ID A0A0G2FKA0_9PEZI Unreviewed; 1492 AA.
AC A0A0G2FKA0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative polyketide {ECO:0000313|EMBL:KKY34489.1};
GN ORFNames=UCDDA912_g05526 {ECO:0000313|EMBL:KKY34489.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY34489.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY34489.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34489.1};
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:KKY34489.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY34489.1};
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:KKY34489.1}.
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DR EMBL; LCUC01000200; KKY34489.1; -; Genomic_DNA.
DR STRING; 1214573.A0A0G2FKA0; -.
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: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; 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; 1.
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; 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; IPR030918; PT_fungal_PKS.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775:SF53; ATROCHRYSONE CARBOXYLIC ACID SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43775; 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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 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; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 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 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 78..522
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1414..1491
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1330..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1492 AA; 161993 MW; 249EB71AA868B8A1 CRC64;
MELLDSQLKP RVPVLSTSTG KPYTVETAGD LFEAIVSELL THAIEWDLVV DSVVEKIVET
SERAVEVTVF GKSQATKDLL TALNGVPNLE TTPRNLIDWV SRKPDSETKG PRGPAQSKIA
IVADRFDLAT HFDPTGKSRN KSSTEYGCFI DEPGLFDAPF FNISPKEAAQ TDPQGRLALV
TAYEALERAG YVPNRTASSH VHRVGTFYGQ AADDYREVNQ GQEVSTYYIP GGCRAFVPGR
INYFFNFWGP SFSIDTACSS SLATIQAACT SLWAGDCDTV VAGGVNVLTN CDGFAGLGQG
HFLTTGPNAC KTWDAEADGY CRADAVGSIV MKRLEDAEAD NDNILGVILS AATNHSAEAI
SITHPLAEAQ SELTRSVMNR AGVDPLDVGF VEMHGTGTQA GDMEEIKSVT DVFAPVGGAT
RRRSPKQPLY IGAVKSNVGH SESAAGITAL IKVLLMFQKD FIPRHVGIKN SLTPKFPKDM
AKRNVHIPFE QVPWARTPGK KRIAVVNNFS AAGGNTSIAI EEPPVRPEPE VSDPRTSHVV
TVSAKSKKSL EGNLKRLLAY LDTHPDTSLG SLSYTTTARR HHHNYRVTVC ASETAVVKKH
LESKLAAVDS QKPIPAPGST PIAFAFTGQG ASYKSMSLEL YHDSPFFRFQ IQNLDSLARS
QGFPSFIPAV DGSFPQDHAH SPVVTQLALV SIEIALARYW NLLGVQPSVV IGHSLGEYAA
MHVAGVLSAS DALYLVGKRA ELLEKKCRIG SHKMMAVSAT LDEIERSAGD APYEVACING
PKQIVLSGPC DEIESLERVL KDAGHRCQVL EVAFAFHSAQ TDAILDEFEA IAKTAVDFKE
PQIPFVSSLL SKVVCDGKTL NANYVRRATR EAVDFVGALY TAEKQGLIED SMAWIEIGPH
PVCMGFVKAN IPSTAVAVAS MRRGQGNWVT LAETLSTLHS AGVDLNWNEF HGPFEKRLRL
LDLPTYAWND KNYWMQYKGD WCLTKGNTFY VGKDKAQSQA SIAPLPNSSL RSSSVHQILE
ESIYADSGKV VMQSDLMQKD FFDAAHGHSM NGCGVVTSSI HADLAYTLGD YLYKKIRPDA
GKVDMDMRNL NVLKGLVSQK YIKTPQLFRV SAEISDIDSG VAHLKWFNAT PAGDVEDPFA
SAELCFGEAK AWLDSWAPMT HLVQSRIEAL EQMSVRGEAT RFSHNMAYRL FANNLVDYAS
KYRGMQSVVL NGLEAFADVT LSHEKAGSWT IPPQYIDSVA HLAGFIMNCS DAMDTQGNFC
VTPGWKSMRF ATKLEAGEKY RSYVKMIPTA EDPSVFMGDV YILQNDAIVG MVGGITFRKY
PRILLNRFFS PPDAGQTNNK TSKAAPPPRP LERRAAPQPP QLVSNTSSGA STPIEPMWTP
SAEKSEASEP PTPTEPVAKK PPAPSAATGD TDAGDSSGLA NKAMRLIADE TAIDEADLVD
EASFASLGVD SLMSLVIAEK FRDDLGVQVS GGLFLEYPTI GDLRGWLVEN YS
//
