ID   RIX1_CANGA              Reviewed;         767 AA.
AC   Q6FW61;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Pre-rRNA-processing protein RIX1;
GN   Name=RIX1; OrderedLocusNames=CAGL0D02706g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
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 and the nucleoplasmic transit of the pre-
CC       60S ribosomal subunits. Regulates pre-60S association of the critical
CC       remodeling factor MDN1. {ECO:0000250|UniProtKB:P38883}.
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:P38883}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38883}.
CC   -!- SIMILARITY: Belongs to the RIX1/PELP1 family. {ECO:0000305}.
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DR   EMBL; CR380950; CAG58444.1; -; Genomic_DNA.
DR   RefSeq; XP_445533.1; XM_445533.1.
DR   AlphaFoldDB; Q6FW61; -.
DR   SMR; Q6FW61; -.
DR   STRING; 284593.Q6FW61; -.
DR   EnsemblFungi; CAGL0D02706g-T; CAGL0D02706g-T-p1; CAGL0D02706g.
DR   GeneID; 2887183; -.
DR   KEGG; cgr:CAGL0D02706g; -.
DR   CGD; CAL0128053; CAGL0D02706g.
DR   VEuPathDB; FungiDB:CAGL0D02706g; -.
DR   eggNOG; ENOG502R65X; Eukaryota.
DR   HOGENOM; CLU_020084_0_0_1; -.
DR   InParanoid; Q6FW61; -.
DR   OMA; WCGINLI; -.
DR   Proteomes; UP000002428; Chromosome D.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR   GO; GO:0120330; C:rixosome complex; IEA:EnsemblFungi.
DR   GO; GO:0003682; F:chromatin binding; 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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR012583; RIX1_N.
DR   PANTHER; PTHR34105; PROLINE-, GLUTAMIC ACID- AND LEUCINE-RICH PROTEIN 1; 1.
DR   PANTHER; PTHR34105:SF1; PROLINE-, GLUTAMIC ACID- AND LEUCINE-RICH PROTEIN 1; 1.
DR   Pfam; PF08167; RIX1; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..767
FT                   /note="Pre-rRNA-processing protein RIX1"
FT                   /id="PRO_0000308916"
FT   REGION          699..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..767
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  87354 MW;  93062B59B8B3C9E5 CRC64;
     MNKAIPVSVL ADQLAESNGF QFHNILYHLK SSDYVDEKLL KSELSVLVVK IQKLLNSNSN
     YSIWKGCHAA VVICTYNPLV LMAYGGKLLD IVYQKLEIKV LQRSTNSLDA QGKQVLNSLV
     NAISVLMNLM RNKTGLSREF LVPKIKAIIP TLITLSQYEP ELVLPILRSL IFKHTTTFKP
     FNAKFKVILT QFLTEGFDTL NEHTQKLVCD CYAYLHMVKT QTYQQQDEHS SHHKTFQDEN
     WMNGMNAVLA EFKPLIELCG EILDFSQDEE LTKLIGKMVP LAAESTSIFR SLTMDMNKST
     TLYDIPKRID VLSKMLMSFI SVPTTYTIRI PLDKLNVTCS ALLSITSKHI PIKRELRRDI
     ELNATINDVF TKIQFAGIRL YSTMVSKFGN VCFSYLSDIF YALSLFIPFK EKSLNIDFEK
     CFALKREFLV VFDLVSKIIA NVGHQLTDID FLLQLIEIGL DLTEERSLIQ NVFQQTNAKK
     EQELSKTKNK NKKDNKRGSL ADLYVSGSQF TLACDLKTFD TLNKFFISII ANQKLATAQM
     TKLSRYAIFT AQTYKQNLGE VPTTFVELLR TLVIQPGNER VTILPMAVNI IKESSDDVFD
     ILSHPRLPMS ILHSIEKSTF DNGEDDEDDN PDLHANEKQQ EYNDQPVERS EQKVVDFVLE
     EPVAVDVKTK ETVQFKDGIT TSEDQVDTKR PRDEEFIIEK SSSAKKFRTE NQPETIPIGV
     SDETVYQETE KVTVNVDTSS NDNEDDEDDS DFEIPAIELS DDDDEDE
//