RRP3_LODEL
ID RRP3_LODEL Reviewed; 504 AA.
AC A5E6W6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=LELG_05355;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981532; EDK47174.1; -; Genomic_DNA.
DR RefSeq; XP_001523509.1; XM_001523459.1.
DR AlphaFoldDB; A5E6W6; -.
DR SMR; A5E6W6; -.
DR STRING; 379508.A5E6W6; -.
DR EnsemblFungi; EDK47174; EDK47174; LELG_05355.
DR GeneID; 5230544; -.
DR KEGG; lel:LELG_05355; -.
DR VEuPathDB; FungiDB:LELG_05355; -.
DR eggNOG; KOG0330; Eukaryota.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; A5E6W6; -.
DR OMA; YDIELYQ; -.
DR OrthoDB; 744428at2759; -.
DR Proteomes; UP000001996; 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 Gene3D; 3.40.50.300; -; 2.
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; 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; 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..504
FT /note="ATP-dependent rRNA helicase RRP3"
FT /id="PRO_0000294651"
FT DOMAIN 129..301
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 327..471
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 34..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 98..126
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 248..251
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 34..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 504 AA; 55596 MW; 97C742731223BC12 CRC64;
MSSKGIQKKT KAVDATKKLA EKIKKQALKQ KALASASSAA STKESLPVSE TISISTSETP
VSDVSELSNK EDLSTKKDQS SASSSSSTSS SSSPPSVQSF TEFDLVPELL ESIQSLKYTQ
PTPIQAAAIP HALQGKDIVG IAETGSGKTA AFAIPILQTL YTAAQPYYAL VLAPTRELAF
QIKETFDALG SSMGLRSVCI IGGMSMMEQA RDLMRKPHVI IATPGRLIDH LEHTKGFSLK
KLQYLVMDEV DRMIDLDYAK AIDQILKQIP SHQRITYLYT ATMSREIEKF KRSLNSPVQV
EIVKLEKVPD KLKQTMCLTS PNTKDTRLIQ IVNLDSMKRV IIFTRTVVHT RRCCLMLLNL
GFKCVELHGQ MPQSRRLGAI NKFKAGTPIL VATDVAARGL DIPAVDLVIN YDIPDPTLYI
HRVGRTARAG KAGKAISLVT QYDLESYLRI ENTLGTKLPK EDLPLDEMQG LQVSVDRALS
KAIQMLRNEE NDNKLRHRGR SNNK
