ID   PESC_SALSA              Reviewed;         582 AA.
AC   B5X171;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
GN   Name=pes1;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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}.
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DR   EMBL; BT044790; ACI33052.1; -; mRNA.
DR   RefSeq; NP_001133338.1; NM_001139866.1.
DR   AlphaFoldDB; B5X171; -.
DR   SMR; B5X171; -.
DR   STRING; 8030.ENSSSAP00000076846; -.
DR   GeneID; 100194837; -.
DR   KEGG; sasa:100194837; -.
DR   CTD; 30228; -.
DR   OrthoDB; 777920at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa20.
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: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   Coiled coil; Nucleus; Reference proteome; Ribosome biogenesis;
KW   rRNA processing.
FT   CHAIN           1..582
FT                   /note="Pescadillo homolog"
FT                   /id="PRO_0000370446"
FT   DOMAIN          323..416
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   REGION          294..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          277..329
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   COILED          517..582
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   COMPBIAS        454..476
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..574
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   582 AA;  68478 MW;  4A7B18DFE39CDF60 CRC64;
     MGGLQKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH KKKVNKGSTA
     PRTFYLLKDI RFLLHEPIVR KFREYKVFVR KLRKAYGKAE WTGVERLRDN KPGYKLDHII
     KERYPTFIDA LRDIDDALSM CFLFSTFART GKCHVQTITL CRRLTVEWMN YVVTSRSLRK
     VFLSIKGIYY QAEVLGQLIT WLVPYQFAHD HPTDVDYRVM ATFTEMYTTL FGFINFRLYQ
     TLNLVYPPKL DSKAESELKA EHEEDYAMDS ESYLEKLSAL SASLARVVAT VEEEENQLDN
     FPTEEEDQEN MQAREKEQKE QEAQKRLFEG LKFFLNREVP RESLAFILRC FGAEVSWDKS
     LCIGGTYEVT DETITHQIVD RPDMDKQYIN RYYIQPQWVF DSVNAKMRLP VEDYFLGTML
     PPHLSPFVEE KDGDYVPPEK LKLMALQRGE KPVQEEDEEE EDEDEEEDDD VDDEEFTEEK
     NLKKMEDTRA QGKTLSVKVT PGKVKPWETG SVGNKVRLEQ EEKAEEKRLA IMMMKKKEKY
     LYDKIMFGKK RTTREVNKLT AKRKAHEDAS KAQKKQKKAK KQ