ID A0A0A1THH6_9HYPO Unreviewed; 700 AA.
AC A0A0A1THH6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ATP-dependent RNA helicase ROK1 {ECO:0000256|ARBA:ARBA00024410};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=ATP-dependent RNA helicase rok1 {ECO:0000256|ARBA:ARBA00024419};
GN ORFNames=VHEMI04925 {ECO:0000313|EMBL:CEJ88905.1};
OS [Torrubiella] hemipterigena.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC Clavicipitaceae incertae sedis; 'Torrubiella' clade.
OX NCBI_TaxID=1531966 {ECO:0000313|EMBL:CEJ88905.1, ECO:0000313|Proteomes:UP000039046};
RN [1] {ECO:0000313|EMBL:CEJ88905.1, ECO:0000313|Proteomes:UP000039046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Horn F., Habel A., Scharf D.H., Dworschak J., Brakhage A.A., Guthke R.,
RA Hertweck C., Linde J.;
RT "Draft Genome Sequence and Gene Annotation of the Entomopathogenic Fungus
RT Verticillium hemipterigenum.";
RL Genome Announc. 3:e01439-e01414(2015).
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 {ECO:0000256|ARBA:ARBA00024310}.
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBUNIT: Interacts with the U3 snoRNA and is associated with the 90S
CC and 40S pre-ribosomes. {ECO:0000256|ARBA:ARBA00024367}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1
CC subfamily. {ECO:0000256|ARBA:ARBA00024355}.
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DR EMBL; CDHN01000002; CEJ88905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1THH6; -.
DR STRING; 1531966.A0A0A1THH6; -.
DR HOGENOM; CLU_003041_1_4_1; -.
DR OrthoDB; 123064at2759; -.
DR Proteomes; UP000039046; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IEA:InterPro.
DR CDD; cd17957; DEADc_DDX52; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR044764; DDX52/Rok1_DEADc.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF15; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:CEJ88905.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000039046}.
FT DOMAIN 185..464
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT DOMAIN 207..420
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 459..628
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..315
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 700 AA; 76658 MW; 7A35D4D1636D1C92 CRC64;
MDILKILSRG TKKTNTASTS ATATGDLPSS GAKVNPQLYN DSVRGQKRKR QANQTDDKVE
DELPEVNFFP APDATSAREQ ESAKKPQRAA SPPRKPTKRL PEDECRQIFR SHRLKLTILS
KDQELKKPKK SSKKKQKKAV AEEDTKNDSK AQLFPQPLES FADLRNTYGI SRRVAENLIA
QGYRVPTEVQ LGCLPLLLRP ELALPDTDGL DNGINFLAVA PTGSGKTVSF LIPAINKIMR
RRALEKSEGS RELEAIIVAP TRELSHQIVN EGLKLLQGTG IKIVGMKKTT NISVEQQEIA
EDSSDEGSDD EDEESADEGK PKRTQKVRPA TQTDILVTTP RLLINFLTSG PSGTQRVLPG
VRDLILDEAD VLLDPLFREH TLSIWTACTN TDLRVSLWSA TMGSNIETMI NEKLEGRAEA
LGLPVKPLLR LVVGLKDTAV PNIIHKLVYT ASEQGKLLAL RQLLHPSRAD DSGPPLRPPF
LVFTQTIDRA TALHEELKYD IPLEAGGPSR IAALHSGLAE SARAAIMRKF RAGDIWVLIT
TDVLARGVDF AGVNGVVNYD VPGSSAVYVH RAGRTGRAGR QGGIAVTFYT KEDIPFVKTV
ANVIAVSEKQ AGKTGDEATV QKWLLDALPN VGKADRKKLR ERGVESRRSG SKAKITSKSG
YERRKENNRR GAIEGSKRRK QAEADGSGDE DGDEWGGIDD
//
