PESC_YARLI
ID PESC_YARLI Reviewed; 590 AA.
AC Q6CDK0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Pescadillo homolog {ECO:0000255|HAMAP-Rule:MF_03028};
DE AltName: Full=Nucleolar protein 7 homolog {ECO:0000255|HAMAP-Rule:MF_03028};
GN Name=NOP7 {ECO:0000255|HAMAP-Rule:MF_03028};
GN OrderedLocusNames=YALI0B23342g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Component of the NOP7 complex, which is required for
CC maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S
CC ribosome. {ECO:0000255|HAMAP-Rule:MF_03028}.
CC -!- SUBUNIT: Component of the NOP7 complex, composed of ERB1, NOP7 and
CC YTM1. The complex is held together by ERB1, which interacts with NOP7
CC via its N-terminal domain and with YTM1 via a high-affinity interaction
CC between the seven-bladed beta-propeller domains of the 2 proteins. The
CC NOP7 complex associates with the 66S pre-ribosome. {ECO:0000255|HAMAP-
CC 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; CR382128; CAG83515.1; -; Genomic_DNA.
DR RefSeq; XP_501262.1; XM_501262.1.
DR AlphaFoldDB; Q6CDK0; -.
DR SMR; Q6CDK0; -.
DR STRING; 4952.CAG83515; -.
DR EnsemblFungi; CAG83515; CAG83515; YALI0_B23342g.
DR GeneID; 2906624; -.
DR KEGG; yli:YALI0B23342g; -.
DR VEuPathDB; FungiDB:YALI0_B23342g; -.
DR HOGENOM; CLU_019619_1_1_1; -.
DR InParanoid; Q6CDK0; -.
DR OMA; TWIVPHY; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
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:0070180; F:large ribosomal subunit rRNA binding; IEA:EnsemblFungi.
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:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Coiled coil; Nucleus; Reference proteome; Ribosome biogenesis;
KW rRNA processing.
FT CHAIN 1..590
FT /note="Pescadillo homolog"
FT /id="PRO_0000370505"
FT DOMAIN 337..446
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT REGION 297..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 489..589
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT COMPBIAS 303..318
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..497
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 590 AA; 67022 MW; AFC7C6262B1C908D CRC64;
MGQIKKKHTA GAARNFITRT QAIRKLQVSL ADFRRLCIFK GIYPREPRSK KKANKGSTAP
VTFYYAKDIQ YLLHEPVLDK FREHKTFAKK LTRALGRGDL HDAKRIDENR PRYHLDHIIK
ERYPTFMDAL RDIDDALSML FLFAALPASD DVSARLVSEA EAICTQWMAF VARERLVRKV
FVSIKGVYYS ANIRGVEVMW LVPFRFPQNI PADIDFRVML TFLEFYTTLL HFVLYKLYNE
NGLVFPPIIN STKLSGVGGI NAYVLESRQN AGVVPQIEGN SEAKVENVSA AVLSKAAKAD
AGEEEEVEEE EEVEDDGLDS FSAEKGDALA QPTFNSTAGQ LFSNFTIFIG REVPLDIIEF
LIIAFGGKVI SESAMDELID NEDETRGNVI DEKTLKQKFN LASVTHQITD RPTLREKVPG
RTYVQPQWVF DSINEGKLLP VSEYAPGERL PAHLSPWGDA GTYDPTADVS DASDDDEDDE
DIEVAPEDYD KDDEEEEAEA EAKQHQRELE AEAKGTKADP AAAPKKAKRK ADKMTKAEKQ
EEEDKKLRMI MMSNKQKKLY KKMQYSNDKK SDREAELKKR RKLNEKKEKR
