ID   MRD1_KLULA              Reviewed;         878 AA.
AC   Q6CQR6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Multiple RNA-binding domain-containing protein 1;
GN   Name=MRD1; OrderedLocusNames=KLLA0D14949g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: Involved in pre-rRNA processing. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RRM MRD1 family. {ECO:0000305}.
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DR   EMBL; CR382124; CAH00819.1; -; Genomic_DNA.
DR   RefSeq; XP_453723.1; XM_453723.1.
DR   AlphaFoldDB; Q6CQR6; -.
DR   SMR; Q6CQR6; -.
DR   STRING; 28985.XP_453723.1; -.
DR   EnsemblFungi; CAH00819; CAH00819; KLLA0_D14949g.
DR   GeneID; 2893292; -.
DR   KEGG; kla:KLLA0_D14949g; -.
DR   eggNOG; KOG0110; Eukaryota.
DR   HOGENOM; CLU_008479_0_0_1; -.
DR   InParanoid; Q6CQR6; -.
DR   OMA; QMFRKFG; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0042134; F:rRNA primary transcript binding; IEA:EnsemblFungi.
DR   GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR   GO; GO:0034462; P:small-subunit processome assembly; IEA:EnsemblFungi.
DR   CDD; cd12568; RRM3_MRD1; 1.
DR   Gene3D; 3.30.70.330; -; 5.
DR   InterPro; IPR034482; Mrd1_RRM3.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 5.
DR   SMART; SM00360; RRM; 5.
DR   SUPFAM; SSF54928; SSF54928; 4.
DR   PROSITE; PS50102; RRM; 5.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..878
FT                   /note="Multiple RNA-binding domain-containing protein 1"
FT                   /id="PRO_0000081642"
FT   DOMAIN          2..90
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          330..408
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          516..588
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          651..734
FT                   /note="RRM 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          752..829
FT                   /note="RRM 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          118..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          852..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..175
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  99011 MW;  35625A409749337E CRC64;
     MSRVIVKGLP IYLKEDRLRD LIEKRLTQKH QSTDVQSYLS DVKLMKNRDG ESRRFAFIGF
     RDEEDAFDCV NYFNGTFVDT SKIEVSMAKS FADPRVPQPM REKRREALKR LREREELLLA
     DKKDSQKKQK SDSNNDGGKK HDIDAEIAKN KQLQEFINTM KPSSQVTSWE TVQSSKTQGE
     DEEAADDEVG EMSSNPLLSQ ALALKGNSRD ADEDTDMFKL PGNESDDEYV SLNGGSNNAN
     TDEPEPQMMS LDTFDTAGPT STDDMAKDEA VSDLDWLKNR RVRIKDGADT PVSKQQQQPD
     TEQQQPEETE VETSQESEEE KSLKKIRETG RLFLRNILYT ATEDDFRKLF SPYGELEEVH
     IAVDTRTGQS KGFAYVLFKN ADNAATAFVE LDKQIFQGRL LHILPADAKK SHKLDEFDLK
     NLPLKKQREL KRKANSAQQT FSWNSLYMNQ DAVLSSVADK LGMKKSELID AENSSSAVKQ
     ALAEASVIGD VRKFFETRGV DLTKFAQLKN SERDDRVILV KNFPYGTTRE EIAELFLPFG
     KLQRLLLPPS GTIAILQFRD VPAARAAFSK ISYKRFKDGI IYLEKGPSDC FTRDAQGDEL
     VESETDIQKA TAKEAKISGA DLLEAQSLPA ADKDDHDDDD DDDDVQAGPT VSIFIKNLNF
     STTSQQLTEK FKPFNGFVVA QVKTKPDPKQ PGKTLSMGFG FAEFKTKEQA NAVISAMEGT
     ILDGHKLQLK LSHRQGTSTT NASSKKKKKN QGKIIVKNLP FEATRKDVFE LFSSFGQLKS
     VRVPKKFDKS ARGFAFVEFL LPKEAENAMD QLQGVHLLGR RLVMEFVEQD PEDVEQQIEK
     MTRKVKKQVN TTKIANMRNS GKRKIDLDED DENDGLQG