ID A0A0G2ERX1_9EURO Unreviewed; 1770 AA.
AC A0A0G2ERX1;
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 synthase {ECO:0000313|EMBL:KKY24989.1};
GN ORFNames=UCRPC4_g02210 {ECO:0000313|EMBL:KKY24989.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY24989.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY24989.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY24989.1};
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:KKY24989.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY24989.1};
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:KKY24989.1}.
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DR EMBL; LCWF01000053; KKY24989.1; -; Genomic_DNA.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; 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; -; 2.
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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF21; NON-REDUCING POLYKETIDE SYNTHASE AUSA-RELATED; 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 SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 261..677
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1431..1509
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1561..1638
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1408..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1770 AA; 192959 MW; 1E6214BE3B100105 CRC64;
MARSKQIAFF GGQGNKSLFS QKLSSQVQRA ADSSSAVALL LSTCHSAFLS EVIDLTSCGP
IPRWAAIDGI KSPLDLLVIH ERFKNNPIVE GVVLCLHQLI TFLTRYPALG QHPVGGVAGF
CSGILPAIVV ASSTNLSEYI NWSKDAIRLA FWMGYRAGEL SAKIEGEEWQ EQPWSLAILG
LSREKVEDLL TAFNGNEATA ARDCTVRVSS TTSKSTIGVV GGGKSLKKLR SKYIAGATIC
EPIQVHALYH GGDTALSAYR KVVLDCQRRG LSFPSLGDLK VPVWSSQDGS KICADSKLEY
SLLEYTIRSV LIEVADWCTT WRNILKSTSR ADRTISVVAI GPGSQSFLLS STRNDIEDSN
VILDITNGTV DESVSSHEDG FAVVGMSVNF PSMPSTLRAF LSGKISYAFG FEGPSIVVDT
ACSSSLVAVS QACQSLARGD CSTALAGGVN AITSPDMYLG LSRAHFLSDR GQCKTFDANA
DGYCRAEGCG LFVIKRLADA VNENDRIYGV IKAVEINQCG NASSITNPHS QTQEKLFEKL
LSRTGFSPGS IDVIEAHGTG TQAGDATEIS SILSVFGGTR SPQEPLYLTS IKANIGHAEA
ASGSAALAKV LLMLMNNKIP PQISLKTLNP RLSSLAISNV QIPTVIEKWV STSKKPRRAL
LNNFGASGSN AAAILQDPPP ISKGAKSAKR KAYVFNISAK HKKTLKRYCD AYQASSETLK
SMAIEDVCYT ATARRQTYDY RLSFVCHTTE DLVTQLENHT EPAYCAASKR RPLVFAFSGQ
GSCFPGMGKS LLLTMPVFRD ALSQCDCILN GLGYPSITPI IQEDYAPQTM EENVLLSQLS
CFALEYALAL MWLSWNIVPD IVIGHSLGEF AALAVSEVIT LKDALWLVGH RAQLMIDNSA
LDPIMEPLRR SCTNINPSTP KYVTGSCYYG RVLKPRDITP EYFANQTRGV VRFSDLIRSI
KHDEALERAV FIEVGPAPTT LSLIKNTFSS PELLLLPSIK RYQDPWDTLC GSLQRLSFQY
VTINWRKVFE GTNAKLVDGP NYPFQLSDLY IPFKERSGTD FAQNGKENVG PAISFHLLEA
MVYSKHGCSP SQFTTRVSTL SDYIKGHVVG GHCLCPASLY HEMLLEAGAV ILGGIQSKSL
HVQHMKFSKP LLHNPRNDER KILLTIGEAS SAPSILGGSP SKFEFQSLCP NERMDAVEHC
SGTILCESCS TTEQYLARKT AYVKRHTNYL LSEHVPKSVF RTNMIYNVVF PRVVSYSRRY
QAIQELAIPE GSLEGYGTFK LPDNDFSEAK GVMSPVFIDT LLHAAGFVAN SHAQLSEACI
CIEVEHYRVL SNKIDTRKAF SVYCSLLDHI EGTLLGEAYA INPDGTVLAA VEGMHFKKLN
LRSFESHLSR SAHHECFNGD VAKFNSATTP KDMSQKNSSE DRVKTDATTV GDPSEIKRTV
LEITSQVCEL PLGSISRQSK LVDLGFDSLM RLELLESLRG RFPTIQLESA FLSGMDTVEE
LQDCVVRMSG KIPAHSTLGN FNFQDGQLDN NNKAHRTRSL STENRTSWGH TVPQALGTDM
NSRTDDIAKV TTIIRDITGV SEAEISPEST LQSLGIDSLM SIELREVLFA RAGQTLSQDE
IDSDFTVSEL GQLVFSQKAS GATSTTSGVA TTTTTDTSHA AVLVNMQTGS KDLPPLFLFH
DGSGMVGMYK TLDQIGCNVF GVANPDLKAD HHWATSLVDM ARHYASAIAA TPTRSVILGG
TSLHILYGLL LNMSWLTSLD RVVFWWNLST
//
