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Database: UniProt
Entry: A0A162CF27_9CRUS
LinkDB: A0A162CF27_9CRUS
Original site: A0A162CF27_9CRUS 
ID   A0A162CF27_9CRUS        Unreviewed;       593 AA.
AC   A0A162CF27;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 24.
DE   RecName: Full=Pescadillo homolog {ECO:0000256|HAMAP-Rule:MF_03028};
GN   Name=EOG090X05E6 {ECO:0000313|EMBL:SVE79463.1};
GN   ORFNames=APZ42_019605 {ECO:0000313|EMBL:KZS15062.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS15062.1, ECO:0000313|Proteomes:UP000076858};
RN   [1] {ECO:0000313|EMBL:KZS15062.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS15062.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS15062.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SVE79463.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CA-CH-1 {ECO:0000313|EMBL:SVE79463.1}, CH-H-1
RC   {ECO:0000313|EMBL:SVE80092.1}, and FR-SA-1
RC   {ECO:0000313|EMBL:SVE80705.1};
RA   Cornetti L.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for maturation of ribosomal RNAs and formation of
CC       the large ribosomal subunit. {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   -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000256|HAMAP-
CC       Rule:MF_03028}.
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DR   EMBL; LRGB01000930; KZS15062.1; -; Genomic_DNA.
DR   EMBL; LR009844; SVE79463.1; -; mRNA.
DR   EMBL; LR010473; SVE80092.1; -; mRNA.
DR   EMBL; LR011086; SVE80705.1; -; mRNA.
DR   AlphaFoldDB; A0A162CF27; -.
DR   STRING; 35525.A0A162CF27; -.
DR   EnsemblMetazoa; XM_032938836.2; XP_032794727.1; LOC116931256.
DR   OrthoDB; 169151at2759; -.
DR   Proteomes; UP000076858; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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: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   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   2: Evidence at transcript level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03028};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858};
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}.
FT   DOMAIN          318..411
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          445..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..473
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..528
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..564
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..593
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  69306 MW;  241F487D64B9745F CRC64;
     MGAPMKKKYE AGEATKYITR AQALKKLQLN LKDFRRLCIL KGVYPREPNN RKKAQKGKLD
     KKTLYYVKDI RFLSHEPLIW KFRDFKIFMR KMKTAMEKGD KETVARLKEN KPSMKLDHLV
     KERYPTFMDA LNDLDDCLTL CFFYSTLPRD TKVPANLISL CRRLTVEFLH YVIAAKALRK
     VFISVKGIYY QIEIKGQPVT ILINHQRGFK PTSASDVDYR IMTNFVDFYT SMLGFINFRL
     YHSINLQYPP KLPGITVKED ATDEDAVEEY NELVAALNSS LVTNVPQAEE EVQIDEFPSA
     EGAEKLEEAK REAEAIERLK SLFKGLKFFI GREVPRESVV FVIRSCDGEA SWDPSIFAGA
     TYDETDESIT HQIVDRPSVD KQYLSRYYIQ PQWLFDCINF RRLLPVEDYF IGANLPPHIS
     PFVTERLGDY IPPERQMLLA LQRGETLPAE QEEEEEEDES EDDSSEEEEE EDKVEKKEPT
     KSQVVKEKKG MKVMRGRVEM PDVKGMEEED KEHYKFRELM IRNKDKRLYR SMMKNRKSRE
     REAKRLENKR KQHEKEEKDL KKSTSSGKAL TAKWSIQPQS ATSDTQTKKM KMV
//
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