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Database: UniProt
Entry: A0A0S7DZU6_9EURO
LinkDB: A0A0S7DZU6_9EURO
Original site: A0A0S7DZU6_9EURO 
ID   A0A0S7DZU6_9EURO        Unreviewed;       844 AA.
AC   A0A0S7DZU6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=ALT_002021 {ECO:0000313|EMBL:GIM42422.1};
OS   Aspergillus lentulus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM42422.1};
RN   [1] {ECO:0000313|EMBL:GIM42422.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM42422.1};
RA   Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT   "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT   lentulus IFM 54703T.";
RL   Genome Announc. 4:e01568-15(2016).
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   -!- SUBUNIT: Associates with pre-ribosomal particles.
CC       {ECO:0000256|ARBA:ARBA00044029}.
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:GIM42422.1}.
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DR   EMBL; BCLY01000016; GIM42422.1; -; Genomic_DNA.
DR   STRING; 293939.A0A0S7DZU6; -.
DR   VEuPathDB; FungiDB:TMP_alenIFM54703_7972; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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; 2.
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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:GIM42422.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242}.
SQ   SEQUENCE   844 AA;  93478 MW;  05D5EDCA093F1777 CRC64;
     MAPNSAIKKR AAAKDDDFVL TLSDDENDVL ENGVEEDGDN AEEDTLSSSR KRKREAAEAP
     KGKNKKQKQS KKSKKGESAA GAVSDDQSGE EGEAEAMDAG EDDGALDSEF EFDVGGNANT
     GVIEGFDGWE ARNGDGSADA AKNGNKKAVD IDDIISRRKA KKDAELKKKQ QKEKKRREEE
     EEEEEEEEEE EEEEEEEEGE DSENEDADSD GGMSVDFQDD ELLAADGFGM GADGADESGD
     DMEKDSSDGD DSDEQGSEDE EDDDDDDAAS DNDSVATPVH HPDDEAASDD ESEAESEVDA
     EEAEKRKAFF APEEKSTAAS TSNRSFQDFN LSRPILRGLA SVNFTTPTPI QQKTIPVALL
     GKDIVGSAVT GSGKTAAFVV PILERLLFRP RKVPTSRVAI LMPTRELAVQ CYNVATKLAT
     HTDITFCQLV GGFSLREQEN ILKKRPDVII ATPGRFIDHM RNSPSFTVDT LEILVLDEAD
     RMLEDGFADE LNEILTTIPK SRQTMLFSAT MTDSVDKLIR VGLNRPVRLM VDSKKNTSMN
     LTQEFVRLRP GREDKRLGYL LYLCNEIYTG RVIVFFRQKR EAHRVRIVFG LLGLKAAELH
     GSMSQEQRIK SVENFREGKV AFLLATDLAS RGLDIKGVET VINYEAPQNH EIYLHRVGRT
     ARAGRSGRAC TIAAEPDRKI VKSAVKAGKA QGAKIVSRVV DPAVADEWAA KAKGLEDEIE
     EVLQEEKLEK QMAQAEMHLT KGENMIKHEA EIMSRPKRTW FETERDKRAA RKLGATELNG
     PSQKDKVKLS NKDKKRLDDA RQRHEGNIGW KKGKADREAP KQGKNKESKN KSDKKNKIKM
     KGKK
//
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