ID A0A2K5ZLX7_MANLE Unreviewed; 589 AA.
AC A0A2K5ZLX7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Pescadillo homolog {ECO:0000256|HAMAP-Rule:MF_03028};
GN Name=PES1 {ECO:0000256|HAMAP-Rule:MF_03028,
GN ECO:0000313|Ensembl:ENSMLEP00000028804.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000028804.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000028804.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|HAMAP-Rule:MF_03028}.
CC -!- SUBUNIT: Component of the PeBoW complex, composed of BOP1, PES1 and
CC WDR12. Within the PeBoW complex BOP1 interacts directly with PES1 and
CC WDR12. The PeBoW complex also associates with the 66S pre-ribosome.
CC Interacts with IRS1 and UBTF. May interact with MAP1B.
CC {ECO:0000256|HAMAP-Rule:MF_03028}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC Rule:MF_03028}. Nucleus, nucleoplasm {ECO:0000256|HAMAP-Rule:MF_03028}.
CC Chromosome {ECO:0000256|HAMAP-Rule:MF_03028}. Note=Appears to localize
CC to the periphery of metaphase chromosomes during mitosis and to the
CC prenucleolar bodies that form in mitotic cells prior to the actual
CC nucleoli. {ECO:0000256|HAMAP-Rule:MF_03028}.
CC -!- PTM: Sumoylated. {ECO:0000256|HAMAP-Rule:MF_03028}.
CC -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000256|HAMAP-
CC Rule:MF_03028}.
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DR RefSeq; XP_011834448.1; XM_011979058.1.
DR AlphaFoldDB; A0A2K5ZLX7; -.
DR STRING; 9568.ENSMLEP00000028804; -.
DR Ensembl; ENSMLET00000052357.1; ENSMLEP00000028804.1; ENSMLEG00000038584.1.
DR GeneID; 105538979; -.
DR KEGG; mleu:105538979; -.
DR CTD; 23481; -.
DR GeneTree; ENSGT00390000002626; -.
DR OMA; QKVTWIV; -.
DR OrthoDB; 169151at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070545; C:PeBoW complex; IEA:Ensembl.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR CDD; cd17709; BRCT_pescadillo_like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 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; PESCADILLO - RELATED; 1.
DR PANTHER; PTHR12221:SF6; PESCADILLO HOMOLOG; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF06732; Pescadillo_N; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|HAMAP-Rule:MF_03028};
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_03028};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03028};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_03028};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_03028}; Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_03028}.
FT DOMAIN 322..415
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 294..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 519..546
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03028"
FT COMPBIAS 301..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..489
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 68330 MW; 4733B105224C5B5E CRC64;
MGGLEKKKYE RGSATNYITR NKARKKLQLS LADFRRLCIL KGIYPHEPKH KKKVNKGSTA
ARTFYLIKDI RFLLHEPIVN KFREYKVFVR KLRKAYGKSE WNTVERLKDN KPNYKLDHII
KERYPTFIDA LRDLDDALSM CFLFSTFPRT GKCHVQTIQL CRRLTVEFMH YIIAARALRK
VFLSIKGIYY QAEVLGQPIV WITPYAFSHD HPTDVDYRVM ATFTEFYTTL LGFVNFRLYQ
LLNLHYPPKL EGQAQAEAKA SEGTYALDSE SSMEKLAALS ASLARVVVPA TEEEAEVDEF
PTDREMSAQE EDRRKELEAQ EKHKKLFEGL KFFLNREVPR EALAFIIRSF GGEVSWDKSL
CIGATYDVTD SRITHQIVDR PGQQTSVIGR CYVQPQWVFD SVNARLLLPV AEYFPGVQLP
PHLSPFVTER EGDYVPPEKL KLLALQRGED PGNLNESEEE EEEDDDNEGD GDEEGKEEEE
EEEDAEAGSE KEEEARLAAL EEQRMEGKKP RVMAGTLKLE DKQRLAQEEE SEAKRLAIMM
MKKREKYLYQ KIMFGKRRKI REANKLAEKR KAHDEAMRSE KKAKKARPE
//
