ID   ROK1_ASPCL              Reviewed;         738 AA.
AC   A1CNK1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=ATP-dependent RNA helicase rok1;
DE            EC=3.6.4.13;
GN   Name=rok1; ORFNames=ACLA_019270;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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-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}.
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DR   EMBL; DS027059; EAW07222.1; -; Genomic_DNA.
DR   RefSeq; XP_001268648.1; XM_001268647.1.
DR   AlphaFoldDB; A1CNK1; -.
DR   SMR; A1CNK1; -.
DR   STRING; 5057.CADACLAP00002677; -.
DR   EnsemblFungi; EAW07222; EAW07222; ACLA_019270.
DR   GeneID; 4701754; -.
DR   KEGG; act:ACLA_019270; -.
DR   VEuPathDB; FungiDB:ACLA_019270; -.
DR   eggNOG; KOG0344; Eukaryota.
DR   HOGENOM; CLU_003041_1_4_1; -.
DR   OMA; HKIKVTD; -.
DR   OrthoDB; 400908at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
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; 2.
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..738
FT                   /note="ATP-dependent RNA helicase rok1"
FT                   /id="PRO_0000282699"
FT   DOMAIN          231..447
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          487..655
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           190..218
FT                   /note="Q motif"
FT   MOTIF           394..397
FT                   /note="DEAD box"
FT   COMPBIAS        13..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..339
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        663..710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         244..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   738 AA;  82019 MW;  266B789BF867EE85 CRC64;
     MDAFKLLTRA TKLKTGATPS SAQSSTRLPS TGKAENPQLF RNSEAEKVLE QAQQGKKRKR
     TAAAEARDAD DDAAELNFFG ARKAAVSSTP TSKEEKQEQE RSGEDDASDE EVEFMDEVQR
     RTVLNAHKIK VTDLRDLEEI QPVRVASEEP KKKKKKRKQQ EEEESKVPLT KKEQKKARRL
     YPEPLVSFKE LRSKYKISSR LAENIAEQGF TVPTEVQLGT LPLLLGGFES KAGESVEPDL
     LVVAPTGSGK TLSFLIPVIN KIVRHHHDQS QEQERGIFSI IVAPTKELAS QIVNEGRKLV
     HGTGVKIALM KKGMRVVERE DEDDDGDDSS SEDGDESSES EHEERPIAKK SKGKAPVTKS
     DILVTTPLQL VNALSTNQTK PMATLPLVRN IVLDEADVLL DPLFRDQTLN IWRACTHPEL
     RASLWSATMG SNVEDLAKST IKERKEAVNQ TKSYPLLRLV VGLKDSAIPN IEHKLIYAAT
     EQGKLLGLRQ LLHPTAASAS DVRLRPPFLI FTQTIPRAVA LHSELRYDIP TEAGGSSRIA
     VLHSDLSDGQ RSEIMKNFRK GEIWILVTTD LLARGVDFRG INGVVNYDIP NSAAVYVHRV
     GRTGRAGREG GIAVTYYTKE DIPYVKSIAN IIDVSEKLRG KTGEKSIQKW LLDALPDLSK
     KDKKELKKHG VKARQSNLKS DKDDKEHRKT RISTKSGFER RIENKKKALI AANRNRKSQA
     QSAADGDSGN ESWDGLEN