ID   RIX1_PICGU              Reviewed;         712 AA.
AC   A5DLL7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Pre-rRNA-processing protein RIX1;
GN   Name=RIX1; ORFNames=PGUG_04168;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408159; EDK40070.2; -; Genomic_DNA.
DR   RefSeq; XP_001483439.1; XM_001483389.1.
DR   AlphaFoldDB; A5DLL7; -.
DR   SMR; A5DLL7; -.
DR   STRING; 4929.XP_001483439.1; -.
DR   EnsemblFungi; EDK40070; EDK40070; PGUG_04168.
DR   GeneID; 5125598; -.
DR   KEGG; pgu:PGUG_04168; -.
DR   VEuPathDB; FungiDB:PGUG_04168; -.
DR   eggNOG; ENOG502R65X; Eukaryota.
DR   HOGENOM; CLU_020084_1_0_1; -.
DR   InParanoid; A5DLL7; -.
DR   OMA; WCGINLI; -.
DR   OrthoDB; 427039at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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..712
FT                   /note="Pre-rRNA-processing protein RIX1"
FT                   /id="PRO_0000308920"
FT   REGION          435..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..601
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..712
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   712 AA;  79400 MW;  6D1D12C9E6A56D8A CRC64;
     MLPLAVILSE LQEPKTIVPV LSSLRSGSPV WSNISGPDQK HLVSRTLNLT RSSIQFRRWF
     GINVIRVLAD NYKIMAGDGS QIIGQLLKLL EQCNQFTSAV YFKSLVECID HVCDSIRGKP
     TMTRELLTPN LPAIIGLYLE KFSHDPAYLV SRLAPYIRAH PTTFRPFGNK LRSKIMETIL
     SPAFSNFPDS SKDIFCNTLS TLCAVEKIEP EERWSSDLFS LIGELSNTLE IYGEFLNFED
     DAELGKLLKK IPRSSSGESE FPSLSIDIND PSSFYSLPER LDILLRLIRG YLSAPTSFVA
     KVPLGIIALV VEAVLSINSR FIPFKREIRD ESTKQIIRNT LQCAHSSALG LLKVLPSIFR
     GSLVPYMRRI LGLLETLIPM KKKSLDTDQI VANEQFICLV LDCVACNISL VSYYQDSTGL
     VRLIDAAMAI VQPRSSSNTS SNTANTISSN GKKKKKQASV PLADVLSHQH LFNISVSEST
     TNHVQSFVNT LISCADLPSA QHNKVCKFVI VEAVKASHHI QEGTVPKQLR NLLVNAVLHP
     GFETTSILPI VCSILKEDEL LSVFRNPRFP PVLKAVEVKE EEEEEEEEEE SEEEPEEAEE
     AEEVVNGSRT EREVAPETKE VEPENKRRKI EIPEAVSVEP QVSEPQISTS LQHSISNQPE
     PAEPKNLRAP EPVKQANNPK LTEPSAAKDL REDFSDDSDF EMPEIDVDSD DE