ID J8LL09_SACAR Unreviewed; 747 AA.
AC J8LL09;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=ATP-dependent RNA helicase DRS1 {ECO:0000256|ARBA:ARBA00044078};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=ATP-dependent RNA helicase drs1 {ECO:0000256|ARBA:ARBA00044094};
GN ORFNames=SU7_2134 {ECO:0000313|EMBL:EJS42747.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS42747.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS42747.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
CC -!- FUNCTION: ATP-binding RNA helicase involved in ribosome assembly.
CC {ECO:0000256|ARBA:ARBA00043881}.
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX27/DRS1
CC subfamily. {ECO:0000256|ARBA:ARBA00043999}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJS42747.1}.
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DR EMBL; ALIE01000139; EJS42747.1; -; Genomic_DNA.
DR AlphaFoldDB; J8LL09; -.
DR HOGENOM; CLU_003041_3_2_1; -.
DR OrthoDB; 149428at2759; -.
DR Proteomes; UP000006968; Chromosome XII.
DR GO; GO:0030684; C:preribosome; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProt.
DR CDD; cd17947; DEADc_DDX27; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR PANTHER; PTHR47959:SF14; DEAD-BOX ATP-DEPENDENT RNA HELICASE 28; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006968};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517}.
FT DOMAIN 226..254
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 257..432
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 443..634
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 17..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 616..656
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 226..254
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 119..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 83723 MW; 7B50EFE58F548C68 CRC64;
MVSGTKKFAD LDFVPTISDS EDDVPVLDSS DDEKVEDKKA AKKGKGKKKQ KKATNVDEVD
EDVHEDLDAG FKFDLDADDT TSNFQGWNFL GESNKDDPEA LVKKDVDLDK IIRRKGGLVK
MAHIDTKGEE EEEEQVKEEK TSNGDDEELA MDGFGMGAST NNENEDGSED ESEEEEEEEE
EEQEELTLEK GGKDDEVVEE DDSEEAKADF YAPEAEGDDA KKQVHGNFNT LSLSRPVLKG
LASLGYVKPS PIQSATIPIA LLGKDIIAGA VTGSGKTAAF MIPIIERLLY KPAKIAATRV
IVLLPTRELA IQVADVGKQI ARFLPGITFG LAVGGLNLRQ QEQLLKTRPD IVIATPGRFI
DHIRNSASFN VDSVEILVMD EADRMLEEGF QDELSEIMGL LPSNRQNLLF SATMNSKIKS
LVSLSLKRPV RIMIDPPKQA AARLTQEFVR IRKRDHLKPS LLFNLIRKLD PMGQKRIVVF
VARKETAHRL RIVMGLLGMG VGELHGSLTQ EQRLDSVNKF KNLEVPVLVC TDLASRGLDI
PKIEVVVNYD MPKSYEIYLH RVGRTARAGR EGRSVTLVGE SSQDRSIVRA AIKSVEEDKS
LTQGKALGRI VDWVQIEETN KLVESMSNTI EEILVEEKEE KEILRAEMQL RKGENMLKHK
KEIQARPRRT WFQSESDKKN SKLLGALSRN KKVTNSKKRK REEAIADDNG ARSYRKTKND
RITDQERTFK KQKSANPNKK KGFTKRR
//
