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Database: UniProt
Entry: A0A2G5HQN4_CERBT
LinkDB: A0A2G5HQN4_CERBT
Original site: A0A2G5HQN4_CERBT 
ID   A0A2G5HQN4_CERBT        Unreviewed;       431 AA.
AC   A0A2G5HQN4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   SubName: Full=Putative rRNA-processing protein ebp2 {ECO:0000313|EMBL:PIA94861.1};
GN   ORFNames=CB0940_08249 {ECO:0000313|EMBL:PIA94861.1};
OS   Cercospora beticola (Sugarbeet leaf spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX   NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA94861.1, ECO:0000313|Proteomes:UP000230605};
RN   [1] {ECO:0000313|EMBL:PIA94861.1, ECO:0000313|Proteomes:UP000230605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=09-40 {ECO:0000313|EMBL:PIA94861.1,
RC   ECO:0000313|Proteomes:UP000230605};
RA   De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA   Thomma B.P., Van De Peer Y., Bolton M.D.;
RT   "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT   several fungal lineages and shown to be expanded in Cercospora beticola
RT   based on microsynteny with recipient genomes.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
CC   -!- SIMILARITY: Belongs to the EBP2 family.
CC       {ECO:0000256|ARBA:ARBA00007336}.
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:PIA94861.1}.
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DR   EMBL; LKMD01000104; PIA94861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5HQN4; -.
DR   OrthoDB; 11782at2759; -.
DR   Proteomes; UP000230605; Chromosome 6.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR008610; Ebp2.
DR   PANTHER; PTHR13028; RRNA PROCESSING PROTEIN EBNA1-BINDING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR13028:SF0; RRNA-PROCESSING PROTEIN EBP2-RELATED; 1.
DR   Pfam; PF05890; Ebp2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT   REGION          1..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..174
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  47602 MW;  3BE423AC901387C6 CRC64;
     MAKALKLKAA LDRQKGVDHK LEKQKKKQKE AEKRKRAKQS KNDADEGDEN EGDEVDFSAL
     ENVLAGAEVI EVDGEEKVDK RQKPKAGNRK ERRAAMLAAK AAAEAEEIAN GGKKEEDAEG
     WETDESEDAE DANGGVEIGP LSDESESESE IENDAAEDDE DDEEDEEDIP LSDLESLASE
     DKEDVVPHQR LTINNTAALA RSLKSIALPA DLPFSAVQAI TSEEPVQIAD VEDDLNRELA
     FYRQSLNAVA AARSKLKAEG VPFSRPTDYF AEMVKSEEQM GKVRAKLLDT EARKKASSDA
     RRQRDLKKFG KQVQIAKLQE RQKEKTATLD RIQTLKRKRQ GADLAANEDD PFDVALEDAA
     TTAAKDKAER RAKGDGPNRK RQKKNEKFGF GGKKRFSKSN DAKSTADDSG YSVKKMKAGS
     KRPGKSKRAR T
//
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