ID   RRP3_PICGU              Reviewed;         475 AA.
AC   A5DQF1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP-dependent rRNA helicase RRP3;
DE            EC=3.6.4.-;
GN   Name=RRP3; ORFNames=PGUG_05502;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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: Required for pre-ribosomal RNA processing. Involved in the
CC       maturation of the 35S-pre-rRNA and to its cleavage to mature 18S rRNA
CC       (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH408161; EDK41404.2; -; Genomic_DNA.
DR   RefSeq; XP_001482482.1; XM_001482432.1.
DR   AlphaFoldDB; A5DQF1; -.
DR   SMR; A5DQF1; -.
DR   STRING; 4929.XP_001482482.1; -.
DR   EnsemblFungi; EDK41404; EDK41404; PGUG_05502.
DR   GeneID; 5124146; -.
DR   KEGG; pgu:PGUG_05502; -.
DR   VEuPathDB; FungiDB:PGUG_05502; -.
DR   eggNOG; KOG0330; Eukaryota.
DR   HOGENOM; CLU_003041_1_1_1; -.
DR   InParanoid; A5DQF1; -.
DR   OMA; YDIELYQ; -.
DR   OrthoDB; 744428at2759; -.
DR   Proteomes; UP000001997; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
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..475
FT                   /note="ATP-dependent rRNA helicase RRP3"
FT                   /id="PRO_0000294653"
FT   DOMAIN          95..266
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          293..437
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          30..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           64..92
FT                   /note="Q motif"
FT   MOTIF           214..217
FT                   /note="DEAD box"
FT   COMPBIAS        30..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         108..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   475 AA;  52814 MW;  4BBD341609955698 CRC64;
     MALKPEKVKS SKSASTVDAK SLAEKIKKNA LKQKKQAPVT EKPEEIVETT SEASQDVNSE
     QQFHTFSELN LVPELMEAIE KLKYTKPTPI QSGAIPHALE GKDIIGLAQT GSGKTAAFAI
     PILQSLWEAQ RPYYALVLAP TRELAYQIKE TFDALGSGMG VRSVCIVGGM DMMDQARDLM
     RKPHILVATP GRIMDHLENT KGFSLKSLQY LVMDEADRLL DMDFGPALDK ILKVIPTKRT
     TYLFSATMTN KIAKLQRASL HEPVKVAVSN KYQTADNLVQ SMMLVSDGYK NTFLIHLLNE
     FMGKSIIVFT RTCAHTQRST LLARILGFSA VPLHGQLTQS QRLGSLNKFK SGKANILIAT
     DVAARGLDIP SVDVVINYDI PTDSKAYIHR VGRTARAGKS GKSISLVTQY DLEMYLRIES
     VLGFKLPKDP SPPRDVLNAL HVHVDRASAE AIKQTKDFHE KRTKKKRDDR DREER