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Database: UniProt
Entry: Q0UMB9
LinkDB: Q0UMB9
Original site: Q0UMB9 
ID   DBP4_PHANO              Reviewed;         803 AA.
AC   Q0UMB9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   29-OCT-2014, entry version 51.
DE   RecName: Full=ATP-dependent RNA helicase DBP4;
DE            EC=3.6.4.13;
GN   Name=DBP4; ORFNames=SNOG_07095;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173)
OS   (Glume blotch fungus) (Septoria nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Pleosporomycetidae; Pleosporales; Pleosporineae;
OC   Phaeosphaeriaceae; Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing
RT   and EST analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: ATP-dependent RNA helicase required for ribosome
CC       biogenesis. Involved in the release of U14 snoRNA in pre-ribosomal
CC       complexes. Required for pre-rRNA cleavage at site A2 (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with
CC       pre-ribosomal complexes (By similarity). {ECO:0000250}.
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. DDX10/DBP4
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; CH445334; EAT85746.1; -; Genomic_DNA.
DR   RefSeq; XP_001797448.1; XM_001797396.1.
DR   ProteinModelPortal; Q0UMB9; -.
DR   SMR; Q0UMB9; 51-259.
DR   EnsemblFungi; SNOT_07095; SNOT_07095; SNOG_07095.
DR   GeneID; 5973938; -.
DR   KEGG; pno:SNOG_07095; -.
DR   InParanoid; Q0UMB9; -.
DR   KO; K14776; -.
DR   OMA; YLGQRAF; -.
DR   OrthoDB; EOG7FR7R5; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
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; -; 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   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF13959; DUF4217; 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.
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    803       ATP-dependent RNA helicase DBP4.
FT                                /FTId=PRO_0000256003.
FT   DOMAIN       80    256       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      269    441       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      93    100       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF        49     77       Q motif.
FT   MOTIF       204    207       DEAD box.
SQ   SEQUENCE   803 AA;  90190 MW;  54ABD87430285A41 CRC64;
     MGAPGITGRT RPTKVKKQAS QQKRKRDDVD VEKLEQAVTE LDPKTGTYND FSDLPLSDPT
     KQGLKACHFA VMTDIQRKAV PLALKGHDIL GAAKTGSGKT LSFIIPVLEN LYRLQHVGAD
     AGLGALILSP TRELAIQIFD VLCKIGKHGH MFAAGLLIGG KSLESERQAL PRMNILVATP
     GRMLQHLSQT AAFLVDDLKM LVLDEADRIL DMGFQRDVDA IIDYLPKERQ TLLFSATQSK
     KVSDLARLSL QDPEYVSVHA EDKSATPKSL QQNYIICPLE EKLDTLWSFI QASKKSKILV
     FFSSAKAVRF VYESFRHMQP GIPLLHIHGR QKQGARLDTT AKFSSAKNSC LFATDVAARG
     LDFPAVDFVI QVDCPDDVDT YIHRVGRTAR YNREGRGVLF LAPSEEEGML KRLEAKKVPV
     EAINVRQKKR QSIKEQLQNM CFQDPALKYL GQKAFMTYVK SVYLQKDKEV FQLKEYDLEA
     FAASLGLPGT PRIKFLKDDN SKQKKQASRQ TIEVSDSDEE EAPKAEKPVR TKYDRMFERK
     NQDVLAEHYK KLVRDGDEEI SAPANDFSGE ATTNGADDDF LAIKRRIPAD DEDEDFGGEA
     SVAPGGRVVH LAGASQPLII DSNRREKLLQ SKKKLTKLMD RGKKLVYDDD GNPHEVYELE
     TEADFKAKGL PEHQRQKFIE AAREVVQTAD VEDKATARAK RKEKLRKRKE RERGEAEDDG
     DEAVELEDTG ENPLANFLAD AQYTDDEQEE VEQPKKKEKK WFQSDSEDEE KSSKKKRKKA
     KQQVVEEPET LEDMEALAAG LLG
//
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