ROK1_ASPTN
ID ROK1_ASPTN Reviewed; 749 AA.
AC Q0CMB0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
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=ATEG_05174;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=EAU34243.1; Type=Erroneous gene model prediction; Evidence={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; CH476600; EAU34243.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001214352.1; XM_001214352.1.
DR AlphaFoldDB; Q0CMB0; -.
DR SMR; Q0CMB0; -.
DR STRING; 341663.Q0CMB0; -.
DR PRIDE; Q0CMB0; -.
DR GeneID; 4320809; -.
DR eggNOG; KOG0344; Eukaryota.
DR OrthoDB; 400908at2759; -.
DR Proteomes; UP000007963; 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 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; 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..749
FT /note="ATP-dependent RNA helicase rok1"
FT /id="PRO_0000282701"
FT DOMAIN 241..457
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 497..665
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 192..224
FT /note="Q motif"
FT MOTIF 404..407
FT /note="DEAD box"
FT COMPBIAS 8..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..352
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 254..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 749 AA; 82178 MW; 01A90298CADEEC0C CRC64;
MDAFKLLTRS TNLKTGRAAA TSAAQTSRLP STGKAANPQL FHNSEADRLL EEKKKHGQKR
KRGHGADDAG SEDEDAADLD FFSSAKRAST GGAVAGKRHQ EQASADKDGD SGSEDGSEMD
EVQRRTVLNA HKIKVTDLRD LDQIQSTNAQ TLQTEEPKKK KKKKAKAQQE EPKTLTKKEQ
KKARRLFPQP LVSFKELRTK YKISRRLAEN IAEQGFTVPT EVQLGTLPLQ LGDSSVQQAS
KPGETVEPDL LVVAPTGSGK TLSFLIPVIN KIVRHHHEQP DERGIFAVVV APTKELASQI
VNEGRKLVQG TGVKITLMKK GMQVVERDGD GDSDEKDVLD EDSADSGSDS EDDEQTTDKK
TKGKAPVTKS DILVTTPLLL VNALSANRTK PLAALPLVRN IVLDEADVLL DPLFREQTLD
IWRSCTHPEL RASLWSATMG SNVEDLAKST IQERKDLSGT TKSYPLIRLV VGLKDSAIPN
IQHKLVYAAT EQGKLLGLRQ LLHPTARTAT DVHLRPPFLI FTQTIPRAVA LHSELLYDIP
PEAGGSSRIA VLHSELSDSQ RSEIMKGFRK GEIWILVTTD LLARGVDFRG INGVVNYDIP
NSAAVYVHRV GRTGRAGREG GVAVTYYTKE DIPYVKSIAN IIDVSEKLRG AGGEKSVQKW
LLDSLPDLSK KDKKELKKHG VKARQSNLKS IKDNKEFRQA KISTKSGYER RMENKKKGAI
AASRNRKSQP QAPSTGADSG DDSWSGLED
