DBP8_VANPO
ID DBP8_VANPO Reviewed; 431 AA.
AC A7TK63;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ATP-dependent RNA helicase DBP8;
DE EC=3.6.4.13;
GN Name=DBP8; ORFNames=Kpol_1062p5;
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-binding RNA helicase involved in 40S ribosomal subunit
CC biogenesis and is required for the normal formation of 18S rRNAs
CC through pre-rRNA processing at A0, A1 and A2 sites. Required for
CC vegetative growth (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. DDX49/DBP8
CC subfamily. {ECO:0000305}.
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DR EMBL; DS480406; EDO17298.1; -; Genomic_DNA.
DR RefSeq; XP_001645156.1; XM_001645106.1.
DR AlphaFoldDB; A7TK63; -.
DR SMR; A7TK63; -.
DR STRING; 436907.A7TK63; -.
DR PRIDE; A7TK63; -.
DR EnsemblFungi; EDO17298; EDO17298; Kpol_1062p5.
DR GeneID; 5545504; -.
DR KEGG; vpo:Kpol_1062p5; -.
DR eggNOG; KOG0340; Eukaryota.
DR HOGENOM; CLU_003041_1_1_1; -.
DR InParanoid; A7TK63; -.
DR OMA; EIKQESM; -.
DR OrthoDB; 744428at2759; -.
DR PhylomeDB; A7TK63; -.
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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
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; 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..431
FT /note="ATP-dependent RNA helicase DBP8"
FT /id="PRO_0000310237"
FT DOMAIN 33..209
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 242..389
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 406..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2..30
FT /note="Q motif"
FT MOTIF 155..158
FT /note="DEAD box"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 431 AA; 47794 MW; 4B684CBEC8AD958D CRC64;
MQDFKSLGLS RWLVESLNAM RITHPTAIQK HCIPEILKGR DCIGGAKTGS GKTIAFAGPM
LSQWSDDPSG MFGVVLTPTR ELAIQIAEQF TALGSSMNIR VCLVVGGESI VKQALELQKK
PHFIIATPGR LAHHILSSGE EVVGGLSRVK YLVLDEADLI LTQTFAADLS TCIAKLPPKQ
KRQTLLFTAT ITDQVRALQN APAQDSKPPL FAYEVENVDN VAVPSTLKLE YLLVPEHVKE
AYLYQLLTCE DYKDSSVIVF VNRTTAAEVL RRTLRSLEVR VASLHSQMPQ SERINSLQRF
RANAARVLIA TDVAARGLDI PTVELVINYD IPQDPDTFIH RSGRTARAGR SGDAISFVTP
RDVSRIEAIE ERINKKMDEC KKVHDTAVIR KALTKVTKAK RESLMDMEKA NFGEKRKTQK
KKNLAEKSLR A