RRP3_YARLI
ID RRP3_YARLI Reviewed; 480 AA.
AC Q6CH58;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=ATP-dependent rRNA helicase RRP3 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P38712};
GN Name=RRP3 {ECO:0000250|UniProtKB:P38712}; OrderedLocusNames=YALI0A12133g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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: ATP-dependent rRNA helicase required for pre-ribosomal RNA
CC processing. Involved in the maturation of the 35S-pre-rRNA and to its
CC cleavage to mature 18S rRNA. {ECO:0000250|UniProtKB:P38712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P38712};
CC -!- SUBUNIT: Interacts with the SSU processome.
CC {ECO:0000250|UniProtKB:P38712}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382127; CAG83933.1; -; Genomic_DNA.
DR RefSeq; XP_500004.1; XM_500004.1.
DR AlphaFoldDB; Q6CH58; -.
DR SMR; Q6CH58; -.
DR STRING; 4952.CAG83933; -.
DR EnsemblFungi; CAG83933; CAG83933; YALI0_A12133g.
DR GeneID; 2906192; -.
DR KEGG; yli:YALI0A12133g; -.
DR VEuPathDB; FungiDB:YALI0_A12133g; -.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; Q6CH58; -.
DR OMA; YDIELYQ; -.
DR Proteomes; UP000001300; Chromosome A.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR CDD; cd17954; DEADc_DDX47; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044765; DDX47/Rrp3_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..480
FT /note="ATP-dependent rRNA helicase RRP3"
FT /id="PRO_0000232280"
FT DOMAIN 95..266
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 277..437
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 64..92
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 214..217
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 480 AA; 53192 MW; 887C459C11232589 CRC64;
MAKATEKRVK RAKKEESGSE SEDNDAIAQE ILDTTKSDNE EEEPKKSSKN YTSVEVDESE
EQTKTFKDLG VIDSICETCE ELKFTKPTPI QAQSIPYALE GRDIIGLAQT GSGKTAAFAI
PVLQSLYENP QPLYCVVLAP TRELAYQISE TFEALGSAMG LRTAVVVGGM NMMTQAVALS
KKPHVIVATP GRLVDHLENT KGFSLRTLKF LVMDEADRLL DMEFGPSLDK ILKVIPRQRN
TYLFSATMTS KVEKLQRASL VDPVRVAVST KYQTADNLLQ YMVFCPFKHK DTHLVYLVSE
NAGNSMIIFA RTKSDTQRIS LLLRNLGYGA IPLHGDLSQT ARLGALNKFK SGSRNILIAT
DVASRGLDIP AVDLVINYDI PSDSKSYIHR VGRTARAGRA GKSVALVSQY DLELYLRIEG
ALGKKLDSYP LESEAVMLFS ERVAEASRAA IQEMKGEDGT KKRSKFDKKR RRDEMDIGEQ
