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Database: UniProt
Entry: A7EE51_SCLS1
LinkDB: A7EE51_SCLS1
Original site: A7EE51_SCLS1 
ID   A7EE51_SCLS1            Unreviewed;      2215 AA.
AC   A7EE51;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDO01117.1};
GN   ORFNames=SS1G_03591 {ECO:0000313|EMBL:EDO01117.1};
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:EDO01117.1, 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; CH476624; EDO01117.1; -; Genomic_DNA.
DR   RefSeq; XP_001595502.1; XM_001595452.1.
DR   STRING; 665079.A7EE51; -.
DR   EnsemblFungi; EDO01117; EDO01117; SS1G_03591.
DR   GeneID; 5492047; -.
DR   KEGG; ssl:SS1G_03591; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; A7EE51; -.
DR   OMA; YSAACAY; -.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion 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   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd00833; PKS; 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; IPR032821; PKS_assoc.
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; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775:SF29; ASPERFURANONE POLYKETIDE SYNTHASE AFOG-RELATED; 1.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
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; 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.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..385
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2126..2203
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2215 AA;  245026 MW;  A2019304520027CF CRC64;
     MGESSTKIEP LAIVGLSFKF PQGMETANSL WKGLASSRSA WSSFPESRLN FDGVYDPDTG
     RLNSFPLKGA HFLNGDISAF DAPFFTIGPS EAAEIDPQSR ILLEVTYRAL ENANRISWYF
     NLRGESINMD TACSSTLVAF HTACERLRSR ESNMAIVAGS NLFLSPDMAM SLNNQNFLSP
     DGRCWSFDEK ANGYGRGEGF GVLVVKRLSD ALENNDPIRA AVLATGTNQD GRTPGIVQPS
     RSAQAQLIRD VYRKAGLDMS QTRYVEAHGT GTSVGDPIEA GAIADAFSHT LSADSPLFIG
     SIKSNIGHLE GTSGIAGLVK SVLILERRMI PGIAGLEHVN HSIVAEHPHL KFPKDLTSWP
     SDSLCRLSIN SFGFGGTNAH VIMEDAAGYL DNREKAINRT QVNGTNHANH DQRPMTNGFH
     HLETRRILVF SAQDENGIKR LESAYNDHWS QMNKDELSDS YMSRLSYTLG NRRSALLWRS
     FATVNSKNDL ITGIKFSRAV RALPRARLAF CFTGQGAQWY AMGRDIQAPI FKQSLRELSE
     LLTDMGCLWS LQAELSRDKE TSRINRPEFS QPICTAIQIA LIDLLEGLDI KPSVAFGHSS
     GEIATAYCVG ALDKRSAMSV AYYRGLLSSK VAEDKMIQGG MLSAGLSAKE VLPYLARVEA
     KFGYSGVVVG CINSPNNVTI TGDIEQINYL NELLEKESIF SRKLLVDVAY HSHHMNAIAA
     AYSEKLGNLS SRNSAKLIPM VSSVTGEVVS SDKLRQPGYW VENMVSPVRF LDAISCAPSL
     RVSEDGSISY NDSKDFFDDV LEIGPHSALQ GPIKDFLKLY GTPVPDWNPQ EAKWRRRIKL
     SEDPWIEDHK IANACILPAS AMLVMAIEAA KIMAKLRSNK AISGFIVQNV VVSRALTIPS
     DPDGTEIEFY LRPCGLASDR EITWSNFRIY IPENDNWVEV CRGQVRATHF EVGDEVDNGL
     EDSLSDEYHR AELWRIRGSS CQKVDMERFY PTLRENGIDF GTAHQTIKNG SYGQNMECVG
     DIALDSWVSK KREFQQMDFT IHPTSLDGLF QLGLLALVGE TSKINPSVIV GLRKLWVSEG
     KINVAGSSIM PTYAKSAMNG ATGTLINTVA FENQALNPVI ILDGLEGKFL EQTKKSTEKQ
     NYHLSWNFDY RPDIELLSKE ELIHAVNVKE YLNDDMFYEK LLSRLEHSNA RGKLYAVLSK
     NLRNILMGKV DALELMFKEP LVKDYYRELY KSTNGLSKTL AYLDILTHKH PNMNILEIGA
     GTGGMTNYLL DVLAQNGARD PRVGTPRFSH YTYTDISAGF FEGAAPLFQN FSDMVTFKVL
     DIEKDPAHQG FEAGGYDCII ADNVLHATRD LDVTIKNVRK LLKPGGKLML FELTVPEVVR
     TNFAFGLLPG WWRFNDKYRS FSAGISDSVW DRVLKSSGFS GIDFNFKDYE EDECHEHSAL
     VSTARGDTLS ISPFLLTVVV LDPQSDLQRK IYELLRHTLQ SAGTENILSM TLKEAATFHG
     NSAFGIVLLE LDRPLLQEMT EPNFKDVKAM FLAFENILWA CKGGGERPDL PEYALVQGAF
     RALRMENIRL KFISLSFEAT STNPTHLANK VFEVYQKVST TAVKDCEQEY VERNGMICID
     RIIDADYMNQ KLSETAEDKP RSDCEFCSAP PVALSIKTPG LLDTLEFVED SAARTNLASD
     EIEIEVEASG VNFRDCLIAL GRIPSMSFGF ECSGTIHRIG SHATKLKLGD RVCASTLGTY
     QTYARCNASN VIPIPSYMSF IDAAALPVVF TTAYYAIVHV AQLRKGESIL IHSAAGGTGQ
     AAIQIAKLLG AEIFVTVGSK SKKDLLISLY QIPEDHIFYS RNAFFVKGIQ RMTGDHGGVD
     VVLNSLSGDL LVDTWQCIAP FGRFLEIGKK DILANGNLPM LPFSRNASFH AIDLNEARKY
     RPGLLLDLKN SITTLLFDDK IRPPQPVHVY GISEVEKAFR YLQSGKNSGK TVIEFRGPDI
     IKSSVFENMT YEDWVGANKC KVSGTWNLHT LLPKGLDHFI VYSSISGAIG GTASVNYSAA
     CAYQDALVHY RNKVGEKATT FNLGVMVDDG VLRDNTAARR AEVPAMMTRP MFRGTWSINE
     QGKTGAKEDV ATDVTSQLHG VASETEAANI IANALMQRLS NALAVPMKNL DSSRPMHIYG
     VDSLIAVELR NWFNQKLDAD IAVFEILGEV TFRDIGFLVA GKSKLVEAIL KKVVK
//
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