ID   ROK1_YEAS7              Reviewed;         564 AA.
AC   A6ZU15;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=ATP-dependent RNA helicase ROK1;
DE            EC=3.6.4.13;
DE   AltName: Full=Rescuer of KEM1 protein 1;
GN   Name=ROK1; ORFNames=SCY_1898;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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. This association requires the presence of RRP5.
CC       Interacts also with OSH3 (By similarity). {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; AAFW02000099; EDN61953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZU15; -.
DR   SMR; A6ZU15; -.
DR   PRIDE; A6ZU15; -.
DR   EnsemblFungi; EDN61953; EDN61953; SCY_1898.
DR   HOGENOM; CLU_003041_1_4_1; -.
DR   Proteomes; UP000007060; 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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..564
FT                   /note="ATP-dependent RNA helicase ROK1"
FT                   /id="PRO_0000310242"
FT   DOMAIN          153..333
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          344..506
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           122..150
FT                   /note="Q motif"
FT   MOTIF           280..283
FT                   /note="DEAD box"
FT   COMPBIAS        62..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         166..173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   564 AA;  63669 MW;  D1C2156E71751041 CRC64;
     MDIFRVLTRG ASVKKESGPK AKAADYSVIN GKDENHKEDN NESQIVKELD FFRNKRIISK
     VEDDREKTTE NDSPNKEEKS GNDDGLIKPV ITNTVEASAL RKSYKGNVSG IDIPLPIGSF
     EDLISRFSFD RRLLNNLIEN GFTEPTPIQC ECIPVALNNR DVLACGPTGS GKTLAFLIPL
     VQQIIDDKQT AGLKGLIISP TKELANQIFI ECFKLSHKIF LEKKRPLQVA LLSKSLGAKL
     KNKVVSDKKY DIIISTPLRL IDVVKNEALD LSKVKHLIFD EADKLFDKTF VEQSDDILSA
     CREPSLRKAM FSATIPSNVE EIAQSIMMDP VRVIIGHKEA ANTNIEQKLI FCGNEEGKLI
     AIRQLVQEGE FKPPIIIFLE SITRAKALYH ELMYDRINVD VIHAERTALQ RDRIIERFKT
     GELWCLICTD VLARGIDFKG VNLVINYDVP GSSQAYVHRI GRTGRGGRSG KAITFYTKQD
     SVAIKPIINV MKQSGCEVSE WMDKMAKMTR KEKESIKNGK AHKERKQITT VPKMDKAKRR
     RQQEMIAASK RRKNEELSKK HFSK