ID A7F6U2_SCLS1 Unreviewed; 2138 AA.
AC A7F6U2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDN98463.1};
GN ORFNames=SS1G_13322 {ECO:0000313|EMBL:EDN98463.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN98463.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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DR EMBL; CH476644; EDN98463.1; -; Genomic_DNA.
DR RefSeq; XP_001585805.1; XM_001585755.1.
DR GeneID; 5481894; -.
DR KEGG; ssl:SS1G_13322; -.
DR VEuPathDB; FungiDB:sscle_03g031520; -.
DR InParanoid; A7F6U2; -.
DR OMA; YEAMEMS; -.
DR OrthoDB; 5396558at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR GO; GO:0009403; P:toxin 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; 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; 2.
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; 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; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR04532; PT_fungal_PKS; 1.
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; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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:UP000001312};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 372..805
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1754..1831
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2138 AA; 234435 MW; CB4F747F3410C572 CRC64;
MDVILFGDQT VDCQSFLKKA LRRKNCPILS TFLEQAHAAL QDELSSLPST SRRHFAVFSS
VSEFTERYFE ADHPDLAVES AITCLAQLTH FIGFFEEHPL AYLEPSNTEV LAVCTGLLAA
SAVASCKSLT SLIPLAVQAV RIAFRLGSRV AAVGNQLESA SDRQKTWSTI VMGLSPEAAE
RALEEFNESR GLIQSTRLYI SAIGTTSITI SGTPTIRAQL FETCEAFQNL QRREIGIRGP
YHAAHLYTPQ DVERILSPEI VKSLSNYSSV LPLVGTAAHK ESISTVDLFR NSIMEILAEQ
VKWERLVKIA VAHVRESKQN EVRVLAMGPT ALGNSLISAL KNGGGLKLSM EDHISYTMEN
TIPRGFTGRM SESKIAIVGM SGRFPNSADH EAFWALLEQG LDVHREIPAD RFDAKAHFDP
SGKGKNKSHS PFGCFINEPG KFDPRFFNMS PREAMQTDPM QRLAISTAYE AMEMSGFVRD
RTPSTQAHRI GTFYGQTSDD WREINAAQDI DTYFITGGVR AFGPGRINYH FGFSGPSYSV
DTACSSSMAA INLAVTSLRA GDCDTVFAGG MNVMTNPDIF SGLSKGQFLS KTGSCKTYDD
GADGYCRGDG VVTLILKRLD DAVADQDPIL GVIAGIATNH SAEAISITHP HAGAQKYLFQ
KVMDEARVDI RDVKYVEMHG TGTQAGDGVE MDSVSSIFAP SNKLRRRLDQ PLFVGSVKAN
VGHGEAVSGA TALVKIMMML KKSMIPPHCG IKTKINQTFP KDLKDRNLNM AFKPTPFPRP
TNGKRYVFMN NFSAAGGNTA TLLEDAPIRQ LEGTDPRTSH VVIVTAKSLA SFRNNVQKIL
SWSRDQPSSC LPSLAYTTSA RRYHYQYRIA VNATDLQSVQ NALSSYTEGP HTPVSNVKPR
VAFAFTGQGS HYLGMGKALF HDVKQFRHDI EDFDQMAQTQ GFPSFIGLID GSITDLSIAS
PVMTQLAILC VEISVAALWQ SWGIEPTAVV GHSLGEYAAL QVAGVISTHD AISLVGNRAQ
LLVSKCTVGS HGMLAVRAGF AAVEPFLSDI EVEKACINGP EETVFSGTVD NMNRLKEVLT
AQGFKNTMLN VPYAFHSAQV EPILEDFIQS AKSAVFHQPR IPVMSTLLGT VVEDSGVFGP
EYLARHCRES VDFLGGVTSA LKDGIVDEKT LFVEIGPHPV CSNMIKAIVG TSTITVPSLS
RNADAWTTTA ASLATLFNAG LDFNWNEYHI NFKNAHEVLD LPAYSFDEKI YWIDYRENWC
LTKGDKQLVA PSEAKQSFST TTVQKILFED VDGDNINVVA ESDLMEPNLR AAISGHLVHG
QPLFPSSIYG DMALTICDYA LKLAQPDAKS VGFNVGSMET HKPLVLDNTA KTHLLQIETK
LDLAHRRGTV NFRTYGADGK PVEQTKCEVT LEDSSSWLKD WDRRKFLVQG RIENLMSHKE
VHKIQRGMAY KLFGALVDYD QRYRGMDEVY LWSEQCEATA KVKFQTSDKD GKFFMSPYWI
DSVCHISGFI MNANDAVDST KHVYISHGWE SMRFAKTMSA DKEYRSYIKM QKVPGGGEMV
AGDVYVFEGD EIIAVVGGIK FQRVPRTLLQ TLLAPKSLPA RAGVKGAPVS AKTATPKPSK
VVSKASSKVV SKQTSKGIFA KALTIMAEEI GCDVAELAGP MRFSDMGVDS LLGLSISGRF
REDLEIDFQS SVFEHEPTVD HLKAYMTRFE DENSAESSGM STPEMVSSHS SDIGDDYIDL
NDAYSENSSV DGDSENAMIV QIIRTTIAEE MGVELEEITD NTDLATMGMD SLMSLSILGA
LREKTGLTLN SELLVENTSV EKIETTLGLR ATKPKVVEIK KTTKISQVSH ASIQPAPPTQ
VAKPINLSQY PPSKSILLQG NPKTATRTLF LLPDGSGVAS SYTPIPQIDT DLAVFGLNCP
FMKDPTEFNI GVPAVTQIYL AEIQRRQPHG PYLLGGWSAG GVLAYECTRQ LIAKGEKVEK
LVLIDSPFPV GLEALPASFH QYCAKIGLLG DGGLESLPKW LLPHFFSTVR ELTAYSDHLG
SLPCINTTNM PQTITIWARD GIVHNEDDLK PEWDPKVRMP NSMDWLTHDR KDLGHNGWEK
LVGEGNVKCM STSGNHFTMM RDPITRDLAK LMKQALEI
//
