MRD1_ASHGO
ID MRD1_ASHGO Reviewed; 838 AA.
AC Q75A83;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Multiple RNA-binding domain-containing protein 1;
GN Name=MRD1; OrderedLocusNames=ADR035C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 517 AND 550-551.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51955.2; -; Genomic_DNA.
DR RefSeq; NP_984131.2; NM_209484.2.
DR AlphaFoldDB; Q75A83; -.
DR SMR; Q75A83; -.
DR STRING; 33169.AAS51955; -.
DR EnsemblFungi; AAS51955; AAS51955; AGOS_ADR035C.
DR GeneID; 4620280; -.
DR KEGG; ago:AGOS_ADR035C; -.
DR eggNOG; KOG0110; Eukaryota.
DR HOGENOM; CLU_008479_0_0_1; -.
DR InParanoid; Q75A83; -.
DR OMA; TALIEYC; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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 InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 5.
DR SMART; SM00360; RRM; 5.
DR SMART; SM00361; RRM_1; 2.
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..838
FT /note="Multiple RNA-binding domain-containing protein 1"
FT /id="PRO_0000081636"
FT DOMAIN 2..88
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 301..379
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 488..560
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 612..695
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 712..789
FT /note="RRM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 195..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 94017 MW; B7F53ABA7707AC06 CRC64;
MSRVIVKGLP IYLEEARLRA HFLKRLQQQG RGSEDQITDV KIVKDKSGNS RRFAFIGYRS
EQDAFDAIEY FNGSFIDTAR IEVAMAKSFA DPRVPTPMRE KRREALKRLR EREDRILAEK
RQKQTKPQHG IDAEISKNKQ LQEFIETMNP KMAAAAANPM ARAAEQPASA NPLLSALHGA
EDDEEVDMFQ LSEQESDDEY TDLHQRPQSA EEDELEEPAV GQDLDAAPAP DAAEDGMATN
QEVSDLEWLK NRRIRIRDGE DAEAAPAPQE QAAEEPAEQE VPQEDEVSAE EAALTKIRAT
GRLFLRNILY DATEEDFKQL FSPYGELEEV HVAVDTRTGQ SKGFAYVLFK DPEHAANAYI
ELDKQIFQGR LLHILPADAK KTHRLDEFDL KNLPLKKQRE LKRKATAAQQ TFSWNSLFMN
QDAVLSSVAA KLGMEKSQLI DPENSGSAVK QALAEAHVIG DVRKYFEARG VDLTQFEKFK
KVTERDDRII LVKNFPHGTT REELAELFLP FGKIERLLMP PSGTIAIIQY RDVPAARGAF
TKLSYKRFKE AILYLEKGPK DCFSREPRGD ELLEGDAAPE DVKEIKKSVE DVMDADSKTP
SSEATAIDGP TVSIFVKNLN FSTTSAQLAE KFKPFSGFVV AQVKTKPDPK NSDKKLSMGF
GFIEFRTKEQ AGAVIAAMDG AVIDGHKIQL KISHKQSSLP KTSKGSKKKI SGKIIVKNLP
FEATRKDVFE LFSSFGQLKS VRVPKKFDKS ARGFAFVEFL LPSEAENAMD QLQGVHLLGR
RLVMQYAEQE SDDVEEQISK MTMKMKKQAA VSKMGALRNS GKRKIDMSDD ENDGLNGF
