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Database: UniProt
Entry: M3HLA2_CANMX
LinkDB: M3HLA2_CANMX
Original site: M3HLA2_CANMX 
ID   M3HLA2_CANMX            Unreviewed;       723 AA.
AC   M3HLA2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Pre-rRNA-processing protein RIX1 {ECO:0000256|ARBA:ARBA00021502};
GN   ORFNames=G210_1306 {ECO:0000313|EMBL:EMG48177.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG48177.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG48177.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003770}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RIX1/PELP1 family.
CC       {ECO:0000256|ARBA:ARBA00010511}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG48177.1}.
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DR   EMBL; AOGT01001213; EMG48177.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3HLA2; -.
DR   STRING; 1245528.M3HLA2; -.
DR   eggNOG; ENOG502R65X; Eukaryota.
DR   HOGENOM; CLU_020084_1_0_1; -.
DR   OMA; WCGINLI; -.
DR   OrthoDB; 2014956at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777}.
FT   DOMAIN          5..184
FT                   /note="Pre-rRNA-processing protein RIX1 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08167"
FT   REGION          436..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..723
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  81948 MW;  F43AFA2EA14B5456 CRC64;
     MSINIILEEI KDTPSSIIPI LSLLHNDKQI LTNLTKPELN HLISRTLNLV RSPQPYNKWC
     GINLIRVLVT DYTILASEGN NLISSLLKVL ESYNYTIDVK ILTSCIDAID VMSDLIRGKP
     TLTREILTPK LSSIIGYYFE YLHFAPHLVL TSLQKILKNH PTTFRPFGNK LSAKLVGLIN
     SPEFVNVPGD LQVAMYDTLA MLPVIEKTEP ETKWYGDVIN ILGEIGELVQ VYQEFLNFKD
     DQELINSLKK LRKPSVKILS DISIDFNRPK SILKISDNVN ILFGLLKSYL SVETPFSVKV
     PLGLVLTTCE VVCSINVKFL AFKGDIRDDT IKKLIQLSLV ENYKSAISVL STLTIFQGSL
     ISHMSTIWSI LETLIPYKNK RVVEKDVLDH ESLYDDLLNC MVDYLSLLGY VSDNTQLLRF
     VDLALILIEP RIKNNNSNND AQSKNSPNPS KKQPKKRKNT SAVPLSDILS HEHLFMDQIP
     TSTIKTVRSF INQIIAKVPQ LPPTQHYKIM RYVIIESIHA KYYNLKHVVP KELKALLIDA
     VLYPGYDKIS ILPIVSSILG DDRLLSVFNN PRFPPLPKYI NMSNQVDIDE EEDDEEEVVA
     VKSDSFSVES IENPFKKRKL EEEDTVVVEE PKVDDVEKPK VDDAEEVTKP ELVVADPKEI
     EEIPVAVEPE VQIEDKIEVD DVVDDIKPVA DIVPETKQEE SEDDESSDFE MPEINLDQDS
     DDE
//
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