ID   DBP7_USTMA              Reviewed;         974 AA.
AC   Q4P0Y5; A0A0D1DP70;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=ATP-dependent RNA helicase DBP7;
DE            EC=3.6.4.13;
GN   Name=DBP7; ORFNames=UMAG_06228;
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. DDX31/DBP7
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CM003161; KIS65851.1; -; Genomic_DNA.
DR   RefSeq; XP_011392582.1; XM_011394280.1.
DR   AlphaFoldDB; Q4P0Y5; -.
DR   STRING; 5270.UM06228P0; -.
DR   PRIDE; Q4P0Y5; -.
DR   EnsemblFungi; KIS65851; KIS65851; UMAG_06228.
DR   GeneID; 23565888; -.
DR   KEGG; uma:UMAG_06228; -.
DR   VEuPathDB; FungiDB:UMAG_06228; -.
DR   eggNOG; KOG0348; Eukaryota.
DR   HOGENOM; CLU_003041_26_2_1; -.
DR   InParanoid; Q4P0Y5; -.
DR   OMA; QMGFERW; -.
DR   OrthoDB; 973872at2759; -.
DR   Proteomes; UP000000561; Chromosome 22.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; 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:0042254; P:ribosome biogenesis; IBA:GO_Central.
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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 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..974
FT                   /note="ATP-dependent RNA helicase DBP7"
FT                   /id="PRO_0000256028"
FT   DOMAIN          236..477
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          531..747
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           200..230
FT                   /note="Q motif"
FT   MOTIF           381..384
FT                   /note="DEAD box"
FT   COMPBIAS        31..46
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..851
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         249..256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   974 AA;  104373 MW;  4019E14C5C481F4C CRC64;
     MDDNDDGLML NFAAPAAGSA SVSSKRSKQT AKARFAQKRT AHQLRKQAPK QNRSVAPIES
     VQGVVTPASA RLSPAPASAN ESPAAKRQRI EATSTSSAAL SAPRFDPRSE TAKSAPITSR
     SSQTTSSAAS SSRKAIAPVT KLAGSSFASA GASSSASKQT NGGIVSTLFP AHGVLEDSSI
     ALTPFQRKAY HPTNAPSVGS DFASCGLDPL LVYHLASKMN IGSNPTAIQK AALPHLLHPG
     LDRDILIQAQ TGSGKTLTYL LPIVQSLLPL CEESFIDRSV GTLAIVLAPT RELARQIYEV
     LEKLVSLALS LKEQNQEVEG TVRRTRWLVP GLLSGGSTKN HEKQRLRKGC PILVSTPGRL
     LDHLQNTSSF DVGKCRWLVL DEADRLLEMG FEEQLTGIVR ALDGRRNLAC TAARQAMPAY
     QEGTAPGDAD WIPDADVMDT LGMAWWAHAR RVVLCSATLD EHVQVLAGKT LVNPKIIRGV
     KSDAAETSTQ VTTDADSTLQ KRAVKFAAPA QLAQSFVTTP PKLRLVTLLS LLRSYISRAR
     RQWQHVDHQA GAGRVIVFMS CTDSVDFHYA AFGGARMNAS ENDASADVQV QDAQLATHVT
     SELIPDVPIY RLHGSMTQQE RISSLKGFSG IRTKHSAERQ GFQGSILLCT SVASRGLDLP
     EVGCVIQLDP PTEGGIEEYL HRVGRTARVG RAGESWLLVL PQELGWVEHV LESHMTIQSS
     DSASCSCSEI ESKKQGSTRK ITPASIELVL QQGMGGTMGT LEYQSRATEV QLAFERWVIS
     GERPSLLARK AFLSHVRAYA THSAEEKQYF NVRALHLGHL AKAFALREAP RSLGAKSSAI
     GASSTPASSH ETTNKKRMRI APDTAESDSS SDSSDDAGSD YESHSNKKGD AFELDKAALA
     KLTESIVANA DGSNRSKKLA REAQKAAAAA GVADDKAKQT DAEARMYAKV RALGKMSKKH
     GVLGAHAADE FQIA