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DRS1_PHANO
ID   DRS1_PHANO              Reviewed;         808 AA.
AC   Q0V1Z7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=ATP-dependent RNA helicase DRS1;
DE            EC=3.6.4.13;
GN   Name=DRS1; ORFNames=SNOG_01967;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(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: 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; CH445327; EAT90179.1; -; Genomic_DNA.
DR   RefSeq; XP_001792589.1; XM_001792537.1.
DR   AlphaFoldDB; Q0V1Z7; -.
DR   SMR; Q0V1Z7; -.
DR   STRING; 13684.SNOT_01967; -.
DR   EnsemblFungi; SNOT_01967; SNOT_01967; SNOG_01967.
DR   GeneID; 5969439; -.
DR   KEGG; pno:SNOG_01967; -.
DR   eggNOG; KOG0338; Eukaryota.
DR   HOGENOM; CLU_003041_3_1_1; -.
DR   InParanoid; Q0V1Z7; -.
DR   OMA; AAHTDIR; -.
DR   OrthoDB; 268859at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
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; 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; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Ribosome biogenesis; RNA-binding.
FT   CHAIN           1..808
FT                   /note="ATP-dependent RNA helicase DRS1"
FT                   /id="PRO_0000256023"
FT   DOMAIN          316..490
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          517..674
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           285..313
FT                   /note="Q motif"
FT   MOTIF           438..441
FT                   /note="DEAD box"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..188
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..214
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..792
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..808
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         329..336
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   808 AA;  89636 MW;  EBB59FAC13E2CBB7 CRC64;
     MAPRIDDDFV FTISDHDDVS DDGGAEEIAA ASAKLAGRGK KRKHTEDPDL NIRPKEAPSK
     KAKKDKKKGK KGKQAEPEPA AEDESDLEIA HPGEDVEGND DIDSEFEFAV GDIDTGFVEE
     FDGWGNAEGT VGREQNAEKK SNAVDIDDII ERRQNKKMAE KDTMSDSEDE ADKDDFSGFG
     EDDELLAEDG FGMGAGSDSD SEGDDEEDGD QDESKINNDS EGGAGESDDE DVAPHVPHPM
     DLEGAESDDA MSEQEDAVEA KKAAAFFAPE ESESGKKKKG AKSIGSFHAM SLSRPIQKGL
     AAIGFTEPTP IQAKAIPIAM QGKDVVGGAE TGSGKTAAFL IPILERLLYR PKKVPTTRVA
     IFMPTRELAV QCFNVATKLA SFTDITFALL AGGFSSREQE VMLKTRPDVV IATPGRFIDH
     MHNTAAFQVE HLEILVLDEA DRMLEEGFET QLNEILTTIP KSRQTMLFSA TMTSTVDKLI
     RIGMDKPVRL MVDAKKHTVK GLTQEFIRLR QGKEDKRLAY LMYICEKIYT ERVIIFFRQK
     KEAHRVRVVF ALCGLKASEL HGNMSQEQRI QAVEAFRSGK SSYLLATDVA SRGLDIKNVS
     TVINYEAPQS HEIYLHRVGR TARAGRSGRA CTLAAEPDRK VVKQAVKQSR DQGSKVVSRQ
     VPVEETDRWM EKLRGLEDEI EDVLKEEKEE RTLSITERDL KRGMNLIEHE AEIKSRPKRV
     WFETEKEKMA EREKGAAALN AAAGGSVKQK KKKLSGKDKK KLDARDERSE GKIWKKAKED
     RGMDTNRAKE KKALAKNKSK KISKLSRR
 
 
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