MRD1_CANGA
ID MRD1_CANGA Reviewed; 861 AA.
AC Q6FXP4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Multiple RNA-binding domain-containing protein 1;
GN Name=MRD1; OrderedLocusNames=CAGL0B04169g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380948; CAG58051.1; -; Genomic_DNA.
DR RefSeq; XP_445151.1; XM_445151.1.
DR AlphaFoldDB; Q6FXP4; -.
DR SMR; Q6FXP4; -.
DR STRING; 5478.XP_445151.1; -.
DR EnsemblFungi; CAG58051; CAG58051; CAGL0B04169g.
DR GeneID; 2886717; -.
DR KEGG; cgr:CAGL0B04169g; -.
DR CGD; CAL0127894; CAGL0B04169g.
DR VEuPathDB; FungiDB:CAGL0B04169g; -.
DR eggNOG; KOG0110; Eukaryota.
DR HOGENOM; CLU_008479_0_0_1; -.
DR InParanoid; Q6FXP4; -.
DR OMA; TALIEYC; -.
DR Proteomes; UP000002428; Chromosome B.
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; 3.
DR PROSITE; PS50102; RRM; 5.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW rRNA processing.
FT CHAIN 1..861
FT /note="Multiple RNA-binding domain-containing protein 1"
FT /id="PRO_0000081639"
FT DOMAIN 2..90
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 325..403
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 512..584
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 640..723
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 738..815
FT /note="RRM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 154..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 97323 MW; 239267D659D0D80C CRC64;
MSRVIVKGLP IYLTEPELQK HFNKRLITTH ATSNVDGLIT DLRILKNREG KSRRFAFIGY
KNEQDALDAV NYFDGSFIYT SKIEVDMAKS FADPRVPKSM KEKKREALKR LREKEEKLLE
EKNKKLKVQD TKSKINIDAE IEKDKQLKEF IETMKPSAQT SSWDKITETA EPESGLAEEQ
ELDDEESSNV NPLLKHALSM KKGDENDSDD EYMSFNNADS KAGSDESNEE EKMISLSELP
VQNEESSAEP KEDDGLAKNE EISDMDWIKQ RRVRIRENGE KVGEEFATNV QDKESEENSQ
ATPAEELQEE IPDEEQAIAK IQKTGRLFLR NILYSSTEDD FKKLFSPYGE LKEVHVAVDT
RTGNSKGFAY VLFAKPEEAV QAYIELDKQI FQGRLLHILA ADEMKDHRLD EFDLKNMPLK
KQRELKKKAA ASKATFSWNS LYMNQDAVLG SVAAKLGVQK ADLIDPENSN SAVKQALAEA
HVIGDVRKYF ETKGVDLTKF SNLKSPSQRD DRVILVKNFP FGTTREELGE LFVPFGKLER
LLMPPAGTIA IVQFRDIASG RSAFSKLAFK RFKGTVIYLE KGPKDCFTKA ASNEDAMEHD
EEKSAKEAGP SSADLLESVS SKKTEDKEDE DEQVVDGPTV SIFIKNLNFK TTSQQLTDRF
KVFSGFVVAQ VKTKPDPKQK NKVLSMGFGF VEFRTKEQAT AVISAMDGTV IDGHKIQLKL
SHRQGNAGSQ EKKKAKNGKI IVKNLPFEAT RKDVFELFNS FGQLKSVRVP KKFDKSARGF
AFVEFVLPKE AENAMDQLQG VHLLGRRLVM QPAEQEAANA EEELERMTKK VRKQAAVSEI
AAMTRNAGKR KLDMEDEEEE F
