DBP4_VANPO
ID DBP4_VANPO Reviewed; 768 AA.
AC A7TJ71;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, 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=Kpol_1004p13;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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; DS480400; EDO17640.1; -; Genomic_DNA.
DR RefSeq; XP_001645498.1; XM_001645448.1.
DR AlphaFoldDB; A7TJ71; -.
DR SMR; A7TJ71; -.
DR STRING; 436907.A7TJ71; -.
DR EnsemblFungi; EDO17640; EDO17640; Kpol_1004p13.
DR GeneID; 5545878; -.
DR KEGG; vpo:Kpol_1004p13; -.
DR eggNOG; KOG0343; Eukaryota.
DR HOGENOM; CLU_003041_26_1_1; -.
DR InParanoid; A7TJ71; -.
DR OMA; YDKMFER; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; A7TJ71; -.
DR Proteomes; UP000000267; 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 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..768
FT /note="ATP-dependent RNA helicase DBP4"
FT /id="PRO_0000310201"
FT DOMAIN 72..246
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 280..439
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 581..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 41..69
FT /note="Q motif"
FT MOTIF 194..197
FT /note="DEAD box"
FT COMPBIAS 585..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 768 AA; 87313 MW; 7918D5E0DB99FF90 CRC64;
MAKKQRYNTT QRKELRKKEV DYIKELETKI DEYDASINKP VFFKDLPISN STLKGLNDSA
FLKLTDIQRD SIPMSLKGYD ILGAAKTGSG KTLAFLIPVL EKLYRERWTE FDGLGALIIS
PTRELAMQIY EVLLKIGTST SFSAGLVIGG KDVKFEMERI SKINILIGTP GRILQHMDQA
IGLNTSNLQM LVLDEADRCL DMGFKKTLDA IVSNLPPTRQ TLLFSATQSQ SLEDLARLSL
TDYKTIGNPD ILNPSNGKVL GPSTPETLQQ SYINVELPDK LDMLYSFIKS HLKSKMIVFL
SSSKQVHFVY ETFRKMQPGI SLMHLHGRQK QKARTETLDK FNRAQHVCLF ATDVVARGID
FPAIDWVVQV DCPEDVDTYI HRVGRCARYG KQGKSMIMLT PQEEEGFLKR LASRKIEPSK
LTIKQSKKKS IKPQLQSLLF KDPELKYLGQ KAFISYIRSV FIQKDKEVFK FEELPTDEFA
NSLGLPGAPK IKMKGTKSVE QIKQMKNASR QLLSLAKTNE DGELVEEKSK QPVRTKYDKM
FERKNQTVLS EHYLNITKAQ AQEDEDDDFI SIKRTDHALN EEELPQLSLP SSRRAQKRAL
SKKASLSTKG NATRVVFDDD GAAHPVYELQ GEEDFIKAGA AEDQKLEYLQ KEKDVMNEVD
VEDKQVAKQK KQEKKRKRLE AIRREMEADM DNESSGEEKV PFLGTGNLSD DMQDPDSDDE
EGSRLRKRSR FETNNNYNDN DSDDGVIQVE EPQTLEDLES LTARLIDN
