ID   RIX1_LODEL              Reviewed;         793 AA.
AC   A5E7U6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Pre-rRNA-processing protein RIX1;
GN   Name=RIX1; ORFNames=LELG_05685;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
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; CH981534; EDK47504.1; -; Genomic_DNA.
DR   RefSeq; XP_001523139.1; XM_001523089.1.
DR   AlphaFoldDB; A5E7U6; -.
DR   SMR; A5E7U6; -.
DR   STRING; 379508.A5E7U6; -.
DR   EnsemblFungi; EDK47504; EDK47504; LELG_05685.
DR   GeneID; 5230248; -.
DR   KEGG; lel:LELG_05685; -.
DR   VEuPathDB; FungiDB:LELG_05685; -.
DR   eggNOG; ENOG502R65X; Eukaryota.
DR   HOGENOM; CLU_020084_1_0_1; -.
DR   InParanoid; A5E7U6; -.
DR   OMA; WCGINLI; -.
DR   OrthoDB; 427039at2759; -.
DR   Proteomes; UP000001996; 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..793
FT                   /note="Pre-rRNA-processing protein RIX1"
FT                   /id="PRO_0000308919"
FT   REGION          452..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        631..646
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..793
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   793 AA;  88981 MW;  22D854549FF4520E CRC64;
     MSIINIVLEG ISENHSSQSI VPVLELLRND KTILSNISKL QLQQLVSRSL QLVRSSDSYS
     KWCGINLIHQ LSSNYVIVAQ SGVQFMSALI AVLESYNSTI NVLILRNCIE CLQVLMHEIR
     GKPALTREIL TPKLSTIITL VMGHIQFDAE TCLNLLYDVI LHHPNTFRPF ANKLRSKLLV
     FLKGGFGVEF VEMPTSLRKI ICQTMAILPI IEKNEPEAKW GNDVKNVISE VTGILNVFDE
     FFNFRDDSSL GKLISKLPGR GERAELGEGD RERVFDDLSI DFNEPRSLLA ISDQVETLLQ
     LLKHYLVGGG ITSVRLPLGL CLTLLEVVFS INARFLSYKS DVRDDEIRQL ISTVLNRVHT
     SGIELLSSLL QFRGALVPHL NQIWTMLEYL VPMIQNKRID AAEVVKNEAV FAKLVECVGL
     YLNLVGAVSD GASLVPFVDV ALTLVEPRKD SAGNMQQSAA DGQQKNQNKN KNQKNKIKKK
     NASSAPMSDI LSHEHLFQQT IPTQTLLAVQ YFFSQVITKV ELPSNQHYKT LRFIIRQCVE
     HKNSNLEQAV PKQLRDLLVN TVLYPGYDKN NALPIVSSIL IDDPIISVFN NPRLPALPKY
     HSMSTSMDNK DVTEVGLEQT TYQRNRNGDD DHDDDDDDDD DDDEEVSASK GSGKKLSAKE
     LAIQNLMREQ AERQKLDREK EANARIEKDA EHEATPSFAF QMEKRPREEI VEEVGKVEKK
     IKVGEHGLVK DTVLKSTVET VVDNKNDVAN VSKNDQAQDA VGADEDNEGS DFEIPEINME
     LDTDEEEEGE EAE