ID ROK1_NEUCR Reviewed; 781 AA.
AC Q7SFC8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 116.
DE RecName: Full=ATP-dependent RNA helicase rok1;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box RNA helicase 16;
GN Name=drh-16; Synonyms=rok1; ORFNames=G17B7.140, NCU00919;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; BX842638; CAE76585.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA35509.1; -; Genomic_DNA.
DR RefSeq; XP_964745.1; XM_959652.2.
DR AlphaFoldDB; Q7SFC8; -.
DR SMR; Q7SFC8; -.
DR STRING; 367110.Q7SFC8; -.
DR PaxDb; 5141-EFNCRP00000000631; -.
DR EnsemblFungi; EAA35509; EAA35509; NCU00919.
DR GeneID; 3880898; -.
DR KEGG; ncr:NCU00919; -.
DR VEuPathDB; FungiDB:NCU00919; -.
DR HOGENOM; CLU_003041_1_4_1; -.
DR InParanoid; Q7SFC8; -.
DR OrthoDB; 123064at2759; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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; IBA:GO_Central.
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; PTHR24031:SF594; ATP-DEPENDENT RNA HELICASE DDX52-RELATED; 1.
DR PANTHER; PTHR24031; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 2.
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; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..781
FT /note="ATP-dependent RNA helicase rok1"
FT /id="PRO_0000232307"
FT DOMAIN 233..487
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 527..689
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 7..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 184..212
FT /note="Q motif"
FT MOTIF 434..437
FT /note="DEAD box"
FT COMPBIAS 86..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..370
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 781 AA; 86883 MW; F973CA7611AAD9F6 CRC64;
MDIFKVLSRG IKAQPKKNQP GAPQLLPSAG AKVNPQFFHD NVGGANAKRG KKRKRKGAQA
NNATESGDED DDASDVDYFA PKPTPEELAA KKDAELKADE PKKQKPKLLE ENECRQILKS
HRLKFTVLAG RVPQDEAATE EKPPKKQKKQ KEDRKKQEEE EKKKKKKDED KKQIYPQPLN
SFGELKYTYG IHPVLADNIT RQGFRVPTEV QMGSLPLQLR PEMALEKATD VEDVKVEKGI
DFLGVAPTGS GKTISFLIPA IDAIIKRRAE DYTPETDEHV LQAIVVAPTR ELASQIVNEG
RKLAIGTGVR VVLMKRTLRL VAESNEQEET EQEAKEEVQD SDSDSEAESE PEEVMKIDEE
EEEEEESDSD AEKKTESRAK GDQKFKKERP ITRVDILVTT PKILLNFLCG GEKEKGKPRI
IKKTLPTVQS LILDEADVLL DPIFRKQTMG IWRACTHPNL GMTCWSATMA SNIEALLTKH
IDKRAKRTPE QTPKPLIRLV VGLKDTAVPN ITHKLIYTAT EPGKLLALRQ LLHPVSSADS
GPPLRPPFLV FTQTIERAQA LHDELKYDIP LEAGGSARVA VLHSSLPDSV RSKIMARFRS
GEVWVLITTD VLARGVDFAG VNGVVNYDVP VSAAAYVHRA GRTGRAGREG GVAVTFYTKD
DIPFVKSVAN VIAMSEKQAG KDIDEKDTVK AAQGSVQKWL LDALPKVAKE DKRKLKVRGV
ESRRTGGKAT ITTKSSWERR RENNRREAIE ASKRRKREAQ KAQKEGGAAP EKAEEEWTGL
D
//
