DRS1_CHAGB
ID DRS1_CHAGB Reviewed; 795 AA.
AC P0C2N7; Q2H8R0;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
GN Name=DRS1; ORFNames=CHGG_03394;
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-binding RNA helicase involved in ribosome assembly.
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 -!- SUBUNIT: Associates with pre-ribosomal particles. {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. DDX27/DRS1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ91459.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408030; EAQ91459.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001229910.1; XM_001229909.1.
DR AlphaFoldDB; P0C2N7; -.
DR SMR; P0C2N7; -.
DR STRING; 38033.XP_001229910.1; -.
DR EnsemblFungi; EAQ91459; EAQ91459; CHGG_03394.
DR GeneID; 4389883; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_002022_1_0_1; -.
DR InParanoid; P0C2N7; -.
DR OrthoDB; 268859at2759; -.
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:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
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; 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.
FT CHAIN 1..795
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000282492"
FT DOMAIN 307..481
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 466..684
FT /note="Helicase C-terminal"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 276..304
FT /note="Q motif"
FT MOTIF 429..432
FT /note="DEAD box"
FT COMPBIAS 7..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 320..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 795 AA; 86730 MW; 6485B5579B1E3AAE CRC64;
MAPSQKRKSL PDDDFIHTIS DNDEPDILDE EEETVPAAVA GRPNKKARTA GAGAVKGKKN
KKEKKGKKGG KSAAAGGDGE DGDEEEEEEV TGLWGANDAD DGAMDSDFEF VAGGGGEDGL
SGFDEEGWGF ENAKKGVVGA GGAGQEVKSG VDLDEIIRRR REKKKGKGLE KVEEEEVEVE
DMGEVDLDLD DEVLAEDGFG MGMEDGEGGV DEEDKGGEDD DEAASDNDSV ATPVQHPDDE
ASEDDDEEDA EEEARRKEFF AAPEETENVG KKGGLSSFQG MSLSRPILRG LTSVGFTKPT
PIQAKTIPIA LMGKDVVGGA VTGSGKTAAF VVPILERLLY RPKKVPTTRV VVLTPTRELA
IQCHSVATKL ASHTDIKFCL AVGGLSLKVQ EGELRLRPDV VIATPGRFID HMRNSASFAV
ETVEILVLDE ADRMLEDGFA DELNEILTTL PKSRQTMLFS ATMTSTVDKL IRVGLNKPAR
IMVDSQKQTA VTLAQEFVRL RPGREEKRMG YLGPYLQDPV HRTSHYLLQA EEDCSPDPDH
LRLAGAFEHR APWKHEPGSA FRDGKVNYLL ATDLASRGLD IKGIDTVINY EAPQSLEIYV
HRVGRTARAG RSGVAITLAA EPDRKVVKAA VRAGKAQGAK IISRVIDAAD ADKWQDQIDE
MDDEIDEILQ EEKEEKQLAQ IEMQVKKGEN LIKHEEEIHA RPKRTWFETQ EDKKKAKELG
RAELNGVRDA MKKKGAGRLS NKDKKKLDSK AERSESKSTG WKKGRAERDG KGAVLNLKKV
TKPKSKAPAG RKGRR
