ROK1_GIBZE
ID ROK1_GIBZE Reviewed; 693 AA.
AC Q4IPI1; A0A0E0RNS2; V6QW04;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=ATP-dependent RNA helicase ROK1;
DE EC=3.6.4.13;
GN Name=ROK1; ORFNames=FGRRES_00877, FGSG_00877;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(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 -!- 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; DS231663; ESU06119.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF72897.1; -; Genomic_DNA.
DR RefSeq; XP_011316604.1; XM_011318302.1.
DR AlphaFoldDB; Q4IPI1; -.
DR SMR; Q4IPI1; -.
DR STRING; 5518.FGSG_00877P0; -.
DR EnsemblFungi; ESU06119; ESU06119; FGSG_00877.
DR GeneID; 23548345; -.
DR KEGG; fgr:FGSG_00877; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G02193; -.
DR eggNOG; KOG0344; Eukaryota.
DR HOGENOM; CLU_003041_1_4_1; -.
DR InParanoid; Q4IPI1; -.
DR Proteomes; UP000070720; Chromosome 1.
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; 2.
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..693
FT /note="ATP-dependent RNA helicase ROK1"
FT /id="PRO_0000232305"
FT DOMAIN 203..415
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 454..623
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 159..187
FT /note="Q motif"
FT MOTIF 362..365
FT /note="DEAD box"
FT COMPBIAS 11..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 693 AA; 76134 MW; 5E0A3E8604A4D106 CRC64;
MDILKLLSRG TKKTQKGSQN AFNPQQKLPS AGTSTNPQLY HDQVRGHKRK RTKNESEPEA
KVDLPEVDFF APKPEPVAEA PVEVDEPVQA PKPTRSSRLL SEDECRQLLR SHRLKITLLS
KTEDQSKVKK SKKKKKAAVE VKKDSKKQLF PQPLDSFGEL RNAYGLSDKV ADNLVFQGYR
VPTEVQMGSL PLLVHPQAAL KDEDGLDGGV DFLAIAPTGS GKTISFLIPA INNILRRRSE
ENTGNIHELE AVIVAPTREL VHQIVSEGQK LCKGTGLKVV SMKKHTHLSA DQVDMAEDSS
EDEEDKESES EDDDKKPSDD KPKQITTPDI LVTTPFLLFK FLTSGPPSTQ KVLPTVRDLI
LDEADVLLDP LFRDATMADW TACTNTNLRV SFWSATMGSN IESMVTEKLT SRAQSLDITP
KPFVRLVVGL KDTAVPNIAH KLIYTASEQG KLLALRQLLH PTASDDSGPP LRPPFLVFTQ
TIDRATALHE ELQYDIPLEA GGAARIAALH SGLTDSARSS IMRKFRAGDI WILITTDVLA
RGVDFAGVNG VVNYDVPGSS AGYVHRAGRT GRAGREGGIA VTFYTKEDIP FVKMVANVIA
VSEKQAGKTG DEAGVQKWLL DALPNVRKAD RKKLKERGNE ARRSGVKSKI SSKSGYERRR
ENNRLGAIEG SKKRKLQAND DSGDDGEWGG IDD
