GenomeNet

Database: UniProt
Entry: Q6C347
LinkDB: Q6C347
Original site: Q6C347 
ID   FAL1_YARLI              Reviewed;         397 AA.
AC   Q6C347;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   16-OCT-2019, entry version 103.
DE   RecName: Full=ATP-dependent RNA helicase FAL1;
DE            EC=3.6.4.13;
GN   Name=FAL1; OrderedLocusNames=YALI0F02695g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal
CC       subunit biogenesis. Required for the processing and cleavage of
CC       35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA
CC       (By similarity). {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
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX48/FAL1
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR382132; CAG77720.1; -; Genomic_DNA.
DR   RefSeq; XP_504915.1; XM_504915.1.
DR   SMR; Q6C347; -.
DR   PRIDE; Q6C347; -.
DR   EnsemblFungi; CAG77720; CAG77720; YALI0_F02695g.
DR   GeneID; 2907785; -.
DR   KEGG; yli:YALI0F02695g; -.
DR   HOGENOM; HOG000268797; -.
DR   InParanoid; Q6C347; -.
DR   KO; K13025; -.
DR   OMA; TRFHDFK; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    397       ATP-dependent RNA helicase FAL1.
FT                                /FTId=PRO_0000232152.
FT   DOMAIN       55    225       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      236    397       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      68     75       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        24     52       Q motif.
FT   MOTIF       173    176       DEAD box.
SQ   SEQUENCE   397 AA;  44964 MW;  F7B0F640271377FB CRC64;
     MAEFDRDLDD ELEFKTSKDV DVTPTFESMD LKDDLLRGIY AYGFEAPSAI QSRAITQIIK
     GRDTIAQAQS GTGKTATFSI SMLEVIDTKH RETQAMVLSP TRELATQIQS VILALGDYMN
     VQCHACIGGT SLSVDMKKLE AGQQVVSGTP GRCLDMIKKG CLRTKNLKML ILDEADELLN
     KGFQEQIYDI YRYLPAATQV VVVSATLPHS VLEMTSKFMT DPVRILVKRD ELTLEGLKQY
     FIAVEQEEWK FDTLCDLYDT LTITQAVIFC NTKKKVDWLT QQMKDNNFTV CSMHGDMAQK
     DRDSIMNEFR SGRSRVLIST DVWARGIDVQ QVSLVINYDL PPNRENYIHR IGRSGRFGRK
     GVAINFATND DITTLRDIEQ YYSTQIDEMP VNVTDMM
//
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