ID   FAL1_CRYNB              Reviewed;         396 AA.
AC   P0CQ73; Q55WQ4; Q5KJJ2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=ATP-dependent RNA helicase FAL1;
DE            EC=3.6.4.13;
GN   Name=FAL1; OrderedLocusNames=CNBC0850;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit
CC       biogenesis. Required for the processing and cleavage of 35S pre-rRNA at
CC       sites A0, A1, and A2, leading to mature 18S rRNA (By similarity).
CC       {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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. DDX48/FAL1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAEY01000013; EAL21945.1; -; Genomic_DNA.
DR   RefSeq; XP_776592.1; XM_771499.1.
DR   AlphaFoldDB; P0CQ73; -.
DR   SMR; P0CQ73; -.
DR   EnsemblFungi; AAW42586; AAW42586; CNC06360.
DR   EnsemblFungi; EAL21945; EAL21945; CNBC0850.
DR   GeneID; 4934749; -.
DR   KEGG; cnb:CNBC0850; -.
DR   VEuPathDB; FungiDB:CNBC0850; -.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   Proteomes; UP000001435; Chromosome 3.
DR   GO; GO:0005730; C:nucleolus; 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; 2.
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   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..396
FT                   /note="ATP-dependent RNA helicase FAL1"
FT                   /id="PRO_0000410247"
FT   DOMAIN          54..224
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          235..396
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           23..51
FT                   /note="Q motif"
FT   MOTIF           172..175
FT                   /note="DEAD box"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   396 AA;  44736 MW;  B674DC780C2CBAC4 CRC64;
     MAGVNVGDDK LVFESSEAVT VAPTFEALNL KEDLLRGIYA YNFEKPSAIQ QRAIIPIIRG
     RDVIAQAQSG TGKTATFSIS MLQSIDTNLR ETQALVLSPT RELAVQIQTV VLALGDYMNV
     SCHACIGGTS VGEDIRKLEA GQQVVSGTPG RVFDMIRRRN LRTKDIKMLI LDESDELLNK
     GFKDQIYDIY RYLPPATQVV VVSATLPHDV LEMTTKFMTD PVRILVKRDE LTLEGIKQFF
     VAVEKEDWKF DTLCDLYDTL TITQAVIFCN TRRKVDWLTE KMREANFTVS SMHGEMVQKE
     RDAIMAEFRG GQSRVLITTD VWARGIDVQQ VSLVINYDLP TSRENYLHRI GRSGRFGRKG
     VAINFVTVDD VRILRDIEQY YSTQIDEMPM NVAELT