ID   DBP2_ENCCU              Reviewed;         495 AA.
AC   Q8SRB2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=ATP-dependent RNA helicase DBP2;
DE            EC=3.6.4.13;
GN   Name=DBP2; OrderedLocusNames=ECU08_1080;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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; AL590448; CAD26414.1; -; Genomic_DNA.
DR   RefSeq; NP_597238.1; NM_001041847.1.
DR   AlphaFoldDB; Q8SRB2; -.
DR   SMR; Q8SRB2; -.
DR   STRING; 284813.Q8SRB2; -.
DR   PRIDE; Q8SRB2; -.
DR   GeneID; 859660; -.
DR   KEGG; ecu:ECU08_1080; -.
DR   VEuPathDB; MicrosporidiaDB:ECU08_1080; -.
DR   HOGENOM; CLU_003041_1_5_1; -.
DR   InParanoid; Q8SRB2; -.
DR   OMA; STMPKFE; -.
DR   OrthoDB; 638613at2759; -.
DR   Proteomes; UP000000819; Chromosome VIII.
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..495
FT                   /note="ATP-dependent RNA helicase DBP2"
FT                   /id="PRO_0000255989"
FT   DOMAIN          118..293
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          305..466
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           87..115
FT                   /note="Q motif"
FT   MOTIF           241..244
FT                   /note="DEAD box"
FT   COMPBIAS        1..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         131..138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   495 AA;  55696 MW;  F77575D6BFB95C57 CRC64;
     MMHRGYGGDR RGFRPSFRSD RNSRYAPRTR REPQRYDPMP ELAPVEFQKN FYQEAESISR
     MTPSEVSSFR KTNEMIVKGT NVPHPIQKFE EAGFSSEVVS SLVEKGFSEP TAIQGQGWPM
     ALSGRDMVGI AQTGSGKTLS FILPALVHAK DQQPLRRGDG PIVLVLAPTR ELVMQIKKVV
     DEFCGMFNLR STAVYGGASS QPQIRALHEG AEVVIATPGR LIDLHDQGHA PLSRVTFLVL
     DEADRMLDMG FEPQLRKIIP KTNANRQTLM WSATWPREVR GLAESYMNEY IQVVVGNEEL
     KTNSKIKQIV EVCSGREKED KLIGVLDNFK GDKVIVFCNM KRTCDDLEYV LNRSGYGAAA
     LHGDKSQNIR DKVLDDFRSG RRPILIATEV AGRGLDVNDV KLVINFDFPG SCEDYVHRIG
     RTARGNTKEG ISHTFFTVGD KANARELIRM LREANQTVPS DLEDMVRVSN DRYGSRSTRH
     GYDYRGRAGR FPYRG