ID   HAS1_CHAGB              Reviewed;         586 AA.
AC   Q2GMX1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP-dependent RNA helicase HAS1;
DE            EC=3.6.4.13;
GN   Name=HAS1; ORFNames=CHGG_10683;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408035; EAQ84279.1; -; Genomic_DNA.
DR   RefSeq; XP_001228610.1; XM_001228609.1.
DR   AlphaFoldDB; Q2GMX1; -.
DR   SMR; Q2GMX1; -.
DR   STRING; 38033.XP_001228610.1; -.
DR   PRIDE; Q2GMX1; -.
DR   EnsemblFungi; EAQ84279; EAQ84279; CHGG_10683.
DR   GeneID; 4397061; -.
DR   eggNOG; KOG0342; Eukaryota.
DR   HOGENOM; CLU_003041_26_5_1; -.
DR   InParanoid; Q2GMX1; -.
DR   OMA; EYEFPAN; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000001056; 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   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; 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..586
FT                   /note="ATP-dependent RNA helicase HAS1"
FT                   /id="PRO_0000256005"
FT   DOMAIN          143..318
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          332..502
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           112..140
FT                   /note="Q motif"
FT   MOTIF           265..268
FT                   /note="DEAD box"
FT   COMPBIAS        1..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   586 AA;  65366 MW;  5D25ABFF1478B332 CRC64;
     MASDLSKKRK FKDSKGSKPE RALASSSKAK KLKRAPTPED SDAERDNSSD PEIENQEPEV
     EVPGPPQDNS EDQEAEENAN AFERQDEPAG LDSAIQKGDG SLLGPSVSTD AQAFSELNLS
     DKTMMSINEM GFTKMTEIQR RGIPPLLAGK DVLGAAKTGS GKTLAFLIPA IEMLNSLRFK
     PRNGTGVIVV TPTRELALQI FGVARELMKN HSQTYGVVIG GANIRAEEDK LGKGVNLLIA
     TPGRLLDHLR RGSFVFKNLK SLIIDEADRI LEVGFEDEMR HIVKILPKEN RQTMLFSATQ
     TTKVEDLARI SLRPGPLYIN VDEEKQFSTV EGLDQGYVIV DADKRFLLLF SFLKKMAKKK
     IIVFLSSCNS VKYYSELLQY IDLQVLDLHG KQKQQKRTNT FFEFCNAKQG TLICTDVAAR
     GLDIPQVDWI VQFDPPDDPR DYIHRVGRTA RGNNTKGRSL LFLQPCELGF LAHLKAAKVP
     VVEYDFPKNK ILNVQSQLEK LIGSNYYLNQ SAKDGYRSYL HAYASHSLRS VFDVQKLDMV
     KVAKGFGFST PPRVDITLGA GMSRDKKPQA RRAYGSQPRQ SGHQRR