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Database: UniProt
Entry: Q6W5P8
LinkDB: Q6W5P8
Original site: Q6W5P8 
ID   Q6W5P8_9ACTO            Unreviewed;      2049 AA.
AC   Q6W5P8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   19-JAN-2010, entry version 44.
DE   SubName: Full=FscF;
GN   Name=fscF;
OS   Streptomyces sp. FR-008.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Streptomycineae; Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=206662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14652074; DOI=10.1016/j.chembiol.2003.10.007;
RA   Chen S., Huang X., Zhou X., Bai L., He J., Jeong K.J., Lee S.Y.,
RA   Deng Z.;
RT   "Organizational and Mutational Analysis of a Complete FR-
RT   008/Candicidin Gene Cluster Encoding a Structurally Related Polyene
RT   Complex.";
RL   Chem. Biol. 10:1065-1076(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Chen S., Huang X., Zhou X., He J., Bai L., Jeong K.J., Lee S.Y.,
RA   Deng Z.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY310323; AAQ82566.1; -; Genomic_DNA.
DR   SMR; Q6W5P8; 4-896, 1373-1752, 1759-2033.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001227; Ac_transferase_dom.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR020842; PKS/FAS_KR.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_reg.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR015083; Polyketide_synth_docking.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Gene3D; G3DSA:3.40.366.10; Ac_transferase_reg; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 2.
DR   PANTHER; PTHR11712; Ketoacyl_synth; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF08990; Docking; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Phosphopantetheine; Transferase.
SQ   SEQUENCE   2049 AA;  213663 MW;  993B5EB7BDF0C0C3 CRC64;
     MPDDKKLVDY LKWVTADLHK TRRRLEEAEA HRREPIAVVG MACRLPGGVA TPEEYWRLLE
     EGRDGIAPFP ADRGWDLDAL NGEGAGSSAA GEGGFVDAAA FDAGFFGISP REAVAMDPQQ
     RILLETTWEA VERAGIDPVS LRGSRTGVYV GTAGVDYVGV VMNSREDAEG HATTGLTASV
     VSGRLSYAFD LAGPAVTVDT ACSASLVAIH LAAQALRNGE CGLALAGGVT VMSTPMGFSG
     FTRQGGISTS GRCKAFADSA DGTGWAEGAG VLVLERLSDA RRNGHQVLAV VRGSAVNQDG
     ASNGLTAPNG PSQQRVIRQA LAGAGLSAAD VDAVEAHGTG TPLGDPIEAQ ALLATYGQDR
     PEDRPLLLGS VKSNIGHSQA AAGVAGVIKT VLAIQHGVLP RSLHIDEASS HVDWGAGNVR
     LLTENTAWPE TGRPRRAGVS SFGISGTNAH VVIEQAPEPE EPATPEDGTP TARPTLVPWP
     VSAKTREALD AQLARVTSVT GAAPLDIGHS LATGRSTFEH RAVLLAGPEG EPAEAARGRA
     TERTLALLFS GQGSQRAGMG RELYERFPVF AEALDAVVAR LDTGLERSLR EVLFVEEGSE
     AAALLDVTGY TQPALFAVEV ALFRLVESWG VSPEFVAGHS VGEIAAAHVA GVFSLDDACR
     LVAARARLMQ ELPTGGAMVA VRATEAEVTP RLTEGLSLAA VNGPDSVVVS GPEGEVTALA
     AEFETEGRKI QRLSVSHAFH SALMEPMLDA FREVARSLEY AEPRVPVVSN VTGALAAPGQ
     LTDPEYWVRH VRETVRFADG VRTLAEAGAD AFLEIGPGGV LTALARQSLD TLDGGTGAVA
     APALRSRRPE QEALLTGLAQ LHVAGVRVDW AAWFTGTGAR RTDLPTYAWQ HRRYWPRPLA
     HAADIPGAGL TPAEHPLLGA AVSLAGSEGV LLTGRVGLRT HPWLADHVMG GLVLFPATAF
     LELAVRAGDQ AGCGRVQELT LTTPLALDPR GAASVQVGVG PPDAAGCRPL AIHSRPEDAA
     DDEPWTQHAT GVLVAGARQV AFGQSAWPPA DATPVDLDGF YERTEYGPLF QGLRAVWTRG
     DEVLAELELP ARADDAALFG LHPALLTAAL HAVEYVELKD ADQGLLPFSW SGVTLHASGA
     ARLRVRITKA GEDTVSIAAV DTAGRPVLSV ESLALRPSGA ARLLKPGTDR STLLGLDWVP
     AEPTGPAAGG PRVALGTDPF GTGTVLAGLD EVTETGTQVL VPVPDGGEDP VTATHEATRA
     TLALLQEWLD GPRPAGARLV FVARGVVAAR PGDPAANLAG AAVWGMVRTA QAEHPADFTL
     VDVEPGAPFP LEAVLAVDEP QAAVRDGQVL VGRLTQLPPP TPQDGPENTD PFGVTRDGTV
     LVTGGTGTLG ARTARHLVTR HGVTRLLLAG RRGPDAPGAA ALREELTALG AHVTVAACDV
     SDRDALAALL GGIPAEHPLT AVVHAAGVLD DAVVTSLTPD RLATVLRSKA DAAWHLHDLT
     RGLGLDAFVL YSSISGVTAR AGQANYVAAN LFLDTLAQHR AAQGLPALSV AWGAWDLDEG
     MAGDLLTDTG RRRIRSGGID TLPGDRALDL LDTALTLGEP LVVATNLAAP PATAHLDEVP
     PLMRGLVRPP RRTAAATTDA PARVLDAASF RENFANLGAG EQETTLRETV VACAAALLGH
     TDTSEIDPDR DFLELGFDSL IGIELRRKLS EITGLQLPAS IVYDSGSPNG LTAWLRTELG
     AQGSGAPQTG AAGGPTENDS MERLFLDGLA QGKVREAQRM LATVAALRPS FEVTAELEDL
     PWPVTLAEGP APTRLVCVSA PTANGGVHQY ATLSGHFRGR RDVTALPLIG FNTGEALPAH
     AEAAARIIAD CTLQAADGKP FVLVGHSSGG SLAYAAAGVL EHTWGIRPEA VVLLDTLSIQ
     HKSDEGVDYN GMMKFNFTAV DDSPVRLTNS RLSAMGRWMV LLNALDVHPT TVPVLEIKCT
     RALIEGVPAP DPERLHLPVV PDAEVRPLDS DHLSLIREDS GPAADLMDAW LTALETTATT
     DAPETAPAG
//
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Ontology (6)   
   GO (6)   
Chemical substance (1)   
   KEGG COMPOUND (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (42)   
   InterPro (23)   
   Pfam (7)   
   PROSITE (3)   
   Blocks (9)   
Literature (1)   
   PubMed (1)   
All databases (51)   
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