ID   ROK1_ASPNC              Reviewed;         729 AA.
AC   A2QAB5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=ATP-dependent RNA helicase rok1;
DE            EC=3.6.4.13;
GN   Name=rok1; ORFNames=An01g10870;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC       biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC       sites A0, A1, and A2, leading to mature 18S rRNA.
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   -!- SUBUNIT: Interacts with the U3 snoRNA and is associated with the 90S
CC       and 40S pre-ribosomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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. DDX52/ROK1
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK37267.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM269980; CAK37267.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001389504.2; XM_001389467.2.
DR   AlphaFoldDB; A2QAB5; -.
DR   SMR; A2QAB5; -.
DR   PaxDb; A2QAB5; -.
DR   EnsemblFungi; CAK37267; CAK37267; An01g10870.
DR   GeneID; 4977763; -.
DR   KEGG; ang:ANI_1_1466014; -.
DR   Proteomes; UP000006706; Chromosome 2R.
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:0030490; P:maturation of SSU-rRNA; IEA:InterPro.
DR   CDD; cd17957; DEADc_DDX52; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR044764; DDX52/Rok1_DEADc.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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..729
FT                   /note="ATP-dependent RNA helicase rok1"
FT                   /id="PRO_0000282700"
FT   DOMAIN          228..441
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          481..649
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          15..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           183..211
FT                   /note="Q motif"
FT   MOTIF           388..391
FT                   /note="DEAD box"
FT   COMPBIAS        45..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..334
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         241..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   729 AA;  80734 MW;  86A8998A74856857 CRC64;
     MDAFKLLTRS TKFKAGNSLS STLPSKGKAE NPQLFRDAEA EKLLESNAFG KKRKRTQAAG
     DSDAEDGNAG DLDFFGSGKR SAASAPSKKD EDGPSEQKDA SDSEGDDSMD EVERRTILNS
     HKIKVTDMRD FEELQPTQPQ KEESKKKKKK RKQQEEEPAQ TLTKKEQKKA RRLFPEPLVS
     FKQLRTKYNI SRRLAENIAE QGFTVPTEVQ LGSLPLLLGD QSVPQKSGTE KSTEPDLLVV
     APTGSGKTLS FMIPVINKIV RHHHEKPEER GILSVVIAPT KELASQIVNE GRKLALGTGV
     KITLMKKGMR VVERDDEDDS KDVLDEDDSE SLGSEDDEKA TAKNSKGKAP VTKSDILVTT
     PLLLVNALSA NRTKPLATLP LVRNVVLDEA DVLLDPLFRD QTLDIWRSCT HPELRASLWS
     ATMGSNVEDL AKSTIKERKD TLSETKSYPL LRLVVGLKDS AIPNIKHKLV YAATEQGKLL
     GLRQLLHPAA ASSTDIRLRP PFLIFTQTIP RAVALHSELR YDIPPEAGGS SRIAVLHSEL
     SDGQRSEIMK QFRKGEIWIL VTTDLLARGV DFRGINGVVN YDIPNSAAVY VHRVGRTGRA
     GREGGIAVTY YTKEDIPYVK SIANVIDVSE KLRGTDEEKS VQKWLLDALP DLSKKKKEEL
     KKHGVKARQT QGTKDDKKTR ISTKSGYERR QENKKKALIS ASRNRKSQPK SGADSGSDDD
     NQGWQGLED