ID   RRP3_ENCCU              Reviewed;         400 AA.
AC   Q8SR63;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=ECU10_0440;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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; AL590449; CAD25763.1; -; Genomic_DNA.
DR   RefSeq; NP_586159.1; NM_001041992.1.
DR   AlphaFoldDB; Q8SR63; -.
DR   SMR; Q8SR63; -.
DR   STRING; 284813.Q8SR63; -.
DR   GeneID; 859808; -.
DR   KEGG; ecu:ECU10_0440; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_0440; -.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   InParanoid; Q8SR63; -.
DR   OMA; YDIELYQ; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
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..400
FT                   /note="ATP-dependent rRNA helicase RRP3"
FT                   /id="PRO_0000256036"
FT   DOMAIN          32..202
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          229..373
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           150..153
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   400 AA;  45226 MW;  8AAA2AAB33E4E957 CRC64;
     MEFGDLRIDE SLIKTCQEKG ITRPTEVQRQ VIPAVLGGGD VIAVSQTGSG KTLAFVLPIV
     SHLLQKNRSF YCLVVAPTRE LSSQIAECFN MFQATGLRVC LLVGGANFNV QANQLSKRPH
     VVVGTPGRIA EHVLKTKSFR TERVRKFVLD EADRFFEQDF VEDLETIIPS LREKRQTLLF
     TATMSDEISK LSSSILKRPK TIRTAEKYET VPALKEYYLF VAMKWKNSAL VELLEMSQGM
     SVIVFVSMCV TARVMSLALA RLGFCSEALH GELSQEKREE AMRSFKESRF NVLVCTDLGS
     RGLDISHVDL VINFDVPKSG KDYIHRVGRT ARAGRSGTAI TLVTQYDVEQ IQKIEFTLEK
     KLEEFKMMKK NFGTICARIE EAIQEAQETL KEERKRNRRP