ID   DBP10_USTMA             Reviewed;        1154 AA.
AC   Q4P3W3; A0A0D1CUM2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=ATP-dependent RNA helicase DBP10;
DE            EC=3.6.4.13;
GN   Name=DBP10; ORFNames=UMAG_05200;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CM003143; KIS70128.1; -; Genomic_DNA.
DR   RefSeq; XP_011388242.1; XM_011389940.1.
DR   AlphaFoldDB; Q4P3W3; -.
DR   SMR; Q4P3W3; -.
DR   STRING; 5270.UM05200P0; -.
DR   EnsemblFungi; KIS70128; KIS70128; UMAG_05200.
DR   GeneID; 23565152; -.
DR   KEGG; uma:UMAG_05200; -.
DR   VEuPathDB; FungiDB:UMAG_05200; -.
DR   eggNOG; KOG0337; Eukaryota.
DR   HOGENOM; CLU_003041_5_1_1; -.
DR   InParanoid; Q4P3W3; -.
DR   OMA; MRWDKKS; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000000561; Chromosome 4.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; IBA:GO_Central.
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..1154
FT                   /note="ATP-dependent RNA helicase DBP10"
FT                   /id="PRO_0000232319"
FT   DOMAIN          177..363
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          446..602
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          16..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          885..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1043..1154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           144..172
FT                   /note="Q motif"
FT   MOTIF           311..314
FT                   /note="DEAD box"
FT   COMPBIAS        17..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..845
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..918
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1061
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1094..1136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         190..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   1154 AA;  126209 MW;  938D52BEC954DCCC CRC64;
     MAKTIDFLAS DGEDNFAART ISATSKPNRN DATASSSKPQ KRARRSTKGS DDDGNDDFDI
     ASSLLASAAE PAAVGMLSSS QQASQKAYAS RVSAKDDDDD DARFIASVMQ HANIKAGLEV
     AKKALSGKNK GKNKLGSGVV TGGGSFQSMG LHPSLLRSLL IRGFTTPTPI QRQAIPAIMS
     QPPRDVVGMA RTGSGKTLAY LIPLINRLNG RHSPTFGIKS LILCPSRELA VQILRVGKEI
     ARGWKADAGE GQDSRGEAIR WAIIVGGESL DEQFGIMSNN PDVVIATPGR MLHLTVEMNL
     DLKSVEYVVF DEADRLFEMG FAEQLEEMLL RLPPTRQTLL FSATLPKKLV EFTKAGLQAN
     PKLVRLDADS KISADLRMAF FSVKPSEKEA ALLVLLRDVI GVPLGEQAAR DLDEEAQFNE
     DASDNQADGQ RSRGYGNRRA EFKGKTKDKH LGNKRKRGGP GGALELLPHQ TIIFCATKHH
     VEYLLLLLTT TGYACSHIYS SLDQATRGIQ MSRFRRGQNS LLIVTDVAAR GIDLPVLEHV
     VNFDFPPQPR TFVHRVGRTA RAGRNGWAWS MCTNAELPYL CDLQLFLARP LVSSHTAIAA
     LANGRDVASA DALGLHDSLI LGTLPREALD LETEFISSSL TNTSSSTAHD FPALRAVADR
     AQQKYEKSIA KASQESHRRA KEMVKLGSIE QINIRTASGR EGQVPEWTLA GSPLEEMAVH
     DVVKRPEVYG LNRANKADAV TSALGSDRMD DKVKRGTDNA LKEADEAAKR AALLAKVNAF
     RPQETVFEIG IRGDATPLGA LMRSRRQTMQ VKTKRAEALE ARKRAIEGGG DAMEDDEEVT
     KPKVAARNKG KKKATAGKAD NDEAVVGDAM VDMEQADEAD ILAAFDTTKP SKAQVQREAL
     TDSETDASES DRDAASARHT KRARTKKAAP TSYRDPNFYL SYEQQGSTSE RGYSLNNARS
     HTDSFIQQAS AVSFDLAGDD ATLGTQSQRP NVTRWDSKKK NFIQATVGAD NKKMIRTESG
     VRLPASFRSG RYEDWKREKR IDMPKTGEIE SNNHRVHERS PPETSVMGLK RFRHTKLSAP
     KTAGVFGNRR PGQPKRQAAK DEVKSARQIQ KDRELKEKRR EKNARPSKSD TNRRAKRGAA
     RRGRGGHGPR GASR