ROK1_MAGO7
ID ROK1_MAGO7 Reviewed; 775 AA.
AC A4RMV8; G4MSF5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ATP-dependent RNA helicase ROK1;
DE EC=3.6.4.13;
GN Name=ROK1; ORFNames=MGG_04523;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001232; EHA53767.1; -; Genomic_DNA.
DR RefSeq; XP_003713574.1; XM_003713526.1.
DR AlphaFoldDB; A4RMV8; -.
DR SMR; A4RMV8; -.
DR STRING; 318829.MGG_04523T0; -.
DR EnsemblFungi; MGG_04523T0; MGG_04523T0; MGG_04523.
DR GeneID; 2678041; -.
DR KEGG; mgr:MGG_04523; -.
DR VEuPathDB; FungiDB:MGG_04523; -.
DR eggNOG; KOG0344; Eukaryota.
DR HOGENOM; CLU_003041_1_4_1; -.
DR InParanoid; A4RMV8; -.
DR OMA; HKIKVTD; -.
DR OrthoDB; 400908at2759; -.
DR Proteomes; UP000009058; Chromosome 2.
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.
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..775
FT /note="ATP-dependent RNA helicase ROK1"
FT /id="PRO_0000294663"
FT DOMAIN 254..485
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 533..698
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 191..219
FT /note="Q motif"
FT /evidence="ECO:0000250"
FT MOTIF 432..435
FT /note="DEAD box"
FT COMPBIAS 79..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 775 AA; 83748 MW; 7F6B5669768B24C9 CRC64;
MDILKVLSRG TKQAPKKPGV PAATLAQANI PSAGVETNPQ LYHDNVGPPP KGKKRKRKSR
TQDHDQADDA VDDDVELSDF DFFAPKTRRD SDGAGSKTKA ADVKKAKKDA DEADKARPIE
LDECKRILRS HRLKYTLLPV QKAAPAKVEK SSAKKKKKKD KGDKVDGAAQ AAQGKSDKLP
VFPQPLVSFS QLRSAYRISP RLADNLAKGS YKVPTEVQLG ALPLLLQPGF ALSHEGDGVD
DDGKGGDGEA LAMLQGASAG VDFLAIAPTG SGKTLSFLLP AINGVLKRRA EKGETGGDSS
NDTKHALEAI VVAPTRELAS QIANEGRKLA MGTGVRVVLM RKGMRVAAEE DSTEKKSEDQ
EEDVFESEDE DSLSEDDEER EKSEKPSKKP NKAPITKADI LVTTPMLLLN FLSKGTSTTK
KRLPRVRSLI LDEADVLLDQ LFREQTMGIW SACRNPNLRV SFWSATMASN IETHILDNLR
AQADDAPAPP LIRLVVGLKD TAVPNISHRL VYTATESGKL LALRQLLHPA SFSTTTSSTT
TPEDETPLRP PFLVFVQTIE RATALHEELK YDIPAAAGGA SRVAVLHSSM PESARAAVIR
RFRAADVWVL ITTDVLARGV DFAGVNGVVN YDVPGSAAAY VHRAGRTGRA GRKGGIAVTF
YTKEDIPFVK NVANVIALSE RQAGAGESAT QKWLLDALPD VSKKDKKELR EKGVESRRSV
AASKGKARIT SKSAWERRKE NNRKGAIEGS KRRKIAARDQ GDGSDDGGEW GGIDD