DRS1_SCHPO
ID DRS1_SCHPO Reviewed; 754 AA.
AC Q09903;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ATP-dependent RNA helicase drs1;
DE EC=3.6.4.13;
GN Name=drs1; ORFNames=SPAC30D11.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329670; CAA91889.1; -; Genomic_DNA.
DR PIR; S62561; S62561.
DR RefSeq; NP_593214.1; NM_001018610.2.
DR AlphaFoldDB; Q09903; -.
DR SMR; Q09903; -.
DR BioGRID; 279586; 3.
DR STRING; 4896.SPAC30D11.03.1; -.
DR MaxQB; Q09903; -.
DR PaxDb; Q09903; -.
DR EnsemblFungi; SPAC30D11.03.1; SPAC30D11.03.1:pep; SPAC30D11.03.
DR GeneID; 2543155; -.
DR KEGG; spo:SPAC30D11.03; -.
DR PomBase; SPAC30D11.03; -.
DR VEuPathDB; FungiDB:SPAC30D11.03; -.
DR eggNOG; KOG0338; Eukaryota.
DR HOGENOM; CLU_003041_3_1_1; -.
DR InParanoid; Q09903; -.
DR OMA; AAHTDIR; -.
DR PhylomeDB; Q09903; -.
DR PRO; PR:Q09903; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; NAS:PomBase.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0006364; P:rRNA processing; ISO:PomBase.
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..754
FT /note="ATP-dependent RNA helicase drs1"
FT /id="PRO_0000055086"
FT DOMAIN 290..464
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 475..641
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 121..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 655..728
FT /evidence="ECO:0000255"
FT MOTIF 259..287
FT /note="Q motif"
FT MOTIF 412..415
FT /note="DEAD box"
FT COMPBIAS 121..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..175
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..206
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..744
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 303..310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 754 AA; 85453 MW; 7A9BFF75F7D53E7C CRC64;
MLWNTQYFRI EGMISLGWPR LAKTSILKFV PIAQNHRIRK MKVQDDFILT IDDSEDDIHY
DDYDADAVDE EMPSNVELKK KSKKATPAKD SDFNGEFLFE ADVNKDLSSA TDMNWDFDMG
SKTESNRASN TVDLDAIISR NRKPDDDEFP SSFPSEEELQ EPEQENIDSD DEDLAIDGFG
AGAIAENEDE SSQDESESEE EDDITEPVPS FANISTQDFN SDSAAGSSDS EEDEEEIAKK
NAFFAEGDKE KSMMTTTHSS FQSMNLSRPI LKGLSNLGFE VPTQIQDKTI PLALLGKDIV
GAAVTGSGKT AAFIVPILER LLYRPKKVPT TRVLILCPTR ELAMQCHSVA TKIASFTDIM
VCLCIGGLSL KLQEQELRKR PDIVIATPGR FIDHMRNSQG FTVENIEIMV MDEADRMLED
GFADELNEII QACPKSRQTM LFSATMTDKV DDLIRLSLNR PVRVFVDNKK TTAKLLTQEF
VRVRPQRELL RPAMLIYLCK ELFHRRTIIF FRSKAFAHKM RVIFGLLSLN ATEIHGSLSQ
EQRVRALEDF RDGKCNYLLA TDVASRGIDI KGIEVVINYE APATHEVYLH RVGRTARAGR
SGRAITLAGE GDRKVLKGVF KNSSAQNTKL VNRNLDFNKV EKFGKEIEEL EPVVQKVLDE
EKQERELKIA ERDLKKGENI MKYGDEIRSR PARTWFQSEK DKQASKASEA KDKKSLAKRK
KQMEKEEVPR AYKKTKNDRL SNKKSTKKSK SKRK
