ID   SPB4_NEOFI              Reviewed;         640 AA.
AC   A1D699;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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}; ORFNames=NFIA_064070;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027690; EAW21243.1; -; Genomic_DNA.
DR   RefSeq; XP_001263140.1; XM_001263139.1.
DR   AlphaFoldDB; A1D699; -.
DR   SMR; A1D699; -.
DR   STRING; 36630.CADNFIAP00005817; -.
DR   EnsemblFungi; EAW21243; EAW21243; NFIA_064070.
DR   GeneID; 4589661; -.
DR   KEGG; nfi:NFIA_064070; -.
DR   VEuPathDB; FungiDB:NFIA_064070; -.
DR   eggNOG; KOG0345; Eukaryota.
DR   HOGENOM; CLU_003041_26_4_1; -.
DR   OMA; DRAIHDK; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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; 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..640
FT                   /note="ATP-dependent rRNA helicase spb4"
FT                   /id="PRO_0000282706"
FT   DOMAIN          45..249
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          283..437
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          531..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          521..629
FT                   /evidence="ECO:0000255"
FT   MOTIF           14..42
FT                   /note="Q motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           197..200
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        539..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..595
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..632
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         58..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   640 AA;  71002 MW;  0560CEA14D5F0E65 CRC64;
     MAPKPPSGTS SRAWDAVTPA LSEWVLEAMS SMGFTRMTPV QASAIPLFMA HKDVVVEAVT
     GSGKTLSFLI PVVEKLLRLE EPIKKHHIGA IIISPTRELA SQIYNVLSSL LAFHPPSAAA
     INPSEDDDAP RPKFPSSTLK VVPQLLLGGS TTPAEDLSTF LKRSPNVLVS TPGRLLELLS
     SPHVHCPQSS FEMLVLDEAD RLLDLGFKET LQNILRRLPK QRRTGLFSAS VSEAVDQIVR
     VGLRNPVKVM VKVKGGSGVD DKRTPASLQM TYLTTPPSHK FAALKRILSS VQPTPLKTIF
     FVSTCSGVDY LSAILPLLLG DDFLLIPLHG KHQANVRQKN FNRFINSHDP AILLTTDVAA
     RGLDIPSVDL VVQIDPPSDP KSFIHRCGRA GRAGRRGLSV VLLHPGREED YVSFLEVRKT
     PVVPFSPLIT FSDADAAAAT ATARKAVLAD RALHDRGQKA FVSWFRSYSK HQASSIFRVS
     DLDWEALGKA WGLLKLPKMP ELRNFTGDKT LGVSLDWNNY AYKDKQREKR RKELLQEAAE
     SGATQSTSNK RRATESVAWS QQAESKNKKL KRREQKKSKH EKARWEKMTE EEKQKVLETE
     KMVEELRKKN EEERRLRRAA AKAAGAKADG DDEEEFQGFD