ROK1_YEAST
ID ROK1_YEAST Reviewed; 564 AA.
AC P45818; D6VTY1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 190.
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; OrderedLocusNames=YGL171W; ORFNames=G1651;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8529880; DOI=10.1016/0378-1119(96)80010-2;
RA Song Y., Kim S., Kim J.;
RT "ROK1, a high-copy-number plasmid suppressor of kem1, encodes a putative
RT ATP-dependent RNA helicase in Saccharomyces cerevisiae.";
RL Gene 166:151-154(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896267;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1033::aid-yea983>3.0.co;2-v;
RA Klima R., Coglievina M., Zaccaria P., Bertani I., Bruschi C.V.;
RT "A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading
RT frames have been detected in the DNA sequence of an 8.8 kb fragment of the
RT left arm of chromosome VII of Saccharomyces cerevisiae.";
RL Yeast 12:1033-1040(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9154839; DOI=10.1128/mcb.17.6.3398;
RA Venema J., Bousquet-Antonelli C., Gelugne J.-P., Caizergues-Ferrer M.,
RA Tollervey D.;
RT "Rok1p is a putative RNA helicase required for rRNA processing.";
RL Mol. Cell. Biol. 17:3398-3407(1997).
RN [6]
RP FUNCTION.
RX PubMed=9848659; DOI=10.1017/s1355838298981511;
RA Torchet C., Jacq C., Hermann-Le Denmat S.;
RT "Two mutant forms of the S1/TPR-containing protein Rrp5p affect the 18S
RT rRNA synthesis in Saccharomyces cerevisiae.";
RL RNA 4:1636-1652(1998).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-166; LYS-172 AND ASP-280.
RX PubMed=10373593; DOI=10.1093/nar/27.13.2753;
RA Oh J.Y., Kim J.;
RT "ATP hydrolysis activity of the DEAD box protein Rok1p is required for in
RT vivo ROK1 function.";
RL Nucleic Acids Res. 27:2753-2759(1999).
RN [8]
RP INTERACTION WITH OSH3.
RX PubMed=12054531; DOI=10.1016/s0006-291x(02)00288-7;
RA Park Y.-U., Hwang O., Kim J.;
RT "Two-hybrid cloning and characterization of OSH3, a yeast oxysterol-binding
RT protein homolog.";
RL Biochem. Biophys. Res. Commun. 293:733-740(2002).
RN [9]
RP ASSOCIATION WITH THE 90S AND 40S PRE-RIBOSOMES, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12628929; DOI=10.1093/emboj/cdg121;
RA Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.;
RT "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.";
RL EMBO J. 22:1370-1380(2003).
RN [10]
RP FUNCTION.
RX PubMed=15013450; DOI=10.1016/j.bbrc.2004.01.039;
RA Yano T., Inukai M., Isono F.;
RT "Deletion of OSH3 gene confers resistance against ISP-1 in Saccharomyces
RT cerevisiae.";
RL Biochem. Biophys. Res. Commun. 315:228-234(2004).
RN [11]
RP FUNCTION.
RX PubMed=15358132; DOI=10.1016/j.bbrc.2004.07.065;
RA Kim J., Jeon S., Yang Y.-S., Kim J.;
RT "Posttranscriptional regulation of the karyogamy gene by Kem1p/Xrn1p
RT exoribonuclease and Rok1p RNA helicase of Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 321:1032-1039(2004).
RN [12]
RP INTERACTION WITH THE U3 SNORNA, AND ASSOCIATION WITH THE PRE-RIBOSOME.
RX PubMed=15523097; DOI=10.1093/nar/gkh904;
RA Vos H.R., Bax R., Faber A.W., Vos J.C., Raue H.A.;
RT "U3 snoRNP and Rrp5p associate independently with Saccharomyces cerevisiae
RT 35S pre-rRNA, but Rrp5p is essential for association of Rok1p.";
RL Nucleic Acids Res. 32:5827-5833(2004).
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. May also have a gene-
CC specific regulatory function since it affects nuclear fusion by
CC regulating KAR4 expression and contributes with KEM1 to ISP-1
CC sensitivity. {ECO:0000269|PubMed:10373593, ECO:0000269|PubMed:15013450,
CC ECO:0000269|PubMed:15358132, ECO:0000269|PubMed:9154839,
CC ECO:0000269|PubMed:9848659}.
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. {ECO:0000269|PubMed:12054531,
CC ECO:0000269|PubMed:15523097}.
CC -!- INTERACTION:
CC P45818; P38713: OSH3; NbExp=3; IntAct=EBI-15686, EBI-12630;
CC P45818; P53254: UTP22; NbExp=3; IntAct=EBI-15686, EBI-1878;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9154839}.
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; Z34901; CAA84384.1; -; Genomic_DNA.
DR EMBL; X85757; CAA59758.1; -; Genomic_DNA.
DR EMBL; Z72693; CAA96883.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07942.1; -; Genomic_DNA.
DR PIR; S59649; S59649.
DR RefSeq; NP_011344.1; NM_001181036.1.
DR AlphaFoldDB; P45818; -.
DR SMR; P45818; -.
DR BioGRID; 33082; 67.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-5111N; -.
DR IntAct; P45818; 21.
DR MINT; P45818; -.
DR STRING; 4932.YGL171W; -.
DR iPTMnet; P45818; -.
DR MaxQB; P45818; -.
DR PaxDb; P45818; -.
DR PRIDE; P45818; -.
DR TopDownProteomics; P45818; -.
DR EnsemblFungi; YGL171W_mRNA; YGL171W; YGL171W.
DR GeneID; 852704; -.
DR KEGG; sce:YGL171W; -.
DR SGD; S000003139; ROK1.
DR VEuPathDB; FungiDB:YGL171W; -.
DR eggNOG; KOG0344; Eukaryota.
DR GeneTree; ENSGT00550000074863; -.
DR HOGENOM; CLU_003041_1_4_1; -.
DR InParanoid; P45818; -.
DR OMA; IRAQHRI; -.
DR BioCyc; YEAST:G3O-30659-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SABIO-RK; P45818; -.
DR PRO; PR:P45818; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P45818; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IDA:SGD.
DR GO; GO:0048254; P:snoRNA localization; IMP:SGD.
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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..564
FT /note="ATP-dependent RNA helicase ROK1"
FT /id="PRO_0000055063"
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..45
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 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT MUTAGEN 166
FT /note="G->D: No cell growth and 2-fold decrease in ATPase
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:10373593"
FT MUTAGEN 172
FT /note="K->G,R,S,W: Slow cell growth."
FT /evidence="ECO:0000269|PubMed:10373593"
FT MUTAGEN 172
FT /note="K->L: No cell growth and drastic decrease in ATPase
FT activity in vitro."
FT /evidence="ECO:0000269|PubMed:10373593"
FT MUTAGEN 280
FT /note="D->A,V: Slow cell growth."
FT /evidence="ECO:0000269|PubMed:10373593"
SQ SEQUENCE 564 AA; 63653 MW; CACB950B8A15D5A2 CRC64;
MDIFRVLTRG ASVKKESGPK AKAADYSVIN GNDENHKEDN NESQIVKELD FFRNKRIISK
VEDDREKTTE NDSPNKEEKS GNDDGLIKPV ITNTVEASAL RKSYKGNVSG IDIPLPIGSF
EDLISRFSFD KRLLNNLIEN GFTEPTPIQC ECIPVALNNR DVLACGPTGS GKTLAFLIPL
VQQIIDDKQT AGLKGLIISP TKELANQIFI ECFKLSYKIF 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
