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Database: UniProt
Entry: A0A226DW08_FOLCA
LinkDB: A0A226DW08_FOLCA
Original site: A0A226DW08_FOLCA 
ID   A0A226DW08_FOLCA        Unreviewed;      1726 AA.
AC   A0A226DW08;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Phthiocerol synthesis polyketide synthase type I PpsD {ECO:0000313|EMBL:OXA49665.1};
GN   ORFNames=Fcan01_15638 {ECO:0000313|EMBL:OXA49665.1};
OS   Folsomia candida (Springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX   NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA49665.1, ECO:0000313|Proteomes:UP000198287};
RN   [1] {ECO:0000313|EMBL:OXA49665.1, ECO:0000313|Proteomes:UP000198287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VU population {ECO:0000313|EMBL:OXA49665.1,
RC   ECO:0000313|Proteomes:UP000198287};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXA49665.1};
RA   Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT   "The genome of Folsomia candida.";
RL   Submitted (DEC-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:OXA49665.1}.
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DR   EMBL; LNIX01000010; OXA49665.1; -; Genomic_DNA.
DR   STRING; 158441.A0A226DW08; -.
DR   Proteomes; UP000198287; 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   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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR001227; Ac_transferase_dom_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; 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; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; 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; PF08242; Methyltransf_12; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198287}.
FT   DOMAIN          13..431
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   1726 AA;  191227 MW;  087B264776ADFC13 CRC64;
     MSPDIEVPGK TLNEPIAIVG VAFRLPGASD GVTLWKNLMS ATDSVDFVPR DRWTSEKGCH
     GLTKEHRSFR AGFIDGDVDK FDATFWGLSP LELGFIDPQA RLLLQLSWEA LESAGITPGS
     LRGTSAAVLM GIWRDEYKDL VVSSSSVIGG EELRRYMGCS IGSSASRIAQ CFGMTGPTEG
     IELGCASSSY AIGAAMRHLR NRRTNLALAG GANLILKPCK TDDFQGVVSP TSRSKVFQED
     ADGFARAEGG IVYVLKRVTD AIKDGDNILG LIRGFGSSQD GLTRNFGTPT IGGEREAMLV
     ALEDAEVNPE DIGWVEMHGT GTRVGDPTEV AATRIAYQIS SGERGHPLTV TSIKANIGHT
     EGVSGAASLL KVLLAMKHGF IPPQLLTADL NHGIDFNGLV IPRTAVHWDG PLAGISSFGI
     TGTNTHMISV GALAELGRKH VEALKLLELE DGDDQLAAYC YTASTCRHHF DEYRSIATGR
     NLFELLKSLR SNNYELNNMT NFQHNTIRIK PTRPTSISFL FPGQGCQYIG MGLELYNSCA
     TYRRHFDEVN SHFIDIGGID LLEWIRDGKD IPFYPQLSIF AVEYALLNMW KEWGVTPNLC
     VVGHSSGEVM AAMAVGVLNL ATAVRLLVFT RQTLINEVEP GQMVALMTDE AMTLQMINQY
     AERCFMENKS ESSWIDISAL NSYNQTVVSG PVETSKKFST FVITYYSTKT SLLKFVDNAF
     HSRSFGKASN TFETNLEKLD FPERNRGVKY ISSMYRRELD DSENLDISYW SKLFTKPVKF
     VGSAAAATTS VGAKLFLEIS PHPTLAPLMK DNCPQNDLIC IPSLMKDAEN WITLLNAIST
     LYLHRVELDW SRIWISLFGE DILRNKVSHL LPTYPFQNEG PFWFSPLTTL SQDSEVVHRN
     KIIHPLLGSM PAVPKFDEIN RITIFETSPG YVEMGFAVAT LLGKTEKFNN IKLSKVEIKT
     VLSLDVKSDI QTNVVYDGEG FNISISSRGD HTEGMWTLHA SLNAKVITPD VYTIKPEKHL
     GNFTGESLPS PYPESLRAGV VTPIFDTDGF GSFMVHPIIL DALLQITLLA QQDSLTTLRV
     PVAISEFELV CSASGNIGKN TCARQIRAQA GINSSTLFIQ GADLKWRTLA SMTNLRTIST
     TTKAVRRTIE GSNEMSDRKD HDQLLPLFVE EWVKDDQLVN YSQSICEQFS SCKTISRPAA
     EIQDYKLISS YIGKCVAETL NLLGFSDFTH NQLITRCDIA LHLGLSHLAP NFLARLLKYA
     GQAGLLKEYS LTEYIVLPYS DCLTHNLLAT NYDKHLPEDW AFVEFYTSKL TSFLSGTESI
     LPYLFPPSLP SLEPPNQIVS NETSVNTNFS AERFYSATIA SYLTEDFIVV FTSFLKDNGQ
     RLRILEVGAG TGSATRELLH HLRDSSSTYT FTDISINFLN RAEASLPHVP GDLEKDALVQ
     VFENETFNVI IANNVLHATT DINRVVENLR LLLSPKGNIF IAEQLHPSAF VHIIFGHCKG
     YWLFNDGIRS DHCLIDGDAW KLVLQSVGYG EVSIVENKDF HFGIIIATNK EDVSPPPSFI
     VIASSDQDQF ANQLVASNKE YATLYNISEA NIVIHPENKI VYCFPQVLKD NIPALNQVRK
     QLEHFLRFSR ALVSVGRVEL ILVSHGLIPV GDTEARYPVA GAIRGFSRTL ANEMLELDIT
     WVDLDDDEST MQQIQEVVAE IRNKGTLRNR DSDPFVTVSF EYNCLH
//
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