DRS1_YEAS7
ID DRS1_YEAS7 Reviewed; 754 AA.
AC A7A0P8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
DE AltName: Full=Deficiency of ribosomal subunits protein 1;
GN Name=DRS1; ORFNames=SCY_3572;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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: Interacts with RRP1 and associates with pre-ribosomal
CC 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; AAFW02000167; EDN59539.1; -; Genomic_DNA.
DR AlphaFoldDB; A7A0P8; -.
DR SMR; A7A0P8; -.
DR PRIDE; A7A0P8; -.
DR EnsemblFungi; EDN59539; EDN59539; SCY_3572.
DR HOGENOM; CLU_003041_3_2_1; -.
DR Proteomes; UP000007060; 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:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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 Phosphoprotein; Ribosome biogenesis; RNA-binding.
FT CHAIN 1..754
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000310216"
FT DOMAIN 264..439
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 450..641
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 623..669
FT /evidence="ECO:0000255"
FT MOTIF 233..261
FT /note="Q motif"
FT MOTIF 387..390
FT /note="DEAD box"
FT COMPBIAS 119..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32892"
SQ SEQUENCE 754 AA; 85102 MW; E9A2696CC750EE25 CRC64;
MVVGTKKYSN LDFVPTISDS EDDVPILDSS DDEKVEAKKT TKKRKGKNNK KKVSEGDNLD
EDVHEDLDAG FKFDLDADDT TSNFQGWNFL AEGESNKDDA EAFVKKDVDL DKIIRRKGGL
VKMAHIDSKQ EEETEKEKVE KENDSDDEEL AMDGFGMGAP MNNGDENQSE EEEEEEEEEE
EEEEEEEEEQ EEMTLEKGGK DDEIDEEDDS EEAKADFYAP ETEGDEAKKQ MYENFNSLSL
SRPVLKGLAS LGYVKPSPIQ SATIPIALLG KDIIAGAVTG SGKTAAFMIP IIERLLYKPA
KIASTRVIVL LPTRELAIQV ADVGKQIARF VSGITFGLAV GGLNLRQQEQ MLKSRPDIVI
ATPGRFIDHI RNSASFNVDS VEILVMDEAD RMLEEGFQDE LNEIMGLLPS NRQNLLFSAT
MNSKIKSLVS LSLKKPVRIM IDPPKKAATK LTQEFVRIRK RDHLKPALLF NLIRKLDPTG
QKRIVVFVAR KETAHRLRII MGLLGMSVGE LHGSLTQEQR LDSVNKFKNL EVPVLICTDL
ASRGLDIPKI EVVINYDMPK SYEIYLHRVG RTARAGREGR SVTFVGESSQ DRSIVRAAIK
SVEENKSLTQ GKALGRNVDW VQIEETNKLV ESMNDTIEDI LVEEKEEKEI LRAEMQLRKG
ENMLKHKKEI QARPRRTWFQ SESDKKNSKV LGALSRNKKV TNSKKRKREE AKADGNGARS
YRKTKTDRIA DQERTFKKQK STNSNKKKGF KSRR
