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Database: UniProt
Entry: A7F1D4_SCLS1
LinkDB: A7F1D4_SCLS1
Original site: A7F1D4_SCLS1 
ID   A7F1D4_SCLS1            Unreviewed;      2524 AA.
AC   A7F1D4;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDN95526.1};
GN   ORFNames=SS1G_11404 {ECO:0000313|EMBL:EDN95526.1};
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:EDN95526.1, 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; CH476638; EDN95526.1; -; Genomic_DNA.
DR   RefSeq; XP_001587412.1; XM_001587362.1.
DR   GeneID; 5483727; -.
DR   KEGG; ssl:SS1G_11404; -.
DR   InParanoid; A7F1D4; -.
DR   OMA; VHTGCFT; -.
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; cd05274; KR_FAS_SDR_x; 1.
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; 3.90.180.10; 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; 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; 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; PF00550; PP-binding; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          26..450
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2434..2508
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          466..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2524 AA;  278201 MW;  204521649837EB7A CRC64;
     MPQSLTVEEA NSFIPMTPDE SQEDQLEAIA VVGFGLNFPQ DADTPENFWK MLVDGRSAMT
     DVPKDRWNID SFYHPSADRH DSMNARGGHF LKEDISLFDA PFFSMPPAEA VCMDPQQRSL
     LECTYHALEN AGMPMASIIG SRTSCYVGSF SREYEAMINR DPQMQAKYVA VGTGTAMLAN
     RLSWFYDLRG SSISLDTACS SSLVALHLAV DNLRSGESNM SIVAGCNLML NPDTNSIPLS
     NLGFLGRDSV CYSFDHRANG YARGEGTAVM VLKPIKQALK DNDIIRAVIR NTGTNQDGRT
     PGITQPSKEA QASLIQETYH RAGLDFKDTG FFEAHGTGTP IGDPREAGAI GIAFKDHVDE
     PLVVGAVKSN IGHLEGASGL AGLIKTILIL EKGVIPRNIW FEKLNPEILA DEWKLKFPTD
     TMAWPKEGLR RASVNSFGYG GANAHVIVDD AYHYLKSRKL AGKHQTVSSP PKVIHTNGMS
     NGTTNGRTYG TTNGTNNGTE IQTTDPEKYR LFVWSASDEG GLRRLSTSYQ KYFQTLHSEK
     ADFLDNLAYT LSRRRSNLPW KSFLVAISIE NIHHELSAGS LSKPVRSSAS LQPNLVFVFT
     GQGAQWYAMG RELMIYPTFQ KVLSHAEKYL TTSLGCAWKL TEELKRSKDS SNVDNPALAQ
     PLCTVIQIAL VELLEEWNIS PHAVVGHSSG EIAAAYCAGG ISKESAYKIA YHRGALANRL
     AQKKRRNGAM IAVALSEAEI VSYLDQVAAQ LGPKRLVVGC VNSPKNITLT GDEECVDLMK
     SLMNTQRIFA RKLQVPVAYH SSHMQEIASE YLKCIRGIVP REVSLTTKAF PTMFSSVTGA
     LATSDRLSQP DYWVENMVSQ VKFAPALSEL CATLLRVQPE QTEIAPLCLV EVGPHAALQR
     AVNETILADD TLSEASYDTT LRNGVNAIRS MMDLVGKLHC RGYKSDILAL NCPQRVEADL
     KPLCDLPEYP FNHSQGYWLE SRISENYRFS EFPRHELLGV RTTDWNPLEA KWRNMIRVSE
     LPWIKDHKFN GSELYPAAGM LVMAIEASRQ TARPNSKIAS YNIENVSFFK ALLVSLDAEG
     VETQFHLRPA KDNTNSSDRK HFNLYLCSSG QWAEICCGTI VTEYEEVNDA EILGPRNDDH
     LHSIWKNGVA RCTRLLDSKD LYENLASFGF GFGPTFQALK QVRWNNECEA TACLEPREWM
     KKVKDSHITL DHVIHPTALD AVMHLTAAAE SKGTSNPLRT MVPTKIEKLW ISNDLLLHAE
     NQTIQIFTHP TFQGYRDTEF SVVAFDNLAH ECQIVLEGYR ATAITSLEPS SAGDARLAFD
     IDWKPAVDLL TDEECSTVCC ATVNKDDFHD PIFIDKAELL CTFYIYHALE ELNRRAYSGE
     SHHTSKYIEW MRKQVDDYTS ANPIPNPEEN KPSLSDEEYF QMLSSELESG AEVDLINEVG
     KNLARILIGD VDALGILFND DLAKGFYGGL TFVPSNKKAS TYIDLLAHKD PTLKILEIGA
     GTGGSTASIL DKLGKHGNDE KGEPRLGKYT YTDISPGFFE AASQRFSDFV DVMEFKVLDI
     EKDPIEQGLN VGEYDVVVAS AVLHATANLE NTLGNVHKML KPNGTLLIIE PCNLEALRIP
     FIFGLLPGWW LSTEEHRFWG PLMSDDTWSS ELKNAGFTGA DICLRDFEDH RHTMSVIISK
     PAGDKISNIL PPIPKTVIVV AERYKKETPL VAYLRSALIF HGISTDVIGC NEITSADLKD
     SVCISLLEID NPFLCNITDD EWERLKTIVR SANGVLWLTR GAENDPALGM ITGLARGLRS
     EYPHLNFVEV ALEENCTTET IVKHSLNVLR KSINSDPIER NENEYWEKDR ILYVNRVVEA
     NYLNTHLTAR TATQKPQQRV LGSKPDTQIS LAIHNPGLLN TLRFEEGEVG RKELSPDQIE
     VHVKAAGLTF KDVQIALGQI PGNYLGLEFS GIVVRVGSDV PEETLKSGDR ICGVAAGAFS
     TKLHVPISQV FKIPDSISFT TAAAIPVSFC IARHSLVNLA KLKKGESILI HSAAGGVGQA
     AIQLARTAEA VIYCTVGSQE KKELLCTKGL ISAASPLKIY GSSEVENAFR FLQSGKSTGK
     TVVEMRSDDI ITAVPSSQPT YSFREDSSYV IIGGLGGLGK STATWMADRG AKHLILLGRS
     GATSQAALEF VAEMELKGIA IAAPPCDVTD EVALLAVLDM CSKTMPPIKG CIQGSMVLRD
     GLFESMSYEN YQDSVRPKVQ GSWNLHKHLP DSLDFFILLA SAGGIVGTRG QSNYASGNTY
     QDALARYRVS RGLKCVSLDL GLIQGVGFAA ENRDTLLAIK KLGYRGIHEK EYLAILDYLC
     DPSLPMMEDP LKSQIITGLE IPKVLLDTAE EAHDAEDWAR WVRRPLFRNL AAMEGLDASK
     SDTGSVSESK KRLSEVDYKA AFAAAGTSAA AAARVASSGL REKLARTLRI PEEDIETQRS
     IHTYGVDSLV AVDLRYWLAK EMKADLSIFE IMGDDSLGKL SWLIAKRTTL FAGEISDAQK
     DQPA
//
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