ID A0A0G2HEF3_9PEZI Unreviewed; 2256 AA.
AC A0A0G2HEF3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative polyketide synthase {ECO:0000313|EMBL:KKY33503.1};
GN ORFNames=UCDDA912_g06544 {ECO:0000313|EMBL:KKY33503.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY33503.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY33503.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY33503.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY33503.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY33503.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-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:KKY33503.1}.
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DR EMBL; LCUC01000243; KKY33503.1; -; Genomic_DNA.
DR STRING; 1214573.A0A0G2HEF3; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000034680; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase 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: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; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
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; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF49; SYNTHASE, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 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; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000034680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..362
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2145..2224
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1546..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2256 AA; 246787 MW; B980C4D4FB87A384 CRC64;
MFRSQCASEG RSQIPSDRFS VDGYYSEHQP KQGTVNFKHG YFLEEGLQHF DAGFFSMSRR
EVERLDPQQR LLLEVVHECM ESAGESDKLA SGLYTITGQG DFLLANRVSF EYDLKGPSLT
VKTACSSAAI AFHLACTALA RGECEGVIVG GTSVFTAPGA SVAMTEQGLV SPEGRSKPFD
ASADGYARAE AVNSVYLRRL DDALRDGTPV RAVVRGSALN SDGKSASLAS PSAEAHELLI
RKAYEAAGLE QADAPYVECH GTGTKVGDPL ETAAIASVFG NKGTYLGSIK ANIGHSEGAS
FITSLIKAVL SLENKTIPPN LHFSTPNPKR QGAQWPQMGQ ELFAAYPTFA ARITDLDTVL
EKIQPQGSTW SIRERILAGP SESRVDEAEF SQPLCTAIQI GLVDVLKEFG VVPDSVVGHS
SGEIAAAYAA GAITAESAIK IAYYRGRISK FARKDGAMLA VGLGPQAIEP FLVDGAVVAC
ENSSASVTVS GDEVAVDEVA SKVRAHNPDV LVRRLRVQQA YHSHHMVECG EIYLENLSAT
VNEPANTRVP FFSSTYGTQL ADKLKLDNQY WRLNLQSPVR FDTAVRSLLK DMSQTDDGKS
RIMLEIGPHS ALAGPLRQIF RDTNRKLLYT SALVRHRNAQ ESLLESIGQL WVHSVQVNLS
ALFPTGGKVL TDLPTYPWYH EQSFWEENRI AKQWRFRKEL PHEILGSPVL EWNDMEPTWR
NILSVEDIPW LGDHKIGKDV VFPAAGYIAM VGEALRQLGG GPAYSLRDVV VGNALVISAR
VEVMTVLHKA QLTTSQRSDW YDFSISSYNG SSWIRNCWGQ VLSGRSTGTP KPELSTLSEK
LPTVVDSRRW YQTMSKVGLN YTGPFRSLDQ VRSHPQSNVA HGTIHDHTEA REPRYSLHPS
TMDNVFQLLT VASAHGQPRL FRTLAVPTFI EHIHVNEQGK GAEVLARVTV EPTSAGGMLG
NGAGYIENAE SDVPDVVFEV VGLKASPVDG GDIIDPDPHA AVELEWKPVF NYANSAELIH
TTKQFTHEIT ELEKLFVLCA ADTLDKLEGV RETVHPYLHK FQTWLHDFIT QMQTDGSRIF
DDAGSLTRLT VGERETRIQN LYDDLLRTEM RNYAIAVNKN RISALDIFQG KAEPLDILME
DNNLHKIYDF LCFWDYNDFL QLLGHNKPTL RVLEIGAGTG GTTGTILSGL RSRYGERLYS
KYTYTDISPG FFSAAQQRFC DHEGIEYKVL DISKDPVAQG FEAGSYDLIL AANVLHATPK
LGETLANVRK LLDPHSGRLL LQELNPIAKC VNFIFGMLPG WWLGADDERL TEPYISPDRW
DQELRAVGFK GADAAVYDHK APFHINATIV ASVDPSWTGK GPLTNGSSAR QQVTFIHSEG
DLSTLQKQYA EELREDQFGV EWQTFAEPPP TSQSIVVTVD LEGPYLDRIS EQSFNQLISW
IAALQPGQKV IWLTRCTQMG RGNDPRFATI LGLARNIRSE MSVAFTTVEI DEPEDAKARQ
VVAKLFGDIH GPRPGGNTVT EPDHEFAISK GVPYIGRFHW TSVNEELQKT QHSPSTTTTT
GAATGTSNST TRLRIGTPGL LQTLQYENIQ LPPLKADEVF IKVSATGMNF KDLLIAMGIV
DTPALGADAA AIGIETAGVV EAVGSAVTTV RPGDRVMAVS IHCFASHVVT REATCIAIPD
ELGFVQAATM PCVYATVIRA LMDVGRMEEG QTVLIHSACG GVGIAAIQLC KMVGSRVLAT
VGSAEKRHYL TETMGIPDAD IFDSRTPSFF PDVMRATGGR GVDLCLNSLS GELLHYSWQC
VAEFGTLLEI GKRDLVGRGK LSLAPFEDNR NYAGVDLSHI FVEKPHLWKS LLGRIVDFFR
DGHISPISPA TVFAARDCQD MFRFMQKGSH IGKIVLEMTD EPSTLIDQAV RSVEDESVVR
LAVNEAKLPI AGVVHGAMVL KDHATRNMPY SNWQAVVVPR VTGAWNLHHA LSSAQLDFFV
LLGSFSGMVG QPGQANYAAS NTFLNAFVQY RHGLGMPASA LEMGPISDVG YVAESPAILE
SMKATSTYAI GEQEYLDALQ LAMSRSSAPP SATPSVFTNP SVIGVGLRST NPLDDPSNRL
VWRRDIRLSI YRNLEKTGNT AGAASASQND AIKNLMSPEH ISDPSVISKL ALEIGRVLYG
FLMRQDDEIA LDKPLSTLGV DSLVSIELRN WCRQHLGLEA SVLEIMQSTL EHLARLAVES
LRCKLNAGSG GDSGGVNGTL AEERDRYDQI LEVKVP
//
