ID   PESC_PICST              Reviewed;         604 AA.
AC   A3LU56;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-MAY-2022, entry version 81.
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}; ORFNames=PICST_71704;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; CP000498; ABN66528.2; -; Genomic_DNA.
DR   RefSeq; XP_001384557.2; XM_001384520.1.
DR   AlphaFoldDB; A3LU56; -.
DR   SMR; A3LU56; -.
DR   STRING; 4924.XP_001384557.2; -.
DR   EnsemblFungi; ABN66528; ABN66528; PICST_71704.
DR   GeneID; 4839029; -.
DR   KEGG; pic:PICST_71704; -.
DR   eggNOG; KOG2481; Eukaryota.
DR   HOGENOM; CLU_019619_1_1_1; -.
DR   InParanoid; A3LU56; -.
DR   OMA; TWIVPHY; -.
DR   OrthoDB; 777920at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
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   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..604
FT                   /note="Pescadillo homolog"
FT                   /id="PRO_0000370501"
FT   DOMAIN          349..448
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   REGION          452..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          468..522
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   COILED          573..604
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   COMPBIAS        474..513
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   604 AA;  69132 MW;  7FC7B162DF0E41AC CRC64;
     MAKIKKRGVS GNAKNFITRT QAVKKLQVSL SDFRRLCIFK GIYPREPRNK KKANKGSTAP
     VTFYYAKDIQ YLSHEPVLAK FREHKTFAKK LQRALGRGEV SDAQKLEANR PKYTLEHIIK
     ERYPTFLDAL RDIDDPLNML FLFANMPATD KVSHRVTKEA EKLTNQWLAY VAKERLIKKV
     FVSIKGVYYQ ANVKGQEIRW LVPFKFPTNI PTDVDFRIML TFLEFYSTLL HFVLYRLYND
     SNLIYPPTID IEKLKGIGGL SSYVLQSKDQ GVSALLPQDK KIVEDDVSVQ GKELSTANIS
     KALEADNEGE EHEEVEQETV ENVELDKFEA SATKTAVDSL VQPSKYASPT STLFSKFIFY
     VGREVPLDIL ELCILSCGGS VVSEVALDDL KTNSPDAYKK LDLSNITHQI IDRPKILQKV
     AGRTYIQPQW IFDCINKSEL LPVNKYAPGE TLPPHLSPWG DAGSYNPEAE KVDQSENAEE
     EEEDEVDEDD EDADEDEEDE EEEDEEEDED LKAQKELELE AAGVKFSEIA EKEKKAAKKA
     SKKRPAEEDE EKELKKIMMT NKQRKLYKKM QYGIDKKETR TQELAKKKRK IEKTKAQLDK
     LSKK