SPB4_CRYNB
ID SPB4_CRYNB Reviewed; 748 AA.
AC P0CR09; Q55IR0; Q5KCY8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=CNBL2730;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAEY01000057; EAL17760.1; -; Genomic_DNA.
DR RefSeq; XP_772407.1; XM_767314.1.
DR AlphaFoldDB; P0CR09; -.
DR SMR; P0CR09; -.
DR EnsemblFungi; EAL17760; EAL17760; CNBL2730.
DR GeneID; 4939322; -.
DR KEGG; cnb:CNBL2730; -.
DR VEuPathDB; FungiDB:CNBL2730; -.
DR HOGENOM; CLU_003041_26_4_1; -.
DR Proteomes; UP000001435; Chromosome 12.
DR GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:EnsemblFungi.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
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:1902626; P:assembly of large subunit precursor of preribosome; IEA:EnsemblFungi.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IEA:EnsemblFungi.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
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; 2.
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 Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..748
FT /note="ATP-dependent rRNA helicase SPB4"
FT /id="PRO_0000410265"
FT DOMAIN 46..260
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 295..460
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 119..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..43
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 207..210
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 627..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 748 AA; 84251 MW; 2362764D5CBE590F CRC64;
MDAPVPAAPA FGGSWAKLNP PLSPWILDVI NSMGFKNMTP VQAGTIPRAV KNQDCVVEAV
TGSGKTLAFT IPVLERLSRR EEPYKKGEIA AIVVAPTREL ATQIHAVFHH FLSSLIPPES
EEETGDVEAH APPFASSSRS PSPQTPDKPL FPLPMLVTSG TPTPYETFQS THPSILIGTP
GRLAAFLLNP RGLAIVRVSE LDVLVLDEAD RLLSSPDHRR DVERIMRHLP KQRRTHLFSA
TMTDAVEEMI GLGLRNPVRI VVNLKDKRKD GEEPKERRTP MALQNTYLVC RHAEKTLQLI
RLLLCESTKH ERSKFIVYFS TCAAVDYFYR ILSRLPSLSK FHLTSFHGEL PPKIRETALS
TFTSHPSSHL SPAVLLCTDV AARGVDFLDI DVVIQYDAPT DPKTFSHRAG RTARAGRRGK
AVVLLGKGRE EDYVGTFQSA NAELMKRKRQ KAQRSILDFL NIRKIPLTKQ PYINAYLEEV
DTPQALDPEA TTLLHSIRQI ILTDRELSDK AAKSFVSAFR AYSKHEASFI FRTLDFDFNS
QAISFGLLRL PAMPEIKDWK KKKEAERQRL EKIKSEGGEV EEKEIIEWED AGVNWDTFAY
ASRQREAARL ATLAQRADNQ SSNDAARAEA RAKRKIKAEM REAWSEQKER KVRKEERKEK
KDAKKKYEWE LEQANGEGDR QSDLANIAKA QAERKKRRER EEESWDEEIG KEYKSLKREI
KEEKSVKESS KGGAGGGGIG GGMFDDLE
