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Database: UniProt
Entry: A0A178DT33_9PLEO
LinkDB: A0A178DT33_9PLEO
Original site: A0A178DT33_9PLEO 
ID   A0A178DT33_9PLEO        Unreviewed;       412 AA.
AC   A0A178DT33;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   SubName: Full=Ebp2-domain-containing protein {ECO:0000313|EMBL:OAL46754.1};
GN   ORFNames=IQ07DRAFT_545744 {ECO:0000313|EMBL:OAL46754.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL46754.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL46754.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL46754.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) 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}.
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DR   EMBL; KV441653; OAL46754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178DT33; -.
DR   STRING; 765867.A0A178DT33; -.
DR   InParanoid; A0A178DT33; -.
DR   OrthoDB; 11782at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..56
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..104
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..149
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   412 AA;  46300 MW;  8AA523C2EC304ADC CRC64;
     MGKSKLKSAL DHHKGRNIKL EKQRKHEKQV HKRKSKREAE EESDEEDNEE DGGVALPLDE
     VEVKVNGKAK KSKKTIAPEP APVADAEWET EGSEDDDSED GDDVLDQLTQ GLSRFEDSES
     DVSGDDDEDE EAEDDDEEED EEDIPLSDLD SVASEDKGDI IPHQRLTINN TTALTAALHR
     IQLPYSKLSF SEHQAVTTDE PVEIEDIEDD LNRELAFYKQ SLSAVKDARA RLKKEGVSFS
     RPADYFAEMV KSDEHMGKIK QKLIDAAAGK KAAAEARKQR DLKKFGKQVQ VAKMQERAKE
     KKDTMEKINQ LKRKRQGADI TTTNEEDLFD VGVNNDESKP SDRRRSTDGK TFNNKRQKKD
     QKYGFGGKKR HAKSNDAQSS GDGRDFSSRK MKGKSFGGAS KRPGKARRAK TH
//
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