DED1_CHAGB
ID DED1_CHAGB Reviewed; 688 AA.
AC Q2HBE7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=ATP-dependent RNA helicase DED1;
DE EC=3.6.4.13;
GN Name=DED1; ORFNames=CHGG_02457;
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 translation initiation.
CC Remodels RNA in response to ADP and ATP concentrations by facilitating
CC disruption, but also formation of RNA duplexes (By similarity).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {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. DDX3/DED1
CC subfamily. {ECO:0000305}.
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DR EMBL; CH408030; EAQ90522.1; -; Genomic_DNA.
DR RefSeq; XP_001228973.1; XM_001228972.1.
DR AlphaFoldDB; Q2HBE7; -.
DR SMR; Q2HBE7; -.
DR STRING; 38033.XP_001228973.1; -.
DR PRIDE; Q2HBE7; -.
DR EnsemblFungi; EAQ90522; EAQ90522; CHGG_02457.
DR GeneID; 4388758; -.
DR eggNOG; KOG0335; Eukaryota.
DR HOGENOM; CLU_003041_16_3_1; -.
DR InParanoid; Q2HBE7; -.
DR OMA; CYRSWVR; -.
DR OrthoDB; 595675at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd17967; DEADc_DDX3_DDX4; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044763; Ded1/Dbp1_DEADc.
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; Cytoplasm; Helicase; Hydrolase; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..688
FT /note="ATP-dependent RNA helicase DED1"
FT /id="PRO_0000281689"
FT DOMAIN 229..419
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 430..590
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 198..226
FT /note="Q motif"
FT MOTIF 363..366
FT /note="DEAD box"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 242..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 688 AA; 72381 MW; 8F8C057B9BEE3F87 CRC64;
MADQLNGDMG NLSLGSPQPG QHPGQQPTAR SYIPPHMRGK MSAPGSPGSP IASPPMNSPP
QPGPGSSPMG GLNNSAWAGN NNFDARAGGG GNWSGGYENG PGPQPWGGPR GGGGFNRNAY
RGPNAGGGGG GNMGGGVGRG EGRWIEGKHV IGNSDPRLER DLFGTADDPS KQHTGINFEK
YDDIPVNPSG RDVPEPVLTF SNPPLDAHLL SNIELARYQI PTPVQKYSIP IVINGRDLMA
CAQTGSGKTG GFLFPIMHQS FTQGPSPIPA QSGGGYRQRK AYPTALILAP TRELVSQIYE
EARKFAYRSW VRPCVVYGGA DIGSQLRQME RGCDLLVATP GRLVDLIERG RISLCNIKYL
VLDEADRMLD MGFEPQIRRI VQGEDMPTTG QRQTLMFSAT FPRDIQMLAQ DFLNDYVFLS
VGRVGSTSEN ITQKVEYVED VDKRSVLLDI LHTHAGGLTL IFVETKRMAD SLSDFLINQN
FPATSIHGDR TQRERERALE LFRNGKCPIL VATAVAARGL DIPNVTHVIN YDLPTDVDDY
VHRIGRTGRA GNTGIATAFF NRGNRGIVRE LLDLLKEANQ EVPAFLETIA RESSFGGGGG
RGRGGGGRGR GGRGGNTDFR KYGGGGGGFG GGGGGFGGGQ HGSGGGGGFG GGGGYGGAPQ
SGGYGGGYSG GYGGGYGNPG GAGGQSWW
