ID   ROK1_COCIM              Reviewed;         730 AA.
AC   Q1E306; J3KAQ0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=ATP-dependent RNA helicase ROK1;
DE            EC=3.6.4.13;
GN   Name=ROK1; ORFNames=CIMG_03057;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704916; EAS32033.3; -; Genomic_DNA.
DR   RefSeq; XP_001243616.1; XM_001243615.1.
DR   AlphaFoldDB; Q1E306; -.
DR   SMR; Q1E306; -.
DR   STRING; 246410.Q1E306; -.
DR   PRIDE; Q1E306; -.
DR   EnsemblFungi; EAS32033; EAS32033; CIMG_03057.
DR   GeneID; 4564331; -.
DR   KEGG; cim:CIMG_03057; -.
DR   VEuPathDB; FungiDB:CIMG_03057; -.
DR   InParanoid; Q1E306; -.
DR   OMA; HKIKVTD; -.
DR   OrthoDB; 400908at2759; -.
DR   Proteomes; UP000001261; 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..730
FT                   /note="ATP-dependent RNA helicase ROK1"
FT                   /id="PRO_0000256043"
FT   DOMAIN          228..442
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          482..650
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          15..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           172..204
FT                   /note="Q motif"
FT   MOTIF           389..392
FT                   /note="DEAD box"
FT   COMPBIAS        15..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        661..717
FT                   /note="Basic and acidic 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   730 AA;  80375 MW;  C7DBC691ACC18D98 CRC64;
     MDAFKLLTRS IKLKGSQLGS SSISSHLPSA GEANNPQLFP ASEADKTRGT KRKRESGEDT
     ELPNEIPVPD FFGSGSTAAE SPKAQRKRVT GKDADAEGQH GEETSMPEEE RKSILKSHKI
     KMTDLRTPPF RAVDTDISGK KSKRKKKKVE EPPPLTRKQL KAAQRLYPEP LTSFDKLRTR
     YHISRRLSDN IASQGYTVPT EVQLGSLPLL LGNAPAPNER TADDESLRSQ SEREPDLLVV
     APTGSGKTLS FMIPLINKIM KHHHDNPGLK EILAIVVAPT KELVAQIVNE GRKLTAGTGV
     KVSAVRKGMR IVEERGQETR SLEEENDGDD STASSDEEIH SSEGEKSKDI PLTKSDILVC
     TPLVLANALS DGGKRDVAPL PSVQKLVLDE ADVLLDPLFR EQTLSIWRAC THPQLRVGLW
     SATMGSNIEE LTKSTIKERQ ELLGLKDESS LIRLVVGLKD TAIPNISHKL VYAATEQGKL
     LGLRQLLHPT STSSSTTHLR PPFLIFTQTI ARAIALHSEL MYDIPAEAGG SSRIAVLHSE
     LSDSKRSDVM AGFRKGEIWV LITTDLLARG VDFRGINGVV NYDIPNSSAS YVHRVGRTGR
     AGREGGVAVT FYTKEDIPYV KNIANVISAS ENLRGTEEGE RIPKWLLDAL PSLSKNDKKD
     LKKYGVKARR PSTISDKTTS KKTRISTKSG FDRRMDNKRK GAIKGSQRRK AREQLNDEES
     EDDVWNGIDD