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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
 
 
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