DBP4_PHANO
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 03-AUG-2022, entry version 90.
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) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC 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 and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- FUNCTION: ATP-dependent RNA helicase required for ribosome biogenesis.
CC Involved in the release of U14 snoRNA in pre-ribosomal complexes.
CC Required for pre-rRNA cleavage at site A2 (By similarity).
CC {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 -!- SUBUNIT: Interacts with the U3 and U14 snoRNAs. Associates with pre-
CC 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 box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX10/DBP4
CC subfamily. {ECO:0000305}.
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DR EMBL; CH445334; EAT85746.1; -; Genomic_DNA.
DR RefSeq; XP_001797448.1; XM_001797396.1.
DR AlphaFoldDB; Q0UMB9; -.
DR SMR; Q0UMB9; -.
DR STRING; 13684.SNOT_07095; -.
DR EnsemblFungi; SNOT_07095; SNOT_07095; SNOG_07095.
DR GeneID; 5973938; -.
DR KEGG; pno:SNOG_07095; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q0UMB9; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0034512; F:box C/D RNA binding; IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0034511; F:U3 snoRNA binding; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
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; SM01178; DUF4217; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..803
FT /note="ATP-dependent RNA helicase DBP4"
FT /id="PRO_0000256003"
FT DOMAIN 80..256
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 269..441
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..77
FT /note="Q motif"
FT MOTIF 204..207
FT /note="DEAD box"
FT COMPBIAS 495..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
