ID   DBP2_CHAGB              Reviewed;         562 AA.
AC   Q2H720;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=ATP-dependent RNA helicase DBP2;
DE            EC=3.6.4.13;
GN   Name=DBP2; ORFNames=CHGG_05545;
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 nonsense-mediated mRNA
CC       decay and ribosome biogenesis through rRNA processing. {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 polysomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {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. DDX5/DBP2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CH408031; EAQ88926.1; -; Genomic_DNA.
DR   RefSeq; XP_001221640.1; XM_001221639.1.
DR   AlphaFoldDB; Q2H720; -.
DR   SMR; Q2H720; -.
DR   STRING; 38033.XP_001221640.1; -.
DR   EnsemblFungi; EAQ88926; EAQ88926; CHGG_05545.
DR   GeneID; 4390416; -.
DR   eggNOG; KOG0331; Eukaryota.
DR   HOGENOM; CLU_003041_16_9_1; -.
DR   InParanoid; Q2H720; -.
DR   OMA; STMPKFE; -.
DR   OrthoDB; 638613at2759; -.
DR   Proteomes; UP000001056; 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..562
FT                   /note="ATP-dependent RNA helicase DBP2"
FT                   /id="PRO_0000255990"
FT   DOMAIN          167..342
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          370..519
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          538..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           136..164
FT                   /note="Q motif"
FT   MOTIF           290..293
FT                   /note="DEAD box"
FT   BINDING         180..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   562 AA;  60326 MW;  4BCBF8E6438DC44E CRC64;
     MSSYGGGGYS SRGGGGGYSG GYDRNGGGGG GYSGSNGYSG GGGGYGGGGY GGGGGGYGGG
     GGGYGGGYGG GGGDRMSNLG AGLQKQNWDL DTLPKFEKSF YQEHPNVAAR SQAEVDKFRR
     DHAMTVAGNN VPSPVETFDE AGFPRYVMDE VKAQGFPAPT AIQSQGWPMA LSGRDVVGIA
     ETGSGKTLTY CLPAIVHINA QPLLAPGDGP IVLVLAPTRE LAVQIQQEIT KFGKSSRIRN
     TCVYGGVPKG PQTRDLSRGV EVCIATPGRL IDMLESGRTN LRRVTYLVLD EADRMLDMGF
     EPQIRKIIGQ IRPDRQTCMW SATWPKEVRA LASDFLTDFI QVNIGSMDLA ANHRITQVVE
     VVNESEKRDK MIKHLEKIME DKESQNKILI FTGTKRVADE ITRFLRQDGW PALSIHGDKQ
     QNERDWVLDQ FKTGKSPIMV ATDVASRGID VRNITHVLNY DYPNNSEDYI HRIGRTGRAG
     AKGTAITFFT TDNSKQARDL VGVLQEAKQH IDPRLAEMVR YGGGGGNSRY GGYRGRGGGG
     FRGGRSQGAN GPNAMPMGNR RW