ROK1_CHAGB
ID ROK1_CHAGB Reviewed; 667 AA.
AC Q2HCV7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP-dependent RNA helicase ROK1;
DE EC=3.6.4.13;
GN Name=ROK1; ORFNames=CHGG_01947;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(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; CH408029; EAQ93712.1; -; Genomic_DNA.
DR RefSeq; XP_001221168.1; XM_001221167.1.
DR AlphaFoldDB; Q2HCV7; -.
DR SMR; Q2HCV7; -.
DR STRING; 38033.XP_001221168.1; -.
DR EnsemblFungi; EAQ93712; EAQ93712; CHGG_01947.
DR GeneID; 4387429; -.
DR eggNOG; KOG0344; Eukaryota.
DR HOGENOM; CLU_003041_1_4_1; -.
DR InParanoid; Q2HCV7; -.
DR OMA; HKIKVTD; -.
DR OrthoDB; 400908at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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; 2.
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.
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..667
FT /note="ATP-dependent RNA helicase ROK1"
FT /id="PRO_0000256042"
FT DOMAIN 224..447
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 432..581
FT /note="Helicase C-terminal"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 175..203
FT /note="Q motif"
FT MOTIF 394..397
FT /note="DEAD box"
FT COMPBIAS 84..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 237..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 667 AA; 72549 MW; 90CC2DA8844B8B0A CRC64;
MDILRVLSRG IKPNPKSKAQ AGGATTQLPS AGALPRPQLF HDPVGSRGKK RKRRRGAQDD
EPEGDDQELS DVDYFAPKKA APEAAPTDVE ESPKKRKIKL LDEDECRQIL RSHRLKLTIL
SDQPQAEAKT EAEEPASKKK SSKKKKKETE GKDKKDKKDE HKKQIFPQPL TSFGELRHTY
DVSPQLAANI AAQGFRVPTE VQMASLPLLL QPTTALKKSE GADIPNIDNG ADFLAVAPTG
SGKTITFLIP AIDGVLRRRA EEGRDTDQHV LEAVVVAPTR ELATQIVNEG RKLAIGTGVR
VVLMKRALKL DVEEVADEKS KDLEEGSGSE QGSGDEESEG EEESEGEEGK TSKEAKPLAR
VDILVTTPKI LLNFLSGKAG ARRLLPSVRS LILDEADVLL DPLFRKQTMA ICRACTHPNV
ALTCWSATMA SNVEALVTKH LLQARQEDRQ PTPALHDELK YDIPLEAGGS ARVAVLHSSM
ADSARSKIMA RFRAGEVWVL VTTDVLARGV DFAGVNGVVN YDVPTSAAAY VHRAGRTGRA
GREGGVAVTF YTKDDIPFVK SVANVIAASE KQAGVQADGG GGGTVQKWLL DALPKVAKED
KRKLKVRGVE SRRTGGKATI TTKSSWERRR EHNRAQAVEA SKRRKRQRRE EGPAAGEAEG
EWGGLED
