ID   ROK1_PICST              Reviewed;         558 AA.
AC   A3GHW9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP-dependent RNA helicase ROK1;
DE            EC=3.6.4.13;
GN   Name=ROK1; ORFNames=PICST_81007;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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. {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; AAVQ01000002; EAZ62890.1; -; Genomic_DNA.
DR   RefSeq; XP_001386913.1; XM_001386876.1.
DR   AlphaFoldDB; A3GHW9; -.
DR   SMR; A3GHW9; -.
DR   STRING; 4924.XP_001386913.1; -.
DR   EnsemblFungi; EAZ62890; EAZ62890; PICST_81007.
DR   GeneID; 4851868; -.
DR   KEGG; pic:PICST_81007; -.
DR   eggNOG; KOG0344; Eukaryota.
DR   HOGENOM; CLU_003041_1_4_1; -.
DR   InParanoid; A3GHW9; -.
DR   OMA; IRAQHRI; -.
DR   OrthoDB; 400908at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
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..558
FT                   /note="ATP-dependent RNA helicase ROK1"
FT                   /id="PRO_0000285153"
FT   DOMAIN          151..329
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          340..504
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          26..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           120..148
FT                   /note="Q motif"
FT   MOTIF           276..279
FT                   /note="DEAD box"
FT   COMPBIAS        32..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..558
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   558 AA;  63183 MW;  EF073310DCE41928 CRC64;
     MDIFRILSRG ASLKKSKDVT TDYALPSAKQ QQYEQHKEDT LQHQVDKEID FFHTKKHNSS
     KSFDSTDSKH TKEEKKEKKE DEEAPPLEIQ TVEDSIKLRK ANHSKVTGED IPLPIGSFQD
     MIGRFRLDSK LLSNLLEAEF VEPTAIQCES LPISLSGRDL IACAPTGSGK TLAFLIPLIQ
     SLLVSSKGRP KNYGITGLVI SPTNELAIQI FQELQILTRG KKLNVAILSK QLANKLNNDI
     VKASKYDIIV STPLRLIDIV KNEKVDLSKV EQLVIDEADK LFDQGFVEQT DDILSHCTYT
     KIRKSMFSAT IPSGVEEMAH SIMRDPIRVI IGRKEAASNT IDQKLVFTGS EEGKLLAIRQ
     MIQEGEFKPP IIIFLQSIHR AKALFHELLY DKLNVDVIHA ERTPKQREEV IKRFKNGDIW
     VLITTDVLAR GVDFKGVNMV INYDVPQTAQ AYVHRIGRTG RGGKAGRAVT FFTKEDDQAV
     KPIINVMKQS GCEAGFSGWM ENMTKMSKNE KKKVKHKEID RKDISTVPKL VKHKRKQREQ
     MIEASKKRKQ EETRNALQ