ID   FAL1_VANPO              Reviewed;         399 AA.
AC   A7TEF4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP-dependent RNA helicase FAL1;
DE            EC=3.6.4.13;
GN   Name=FAL1; ORFNames=Kpol_1036p3;
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 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; DS480380; EDO19261.1; -; Genomic_DNA.
DR   RefSeq; XP_001647119.1; XM_001647069.1.
DR   AlphaFoldDB; A7TEF4; -.
DR   SMR; A7TEF4; -.
DR   STRING; 436907.A7TEF4; -.
DR   EnsemblFungi; EDO19261; EDO19261; Kpol_1036p3.
DR   GeneID; 5547596; -.
DR   KEGG; vpo:Kpol_1036p3; -.
DR   eggNOG; KOG0328; Eukaryota.
DR   HOGENOM; CLU_003041_1_0_1; -.
DR   InParanoid; A7TEF4; -.
DR   OMA; HLGDYMN; -.
DR   OrthoDB; 726081at2759; -.
DR   PhylomeDB; A7TEF4; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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; 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; 2.
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..399
FT                   /note="ATP-dependent RNA helicase FAL1"
FT                   /id="PRO_0000310178"
FT   DOMAIN          54..227
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          238..399
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           23..51
FT                   /note="Q motif"
FT   MOTIF           173..176
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   399 AA;  45005 MW;  302233E363D1A3BC CRC64;
     MSFSREEDKK LKFKTSKKLK ISPTFESMNL KDDLLRGIYG YGFEAPSAIQ SRAITQIISG
     TDVIAQAQSG TGKTATFTIG MLQAIDLKRK DLQALVLSPT RELASQINQV VSNLGDYMNV
     QSYAMTGGKT MKDDLNRMQK NGCQVVSGTP GRVLDMFKRH LLNTRNVQML ILDEADELLG
     ESLGFKQQIY DIFTKLPAAC QVVVVSATMS KDILEVTKKF MSDPVKILVK RDEISLEGIK
     QYYVNVEKED WKFDTLCDLY DSLTITQCVI FCNTKKKVDW LSAKLTQSNF AVVSMHGDMK
     QEDRNKVMSD FRSGHSRVLI STDVWARGID VQQVSLVINY DIPEIMENYI HRIGRSGRFG
     RKGVAINFIT SSDLSKMKEI EKYYRIKISP VPADLSTIS