GenomeNet

Database: UniProt
Entry: Q8SR49
LinkDB: Q8SR49
Original site: Q8SR49 
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   16-OCT-2019, entry version 102.
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};
GN   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.,
RA   Weissenbach J., 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
CC       60S ribosomal subunits. Binds 90S pre-ribosomal particles and
CC       dissociates from pre-60S ribosomal particles after processing of
CC       27SB pre-rRNA. Required for the normal formation of 18S rRNA
CC       through the processing of pre-rRNAs at sites A0, A1 and A2, and
CC       the normal formation of 25S and 5.8S rRNAs through the processing
CC       of pre-rRNAs at sites C1 and C2. {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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX55/SPB4
CC       subfamily. {ECO:0000305}.
DR   EMBL; AL590449; CAD25788.1; -; Genomic_DNA.
DR   RefSeq; NP_586184.1; NM_001042017.1.
DR   SMR; Q8SR49; -.
DR   PRIDE; Q8SR49; -.
DR   GeneID; 859833; -.
DR   KEGG; ecu:ECU10_0690; -.
DR   EuPathDB; MicrosporidiaDB:ECU10_0690; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   eggNOG; ENOG410XNT7; LUCA.
DR   HOGENOM; HOG000268803; -.
DR   InParanoid; Q8SR49; -.
DR   KO; K14809; -.
DR   OMA; IQFEDHM; -.
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: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   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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    463       ATP-dependent rRNA helicase SPB4.
FT                                /FTId=PRO_0000256047.
FT   DOMAIN       35    205       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      226    382       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      48     55       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF         4     32       Q motif. {ECO:0000305}.
FT   MOTIF       153    156       DEAD box. {ECO:0000305}.
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
//
DBGET integrated database retrieval system