DBP3_PHANO
ID DBP3_PHANO Reviewed; 592 AA.
AC Q0UY62;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ATP-dependent RNA helicase DBP3;
DE EC=3.6.4.13;
GN Name=DBP3; ORFNames=SNOG_03302;
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 60S ribosomal subunit
CC synthesis. Involved in efficient pre-rRNA processing, predominantly at
CC site A3, which is necessary for the normal formation of 25S and 5.8S
CC rRNAs (By similarity). {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. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; CH445328; EAT90033.1; -; Genomic_DNA.
DR RefSeq; XP_001793872.1; XM_001793820.1.
DR AlphaFoldDB; Q0UY62; -.
DR SMR; Q0UY62; -.
DR STRING; 13684.SNOT_03302; -.
DR PRIDE; Q0UY62; -.
DR EnsemblFungi; SNOT_03302; SNOT_03302; SNOG_03302.
DR GeneID; 5970729; -.
DR KEGG; pno:SNOG_03302; -.
DR eggNOG; KOG0331; Eukaryota.
DR HOGENOM; CLU_003041_1_5_1; -.
DR InParanoid; Q0UY62; -.
DR OMA; KKKTHDM; -.
DR OrthoDB; 471730at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; 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:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000464; P:endonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); 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; 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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..592
FT /note="ATP-dependent RNA helicase DBP3"
FT /id="PRO_0000255994"
FT DOMAIN 209..382
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 413..562
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 179..206
FT /note="Q motif"
FT MOTIF 330..333
FT /note="DEAD box"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 222..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 592 AA; 64007 MW; 3F51B4398EAC4C6F CRC64;
MGKRPIEDDA VASSELSRKK SKKEKSGKSK KSVIGEGADT NGHAPAAETT VDGSENEALS
KAERKAAKKA KKEAKEASKA GKADAPTVEN DEEAAKAARK AARKAEKKKL KEAEKTASSA
PTEASSVPAQ TLSSSNAGSY TEHTELAQLP QSEIDAFLTK NTMTIEDPKP AARKLRPIVN
FKYLPVTDES QRAPFAGFTA PTPIQAATWP FLLSGRDMVG VAETGSGKTL AFGVPCVRAI
LSLPKDKRKG IKAVIVSPTR ELAVQIYDQL VALAHPAGLS VVCVYGGVPK DPQVAACRKA
HIVVATPGRL NDLIGDGSAD LSNADYVVLD EADRMLDKGF EEPIRQIISQ TPKKRQTLMF
TATWPPSVRD LASTFMVSPV RITIGDNQSG ELRANVRIKQ LVEVLDPHAK EQRLLQLLKQ
YQSGKNKDDR ILVFCLYKKE AMRIENFIRM KGFRVGGIHG DLSQEKRSAS LAAFKEGQVP
LLVATDVAAR GLDIPAVKLV INVTFPLTAE DYVHRIGRTG RAGKEGLAIT FFTEHDKGLS
GSLINVLKAA NQEVPEELLK FGTTVKKKEH GAYGAFYKDV DNTKAATKIT FD
