ID   DBP10_VANPO             Reviewed;         977 AA.
AC   A7TGW7;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; ORFNames=Kpol_1032p11;
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   -!- 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. DDX54/DBP10
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS480389; EDO18419.1; -; Genomic_DNA.
DR   RefSeq; XP_001646277.1; XM_001646227.1.
DR   AlphaFoldDB; A7TGW7; -.
DR   SMR; A7TGW7; -.
DR   STRING; 436907.A7TGW7; -.
DR   EnsemblFungi; EDO18419; EDO18419; Kpol_1032p11.
DR   GeneID; 5546706; -.
DR   KEGG; vpo:Kpol_1032p11; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   InParanoid; A7TGW7; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   PhylomeDB; A7TGW7; -.
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; IPR012541; DBP10_C.
DR   InterPro; IPR033517; DDX54/DBP10.
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   PANTHER; PTHR24031:SF292; PTHR24031:SF292; 1.
DR   Pfam; PF08147; DBP10CT; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM01123; DBP10CT; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT   CHAIN           1..977
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000310246"
FT   DOMAIN          152..324
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          403..554
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          871..977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           121..149
FT                   /note="Q motif"
FT   MOTIF           272..275
FT                   /note="DEAD box"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..57
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..107
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..925
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..977
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         165..172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   977 AA;  110240 MW;  16BE91CB63D545BD CRC64;
     MGIISKRKRH VEDSNSSSDD DDGFDITSNI GLNTADSSDE SESSGDDEEE VQDIVDFSDE
     EDTKKKPKSS NKTLTDNNSF PSLEISDDED SNNKGDHEDD DDDLNDYFSI NNSEKSKHKK
     GSFPSFGFSK LILSNVHKKG FRQPTPIQRK TIPLILQKRD IVGMARTGSG KTAAFVLPMI
     EKLKSHSSKI GARAVILSPS RELALQTHRV FKEFSKGTHL RSVLLTGGDS LEDQFSMMMS
     NPDVIVATPG RFLHLKVEMS LDLKTVEYVV FDEADRLFEM GFQEQLNELL AALPMNRQTL
     LFSATLPSSL VDFAKAGLTN PVLVRLDAET KISENLEILF LSTKNEEREN NLLYLLQDVI
     KIPLGTDDQI KKLSDFNKSL SDSDSEDEDN KGKQNSRKSK KGKFQKLKVS ASNELPTEKS
     TIVFAPTRHH VEYITQLLKD SGFLVSYLYG TLDQHARKRQ LLNFRAGLTS ILVVTDVAAR
     GVDIPMLANV INYSLPASSK IFIHRVGRTA RAGNRGWAYS IVSETELPYM LDLELFLGKK
     ILLTSMYEAS CKLMKSKWIA DGNTESSFED PKISYTNRLV LGSAPRYDIE SVGDLYKNII
     ESNFDLQMAK KVSLKAEKLY CRTRTAASPE SIKRSKEVIA SGWDEQNIRF GRNLEKEKLN
     FLAKFQNRRN KETVFEFGKN PNDDTAILMQ KRRKQIAPIQ RKARKRQELL DKERVAGLTH
     KIEDEILKGE DHEAGYSVPE EALKSFEDAD KILEEQESSR KKKSKTFRDP NFFISHYAPA
     GDIQDKQLQI TSGFTNDAAQ AAYDLNDDDK VQVHKQTATV KWDKKRKKYV NMQGIDNKKY
     IIGESGQKIP ASFKSGKFAE WSKSRNIKGI KTGARETSIP TNLLSDPTTD SGSQRGPGGR
     FKHKQNKAPR LPDKFRDDYQ SQKKKVQSAI ERGVSVKGFG GSSGNTELKT TAQIRKERMA
     KEKKRQKNAR PTKKRKF