DRS1_VANPO
ID DRS1_VANPO Reviewed; 752 AA.
AC A7TJM9;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
GN Name=DRS1; ORFNames=Kpol_534p53;
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 ribosome assembly.
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: Associates with pre-ribosomal particles. {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. DDX27/DRS1
CC subfamily. {ECO:0000305}.
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DR EMBL; DS480402; EDO17572.1; -; Genomic_DNA.
DR RefSeq; XP_001645430.1; XM_001645380.1.
DR AlphaFoldDB; A7TJM9; -.
DR SMR; A7TJM9; -.
DR STRING; 436907.A7TJM9; -.
DR EnsemblFungi; EDO17572; EDO17572; Kpol_534p53.
DR GeneID; 5545797; -.
DR KEGG; vpo:Kpol_534p53; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_2_1; -.
DR InParanoid; A7TJM9; -.
DR OMA; AAHTDIR; -.
DR OrthoDB; 268859at2759; -.
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:0042254; P:ribosome biogenesis; 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; IPR000629; RNA-helicase_DEAD-box_CS.
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; 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; Coiled coil; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..752
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000310215"
FT DOMAIN 262..437
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 448..611
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 24..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 631..698
FT /evidence="ECO:0000255"
FT MOTIF 231..259
FT /note="Q motif"
FT MOTIF 385..388
FT /note="DEAD box"
FT COMPBIAS 26..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..209
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..752
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 752 AA; 84998 MW; 2FACC25F9AFD3EFA CRC64;
MAVTSDRKNN RKKAITKFND LDFVPTISDS EEDVPDLDDS DDELLTSENK SVKTPAKSKK
GKKNDPVKIN GNGDEVAEDL NPDFRFNIDG GELSTNFQGW DFVGDQKEND DDMKKDVDLD
GIIRRKGGLL NMAHIEVAEE EEEEEEEEEE EEEEEEEELA MDGFGMGATK KNEQEEAGDE
DDDDNEEEEE EEVDDDKEDD DEEREEDTAE EMASFYAPES ESSEATSTVH STFNSLTLSR
PVLKGLSDLG YTKPSPIQSA TIPIGLSGKD IIAGAVTGSG KTAAFMIPII ERLLYKPAKV
ASTRVIVLTP TRELAIQIAD VGKKIGKYVS GLTFGLAVGG LNLRQQEQEL KTRPDIVIAT
PGRFIDHVRN SSSFNVDSVE VLVMDEADRM LEEGFQEELN EILTLLPSKR QTLLFSATMN
SRIKSLISLS LRKPVRIMIN PPKQAAARLT QEFVRIRKRD HLKPALLFYL IRKLDGTGQK
RIVVFVARKE MAHKLRIILG LLGMKVGELH GSLTQEQRLQ SVNNFKSLEV PVLICTDLAS
RGLDIPKIEV VINFDMPKSY EIYLHRVGRT ARAGREGRSV TFVGESSQDR SIVRSAIKSV
EESSSKNKAV SRNVEWTQIE ETNKLVESFG ETIDDILVEE KQEKEILRAE MQLRKGENMI
KHKKEIQSRP KRTWFQSEAE KKNAKILDTL QKNKKTVNSK KRKRLEALED NDNSRSYKKT
QKDRVVDQER SMKKQKIANG KKSKNKKKFN KR
