MRD1_EMENI
ID MRD1_EMENI Reviewed; 819 AA.
AC Q5BGA9; C8VTG4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Multiple RNA-binding domain-containing protein 1;
GN Name=mrd1; ORFNames=AN0421;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000007; EAA66520.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF89520.1; -; Genomic_DNA.
DR RefSeq; XP_658025.1; XM_652933.1.
DR AlphaFoldDB; Q5BGA9; -.
DR SMR; Q5BGA9; -.
DR STRING; 162425.CADANIAP00002277; -.
DR EnsemblFungi; CBF89520; CBF89520; ANIA_00421.
DR EnsemblFungi; EAA66520; EAA66520; AN0421.2.
DR GeneID; 2876194; -.
DR KEGG; ani:AN0421.2; -.
DR VEuPathDB; FungiDB:AN0421; -.
DR eggNOG; KOG0110; Eukaryota.
DR HOGENOM; CLU_008479_0_0_1; -.
DR InParanoid; Q5BGA9; -.
DR OMA; TALIEYC; -.
DR OrthoDB; 1428854at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
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: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; 1.
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..819
FT /note="Multiple RNA-binding domain-containing protein 1"
FT /id="PRO_0000081641"
FT DOMAIN 4..76
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 295..373
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 478..550
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 592..675
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 697..774
FT /note="RRM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 80..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 91400 MW; 13BF1DA4720D1D4E CRC64;
MESTRVFVSG LPPTLTNDQL KKHFETRFHV TDAHVLPKRR IGFVGFKSSE AAQQAVSYFN
KTYMRMSKIS VDIAKPIDAE PAHRKDSRTA QPDDALGNNL KRKRDGDTIK DSKTQEYLSL
LQQPSKTRTW ANDDQLPDPD ETDSHAQEQE QPFDVDDQEE LTYAQRKKAK LGQDANESSH
VPVVAGYQPT TDESDGQPSP EKHEEELEDP QKDQAPVSDS DWLRSKTSRL LGLLDEDEQE
TFASPAAATN PTPIINSNVE KPEAESPEKP AESDLTKAPT AAEVDTNIEN IRISARLFVR
NLSYETKESE LEPVFSPFGK IEEIHVAFDT RFTTSKGFAY VQYADPDAAV EAYRNLDGKI
FQGRLLHILP ASQKKTYKLD EHELSKLPLK KQKQIKRKQE AASSTFSWNS LYMNADAVMS
SVAERIGVSK ADLLDPTSSD AAVKQAHAET HVIQETKAYF KANGVNLDAF KQRERGNLAI
LVKNFSYGTK TEDLRKLFEP FGQITRLLMP PSGTIAIVAF ARPDEAQKAF KSLAYRKLGD
SILFLEKAPK DLFEADVPPQ NPLPETKAVS QGFSTADTFA ADEGDEEVMA TATLFIKNLN
FSTTNQSLIE AFRPLDGFVS ARIKTKPDPK NPGQTLSMGF GFADFKTKAQ AQAALAVMNG
YTLDRHTLVV RASHKGMDAA EERRKEDTAK KIAARRTKII IKNLPFQATK KDVRSLFGAY
GQLRSVRVPK KFDRSARGFG FADFVSAREA ENAMDALKNT HLLGRRLVLE FANEEAIDAE
EEIQRIEKKV GEQLDRVKLQ KLTGAGRKKF TVGAQDDES
