SPB4_DEBHA
ID SPB4_DEBHA Reviewed; 614 AA.
AC Q6BSM3;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=DEHA2D07744g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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-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; CR382136; CAG86941.1; -; Genomic_DNA.
DR RefSeq; XP_458797.1; XM_458797.1.
DR AlphaFoldDB; Q6BSM3; -.
DR SMR; Q6BSM3; -.
DR STRING; 4959.XP_458797.1; -.
DR PRIDE; Q6BSM3; -.
DR EnsemblFungi; CAG86941; CAG86941; DEHA2D07744g.
DR GeneID; 2901449; -.
DR KEGG; dha:DEHA2D07744g; -.
DR VEuPathDB; FungiDB:DEHA2D07744g; -.
DR eggNOG; KOG0345; Eukaryota.
DR HOGENOM; CLU_003041_26_4_1; -.
DR InParanoid; Q6BSM3; -.
DR OMA; DRAIHDK; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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 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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..614
FT /note="ATP-dependent rRNA helicase SPB4"
FT /id="PRO_0000232327"
FT DOMAIN 41..233
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 260..431
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 514..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 510..581
FT /evidence="ECO:0000255"
FT MOTIF 10..38
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 181..184
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 514..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 614 AA; 70389 MW; 9AB5F7CC840C5D1B CRC64;
METREGSLTW SVLKCDLHPW IKEAIKSLGY PTMTPVQAST IPLFSGNKDV VVEAVTGSGK
TLAFVIPVLQ KLSNRLYNID EEGENPEPVK KGHMLSIILS PTRELAKQIQ TVFDKVLEYI
PEDKATIKTQ LLVGSLSSVR EDIDYFLTNK THILIATPGR LLDFLSSNYV KTNSVEIAVL
DEADKLLDIS FERDVIKILK QLPKQRRTGL FSATISSAGD TIFRTGMANP VKIVVKSKNS
KNAAPTSLNV SYMHVEPETK ISALIALIKD YRFQKCIVYF PTCTSVKHFY SVFQTLVNVE
EEDRYKFFSL HGQLSTKPRL KTLQNFSEGD SMLHKHVLLT TDVAARGIDI PDVDLVIQLD
PPTDPDVFFH RSGRTGRANK VGQAIVMLNN NSREEDYVNF MEVKGMTMSN MECPNISKIH
DKFQKKFRKY MLEDRARHEL AIKSYVGFVR YYSKHMASSI FRLQTLDYVG LGKMYGLLRL
PKMPESRYIP NEEMPEDGWL GDVIDMDKYE YADKQKEESR KKNLEEDKAR KVHDAKKRKE
LKVKNEAWSS KTDKIETKQE RREKMKRKRE AIEKQLMDDS SSDEETKVDW KEMVKTNKKK
KTPSDSMQGS FDDL
