ID A0A2S6C3H0_9PEZI Unreviewed; 760 AA. AC A0A2S6C3H0; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 05-JUN-2019, entry version 5. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PPJ54246.1}; GN ORFNames=CBER1_05123 {ECO:0000313|EMBL:PPJ54246.1}; OS Cercospora berteroae. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae; OC Cercospora. OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ54246.1, ECO:0000313|Proteomes:UP000237631}; RN [1] {ECO:0000313|Proteomes:UP000237631} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631}; RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C., RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A., RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.; RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic RT mechanisms and extends production to the genus Colletotrichum."; RL bioRxivorg 0:0-0(2017). 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:PPJ54246.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PNEN01000569; PPJ54246.1; -; Genomic_DNA. DR Proteomes; UP000237631; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR007941; DUF726. DR PANTHER; PTHR17920; PTHR17920; 1. DR Pfam; PF05277; DUF726; 1. DR SUPFAM; SSF53474; SSF53474; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000237631}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000237631}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294 317 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 337 355 Helical. {ECO:0000256|SAM:Phobius}. FT REGION 1 24 Disordered. {ECO:0000256|MobiDB-lite: FT A0A2S6C3H0}. FT REGION 83 117 Disordered. {ECO:0000256|MobiDB-lite: FT A0A2S6C3H0}. FT REGION 150 188 Disordered. {ECO:0000256|MobiDB-lite: FT A0A2S6C3H0}. FT REGION 653 682 Disordered. {ECO:0000256|MobiDB-lite: FT A0A2S6C3H0}. FT REGION 709 760 Disordered. {ECO:0000256|MobiDB-lite: FT A0A2S6C3H0}. FT COILED 266 287 {ECO:0000256|SAM:Coils}. FT COMPBIAS 150 178 Polyampholyte. {ECO:0000256|MobiDB-lite: FT A0A2S6C3H0}. FT COMPBIAS 709 753 Polar. {ECO:0000256|MobiDB-lite: FT A0A2S6C3H0}. SQ SEQUENCE 760 AA; 83524 MW; 8E6E6D1DF0FF2414 CRC64; MFNKISTPFS NRANGGAGEE EAQGETLTTI LSTHEDRTAL TLLIADCTEA MKQNIEDAFD ATQTGSNTSL VVEDLREALP DVDAEASDEK VQSETEDAVQ KQKELEKEQK ELAQREKELA EAKSKELKSA ALEHWDKWRS SVIQRVGEVL NSHEEEERRQ KRESESSKKK EEEARAASPP MRFESPPKYD KAVDDSMRAL YPPIDCPLRR LTEEQRTLIL HCLLLLLLSL EHYHAESRIL LLRLSTSLDL PIDVLGLDES KVARGLLAAA ENMTADEETK KKAEENKTAR RWKVGLATAA GAALIGVTGG LAAPLLAAGV GTVMGGIGLA GTATAGYLGA LAGSGVLVGG LFGAYGGRMT GKMMDEYAKE IEDFGFEPVR TRHRPRKIEK EFRRLRVAIG ISGWLTKQEE VVEPWKVIGV QLESFALRWE LEALMNLGNS ISTFVTSTAW AYAKTEIIKR TLLGALYAGL WPLALLKVGR IIDNPFSVAN HRAQKCGEVL ADALINKAQG ERPVTLIGYS MGAKVVYACL QQLAERKAFG LVENAILIGT PASATSAEWR NLRAVVSGRL VNIYSTNDYV LGYLYRSQSI SLGVAGLQAI EHVKGVENFD VSSLVNGHTR YRFLTGPILQ QIGFEDVDLE GLKEEEVGLK ELDEKENRER AENEEKEKAK GSSSKEVSDE YVQGLEKEVE KKNEQSYIGW AQSKMVSAGS SVSAAYDKAT AQWRQRTKKN DSAMAGTGTP NVQTKSTEEQ PPALPQRPAQ //