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 27-MAR-2024, entry version 75.
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; 294746.A5DQF1; -.
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; GIGIKCC; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030684; C:preribosome; IEA:UniProt.
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 CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF21; RNA HELICASE; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
