ID   RIX1_DEBHA              Reviewed;         751 AA.
AC   Q6BUR3;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   24-JAN-2024, entry version 85.
DE   RecName: Full=Pre-rRNA-processing protein RIX1;
GN   Name=RIX1; OrderedLocusNames=DEHA2C08690g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382135; CAG86123.2; -; Genomic_DNA.
DR   RefSeq; XP_458056.2; XM_458056.1.
DR   AlphaFoldDB; Q6BUR3; -.
DR   SMR; Q6BUR3; -.
DR   STRING; 284592.Q6BUR3; -.
DR   GeneID; 2900509; -.
DR   KEGG; dha:DEHA2C08690g; -.
DR   VEuPathDB; FungiDB:DEHA2C08690g; -.
DR   eggNOG; ENOG502R65X; Eukaryota.
DR   HOGENOM; CLU_020084_1_0_1; -.
DR   InParanoid; Q6BUR3; -.
DR   OMA; WCGINLI; -.
DR   OrthoDB; 2014956at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
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   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.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ribosome biogenesis; rRNA processing.
FT   CHAIN           1..751
FT                   /note="Pre-rRNA-processing protein RIX1"
FT                   /id="PRO_0000308917"
FT   REGION          447..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          588..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          693..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..623
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..751
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  84823 MW;  222A04EFF6E8AEC5 CRC64;
     MSLPLDVILE DLESSPKSII PILATLHRDK AFLNDISKTD LKHLVSRSLN LSKSHIAYNK
     WCGINLIKVL SNNYNILANE GVNFMSQLIK ILENYNQSID PKILSSTVEC LNNLCNQIRG
     KPTLTREVLT PKLPTIITLF MEKVAYQPSL ILRSLNSLIR KHPTTFRPYG NKLRNRLIEL
     LSSESYSAFP QELKQIICET LATLPIIEKT EPEAKWQGDI VDIVKELSQV LLIYDEFLSL
     NDDSDLMELF KKIPRTRESE ESESSFKFAS LEIDINKPDT IFQISDRVEL LLSIMKAYLL
     SETQFSVRVP VGLVLIINEI ICSISTKFVP FRKDIRDEKV KKLIKSTTLL NQFNSIKLLS
     ELPIKYQGSL VPHLNNILAF LEILIPFSNK KIDYQEVLSN EIFMCRLLEC TGNFISLVSS
     LSDASLLIRF IDVALCLVEE RALNTSPVSD GKKQNQQANG NKKKNKKKNK ESVPLSDLLS
     HQHLFNETIP LSTLNATRRF LNMVITRVNL PPTQHYRVFR YMIIEATVAK SYNKDQNISQ
     ELKQLLINSV LYPGFEKNSM LPIITSLLGD DPLLSVFNNP RFPPLPTYIK KSGSVIEDDE
     EEEESENEDE EMEENENDGS LNVDEESQLE SSAKRRKIDI SESSAGGGSD QPETVLPGIV
     LEDTKTKEKI FTNVNPDSVI QFAETSEIVE DVVPEPEATR TEVVTKSSVG TIPTPENPVA
     TSVSVSVDKN EHDESDFEIP DIDVGDDSDD E
//