ID   HAS1_CANGA              Reviewed;         494 AA.
AC   Q6FIL3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ATP-dependent RNA helicase HAS1;
DE            EC=3.6.4.13;
GN   Name=HAS1; OrderedLocusNames=CAGL0M13519g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., 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 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.
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   -!- SUBUNIT: Associates in the nucleolus with the 60S and pre-60S ribosomal
CC       subunits. {ECO:0000250}.
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. DDX18/HAS1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR380959; CAG62911.1; -; Genomic_DNA.
DR   RefSeq; XP_449931.1; XM_449931.1.
DR   AlphaFoldDB; Q6FIL3; -.
DR   SMR; Q6FIL3; -.
DR   STRING; 5478.XP_449931.1; -.
DR   EnsemblFungi; CAG62911; CAG62911; CAGL0M13519g.
DR   GeneID; 2891222; -.
DR   KEGG; cgr:CAGL0M13519g; -.
DR   CGD; CAL0136209; CAGL0M13519g.
DR   VEuPathDB; FungiDB:CAGL0M13519g; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_5_1; -.
DR   InParanoid; Q6FIL3; -.
DR   OMA; EYEFPAN; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005635; C:nuclear envelope; IEA:EnsemblFungi.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030687; C:preribosome, large 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:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:EnsemblFungi.
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:1990417; P:snoRNA release from pre-rRNA; IEA:EnsemblFungi.
DR   CDD; cd17942; DEADc_DDX18; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR044773; DDX18/Has1_DEADc.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
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; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 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..494
FT                   /note="ATP-dependent RNA helicase HAS1"
FT                   /id="PRO_0000232208"
FT   DOMAIN          60..236
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          250..420
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           29..57
FT                   /note="Q motif"
FT   MOTIF           183..186
FT                   /note="DEAD box"
FT   MOTIF           262..278
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   BINDING         73..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   494 AA;  55645 MW;  D45C306E58C4690D CRC64;
     MAQTKRSRDE SEKEEVVVKA DVESSDVDHS FKSLNLSQPT MRAIEKMGFS KMTPVQARTI
     PPLMAGRDVL GAAKTGSGKT LAFLLPTIEL LHSLKFKPRN GTGVIIITPT RELALQIFGV
     VRELMEFHSQ TFGIVIGGAN RRQEAEKLMK GVNLLVATPG RLLDHLQNTK GFIFKNLKAL
     VIDEADRILE IGFEDEMRQI IKILPNEDRQ SMLFSATQTT KVEDLSRISL RPGPLFINVV
     SEHDSSTADG LEQGYVVCES DKRFLLLFSF LKRNQKKKII VFLSSCNSVK YYAELLNYID
     LPVLELHGKQ KQQKRTNTFF EFCNAERGIL ICTDVAARGL DIPAVDWIIQ FDPPDDPRDY
     IHRVGRTARG TNGKGKSLMF LIPNELGFLR YLKAAKVPLN EYEFPTNKIA NVQSQLEKLI
     KSNYYLHQTA KDGYRSYLQA YASHSLKTVY QIDKLDLAKV AKSYGFPVPP KVNITIGASG
     KTPTVVKKRK THKH