ID   PESC_VANPO              Reviewed;         588 AA.
AC   A7TSA8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Kpol_359p6;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480504; EDO14845.1; -; Genomic_DNA.
DR   RefSeq; XP_001642703.1; XM_001642653.1.
DR   AlphaFoldDB; A7TSA8; -.
DR   SMR; A7TSA8; -.
DR   STRING; 436907.A7TSA8; -.
DR   EnsemblFungi; EDO14845; EDO14845; Kpol_359p6.
DR   GeneID; 5542873; -.
DR   KEGG; vpo:Kpol_359p6; -.
DR   eggNOG; KOG2481; Eukaryota.
DR   HOGENOM; CLU_019619_1_1_1; -.
DR   InParanoid; A7TSA8; -.
DR   OMA; TWIVPHY; -.
DR   OrthoDB; 777920at2759; -.
DR   PhylomeDB; A7TSA8; -.
DR   Proteomes; UP000000267; 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   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..588
FT                   /note="Pescadillo homolog"
FT                   /id="PRO_0000370504"
FT   DOMAIN          344..437
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   REGION          446..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          512..588
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03028"
FT   COMPBIAS        457..496
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   588 AA;  67249 MW;  AEDC3A79120A584E CRC64;
     MRIKKKNTSG NAKNFVTRSQ AVRKLQVSLA DFRRLCIFKG IYPREPRNKK KANKGSTAPT
     TFYYAKDIQY LMHEPVLNKF REHKTFAKKL TRALGRGEVS SAKKLDENRT SYKLDHIIKE
     RYPSFPDAVR DIDDALNMLF LFANLPATDQ VSSKITKDAN EICNQWLAYV ARERLVRKVF
     VSIKGVYYQA SIRGEDVRWL VPFKFPENIP SDIDFRIMLT FLEFYSTLLH FVLYKLYTDS
     DLVYPPKVDI AKNKIISGLS SYILESETEE NVLTATKLSE PTGETSNIDS ETLKLAMKAD
     ENVDDTNPED EQTENVETVE LDAFQDNNKN KGDILAQPSQ YESPVSTLFS DFVFYVGREV
     PIDILEFLIL SCGGSVISEA ALDKLETKDI DFSKVTHQIV DRPVLKNKVA GRTYIQPQWI
     FDCLNKAKLV PANLYLPGET LPPHLSPWGD ASGYDPNVSD AEEEGEDDED EDSEEGSGAE
     VEENVDEDED DEELRAQKEL ELEAQGVKYS DIKDTEVKSK NKKRKAASTE AEEEKDLKMI
     MMSNKQRKLY KKMKYSNAKK EEKVENLKKK KKQISKTKEK LTKLEGKK