ID   DBP2_CHATD              Reviewed;         556 AA.
AC   G0SFM2;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   16-MAR-2016, sequence version 2.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=ATP-dependent RNA helicase DBP2;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 2;
GN   Name=DBP2; ORFNames=CTHT_0071350;
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=759272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- FUNCTION: ATP-dependent RNA helicase involved nonsense-mediated mRNA
CC       decay and ribosome biogenesis through rRNA processing.
CC       {ECO:0000250|UniProtKB:P24783}.
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         Evidence={ECO:0000250|UniProtKB:P24783};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P24783}. Nucleus
CC       {ECO:0000250|UniProtKB:P24783}.
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       {ECO:0000250|UniProtKB:P24783}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EGS17787.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; GL988047; EGS17787.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_006697405.1; XM_006697342.1.
DR   AlphaFoldDB; G0SFM2; -.
DR   SMR; G0SFM2; -.
DR   STRING; 759272.G0SFM2; -.
DR   EnsemblFungi; EGS17787; EGS17787; CTHT_0071350.
DR   GeneID; 18261173; -.
DR   KEGG; cthr:CTHT_0071350; -.
DR   HOGENOM; CLU_003041_16_9_1; -.
DR   OrthoDB; 638613at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; 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; 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; Nonsense-mediated mRNA decay;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN           1..556
FT                   /note="ATP-dependent RNA helicase DBP2"
FT                   /id="PRO_0000435812"
FT   DOMAIN          160..335
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          347..512
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          534..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           129..157
FT                   /note="Q motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT   MOTIF           283..286
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         173..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   556 AA;  60625 MW;  D008464162849C27 CRC64;
     MSSYGGGYSG GGGGYSNNYD RNGGYSNGYS GSNGYSGGGG GYGSHGSRSY GGGGYGGGYG
     GGDRGGDRMA GLGSGLQKPN WDLATLPKFE KSFYKEHPNV TARSMAEVEK FRRDHNITVS
     GRDVPKPVET FDEAGFPRYV MDEVKAQGFP APTAIQAQGW PMALSGRDVV GIAETGSGKT
     LTYCLPAIVH INAQPLLAPG DGPIVLVLAP TRELAVQIQQ EINKFGKSSR IRNTCIYGGV
     PKGPQIRDLQ RGVEVCIATP GRLIDMLESG KTNLRRVTYL VLDEADRMLD MGFEPQIRKI
     ISQIRPDRQT LMWSATWPKE VRNLAADFLT DFIQVNIGSL DLAANHRITQ IVEVISESEK
     RDRLIKHLEK IMDSRDTQNK CLIFVGTKRV ADDITRFLRQ DGWPALSIHG DKQQNERDWV
     LDQFKTGKSP IMVATDVASR GIDVRNITHV INYDYPNNSE DYIHRIGRTG RAGAKGTAIT
     FFTTENAKQA RDLVSVLQEA KQHVDPRLLE MARYSGGGGS SRYGGYRGRG GGGYRGGHRS
     AAHSGANAVP VANRRW