DBP4_ASPFU
ID DBP4_ASPFU Reviewed; 787 AA.
AC Q4WM60; Q8NJM5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=ATP-dependent RNA helicase dbp4;
DE EC=3.6.4.13;
GN Name=dbp4; ORFNames=AfA12H2.06, AFUA_6G11070;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RA Harris D.E., O'Neil S., Knowles D.G., Hall N., Quail M.A., Woodward J.R.,
RA Denning D.W., Anderson M.J., Barrell B.G.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD37144.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL807577; CAD37144.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AAHF01000006; EAL88954.1; -; Genomic_DNA.
DR RefSeq; XP_750992.1; XM_745899.1.
DR AlphaFoldDB; Q4WM60; -.
DR SMR; Q4WM60; -.
DR STRING; 746128.CADAFUBP00007513; -.
DR EnsemblFungi; EAL88954; EAL88954; AFUA_6G11070.
DR GeneID; 3508297; -.
DR KEGG; afm:AFUA_6G11070; -.
DR VEuPathDB; FungiDB:Afu6g11070; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q4WM60; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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..787
FT /note="ATP-dependent RNA helicase dbp4"
FT /id="PRO_0000232194"
FT DOMAIN 78..252
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 278..437
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 47..75
FT /note="Q motif"
FT MOTIF 200..203
FT /note="DEAD box"
FT COMPBIAS 494..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 787 AA; 89304 MW; 2B243F55A9D144B4 CRC64;
MAPAAGPRTG KHAKPQRSKT LKRKRGQEEL SSLIQRVEDL DLKGIFKSFS DLPLSEPTAS
GLASSHYKTL TDIQSRAISH ALKGRDILGA AKTGSGKTLA FLVPVLENLY RKQWAEHDGL
GALILSPTRE LAIQIFEVLR KIGRYHTFSA GLVIGGKSLK EEQERLGRMN ILVCTPGRML
QHLDQTALFD TYNLQMLVLD EADRILDLGF QQTVDAIIGH LPKERQTLLF SATQTKKVSD
LARLSLQDPE YVAVHETASS ATPSKLQQHY VITPLPQKLD ILWSFIRSNL KSKTMVFLSS
GKQVRFVYES FRHLQPGIPL MHLHGRQKQG GRLDIVTRFS QSKHCVLFST DVAARGLDFP
AVDWVIQLDC PEDADTYIHR VGRTARYERE GRAVLFLDPS EEEGMLKRLE QKKVPIEKIN
IKANKQQSIK DQLQNMCFKD PELKYLGQKA FISYVKSVYI QKDKEIFKLK ELKLDEFAAS
LGLPGAPRIK FIKGDDTKQR KNAPRAAAHL LSDDDDTDEE DGEKKSKKKE EPQVRTKYDR
MFERRNQDVL AEHYSKLIND DGTMVAPNAG AGADADEDDD FLSVKRRFDA GDKDLGSSGD
EDDESEKGNK KNVKVRREKL LKSKKKLLKF KGKGTKLVYD DEGNPHELYE LEDEEQFKAR
GDAKDQQAKF LAEEAERTRL ADMEDKEIAK QKRREKKEKR KARERELLAE AEEEETLVQL
PPYEGDQDDE APRPSKKPKV KFTEANDREE AEPWYKKSKK SSDQAAHTPR QIQTLEDLES
LATGLLG
