ID   DBP7_DEBHA              Reviewed;         798 AA.
AC   Q6BKH3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=ATP-dependent RNA helicase DBP7;
DE            EC=3.6.4.13;
GN   Name=DBP7; OrderedLocusNames=DEHA2F21978g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S
CC       ribosomal subunits and is required for the normal formation of 25S and
CC       5.8S rRNAs. {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: Nucleus, nucleolus {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   -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR382138; CAG89699.1; -; Genomic_DNA.
DR   RefSeq; XP_461298.1; XM_461298.1.
DR   AlphaFoldDB; Q6BKH3; -.
DR   SMR; Q6BKH3; -.
DR   STRING; 4959.XP_461298.1; -.
DR   EnsemblFungi; CAG89699; CAG89699; DEHA2F21978g.
DR   GeneID; 2903403; -.
DR   KEGG; dha:DEHA2F21978g; -.
DR   VEuPathDB; FungiDB:DEHA2F21978g; -.
DR   eggNOG; KOG0348; Eukaryota.
DR   HOGENOM; CLU_003041_26_2_1; -.
DR   InParanoid; Q6BKH3; -.
DR   OMA; AVHIKAD; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005730; C:nucleolus; 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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR025313; DUF4217.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01178; DUF4217; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..798
FT                   /note="ATP-dependent RNA helicase DBP7"
FT                   /id="PRO_0000232254"
FT   DOMAIN          194..389
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          443..670
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           161..190
FT                   /note="Q motif"
FT   MOTIF           321..324
FT                   /note="DEAD box"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         207..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   798 AA;  89335 MW;  E12182043B9E1C41 CRC64;
     MDEDDGLLLN FAAPSSSEPT GNKAKKSGNK VTGGRWKDRR KLQLSLQGRG RNQKKEKIVA
     TGVNSTDIDN SRLDRAKESL DTAKEKPAQE KRRVPTNQDH LGPSSKRIKF KETSGEFGGK
     NSSYVSSLFT SNEASSTLTP TDTSAATTTY LPSNAPLKDA TTFDGLGLND KLATHLTESL
     RFKAPTKVQR SVIPSLIATQ RDLFVKAQTG SGKTLSFLLP IFHKLMSEEK YKITRESGLF
     AIILVPTREL CTQIYGVLET LVRCHHHIVP GIVIGGEKKK SEKARLRKGV NILVATPGRL
     ADHMENTTSL DVSQLRWLIL DEGDRLTELG FEETITKITD NISKNSKISE TIHKYQGLPT
     ERVNVLCSAT IQDNVKKLGN MILNNPETIS VDSNKQIEGT LNFDDEEEQN NFDSNNSEGK
     RMSAPDQLIQ KILVVPPKLR LVALSAMLKK LSKETNSLDD GVNRRTIVFF SCSDSLNFHF
     DVFTRNGNMF KKRKNRETDK FETVEVPYYS KYDNEDDNEE DKPSILTAPI LGSNSCVYKL
     HGSLSQQQRA TTLQAFIKEK NEGKNSAKHS ILFCTDVASR GLDLPNISSV IEYDPPFSVE
     DHLHRIGRSA RVGNEGSAVL FLLPGNEEGY VDGKIRVVHP KEDNLRIISY EDVLKEGFAE
     PEEDQEEKKA STKPDPKKRF GKWDIHATTW HLDVERWLLE DSTAHDRAVQ AFTSHIRAYA
     THLSTERSFF NVKLLHLGHL AKSFGLRETP KKLGKSVGGN TGLQDVNNSK KIKKEDPRKK
     MLRMAKMAIN SNSSEFNY