RRP3_CHAGB
ID RRP3_CHAGB Reviewed; 493 AA.
AC Q2H1Q8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=ATP-dependent rRNA helicase RRP3 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P38712};
GN Name=RRP3 {ECO:0000250|UniProtKB:P38712}; ORFNames=CHGG_04288;
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 rRNA helicase required for pre-ribosomal RNA
CC processing. Involved in the maturation of the 35S-pre-rRNA and to its
CC cleavage to mature 18S rRNA. {ECO:0000250|UniProtKB:P38712}.
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 Evidence={ECO:0000250|UniProtKB:P38712};
CC -!- SUBUNIT: Interacts with the SSU processome.
CC {ECO:0000250|UniProtKB:P38712}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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 {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC subfamily. {ECO:0000305}.
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DR EMBL; CH408032; EAQ87669.1; -; Genomic_DNA.
DR RefSeq; XP_001223502.1; XM_001223501.1.
DR AlphaFoldDB; Q2H1Q8; -.
DR SMR; Q2H1Q8; -.
DR STRING; 38033.XP_001223502.1; -.
DR PRIDE; Q2H1Q8; -.
DR EnsemblFungi; EAQ87669; EAQ87669; CHGG_04288.
DR GeneID; 4392976; -.
DR eggNOG; KOG0330; Eukaryota.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; Q2H1Q8; -.
DR OMA; YDIELYQ; -.
DR OrthoDB; 744428at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd17954; DEADc_DDX47; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR044765; DDX47/Rrp3_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 InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; PS00039; DEAD_ATP_HELICASE; 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..493
FT /note="ATP-dependent rRNA helicase RRP3"
FT /id="PRO_0000256037"
FT DOMAIN 96..267
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 291..439
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 65..93
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 215..218
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 479..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 493 AA; 53868 MW; 5E3995BA4CC4995D CRC64;
MSAKRRKVSS GNGAIKEASI QIQKPKTKPQ PVTAPVEPSA VPNSEAESET IDDASGEESE
EPAPKTFQDL GIVDSLCDAC KELGWKKPTP IQQESIPLAL QDRDIIGLAE TGSGKTGAFA
LPILQALLDK PQPLFALVLA PTRELAAQIA QSFEALGSLI SLRCALILGG LDMVQQAIAL
GKKPHVVVAT PGRLLDHLEK TKGFSLRNLR YLVMDEADRL LDMDFGPILD KILKFLPRER
RTFLFSATMS SKVESLQRAC LRDPLKVSIS SSKYQTVSTL VQNYVFIPHT HKDTYLIYLC
NEFAGQTIII FTRTVIETQR IAILLRTLGM GAIPLHGGLS QSARLGALNK FRAGSRDILV
ATDVAARGLD IPNVDCVLNL DLPGDSKTYV HRVGRTARAG RSGHAISFVT QYDLELWLRI
EAALGTKLTE YSLEKDDVMV FRPRVEEAQR IAKTEIKALM DDRGKKGSVL KGGKGRKRGP
PGSSRDHMDA EEG
