GenomeNet

Database: UniProt
Entry: Q6BT27
LinkDB: Q6BT27
Original site: Q6BT27 
ID   FAL1_DEBHA              Reviewed;         399 AA.
AC   Q6BT27;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   16-OCT-2019, entry version 99.
DE   RecName: Full=ATP-dependent RNA helicase FAL1;
DE            EC=3.6.4.13;
GN   Name=FAL1; OrderedLocusNames=DEHA2D04048g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG86782.1; -; Genomic_DNA.
DR   RefSeq; XP_458643.1; XM_458643.1.
DR   SMR; Q6BT27; -.
DR   STRING; 4959.XP_458643.1; -.
DR   PRIDE; Q6BT27; -.
DR   EnsemblFungi; CAG86782; CAG86782; DEHA2D04048g.
DR   GeneID; 2901057; -.
DR   KEGG; dha:DEHA2D04048g; -.
DR   InParanoid; Q6BT27; -.
DR   KO; K13025; -.
DR   OMA; TRFHDFK; -.
DR   OrthoDB; 726081at2759; -.
DR   Proteomes; UP000000599; Chromosome D.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   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    399       ATP-dependent RNA helicase FAL1.
FT                                /FTId=PRO_0000232146.
FT   DOMAIN       57    227       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      238    399       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      70     77       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        26     54       Q motif.
FT   MOTIF       175    178       DEAD box.
SQ   SEQUENCE   399 AA;  45258 MW;  05CDC6DFC9A73154 CRC64;
     MDDFDRDVDN ELEFSAKSTK NIKVHATFES MNLKTDLLKG IYGYGFEAPS AIQSRAIMQI
     ISGKDTIAQA QSGTGKTATF SIGMLEVIDT KSKDCQALIL SPTRELAQQI QSVVKHLGDY
     MNVHTHACIG GTHVGEDIKK LQQGQQIVSG TPGRVVDMIK RRNLATRNIK MMILDEADEL
     MTKGFKEQIY EIYRYLPPGV QVVVVSATLS REVLEVTGKF TTDPVKILVK RDDITLEGIK
     QYHIQCEKED WKFDTLCDLY DSLTITQAVI FCNTKVKVNW LTDQMKKANF TVVAMHGDMK
     QDERDSIMND FRTGNSRVLI STDVWARGID VQQVSLVINY DLPTDKENYV HRIGRSGRFG
     RKGVAINLVT KEDVDELRDI ERFYRIRIKE MPVNVNDIM
//
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