GenomeNet

Database: UniProt
Entry: Q2HBE7
LinkDB: Q2HBE7
Original site: Q2HBE7 
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   11-DEC-2019, entry version 67.
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}.
DR   EMBL; CH408030; EAQ90522.1; -; Genomic_DNA.
DR   RefSeq; XP_001228973.1; XM_001228972.1.
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   eggNOG; ENOG410XNTI; LUCA.
DR   InParanoid; Q2HBE7; -.
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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003743; F:translation initiation factor activity; 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; 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   NP_BIND         242..249
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           198..226
FT                   /note="Q motif"
FT   MOTIF           363..366
FT                   /note="DEAD box"
FT   COMPBIAS        63..152
FT                   /note="Gly-rich"
FT   COMPBIAS        596..684
FT                   /note="Gly-rich"
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
//
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