RRP3_PICST
ID RRP3_PICST Reviewed; 484 AA.
AC A3LS22;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 70.
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=PICST_57234;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN65488.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000497; ABN65488.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001383517.2; XM_001383480.1.
DR AlphaFoldDB; A3LS22; -.
DR SMR; A3LS22; -.
DR STRING; 4924.XP_001383517.2; -.
DR EnsemblFungi; ABN65488; ABN65488; PICST_57234.
DR GeneID; 4838114; -.
DR KEGG; pic:PICST_57234; -.
DR eggNOG; KOG0330; Eukaryota.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; A3LS22; -.
DR OrthoDB; 744428at2759; -.
DR Proteomes; UP000002258; Chromosome 3.
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..484
FT /note="ATP-dependent rRNA helicase RRP3"
FT /id="PRO_0000285150"
FT DOMAIN 102..273
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 300..444
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 71..99
FT /note="Q motif"
FT /evidence="ECO:0000305"
FT MOTIF 221..224
FT /note="DEAD box"
FT /evidence="ECO:0000305"
FT COMPBIAS 13..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 484 AA; 54357 MW; 0EFF6C4840C99EAC CRC64;
MAIVGSNSVS KKPKHTKRND ARDLAEKIKR NALKKQEQDK KQQLEEESKP ESSQKSKNIV
EVNPDDEVKF STFSELKLVP ELLEAIQQMK FSKPTPIQSE AIPHALEGKD IIGLAQTGSG
KTAAFAIPIL QSLWEAQTPY FGLVLAPARE LAYQIKETFD ALGSTMGVRT VCLVGGMDMM
DQARDLMRKP HIIIATPGRI MDHLEHTKGF SLKMLKYFVM DEADKLLDLE FGPVLDKILK
QIPSKRTTYL FSATMTNKIE KLQRASLHNP VRVAVSSKYQ TADNLIQSMM LVSDGYKNTY
LIHLLNEFVG KSIIIFARTR AHTQRTSILC RILGFSAVPL HGDLTQAQRL GSLNKFKSGT
ANILIATDVA ARGLDIPSVD VVINYDIPTD SKAYVHRVGR TARAGRSGKS ISLVTQYDLE
MYLRIEQSIQ KKLPKDPSPP KAMLDALHVH VDRAYAEAIR QTKEFHEKTR RGRRGKDDKD
REEH
