PESC_PLAF7
ID PESC_PLAF7 Reviewed; 643 AA.
AC Q8IIS5; A0A144A022;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
DE Short=PfPES {ECO:0000303|PubMed:14698441};
GN Name=PES {ECO:0000303|PubMed:14698441}; ORFNames=PF11_0090, PF3D7_1107700;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP INTERACTION WITH YVH1, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=14698441; DOI=10.1016/j.molbiopara.2003.11.005;
RA Kumar R., Musiyenko A., Cioffi E., Oldenburg A., Adams B., Bitko V.,
RA Krishna S.S., Barik S.;
RT "A zinc-binding dual-specificity YVH1 phosphatase in the malaria parasite,
RT Plasmodium falciparum, and its interaction with the nuclear protein,
RT pescadillo.";
RL Mol. Biochem. Parasitol. 133:297-310(2004).
CC -!- FUNCTION: Required for maturation of ribosomal RNAs and formation of
CC the large ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_03028}.
CC -!- SUBUNIT: Interacts with dual specificity protein phosphatase YVH1.
CC {ECO:0000269|PubMed:14698441}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14698441}. Nucleus,
CC nucleolus {ECO:0000255|HAMAP-Rule:MF_03028}. Nucleus, nucleoplasm
CC {ECO:0000255|HAMAP-Rule:MF_03028}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC including in rings, trophozoites and schizonts (at protein level)
CC (PubMed:14698441). Expression increases in trophozoites and schizonts
CC (PubMed:14698441). {ECO:0000269|PubMed:14698441}.
CC -!- SIMILARITY: Belongs to the pescadillo family. {ECO:0000255|HAMAP-
CC Rule:MF_03028}.
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DR EMBL; LN999945; CZT98743.1; -; Genomic_DNA.
DR RefSeq; XP_001347765.1; XM_001347729.1.
DR AlphaFoldDB; Q8IIS5; -.
DR BioGRID; 1206041; 1.
DR IntAct; Q8IIS5; 1.
DR STRING; 5833.PF11_0090; -.
DR PRIDE; Q8IIS5; -.
DR EnsemblProtists; CZT98743; CZT98743; PF3D7_1107700.
DR GeneID; 810641; -.
DR KEGG; pfa:PF3D7_1107700; -.
DR VEuPathDB; PlasmoDB:PF3D7_1107700; -.
DR HOGENOM; CLU_019619_1_0_1; -.
DR InParanoid; Q8IIS5; -.
DR OMA; TWIVPHY; -.
DR PhylomeDB; Q8IIS5; -.
DR Proteomes; UP000001450; Chromosome 11.
DR GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
DR GO; GO:0070545; C:PeBoW complex; IBA:GO_Central.
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: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); IEA:UniProtKB-UniRule.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:GeneDB.
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 SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..643
FT /note="Pescadillo homolog"
FT /id="PRO_0000370473"
FT DOMAIN 378..474
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 305..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 531..615
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 305..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 77180 MW; 86A0F6C6BB5EC494 CRC64;
MHIHKLKKKI KKKKEGKYLT KKHILRKLFL NEEEFRKLCI FKGIYPKDFK EIPLKYRKKF
YKHKVFYTRN DFLKLSHEKI INDFRKIKIY LKKYKKCKLT LEDFTRSKNI VANFPVYKLE
HIIKERYPIL SYAVDHLDDA LSCIIAYSQL PSNHKYGIKN NMVKTCEMLK DHFHYYVYKT
NRIKKAFISV KGYYLQAEIL KKKVTWIIPH IFTPYLDTSI DFKLISDFIE YYIALLKFVL
FKLYKLDNML YPPKQDNDLK NEKLAHLSYD KDYSTNENNI DINMNQELQS KCNVNTNEDL
NTCQEKTKEK NHKSDNNPHE HTTNIDNNNF NNIHLQDNCD LNKNEGKNLT NNIIHKNSEA
DNGHVHPDDH IDIDEHNKLK ELFKNHIFYI HNDMPFDVLS IIILSCGGKI SWNSRISPIH
YDDNNITHEI YEKDKNTIHL NNPENEYKRI HIQPQYIFDC LNEKNILPCS DYLTEKENLP
VHLSPFIEDE NFKNLVKKEE YTINKMLNQK IKEEQYKDFS KENNNIFKSP NYKEEEEEEN
DDRETANLIL NNKRQAALNN QLERENEDIN QLKENDTILN KQTDQTQILK TQNLKSQEQE
IQRHKIVLSK KKRKLFARID MAQKRQKATI DKFMKKINKN KSK
