ID   ROK1_LODEL              Reviewed;         553 AA.
AC   A5E1N2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=ATP-dependent RNA helicase ROK1;
DE            EC=3.6.4.13;
GN   Name=ROK1; ORFNames=LELG_03519;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981527; EDK45340.1; -; Genomic_DNA.
DR   RefSeq; XP_001525591.1; XM_001525541.1.
DR   AlphaFoldDB; A5E1N2; -.
DR   SMR; A5E1N2; -.
DR   STRING; 379508.A5E1N2; -.
DR   EnsemblFungi; EDK45340; EDK45340; LELG_03519.
DR   GeneID; 5232406; -.
DR   KEGG; lel:LELG_03519; -.
DR   VEuPathDB; FungiDB:LELG_03519; -.
DR   eggNOG; KOG0344; Eukaryota.
DR   HOGENOM; CLU_003041_1_4_1; -.
DR   InParanoid; A5E1N2; -.
DR   OMA; IRAQHRI; -.
DR   OrthoDB; 400908at2759; -.
DR   Proteomes; UP000001996; 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   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..553
FT                   /note="ATP-dependent RNA helicase ROK1"
FT                   /id="PRO_0000294662"
FT   DOMAIN          151..327
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          338..502
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          528..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           120..148
FT                   /note="Q motif"
FT   MOTIF           274..277
FT                   /note="DEAD box"
FT   COMPBIAS        534..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   553 AA;  62110 MW;  98AC2CE9FCA28001 CRC64;
     MDIFRILSRG ASINKKKDQT STNSSLIKLS LPSTANKHEH LLDEVERETD FFRTKSHRKL
     DEPSSKILKS KNKDEERESV AEIVPPLELE SEEDARVFRN LHKSKVTGDD IPIPIGSFQD
     MIGRFKIDKR VLSNLLDAEF VEPTPIQCEA IPITLANRDL IACAPTGSGK TLAFLIPLLQ
     QLVSQNVLKN HGIRGLIISP TNELAVQIFQ QLEIISKGKG LNIAILSKQL AGKISNDVVK
     ASKYDILVST PLRLIDVVKL GKVDLSKVTQ LVIDEADKLF DHGFAEQTDE LLSHCTNVKI
     RKSMFSATIP SGVEEMAHSI MKDPIRVIIG HKEAASNTIE QKLVFTGNEE GKLLAIRQMI
     QNGEFKPPII IFLQSITRAK ALFHELVYDK LNVDVIHAER TPKQRDEVIK RFKNGDIWVL
     ITTDVLARGV DFKGVNMVIN YDVPQSAQAY VHRIGRTGRG GRSGKAVTFF TKEDDKAVKP
     IINVMKQSGC TDGLSDWMED LGKLSKREKR AVKTHEIERK KISTVPSVIK QKRKQRQNMI
     EASKRRKQAE SEQ