DBP7_PICST
ID DBP7_PICST Reviewed; 733 AA.
AC A3LWH3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=ATP-dependent RNA helicase DBP7;
DE EC=3.6.4.13;
GN Name=DPB7; ORFNames=PICST_60418;
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-binding RNA helicase involved in the biogenesis of 60S
CC ribosomal subunits and is required for the normal formation of 25S and
CC 5.8S rRNAs. {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 -!- MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX31/DBP7
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000499; ABN67277.2; -; Genomic_DNA.
DR RefSeq; XP_001385306.2; XM_001385269.1.
DR AlphaFoldDB; A3LWH3; -.
DR SMR; A3LWH3; -.
DR STRING; 4924.XP_001385306.2; -.
DR PRIDE; A3LWH3; -.
DR EnsemblFungi; ABN67277; ABN67277; PICST_60418.
DR GeneID; 4839286; -.
DR KEGG; pic:PICST_60418; -.
DR eggNOG; KOG0348; Eukaryota.
DR HOGENOM; CLU_003041_26_2_1; -.
DR InParanoid; A3LWH3; -.
DR OMA; AVHIKAD; -.
DR OrthoDB; 973872at2759; -.
DR Proteomes; UP000002258; Chromosome 5.
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; 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; 2.
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..733
FT /note="ATP-dependent RNA helicase DBP7"
FT /id="PRO_0000285147"
FT DOMAIN 177..372
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 406..596
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 144..173
FT /note="Q motif"
FT MOTIF 304..307
FT /note="DEAD box"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 733 AA; 81740 MW; 0222BD8393478C76 CRC64;
MDEDDGLLLN FAVPDVSVSS GSNKRTTSKV TGGKWKDRRK LQLSLQGRGR NQKKDRSATG
KDDGKKHEND ESNDSKKRPT IEPIHGPTSK MIKFSESKGE FGGKNNSYVS SLFTSNQSSS
QLKVTKESDE KTYLPSNAPV EDASTFEGLG INERLSKHLT ETLRFKNPTK VQKSVIPTML
STERDLFIKA QTGSGKTLSF LLPIFHKLMM ENKHKINRDS GLFAVILTPT RELATQIYGV
LETLTRCYHH IVPGIVIGGE KKKSEKARIR KGVNILVGTP GRLADHMENT ESLDISQLRW
LILDEGDKLV ELGFEETITK ITNLITRNSQ IMESMHKWQG LPVRRINLLC SATMQNNVEK
LGSIILNNPE MISDGSSSGK HSEEVTAPDQ LIQNVVVVPP KLRLVTLSAI LKKISSDMSG
TNNSTRTIVF FSCSDSVNFH FDVFTRGGNT FKKVKNDESG KLETVEVEND TPLIGQGTAV
YKLHGSLSQQ TRTSTLQAFI KDSKSNHSIL FCTDVASRGL DLPNIASVIE YDPPFTIDDH
LHRIGRSARV GKEGTATLFL LPGNEEGYVD GKLQVVHPKE GNLRIVNYEN YLKDGFSAKS
NNEDTKKKSK DPKSREGKWD IHATTWHLDI ERWLLEDSGA HDKAVQAFTS HIRAYATHLS
SERNYFNVKL LHLGHLAKSF GLRETPKKLG KSVESNSGIQ GASKKTKKED PRKKMLRMAK
MALKSNSDEF NYS
