ID   RIX1_ASHGO              Reviewed;         764 AA.
AC   Q75DU5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Pre-rRNA-processing protein RIX1;
GN   Name=RIX1; OrderedLocusNames=ABL072C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 616.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016815; AAS50699.2; -; Genomic_DNA.
DR   RefSeq; NP_982875.2; NM_208228.2.
DR   AlphaFoldDB; Q75DU5; -.
DR   SMR; Q75DU5; -.
DR   STRING; 33169.AAS50699; -.
DR   EnsemblFungi; AAS50699; AAS50699; AGOS_ABL072C.
DR   GeneID; 4618956; -.
DR   KEGG; ago:AGOS_ABL072C; -.
DR   eggNOG; ENOG502R65X; Eukaryota.
DR   HOGENOM; CLU_020084_0_0_1; -.
DR   InParanoid; Q75DU5; -.
DR   OMA; WCGINLI; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097344; C:Rix1 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:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012583; RIX1_N.
DR   Pfam; PF08167; RIX1; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..764
FT                   /note="Pre-rRNA-processing protein RIX1"
FT                   /id="PRO_0000308914"
FT   REGION          611..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..721
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..764
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   764 AA;  85366 MW;  EEC1C49C79EB2866 CRC64;
     MTSQVVPLST FVQHLESCEG YEFRTMIKML ASPAYAKQQL LKDELSVFMA KVLKLLRSKD
     DYQVWKGCHI ATVFCTYNPV VLCSFGGELM GILYRALEDA TKYYGDSVQT EQRKVMVRAL
     VKTLDTLMDL IRGKPSLTRE ALTPHLSAII PMLISFGRCE PNLSLPVIKK LLSKHSTTFR
     PHVGKLKQLL TELYGHYQSL DPVTRKVVCD TAAYLHLTQK PGNNANEHQA HHKSFPDEHW
     RAGLFSVLSQ FGPVVRLWGE ILDIGSDENL ARLLETLPRD TANDTSPLLP ALTVDINKPV
     TLWHISARLE QLTDMVESFI RLPTLFPTRI PLGELVKVSE ILLSLTTNYL PLKRGLRRDA
     ALTGSIRSAL PETQLQGIRL LRCLSDHIGK NLITYMPAIL SSMELFIPLK DKKTSIDYQK
     CVDLQNGLLQ LTALMNSIAQ HLGHKVEEMS LAIKLVDICA YIIEHKQNLD SAFSSTSGTA
     KAAGGAKKKE YKAKTGSMSD LFSHPHKFLH PVPLENYTVV NTYYNMALTH WKLPSTQQAK
     ITKYCIYYSL SFKEKLGYIP QTFIELLNTI VLFPGKDRFS ILPIAVHLLK ETGDPVFDVL
     CNPKLPLEMI QIRRQPTSSE DDTATSEAEE YAAPADQDDE HLSDDEHTTV DDGVATNAVM
     GLNNLVSSET LRSEQDSALE TQHPEQARTS NLVPDEASEG REDARIFKKR SSSDEQDPPS
     KRTRAVAAQT PVPAAVPVDN GEPESDDGSD FEIPEIELSD ADEE