ID   DBP6_VANPO              Reviewed;         637 AA.
AC   A7TFZ9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=ATP-dependent RNA helicase DBP6;
DE            EC=3.6.4.13;
GN   Name=DBP6; ORFNames=Kpol_1028p29;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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   -!- SUBUNIT: Associated with pre-ribosomal particles. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC       subfamily. {ECO:0000305}.
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DR   EMBL; DS480385; EDO18756.1; -; Genomic_DNA.
DR   RefSeq; XP_001646614.1; XM_001646564.1.
DR   AlphaFoldDB; A7TFZ9; -.
DR   SMR; A7TFZ9; -.
DR   STRING; 436907.A7TFZ9; -.
DR   EnsemblFungi; EDO18756; EDO18756; Kpol_1028p29.
DR   GeneID; 5547069; -.
DR   KEGG; vpo:Kpol_1028p29; -.
DR   eggNOG; KOG0350; Eukaryota.
DR   HOGENOM; CLU_003041_15_2_1; -.
DR   InParanoid; A7TFZ9; -.
DR   OMA; HLEWLVI; -.
DR   OrthoDB; 973872at2759; -.
DR   PhylomeDB; A7TFZ9; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
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; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
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.
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..637
FT                   /note="ATP-dependent RNA helicase DBP6"
FT                   /id="PRO_0000310239"
FT   DOMAIN          222..402
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          434..608
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           198..206
FT                   /note="Q motif"
FT   MOTIF           342..345
FT                   /note="DEAD box"
FT   COMPBIAS        11..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..83
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         235..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   637 AA;  72193 MW;  818142556846B136 CRC64;
     MFAVRFDPSQ LVEESVEDEA PKKVIPLKRS KSDEEDESSE EETESSEDEE EKEKEEVADE
     DSMDVDDESS GDDDEEAEEG EVDAASDHPD KHNSVMSRFQ QTLALQDKMD SESLVNENEE
     VNDENIVESH NLERIPQPAK VKESAVAPAA VSQYKSAAWL NTETIHYDSS MVRKFSDFED
     QIDPKLLKNI QQNFSTDTFP IQSILLETLL PTLNFSYNIT KKNFTRRVGD VLVNASTGSG
     KTLAYSIPIL QILSKRTVNK LRALVIVPTK LLINQVYETF NNLAQGTSLI VSISKLENSL
     KEENKKLLQN EPDILITTPG RLVDHLQSGA VNLRNLKFLV LDEADRLLNQ SFQNWCNELL
     NKLKTDKQDH MPGNIVKMVF SATLTTNTEK LHGLQFYNPK LFVMDSVKLY HLPRMLQEYN
     LHIPTAKTSY KPLFLLRLLS EINGSKMLVF VKSNESSLRL ASLLSIMIEH KLGSQFDINS
     VNSNNTKAEN RRIVNEFASN NNTSKVQVLI TTDVMSRGVD INDITDVLNY DVPISSQQYI
     HRCGRTARAQ SKGTAYNMLI GKGERTFWAT HIDNDISRDI DGCQPQVWGQ HDQQNQKDEG
     QEEEAQVLPL LTVDPETESI YKECLNSLKE KVDTNRK