DRS1_ASHGO
ID DRS1_ASHGO Reviewed; 734 AA.
AC Q75F95;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=ATP-dependent RNA helicase DRS1;
DE EC=3.6.4.13;
GN Name=DRS1; OrderedLocusNames=AAL164C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016814; AAS50202.1; -; Genomic_DNA.
DR RefSeq; NP_982378.1; NM_207731.1.
DR AlphaFoldDB; Q75F95; -.
DR SMR; Q75F95; -.
DR STRING; 33169.AAS50202; -.
DR EnsemblFungi; AAS50202; AAS50202; AGOS_AAL164C.
DR GeneID; 4618422; -.
DR KEGG; ago:AGOS_AAL164C; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_2_1; -.
DR InParanoid; Q75F95; -.
DR OMA; AAHTDIR; -.
DR Proteomes; UP000000591; Chromosome I.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
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:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
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..734
FT /note="ATP-dependent RNA helicase DRS1"
FT /id="PRO_0000227955"
FT DOMAIN 250..425
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 436..599
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 116..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 619..697
FT /evidence="ECO:0000255"
FT MOTIF 219..247
FT /note="Q motif"
FT MOTIF 373..376
FT /note="DEAD box"
FT COMPBIAS 118..135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 734 AA; 81244 MW; 0C77B6A9AE0162F0 CRC64;
MGTKKVNQFK DFVPTISDSE EDIPDLDASD DEYETAGKVK SRKKTKKGRK GGAVIADDED
AHADLNPEFH FNDEGAEGTT DFSGWDFVGD GERAEQKDVD LDGIIRRKGG LVQLAGVEES
EEEVEEAESA AGASDDEELA LDGFGMGAVA QREAAGAADE SDSESDKDSD NSAEEAVELD
GVEFGDEQEE AREEDTAEEM AQFYAPSNEG EEAKNVVHST FNSLSLSRPV LKGLAALGYT
KPSPIQGATI PIALLGKDVI AGAVTGSGKT AAFMIPIIER LLYKPAKIAS TRVLVLTPTR
ELAIQVADVG KKLGKFVSGL TFGLAVGGLN LRQQEQALKL RPDIVIATPG RIIDHIRNSA
SFSVDSVEVL VIDEADRMLE DGFQDELNEI MSLIPSKRQT LLFSATMNSR IKQLISLSLK
KPVRIMIDPP KQAANKLTQE FVRLRKREHL KPALLYHLLR KLDSTGQKRI VVFVARKEVA
HRLRVILGLL GMKAGELHGS LTQEQRLQSV NNFKSLDVPV LVCTDLASRG LDIPKIEVVI
NYDMPKTYEI YLHRVGRTAR AGREGKSVTL VGESTQERSI VKDAIKSVDG SKGSGRACGR
VVDWKQVEEI HKLVQAKEDV IGEILEEEKQ EKEILRAEME IRKGENMLKF KEEINARPRR
TWFQSESEKK NSSILQALSK NKKVTNSKKR KREEAQQEVG SRQYKKTQKD RTTNQELAFR
KQKKGGNKKK KVRK
