ID   A0A1G4KGF4_9SACH        Unreviewed;       408 AA.
AC   A0A1G4KGF4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   SubName: Full=LANO_0G04214g1_1 {ECO:0000313|EMBL:SCV03451.1};
GN   ORFNames=LANO_0G04214G {ECO:0000313|EMBL:SCV03451.1};
OS   Lachancea nothofagi CBS 11611.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCV03451.1};
RN   [1] {ECO:0000313|EMBL:SCV03451.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 11611 {ECO:0000313|EMBL:SCV03451.1};
RA   Devillers H.;
RL   Submitted (MAR-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; LT598453; SCV03451.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4KGF4; -.
DR   OrthoDB; 11782at2759; -.
DR   Proteomes; UP000189911; Chromosome g.
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..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..111
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..161
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   408 AA;  47438 MW;  B964B82DDECDFB23 CRC64;
     MAKGFKLKEM LSHQKEAAKA DRKESAKKAQ QKQILEKQQN TPLVVSHDDI VEKEALDAES
     KEEQPEVYQS KALSRKERRK QKKYEKKVQP EVNVEDAEDE EDEEDEDELE TNGRLDLDRL
     EMSEPEDEDD DEEEEDNDDE NEEQEEKEEE EEEDVPLSDV ELDSDADVVP HQKVTINNTK
     AMNHALERIQ LPWKKHTFQE HQSITSATNS DEGIKDIYDD TERELAFYRQ SLDAVTQAKQ
     KLQGLRVPFK RPLDYFAEMV KSDEHMDRLK SKLVNEASDR KAREDARKQR SLKKFGKQVQ
     NATLQSRLKD KKETLDRIKS LKQKRKHNEI DDAAFDVGVE EAASEKPEKR QKPNGKRLAK
     DSKYGQGGMK RFKRKNDAKS SSDVSDFSSN KMKGKTSRPG KNRRSKRF
//