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