DBP4_PICST
ID DBP4_PICST Reviewed; 765 AA.
AC A3GGE9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=ATP-dependent RNA helicase DBP4;
DE EC=3.6.4.13;
GN Name=DBP4; ORFNames=PICST_51414;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(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; AAVQ01000001; EAZ63509.2; -; Genomic_DNA.
DR RefSeq; XP_001387532.2; XM_001387495.1.
DR AlphaFoldDB; A3GGE9; -.
DR SMR; A3GGE9; -.
DR STRING; 4924.XP_001387532.2; -.
DR PRIDE; A3GGE9; -.
DR EnsemblFungi; EAZ63509; EAZ63509; PICST_51414.
DR GeneID; 4851348; -.
DR KEGG; pic:PICST_51414; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; A3GGE9; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
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 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..765
FT /note="ATP-dependent RNA helicase DBP4"
FT /id="PRO_0000285141"
FT DOMAIN 78..252
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 266..438
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..735
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 501..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..735
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 765 AA; 87257 MW; E581A5E1A0AF8379 CRC64;
MAKPRRNNKN KKGQSRSQAR EKEEAELLKL QERIDQYDPA VDEKSISQFS DLPITQETLR
GLNESSFMSL TDIQKKTIPI ALKGEDLMGT ARTGSGKTLA FLIPVVESLI RNKITEHDGL
AALIVSPTRE LAVQTFEVLT KIGKYNTFSA GLVTGGKDVQ YEKERVSRMN ILVGTPGRIS
QHLNEAVGME TSNLQVLVLD EADRCLDMGF KKQIDNIVGH LPPTRQTLLF SATVSDSVKD
LARLSLTNPK RIGVSSDQDV SATPESLDQY YIRIPLDEKL DVLWSFIKSH LKSKILVFFS
SSKQVQYAYE TFRTLQPGIS LLKLYGRHKQ TSRLETTVKF TQAQYACLFA TDIVARGLDF
PAIDWVVQVD CPEDAVTYVH RVGRAARFGR QGKSLLMLLP SEEEGMLKRL ENNKIEPKFM
NIKQKSKKSI RPQLQSLCFK DPMIKNLGQR AFISYYKSVY IQKDKDVFKV EELPSEKYAA
SLGLPGAPKI KIKGGSSSKE KKNASRQLVA LSKTNEDGES VENEASKVRT KYDRMFERKN
QNVLSEHYLK LNGSQTKEDE DEEEEDDFMS VKRKDHELTE VELPDLTIPV SKRQAKKALS
KKLSISTKGN PTKLKFDDEG VAHAIYELED EEDFIKRGDA KEQKKAFVSR ETEVMNEADE
EDKIMAKEKR QEKKRKRKEV EKRMRDEELQ SGDDEETVYT LGGDVDLERD MEYSTDEEEQ
PQNKKPKWFE NDKHNRKNPV NHIVEIDEPE TLEDLESLTA RLLQH
