ID A0A194V8M3_9PEZI Unreviewed; 2754 AA.
AC A0A194V8M3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Conidial yellow pigment biosynthesis polyketide synthase {ECO:0000313|EMBL:KUI60239.1};
GN ORFNames=VP1G_07453 {ECO:0000313|EMBL:KUI60239.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI60239.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN714746; KUI60239.1; -; Genomic_DNA.
DR STRING; 694573.A0A194V8M3; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000078576; 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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 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; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR013120; Far_NAD-bd.
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; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR45681:SF6; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45681; POLYKETIDE SYNTHASE 44-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18558; HTH_51; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:UP000078576};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 435..868
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1792..1866
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1769..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1871..1931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2754 AA; 300890 MW; 684E4E9495EF1C26 CRC64;
MGSISYGLEE AALLVFGSQL ESLSMASLND IRDTLLDSPS RQWVLDTVLR LTACWDALAT
AAPEITDTIG HDRGKHLLAD LNSWLRQGPT GDQGNDLLRD LDALPSMILS PLVVLTHLAQ
YRRYLSELSK RAGKDEAKTD MHAELVNSKK TATLGFCMGC VSAFAVASAG NQEELDKYGS
VAVRLAVVGG ALIDAQDAWN TEQGLGPSKS YASAWRNASQ REEMQRIVDG MFPEAYISVL
YDEARATVTT SERAASRLLR KLRKGGITTA EVGFHGDIHS PKPETKTKVS EVIAFCNTMP
DLQLPDSANL AMPTFTNAGE GISIGPGAGA MHEITLRTVF VQQCDWYGTF SAVKAARLDS
DEGTEVLAFG PDKCVPPTLI RQLGSRLVHF ADLPLEKELP AQPLIDETKK EHVEESRPEV
EQPQKHKVDL ADIDENAIAV IGMSIKVAGA DDLDEFSQML RTGESQHELI TPDKMAFNES
LFREKDQRQW YANFMRDRDA FDHKFFKRSP RESASMDPQQ RLLLQSAYQA VEQAGYFTEP
TRSGRNDDDN WRDSKRQHVG VYIGTPAVDY EHNVAGHAPN AFTATGNLQS FLAGRVAHWF
GWTGPALTLD TACSSSAVAI HSACRDLLSG QCSAALAGGV ALCTNPTWFQ NLAAASFLSP
TGQCKPFDHK ADGFCRAEGS VVVFLKKLSD AVTDGNPILG CIASSAVYQN QNSTPMFVPN
SPSLSQLFKD VLKEAKIPPG DISLVEAHGT GTPVGDPAEY QSIKEIMGGR EIRSKPLPIG
SVKGHVGHAE GASGAVSLIK VLMMMRENFI PPQASFSKMN PGIKASPSDM LEVVTSLRPW
SDNHNDNKKA LINNYGACGS NAAMVVTQSQ YHNTGISSAT IRNRPEELQK QRFPFNITGL
DVRSIKAYAE KLASFLKSQM QSKSGVTLAD LSFNINRQYN PALNQSLIFS CGSITELHDT
ISRVASADSA APAIIPSRPE RPVIFCFGGQ VSTFVGLDRD LYDSVAVLRQ YLDECDATMQ
SLPLGLGSIY PDIFSRSPCD DPVRLQTMLF AMQYACARTW MDCGISGKIA AVVGHSFGEL
TALCVSGVLS LQDAIRLVAS RAQLVRDNWG PDRGAMMAVE ADESIVRELV TQAGRSGVVV
DIACYNGPRS FTLAGPVEAI DAVGDTIAHD VKFSGIKSKK LNVTNAFHSS LVDPLRDGLE
EIGKDLTFRK PSIPLERATK TRSADGSLTP QFVADHMRNP VFFNHAVQRL AEEYPSAIFL
EAGSSSTITV MASRALATSG GSSNHFQAVN ITNDKGLDNL TDTTVSLWKQ GLRVSFWAHH
ARQTNEYMTL LLPPYQFEKS RHWLEMKSPT EALNKALASL SQGNTQQRGE NERHEVSEKD
LGLWSFIGYR DEDEKNHNRG KKHSNKQLSR RPRFRINTGS EKYNKFFSGH IIAQTAPICP
GTLQVDMAIE ALFSIHPEWK KEGLQPVVHD MVNHNPLCAD PTRIVWLDYE SLNPEQTRWQ
WSISSTSRDS VDRSNDQQMY VAGQLNVRSP TDPAYVAEFS RFERLVSHSM CTALLAAAGR
DDGSEADLEV LRGRNVYRTF GEVVDYAEMY RGVQAVVGRN STNECAGRVT GRHTGETWVD
VLLDDSFSQV AGLWVNCMTD SDPSDMFIAN GIELSMRSPR GIINRPGHAQ SAWHVYGRNT
RQSDTGYLSD AFVFDATTGE LAEAFLGIQY SRMPKMMMSR LLTMLTKDKS VLKSGANVKA
VAPVQKTTTT FGSATVDTPL KDADVIQIGS KSKEKQKKKK TVQKPSSSPR QADITTEVMK
LVALVAGMEA SELTLDTEVA DVGIDSLMGM ELAREVESAF KCSVDQAALL EATNVRQLVG
LISTILSGPD LGDASASSGT TEASSDEDDD FSSDHEDTAS SIGDSDVQTT STYQPDSGTS
SNATKQSAGP VKDLDLSSAD ILDAFGEIKL SSDKRLCDAK TDNFDRIVFP DTSRLCVTLI
VEAFEKLGCS LRSASAGDVL DRVPFQTQYE RLVAWLYRFL EQDARLLKVD PVSGQITRTA
VVVPNKSSEA VLEEFCEMHP DWAVTAKLIH YAGKPLASIL AGETDGVRIL FGSAEGRELM
AAHYRKNPHA AMLGEQMRDT LGLLARKIQA AGAGMLKILE MGAGTGGTTH ILVPYLASLG
IEVEYTFTDL SSSMVAQARR TLGKQYPFMR FAVHDIEKPP AVDLYGQHII IASNAIHATH
NLLQSVANVH QALRSDGFLM MLEQTEDIPL SNLIFGLFEG WWLFDDGRTH AVVQTSDWER
TLHKAGYGHV DWTDGHLPEN TLQRVIIALA SGPPRERLPI PETRPDAPQP LTRNLATREA
ETERYIAKYT ADWTGPSSAG SKAEKKAEEN RHDAVVLVTG ATGSLGSHLV AAIAENPNVA
TVVCINRRST TALVEARQDD AFSKRGISLK PGAHGKLRVL ETDTSRPQLG LARSDYDWLV
QHGTHIVHNA WPMSGTRALP GFEPQFQAMR NLLDLAHDMA LSGGDGARRI GFQLVTSIGV
VGHAGQGRVR EQRVPITAVL PTGYCEGKWI CERMLDETLH KHPAFFRPMV VRPGQIAGST
TSGFWNPVEH FAFLVKSAQS IGVFPDLDGV QQWVPVDKAA AAMAELLHIG NESNAPLPSP
VYHIDNPIGQ PWKDTTPVLA KALGIPPHGV VPYREWLRRV SHSPLAETEN PVGAQPMLFD
FLDRNFERMS CGGLVLDTTQ AQQHSGTMAA LGPVTSDVVE KYVKMWKQIG FLAS
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