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Database: UniProt
Entry: A0A0S7E0B4_9EURO
LinkDB: A0A0S7E0B4_9EURO
Original site: A0A0S7E0B4_9EURO 
ID   A0A0S7E0B4_9EURO        Unreviewed;      1832 AA.
AC   A0A0S7E0B4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   23-MAY-2018, entry version 17.
DE   SubName: Full=Conidial yellow pigment biosynthesis polyketide synthase {ECO:0000313|EMBL:GAQ08560.1};
GN   ORFNames=ALT_5881 {ECO:0000313|EMBL:GAQ08560.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GAQ08560.1, ECO:0000313|Proteomes:UP000051487};
RN   [1] {ECO:0000313|EMBL:GAQ08560.1, ECO:0000313|Proteomes:UP000051487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GAQ08560.1,
RC   ECO:0000313|Proteomes:UP000051487};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Aspergillus lentulus strain IFM 54703T.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:GAQ08560.1}.
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DR   EMBL; BCLY01000009; GAQ08560.1; -; Genomic_DNA.
DR   EnsemblFungi; GAQ08560; GAQ08560; ALT_5881.
DR   Proteomes; UP000051487; Unassembled WGS sequence.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.40.366.10; -; 1.
DR   Gene3D; 3.40.47.10; -; 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; IPR032821; KAsynt_C_assoc.
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; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020807; PKS_dehydratase.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR030918; PT_fungal_PKS.
DR   InterPro; IPR032088; SAT.
DR   InterPro; IPR016039; Thiolase-like.
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; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF16073; SAT; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF52151; SSF52151; 2.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051487};
KW   Phosphopantetheine {ECO:0000256|PROSITE-ProRule:PRU00258};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051487};
KW   Transferase {ECO:0000256|SAAS:SAAS01038082}.
FT   DOMAIN     1754   1831       Carrier. {ECO:0000259|PROSITE:PS50075}.
FT   COILED     1761   1781       {ECO:0000256|SAM:Coils}.
FT   MOD_RES    1791   1791       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00258}.
SQ   SEQUENCE   1832 AA;  198778 MW;  9525CF4089519E0F CRC64;
     MDWTTETPNT EPSLVTATPS TTESLVDPAK MKVGYFGNEF PHDDLHDLSR RLYNWSKDRQ
     HTLLATFIHE ATSAVREEVR LLPATLRALI PPFETIFSLV SHADLRHGPL GGCIDGMLLC
     AVQLATFIGY YEDSTEDTFQ WHNADACLAG LGTGLLSTVA VSVSPTLADM PVTGAEVVRI
     AFRLGILVHE VSRNLQAPAS DGGPGDSWAY VVPDAVADDV QSELDAFHNA KKTPESSKVF
     ISALSRTSVT ISGPPTRLKD LFLVSDYFRD RRFVPLPVYG GLCHASHVYS KKHVDSIVNT
     ESSSLVSLDS RLAPRVPIFA TSNGKPFPAK TVSGLFRDIV EELLTQRIEW DNVIEGVIQH
     AKCTAVSETL VLMFRTSLPA RDLVEALNSE SLPFKGRTQD LVPWVTKPQA EQRGPRGPQQ
     AKIAIVGMSC RLPGGADDTE KFWEILNQGL DVHKKIPADR FDVESHCDPS GERLNTSLTP
     YGCFIDEPGL FDAPFFNMSP REAVQTDPMQ RLAIVTAYEA LERAGYVANR TASTNLHRIG
     TFYGQASDDY REVNTAQEIG TYFITGGCRA FGPGRINYFF KFSGPSYSID TACSSGLATI
     HVACNSLWNG DTDMAVAGGM NVLTNSDAFA GLSKGHFLSK TPNACKTWDC EADGYCRADG
     VATVIMKRLE DAEADNDNIL GVIVAAGTNH SANAVSITHP HAGHQADLTR EILSKAAIDP
     LDVSYVEMHG TGTQAGDAQE IQSVVDVFAP LSSTKRRATK QPLYIGAVKA NVGHGEAVAG
     TTALLKVLLM LEKKTIPPHV GIKNSINPGF PKDLDKRNLH IAYQSTPWVQ SSSDKRRVAV
     VNNFSAAGGN TSIVLEEGPV RSIQDSDKDT RPMHVVAVSA KSKVSLKGNL QRLIHYLESN
     PDVSLSHLGY TTTARRNHHN HRVAVSTSAV PQLVRQLNSL LQSADTHKPI PSTGAPPVVF
     VFTGQGAAHR SMNLELFRDS PCFRSQMLYL DSLCQSQGFP SIIPAVDGSH PQDYTHPPTV
     TQLALVCIEL ALVAYWESLG VRPEVVVGHS LGEYAALHVA GVLSAADTIY LVGQRARMLE
     KKCQIGSHKM LAVRAALDEV QSKANGKPFE VACLNGPKDT VLSGTVGEME ALAEELEQSG
     IKCYHLDVAF AFHSAQTDPI LHELEETAQT GVLFQPPRLP IISPLLGKVI FDEKTVNAKY
     ICRATRETVN FVAAVEKALA MSTVDETMVW IEIGPHPVCV GFVRSIMSTM NMAVPSFRRG
     ENNWQTLSQS LAAVHAAGVE VDWNEFHRPF EHGLRLLDIP TYAWNNKTHW HQYNGDWALT
     KGNNYYDSKK KSAAVGSPLA AAPVSSLRTS LVHRVIEESF SDTAGKVIVQ SDMMQADFLA
     AAWGHQMNGA GVVTSSIHAD IAWTLGKYLL DSLKPNSKKS VVDMEISNLV VREGLVAQKN
     RSVPQLIQVS ISTADIDSGV AYLEWHNVTN DGVSLADEEP IVTAQIRYGT AGDYLSSWVP
     ALHLVQGRIE ALSRLADDGI ANRLSNSMAY LLFADRLVDY ADRYRGMQSV VLNGLEAFAD
     VRTKPDDEGG VWTVPPFFID SVCHLAGFVM NVSDAIDTKN NFCVTPGWGS LRMARPLVAG
     GRYRSYVKMI PTAEDPTVYL GDVYVLEGDE IIGVMQAMKF RRYPRVLLNR FFTPADIKNP
     TSGSTPAANG ARSSAQSTKL VSASAPLPKP ANVAEPVPTP APAPAPAPAP APAPATEPVP
     VQGKKQDTAA PPAVASNSTA AKALELVAAE AAIELSELQD DVSFANLGVD SLMSLVIAEK
     LRQQLGITVS GSLFLEYPTV RDLRVWLDEY YS
//
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