ROK1_DEBHA
ID ROK1_DEBHA Reviewed; 550 AA.
AC Q6BP45;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=ATP-dependent RNA helicase ROK1;
DE EC=3.6.4.13;
GN Name=ROK1; OrderedLocusNames=DEHA2E16632g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(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.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382137; CAG88281.2; -; Genomic_DNA.
DR RefSeq; XP_460025.2; XM_460025.1.
DR AlphaFoldDB; Q6BP45; -.
DR SMR; Q6BP45; -.
DR STRING; 4959.XP_460025.2; -.
DR PRIDE; Q6BP45; -.
DR EnsemblFungi; CAG88281; CAG88281; DEHA2E16632g.
DR GeneID; 2902212; -.
DR KEGG; dha:DEHA2E16632g; -.
DR VEuPathDB; FungiDB:DEHA2E16632g; -.
DR eggNOG; KOG0344; Eukaryota.
DR HOGENOM; CLU_003041_1_4_1; -.
DR InParanoid; Q6BP45; -.
DR OMA; IRAQHRI; -.
DR OrthoDB; 400908at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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; 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; 2.
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..550
FT /note="ATP-dependent RNA helicase ROK1"
FT /id="PRO_0000232303"
FT DOMAIN 145..322
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 333..497
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 53..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..142
FT /note="Q motif"
FT MOTIF 269..272
FT /note="DEAD box"
FT COMPBIAS 53..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 550 AA; 62130 MW; F74D6CF8EE12C3FD CRC64;
MDIFRILSRG ASLKKSKDIT TDYAVPSRKQ FVNEKQKEEN LKSVVDKEVD FFHTKKHTSH
KETEKKNDEG EDEIEDEVPP LTISSDDDAR KLRKLNKSKV SGEDIPLPIG SFEDLIGRYK
LDKKLLSNLI DAGFTEPTPI QDEAIPISLE GRDLIACAPT GSGKTLAFLI PLVQTILQSN
PNVKNYGIRG LIISPTNELA VQIFQELNTM TKGKKMKIGI LSKQLANKIN NKIINSSKYD
ILVSTPLRLI DSIKNETISL SKVEQLVIDE TDKLFDQGFV EQTDEILSNC TNTKLRKSMF
SATIPSGVEE MAQSIMKDPI RVIIGHKEAA SNTIEQKLVF TGNEEGKLLA IRQMIQQGEF
KPPIIIFLQS ITRAKALFHE LLYDRLNVDV IHAERTPKQR DEVIKRFKSG DIWVLITTDV
IARGVDFKGV NLVINYDVPQ SAQAYVHRIG RTGRGGKAGK AVTFFTKEDD KAVKPIINVM
KQSGCESGYS GWLEDMHKLS KNEKKDVKKH EIKRKQISTV PKIMKQKRKQ REEMIDASKR
RKQESQSNTE
