRQSGLDPK
ECGFVEAHGT GTKVGDPIEA TALHNVLGQG RTARDPLYIG SVKSNIGHLE AASGIAGIIK
AALMLERGFI LPNHDFKIPN PKIPWKEWSI KVPINQRPWP RGKKYISVNN FGFGGTNGHV
VLQAAPFRSK PSFERDMSTA MNKQRKLYPF TANDKATLAA VTKNAVIYLE QRPEIFQADL
MDNIAYTLGQ RRSHLQVRTT ISSQDSFGLI EAINGEKYTS SKELEPLRIG FIFTGQGAQW
WGMGRELFEQ YPVFSSAIEH ADRCLRILGA SWSLAEELSR DADTSLVNEA HISQPACTAV
QLALTDLLAS WNILPEAVAG HSSGEIGAAY AAGIITFESA MAIAYHRGRL IPILKAEHPD
LKGRMMAIGG SKEEFQPIID NLKEKEVRIA CYNSPSSLTI SGDEPALAEL EKICEEKGAF
NRRLMIDTAY HSHHMNLVAK EYQASLQKLK APAETTVRFH SSLHGRLADA SELHASYWVD
NLTCAVRFDE ALQTMLEPVG EHRTGVNMLV ELGPHSGMQG PIKQILKHVG GPAAKIPYAS
ALIRKKDAVE TAMDVAGALF SRGLAIDFEA INFPRAHSAP KPPMLLTDLP RYPWNYSTKY
WQESRTTHKH KNRTAKRSDI LGVEAIYSSD LEPTWRNIVR LDDLPWLRHH RIQSLNVFPL
SAFLVMALEA SAQHAGKKGR TVDSFELRDV SVVKPLIVPD EDIEMTITLR PHQESGSSLL
PASASDANLC QFRISSYTQA KGWTEHCIGL VGTQTTEEKA NDVDGARQTS TAAAAVRYAK
LLVGDASGSA VNSAKMYDTL NELGVSFGPT FQGVENCRAT DNAACADLAV IDVANEMPNY
YLSSPSLHPS FLESLIELYW PILGAARTDA GVRNVYLPAS LERLTVSAKA IALSQQPGNL
LSAYCTAENI TAAVAAEKSA KVTLFATADR ESSESLITLE NLVISPMIEG QGDLDGSANG
ARELCYKLDW EPVLEPVEPV EGAASGFPDA KVVIIHEDSQ SQQAIASGLS TILEKATGVV
PDTGSLETVD VAGKICVFLS ELSRPVLSTL TETEFNTLKS VLTTAEACLW VVRGAYSKSS
NPDANMILGL SRAIRSESAM KFATLDLDAA HVLPEDETAG AVARVFEAAF GATASNTSDL
EFSEKNGSFF TPRIIDDADM NEYVHRQTHP DIIEPTAFGA DGRSLKMTLG RSGALDTVHF
VDDLDLAETD LAIDEIEIEV KAIGVNARDL AAATKGQVNS MGIEASGLVK AVGSAVTQFR
AGDRVAALTP AHGSFATHTR TTATLAFKLP ASISFEAGAA LPLAYITAYH SLIELGRLAE
GDSILIHAAS GAVGQAAICL AQMIGADVYA TVSSADKKAL LTEEYHIPEA NIFYSRDNSF
GRAVRQATGG QGVDVVLNSL SSAQAVRESW ASLNKFGRFV DIAARDTLSS RRLLEMSSAD
ASNASYMSVD IFALASERPK TVRRLVTDVS SLLTYGKIRP AAPITSFPIS DIENALKAVH
STAASRTPGK LVVVPHAYDV VRATVSQNHM TDLLKADATY VLVGGTGGLG RSMARWMSKR
GAKHIVLVSR TGSATGEVKA LIDDLATETG TNVYVRQCDV VDRKSVDNLL EVGLSGLPPV
RGIVHGTMVL RDVLFEKMTF EDYDKVIEGK VRGGWNFHHA LNETQAPLDF FVAISSAAGA
VGNRGQGAYA AANCFLNALV QLRRAAGQPA SSLDLTMVSD SGYLANNADK LAEVARNLGS
DSICEAEVLA LLGAAITGRL DETCEGHTIT GMRITPSMQP FWTQDAKFKH LRVAMEEKAA
AENAANGGTV AVSFNALLKT AQTLPEAEEA VSAGLVDKIS AVLMMEPEDM DVTRSLSHYP
LDSLVAIEIR NFITREFEAN MQVLELLSSG SIQTLAKAVC AKSKLVSFSS
//
