RRP3_VANPO
ID RRP3_VANPO Reviewed; 506 AA.
AC A7TS37;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=Kpol_1005p11;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480497; EDO14923.1; -; Genomic_DNA.
DR RefSeq; XP_001642781.1; XM_001642731.1.
DR AlphaFoldDB; A7TS37; -.
DR SMR; A7TS37; -.
DR STRING; 436907.A7TS37; -.
DR EnsemblFungi; EDO14923; EDO14923; Kpol_1005p11.
DR GeneID; 5542951; -.
DR KEGG; vpo:Kpol_1005p11; -.
DR eggNOG; KOG0330; Eukaryota.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; A7TS37; -.
DR OMA; YDIELYQ; -.
DR OrthoDB; 744428at2759; -.
DR PhylomeDB; A7TS37; -.
DR Proteomes; UP000000267; 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..506
FT /note="ATP-dependent rRNA helicase RRP3"
FT /id="PRO_0000310233"
FT DOMAIN 117..289
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 312..460
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 86..114
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 236..239
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 51..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 506 AA; 56182 MW; 756C49981080285C CRC64;
MSGKVDKKKG SSVKKTEGKS KEISALAAKI RAKALENQKK MLKNSETTSD QEDDPSESEE
EEGSDSEDVE VSKDKQEEEE EGETFESFSD LDLVPELIEA CKNLNFAKPT PIQARSIPPA
LQGHDIIGLA QTGSGKTAAF AIPILNRLWH DQQPYYACIL APTRELAQQI KETFDSLGSL
MGVRSACIVG GMNMMDQARD LMRKPHIIIA TPGRLMDHLE NTRGFSLRKL KFLVMDEADR
LLDMEFGPVL DRILKIIPTQ GRTTYLFSAT MTSKIDKLQR ASLTNPVKCA VSNKYQTVDT
LVQTLIVVPG GLKNTYLIYL MNEFIGKTII VFTRTKANAE RITTLANLLE FSATALHGDL
NQNQRTGSLD LFKAGRRSIL VATDVAARGL DIPSVDIVIN YDIPVDSKSY IHRVGRTARA
GRSGKSISLV SQYDLELILR IEDVLGKKLP KENVNKDAIL TLRDSVDKAN GEVVMELNRR
NKEKIARGKG RRGRMAARDD MDKGER
