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Database: UniProt
Entry: Q4P7M1
LinkDB: Q4P7M1
Original site: Q4P7M1 
ID   DBP9_USTMA              Reviewed;         686 AA.
AC   Q4P7M1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   29-OCT-2014, entry version 63.
DE   RecName: Full=ATP-dependent RNA helicase DBP9;
DE            EC=3.6.4.13;
GN   Name=DBP9; ORFNames=UM03892;
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.,
RA   Saville B.J., Banuett F., Kronstad J.W., Gold S.E., Mueller O.,
RA   Perlin M.H., Woesten H.A.B., de Vries R., Ruiz-Herrera J.,
RA   Reynaga-Pena C.G., Snetselaar K., McCann M., Perez-Martin J.,
RA   Feldbruegge M., Basse C.W., Steinberg G., Ibeas J.I., Holloman W.,
RA   Guzman P., Farman M.L., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   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.,
RA   Muensterkoetter M., Haase D., Oesterheld M., Mewes H.-W.,
RA   Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.K.,
RA   Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen
RT   Ustilago maydis.";
RL   Nature 444:97-101(2006).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in the biogenesis of
CC       60S ribosomal subunits and is required for the normal formation of
CC       25S and 5.8S rRNAs. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD
CC       box family of RNA helicases and controls ATP binding and
CC       hydrolysis.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX56/DBP9
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00541}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00542}.
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DR   EMBL; AACP01000132; EAK85065.1; -; Genomic_DNA.
DR   RefSeq; XP_760039.1; XM_754946.1.
DR   ProteinModelPortal; Q4P7M1; -.
DR   STRING; 5270.UM03892.1; -.
DR   EnsemblFungi; UM03892T0; UM03892P0; UM03892.
DR   GeneID; 3631977; -.
DR   KEGG; uma:UM03892.1; -.
DR   eggNOG; COG0513; -.
DR   HOGENOM; HOG000253015; -.
DR   InParanoid; Q4P7M1; -.
DR   KO; K14810; -.
DR   OMA; CILMSAT; -.
DR   OrthoDB; EOG783N4K; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR000560; His_Pase_superF_clade-2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
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; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    686       ATP-dependent RNA helicase DBP9.
FT                                /FTId=PRO_0000232346.
FT   DOMAIN       90    275       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      288    543       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     103    110       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        59     87       Q motif.
FT   MOTIF       221    224       DEAD box.
SQ   SEQUENCE   686 AA;  75202 MW;  C7F924882EF3AFF8 CRC64;
     MSEPSSSKVK ADSLLPPAKS TTAATAARSA NGSTNTGASQ LTKHGIELPS QEDAERLGFN
     VFSHILDPRL LRALADLGYG IPTPIQQKAI PLALAGKDIL ARARTGSGKT LAYGLPLLQK
     VLDAKSAVAK SDANHQLTRA LVLVPTRELA EQVFRHLSVV IEYVRDDIRL VNVAREASEK
     VQRLLLSEKP DVVIATPSKA LNYLQNASLD LKSGMESLAI DEADLILSYG HDADVKSLLG
     ANFLPSHFQS FLMSATMTSD VSKLKGLLLR NPVVLKLNHD DEAASGSNLV QFYTKTTEED
     KFLLAYVILK LKLIRGKAIL FVNELERGYR LKLFLEKFGL RACVLNAELP INSRYSIVEE
     FNKGKFDYIV ATDEPTGASG NMQDDEGDDE EEDADEREAD EVDEQAEDQR EAGKKRKSSE
     HAGAETKSNK SKVSQHRKGK NGASEYGVSR GVDFINVSCV INFDLPTSVD SYIHRVGRTA
     RGGASGTALS FVVPSDQVGR SKYLYCASTT RDESVFKMLN KPSTISLLGS ALQEWKYDSS
     SVAGFHYRVT DTLKSITKAL IREARIKELK NEILTSSKLQ SHFEDHPDDL AFLQHDKALL
     TSRAQQSHLK HVPQYLVPKI INPGAKLTKS SGSEYKGYVP KNKIKDGAND RKNKGGKRRS
     STGKNTTGAA GKSRKKVDPL RKFSNK
//
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