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Database: UniProt
Entry: A0A2S6BVN0_9PEZI
LinkDB: A0A2S6BVN0_9PEZI
Original site: A0A2S6BVN0_9PEZI 
ID   A0A2S6BVN0_9PEZI        Unreviewed;       501 AA.
AC   A0A2S6BVN0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PPJ51539.1};
GN   ORFNames=CBER1_09193 {ECO:0000313|EMBL:PPJ51539.1};
OS   Cercospora berteroae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ51539.1, 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   bioRxiv 0:0-0(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PPJ51539.1}.
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DR   EMBL; PNEN01001750; PPJ51539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S6BVN0; -.
DR   STRING; 357750.A0A2S6BVN0; -.
DR   OrthoDB; 120564at2759; -.
DR   Proteomes; UP000237631; Unassembled WGS sequence.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR041667; Cupin_8.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR003347; JmjC_dom.
DR   PANTHER; PTHR12480; ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD; 1.
DR   PANTHER; PTHR12480:SF21; JMJC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13621; Cupin_8; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000237631}.
FT   DOMAIN          63..109
FT                   /note="F-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50181"
FT   DOMAIN          263..425
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  56520 MW;  0ED46FD00A08E494 CRC64;
     MAVSQQLDSG YHSPAFDSSQ PPVKKRKQHD GDGEDATFVR RHPLGVRPSG NALTSSVNLK
     QAAGHFALLP DELLSALLEI LLAQDLLRLG GTCRALHAFT RNEELWRSLF VESAPKNFAW
     KGTWRSTYLS QDASREPKVD CSHLFSDVLH RPFFCANVPL HPYAENIPKQ NEISRLSDLS
     HEEFAEKWYD RPFILTWPVK QWPVYKTWST DRLVEKYADV PFRAEAVDWP LKTYVEYMND
     SRDESPLYLF DRAFAEKMQI KVTSEPSPDA DYWEPACFGP DLFHLLGEQR PDHRWLIVGP
     DRSGSTFHKD PNATSAWNAV LKGSKYWIMF PSSPSIPPPP GVFVSEDQSE VTSPLSIAEW
     LLGFHAEARR TPGCKEGICG EGEVLYVPSG WYHLVLNLEA SIAITQNLVP RSRLGAVLHF
     LNGPKCNISG FSDGVEDPYT LFVDRLREHD PQLLEEGLKE MERLSKIGRG WEELTKGTKE
     ANGEDGGFSF GFGGDDDDDI P
//
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