ID   SPB4_ENCCU              Reviewed;         463 AA.
AC   Q8SR49;
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 SPB4 {ECO:0000305};
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:P25808};
GN   Name=SPB4 {ECO:0000250|UniProtKB:P25808}; OrderedLocusNames=ECU10_0690;
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-binding RNA helicase involved in the biogenesis of 60S
CC       ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates
CC       from pre-60S ribosomal particles after processing of 27SB pre-rRNA.
CC       Required for the normal formation of 18S rRNA through the processing of
CC       pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and
CC       5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
CC       {ECO:0000250|UniProtKB:P25808}.
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:P25808};
CC   -!- SUBUNIT: Component of pre-60S ribosomal complexes.
CC       {ECO:0000250|UniProtKB:P25808}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:P25808}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL590449; CAD25788.1; -; Genomic_DNA.
DR   RefSeq; NP_586184.1; NM_001042017.1.
DR   AlphaFoldDB; Q8SR49; -.
DR   SMR; Q8SR49; -.
DR   STRING; 284813.Q8SR49; -.
DR   PRIDE; Q8SR49; -.
DR   GeneID; 859833; -.
DR   KEGG; ecu:ECU10_0690; -.
DR   VEuPathDB; MicrosporidiaDB:ECU10_0690; -.
DR   HOGENOM; CLU_003041_1_3_1; -.
DR   InParanoid; Q8SR49; -.
DR   OMA; DRAIHDK; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000819; Chromosome X.
DR   GO; GO:0005730; C:nucleolus; 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; IPR025313; DUF4217.
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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 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..463
FT                   /note="ATP-dependent rRNA helicase SPB4"
FT                   /id="PRO_0000256047"
FT   DOMAIN          35..205
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          226..382
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          444..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           4..32
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           153..156
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        447..463
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         48..55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   463 AA;  52014 MW;  529C68CCD9CAEF79 CRC64;
     MGCKGIEDVA MNGRLKKEIE ENGFGKMTEV QLKCIPEVLK GKDVVVQSPT GTGKTMAFLA
     PILSCIYDGK GRGRPGVTAV VITPTRELAL QIREVAGLFD VKCECFIGGM SIEEDYKRMK
     EEFSIAVGTP GRLLEIVGKE TKKFSSLSHL VLDEADKLLG FGFEEKLMQL LAKLPRNRVT
     GLFSATRNDS VDKLSRVFLR NPVSINVGNN EMPVALEYIV VSPMEKLLVL MDIVTGRRCI
     VFFATCSEVD FFSGLVSRAG FGNICKIHGK ISQDERNRVY EEFFQRDGLL FCTDVAARGI
     DFRGVDLVVH FDVPKEYSSI VHRSGRTARN GSKGESVLFV MPNERAYVEF LKLKGIPAVE
     SSYRMKSSLS YQDIKSMISP ELLGLSVKAF VSYIRSYKEH FVSYILDYKG LDFDSLAELF
     FLERIPGMAE LRNVKFEKFT KPARDGKKRA LPKKKYRKKR AIK