ID   ROK1_NEOFI              Reviewed;         738 AA.
AC   A1D1E3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=ATP-dependent RNA helicase rok1;
DE            EC=3.6.4.13;
GN   Name=rok1; ORFNames=NFIA_009150;
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-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; DS027688; EAW22236.1; -; Genomic_DNA.
DR   RefSeq; XP_001264133.1; XM_001264132.1.
DR   AlphaFoldDB; A1D1E3; -.
DR   SMR; A1D1E3; -.
DR   STRING; 36630.CADNFIAP00001418; -.
DR   PRIDE; A1D1E3; -.
DR   EnsemblFungi; EAW22236; EAW22236; NFIA_009150.
DR   GeneID; 4591949; -.
DR   KEGG; nfi:NFIA_009150; -.
DR   VEuPathDB; FungiDB:NFIA_009150; -.
DR   eggNOG; KOG0344; Eukaryota.
DR   HOGENOM; CLU_003041_1_4_1; -.
DR   OMA; HKIKVTD; -.
DR   OrthoDB; 400908at2759; -.
DR   Proteomes; UP000006702; 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; 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..738
FT                   /note="ATP-dependent RNA helicase rok1"
FT                   /id="PRO_0000282702"
FT   DOMAIN          236..448
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          488..656
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          13..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          319..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           191..219
FT                   /note="Q motif"
FT   MOTIF           395..398
FT                   /note="DEAD box"
FT   COMPBIAS        17..38
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..342
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        664..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..730
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         249..256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   738 AA;  82229 MW;  3C91F9397D9A6872 CRC64;
     MDAFKLLTRA TKLKGGAAPS SAQSSTRLPS TGKAANPQLF RSSEADKVLE EARHGKKRKR
     VAGPEAAESD DDGAELNFFG SSKARRSSAS MAKEQEKEQQ EQQEHRDDTS DADDADEMDE
     VQCRTVLNAH KIKVTDMRDL EEIQTVRVES EEPKKKKKKR KQQEESTPAL TKKEQKKARR
     VYPQPLVSFK ELRTRYKISR RLAENIAEQG FSVPTEVQLG TLPLLLEGFK VSGNSKDAES
     IEPDLLVVAP TGSGKTLSFL IPVINKIVRH HHEQEEERGI FSVVVAPTKE LASQIVNEGR
     KLVHGTGVKI TLMKKGMRVV DREDDDDENS HSEDSEEGSE SEQDEPSTTR KKKGKAPVTK
     SDILVTTPLL LVNALSANRT KPMATLPLVR NIVLDEADVL LDELFRDQTL DIWRACTHPE
     LRASLWSATM GSNIEDLAKS TIKERKQAYD RTNSYPLLRL VVGLKDSAIP NIEHKLVYAA
     TEQGKLLGLR QLLHPAAASA SDVRLRPPFL IFTQTIPRAI ALHSELRYDI PAEAGGSSRI
     AVLHSDLSDG QRSEIMKNFR KGEIWILVTT DLLARGVDFR GINGVVNYDI PNSAAVYVHR
     VGRTGRAGRE GGIAVTYYTK EDIPYVKSIA NIIDVSEKLR GKDGEKSIQK WLLDALPDLS
     KKDKKELKKH GVKARQSNLK SVKDDKEHRK TRISTKSGFD RRMENKKKAL IAASRNRKSK
     TQSTDPGSDN ESWDGLDG