ID   IPI1_KLULA              Reviewed;         381 AA.
AC   Q6CJZ2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Pre-rRNA-processing protein IPI1;
GN   Name=IPI1; OrderedLocusNames=KLLA0F14839g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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 RIX1 complex required for processing of ITS2
CC       sequences from 35S pre-rRNA. {ECO:0000250|UniProtKB:P38803}.
CC   -!- SUBUNIT: Component of the RIX1 complex, composed of IPI1, RIX1/IPI2 and
CC       IPI3 in a 1:2:2 stoichiometry. The complex interacts (via RIX1) with
CC       MDN1 (via its hexameric AAA ATPase ring) and the pre-60S ribosome
CC       particles. {ECO:0000250|UniProtKB:P38803}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38803}.
CC   -!- SIMILARITY: Belongs to the IPI1/TEX10 family. {ECO:0000305}.
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DR   EMBL; CR382126; CAG98455.1; -; Genomic_DNA.
DR   RefSeq; XP_455747.1; XM_455747.1.
DR   AlphaFoldDB; Q6CJZ2; -.
DR   SMR; Q6CJZ2; -.
DR   STRING; 28985.XP_455747.1; -.
DR   EnsemblFungi; CAG98455; CAG98455; KLLA0_F14839g.
DR   GeneID; 2894783; -.
DR   KEGG; kla:KLLA0_F14839g; -.
DR   eggNOG; KOG2149; Eukaryota.
DR   HOGENOM; CLU_050252_2_0_1; -.
DR   InParanoid; Q6CJZ2; -.
DR   OMA; CAGGWVK; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR   GO; GO:0097344; C:Rix1 complex; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0006267; P:pre-replicative complex assembly involved in nuclear cell cycle DNA replication; IEA:EnsemblFungi.
DR   GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:EnsemblFungi.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024679; Ipi1_N.
DR   InterPro; IPR037947; TEX10/Ipi1.
DR   PANTHER; PTHR16056:SF2; PTHR16056:SF2; 1.
DR   Pfam; PF12333; Ipi1_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..381
FT                   /note="Pre-rRNA-processing protein IPI1"
FT                   /id="PRO_0000308721"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  42601 MW;  01D9A08DF5B16CB1 CRC64;
     MAKKTVRQQD FMKRKLKVGK PKQKPSNVTD TSFQMKRISL PSQTKISSGS NGKSAGNGTG
     VLDLNQEVIK RVSLLRHHSD VTRKETVLYF ESMISRIIHL PSMNNLMQSS IPLMCDSSKQ
     VRDELANLLD TIGKHDANVL KLQIRAITLY LNNAMTHIIA PIQRDSGMFV QVVLKYCADE
     LVRHAWIKML KGFFQVLGWT IVTQGNNKAK GKSISMGITS SSVLSMNKNK KHKNENLKAM
     LQFIRAGVLG AAAIGHEDRN PEQGNGANSV SPLLQQRYVP YMIPEFPQPY AYLKLFTRQF
     AKGELTSTGA ETSSTDSGNM TLEELETLSC EDTHTRRMVF NQHFYPSIQR QLPALIKDGG
     ECGRTAHSFS STLEEILQIT V