ID   PESC_XENTR              Reviewed;         580 AA.
AC   Q6DEV3; Q28JA9; Q6P1T6;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
GN   Name=pes1; ORFNames=TNeu102a04.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the PeBoW complex, which is required for
CC       maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_03028}.
CC   -!- SUBUNIT: Component of the PeBoW complex, composed of bop1, pes1 and
CC       wdr12. The complex is held together by bop1, which interacts with pes1
CC       via its N-terminal domain and with wdr12 via a high-affinity
CC       interaction between the seven-bladed beta-propeller domains of the 2
CC       proteins. The PeBoW complex associates with the 66S pre-ribosome.
CC       {ECO:0000255|HAMAP-Rule:MF_03028}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03028}.
CC   -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP-
CC       Rule:MF_03028}.
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; CR759982; CAJ82755.1; -; mRNA.
DR   EMBL; BC064875; AAH64875.1; -; mRNA.
DR   EMBL; BC076991; AAH76991.1; -; mRNA.
DR   RefSeq; NP_989410.1; NM_204079.1.
DR   AlphaFoldDB; Q6DEV3; -.
DR   SMR; Q6DEV3; -.
DR   DNASU; 395049; -.
DR   GeneID; 395049; -.
DR   KEGG; xtr:395049; -.
DR   CTD; 23481; -.
DR   Xenbase; XB-GENE-480670; pes1.
DR   InParanoid; Q6DEV3; -.
DR   OrthoDB; 777920at2759; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0070545; C:PeBoW complex; ISS:UniProtKB.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; ISS:UniProtKB.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   HAMAP; MF_03028; Pescadillo; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR010613; PES.
DR   PANTHER; PTHR12221; PTHR12221; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF06732; Pescadillo_N; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..580
FT                   /note="Pescadillo homolog"
FT                   /id="PRO_0000370448"
FT   DOMAIN          323..416
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   REGION          291..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..307
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..481
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        482..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        452
FT                   /note="P -> PE (in Ref. 2; AAH64875)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        460..466
FT                   /note="Missing (in Ref. 1; CAJ82755)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="K -> E (in Ref. 1; CAJ82755)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   580 AA;  68001 MW;  AB98ED3715A884AD CRC64;
     MGGLEKKKYE RGSATNYITR NKARKKLQLS LPDFRRLCIL KGIYPHEPKH KKKVNKGSTA
     PRTFYLLKDI KFLLHEPIVG KFREYKVFVR RLRKAYGKRE WDAVDRIRDN KPAYKLDHII
     KERYPTFIDA VRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLSVEFLN YVIASRSLRK
     VFLSIKGIYY QADILGQTVT WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ
     TLNLQYPPKL DYFSEADLKS DNEDKYALET EAYMEKLAAL SASLSRVIPS EPEEENEVDE
     FPADPENAGQ EEEQKKQLQE EEKHKSMFVG LKFFLNREVP RDALAFIIRS FGGEVSWDAS
     VCIGATYNSA NPSITHHIVD RPSIQTQIIN RYYLQPQWVF DCVNARMLLP VEDYFPGVLL
     PPHLSPFVQE KEGDYIPPEK LRLMALQKGE NPEDDDDDDE EDDEDEEEDD EDEDDEENEE
     EEEDKKLRHL ENKKVGQNKL NVRITAGKVK VEDRTQAAEQ EKTEEKRLAI MMMKKKEKYL
     YNKIMFGKKR KVREANKLAL KRKAHDESVK VERKKKAKKH