FAL1_ASHGO
ID FAL1_ASHGO Reviewed; 398 AA.
AC Q755W0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ATP-dependent RNA helicase FAL1;
DE EC=3.6.4.13;
GN Name=FAL1; OrderedLocusNames=AER408W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 211.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS53087.2; -; Genomic_DNA.
DR RefSeq; NP_985263.2; NM_210617.2.
DR AlphaFoldDB; Q755W0; -.
DR SMR; Q755W0; -.
DR STRING; 33169.AAS53087; -.
DR EnsemblFungi; AAS53087; AAS53087; AGOS_AER408W.
DR GeneID; 4621479; -.
DR KEGG; ago:AGOS_AER408W; -.
DR eggNOG; KOG0328; Eukaryota.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q755W0; -.
DR OMA; HLGDYMN; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0097078; C:FAL1-SGD1 complex; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:EnsemblFungi.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
DR GO; GO:0032774; P:RNA biosynthetic process; IEA:EnsemblFungi.
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; 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..398
FT /note="ATP-dependent RNA helicase FAL1"
FT /id="PRO_0000227942"
FT DOMAIN 54..226
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 237..398
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 398 AA; 44582 MW; F3BC1D8F56A04A5B CRC64;
MSFDRNQDGK LKVKTSSKLP VSPTFESMKL QENLLRGIYG YGFEAPSAIQ SRAITQIIRG
KDVIAQAQSG TGKTATFTIG MLQVIDSSSK DLQALVLSPT RELAAQISQV VRNLGDYMNV
VALACTGGKA LQQDISKVNK GCHVMSGTPG RVLDMIKRRI INTRHVKMLV LDEADELLSE
TLGFKQQLYD IFTKLPSSVQ VVVVSATMSK DVLEVTKKFM SDPVKILVKR DEVSLEGIKQ
YHINVDKEEW KFDTLCDLYD SLTITQCVIF CNTKKKVDWL SHKLIQNNFA VASIHGDMKQ
DDRDKVMSDF RSGSSRVLIS TDVWARGIDV QQVSLVINYD LPELLENYIH RIGRSGRFGR
KGVAINFITR EEVTKLKSIE KHYSIKIKPM PADIDSLS
