DBP4_CHAGB
ID DBP4_CHAGB Reviewed; 825 AA.
AC Q2H2J1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATP-dependent RNA helicase DBP4;
DE EC=3.6.4.13;
GN Name=DBP4; ORFNames=CHGG_04005;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408032; EAQ87386.1; -; Genomic_DNA.
DR RefSeq; XP_001223219.1; XM_001223218.1.
DR AlphaFoldDB; Q2H2J1; -.
DR SMR; Q2H2J1; -.
DR STRING; 38033.XP_001223219.1; -.
DR EnsemblFungi; EAQ87386; EAQ87386; CHGG_04005.
DR GeneID; 4391717; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; Q2H2J1; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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 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..825
FT /note="ATP-dependent RNA helicase DBP4"
FT /id="PRO_0000256000"
FT DOMAIN 84..258
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 284..439
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 53..81
FT /note="Q motif"
FT MOTIF 206..209
FT /note="DEAD box"
FT COMPBIAS 15..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..695
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 825 AA; 91324 MW; 52D67004262A40A3 CRC64;
MAAGNAKGGF AHRNKSVPKK TDAKSLKRKR GQEDLGKLKA AIEELDPKSP AIKQFTDLPL
CEATASGLRA SHFEVLTDVQ RAAIPLALKG RDILGAAKTG SGKTLAFLVP VLEKLYHAKW
TEYDGLGALI ISPTRELAVQ IFEVLRKIGR NHFFSAGLVI GGKSLKEEAE RLGRMNILVC
TPGRMLQHLD QTANFDVNNL QILVLDEADR IMDMGFQSAV DALVEHLPTT RQTLLFSATQ
SKRVSDLARL SLKEPEYVSA HEAAVSATPT NLQQSYIVTP LAEKLDTLFG FLRTNLKSKI
IVFFSSGKQV RFVFESFKRM QPGIPLLHLH GRQKQVARME ITSRFSSAKY GCLFATDVVA
RGVDFPAVDW VVQADCPEDA DTYIHRVGRT ARYESKGRAV LFLEPSEEAG FLKRLEQKKV
PLQKVNVREN KKKSIKNELQ SYNFQSPDLK YLGQKAFISY TRSIYLQKDK EVFNFNKLDL
DGYAASLGLA GTPQIKYQKG DDIKRLKNAS RAAISSGSES DSDDEGKPKK DKKQVRTKYE
KMAERQNQDI LSSHYRKLLG EDGDAAASDD DDDFLSVKRV LADDAQIDAA AGGDATNTTT
TEPKVIKLGN SELIIDSNRR EKLLKSKKKL LKYMDKGTKL VFDDDGVARP VYELQDEDDF
AQQGPAAALR QQFVAAESEK VKEADVDDKQ AAKMRRREKR ERQKARERGE ELERVGAGGG
GGGVAMLDGG EGDEGDEDPL ALLRSLPIAG EESDGGRGGG GEDEGDDGEV EPPRKKARKW
FQDDSDQEEE ERQKKKKGGK KVIEMAEEPE NLEDLEALAA GLLED
